Marius Clore publications

G. Marius CLORE: publications

h-index: 118 from Web of Science (Institute for Scientific Information); 136 from Google Scholar (the h index is defined as the number of papers h that have h or more citations; J. E. Hirsch (2005) Proc. Natl. Acad. Sci. U.S.A. 102, 16569-16572. PDF Pubmed; P. Ball (2005) Nature 436, 900)

1977

1. Clore, G.M. & Chance, E.M. (1977) A computer analysis of cyanide stimulated oxygen uptake in Chlorella protothecoides. FEBS Lett. 79, 353-356. PDF FEBS

1978
2. Clore, G.M. & Shephard, E.P. (1978) Exact solution of the mass transfer equations of gel filtration chromatography by means of a formal inversion of the Laplace transform, and the derivation on an equation for the time spent by a molecule in the gel phase. J. Chromatogr. 152, 1-10. PDF J. Chromatogr.
3. Clore, G.M. & Chance, E.M. (1978) The mechanism of the reaction of fully reduced membrane bound cytochrome oxidase with oxygen at 176 K. Biochem. J. 173, 799-810. pubmed PDF
4. Clore, G.M. & Chance, E.M. (1978) The kinetics of the reaction of ferricyanide pretreated mixed valence state membrane bound cytochrome oxidase with oxygen at 173 K. Biochem. J. 173, 811-820. pubmed PDF
5. Clore, E.M. & Chance, E.M. (1978) The kinetics and thermodynamics of the reaction of solid state fully reduced membrane bound cytochrome oxidase with carbon monoxide as studied by dual wavelength multichannel spectroscopy and flash photolysis. Biochem. J. 175, 709-725. pubmed PDF

1979
6. Clore, E.M. & Chance, E.M. (1979) Low temperature kinetics of the reaction of fully reduced membrane bound cytochrome oxidase with oxygen in the Soret, a and near infrared regions. Biochem. J. 177, 613-621. pubmed PDF
7. Clore, G.M. (1979) The mechanism of the fully reduced and mixed valence state membrane bound cytochrome oxidase-oxygen reactions in the 173-176 K temperature range. In Cytochrome Oxidase (King, T.E., Orii, Y., Chance, B. and Okunuki, K., eds.) pp. 341-352, North Holland Elsevier, Amsterdam.
8. Denis, M. & Clore, G.M. (1979) A temperature induced absorption band centered in the region of 666 nm related to the configuration of the active site in frozen cytochrome oxidase. Biochim. Biophys. Acta 545, 483-495. pubmed PDF
9. Karlsson, B., Andreasson, L.E., Aasa, R., Malmstrom, B.G. & Clore, G.M. (1979) Studies of the reaction of cytochrome c oxidase with oxygen at low temperature. Acta Chem. Scand. Ser. B 33, 615-618. PDF Acta Chem. Scand.

1980
10. Clore, G.M., Andreasson, L.E., Karlsson, B., Aasa, R. & Malstrom, B.G. (1980) Characterization of the low temperature intermediates of the reaction of fully reduced soluble cytochrome oxidase with oxygen by electron paramagnetic resonance and optical spectroscopy. Biochem. J. 185, 139-154. pubmed PDF
11. Clore, G.M., Andreasson, L.E., Karlsson, B., Aasa, R. & Malmstrom, B.G. (1980) Characterization of the intermediates in the reaction of mixed valence state soluble cytochrome oxidase with oxygen at low temperatures by optical and electron paramagnetic resonance spectroscopy. Biochem. J. 185, 155-167. pubmed PDF
12. Clore, G.M. (1980) Chracterization of the intermediates in the reaction of membrane bound mixed valence state cytochrome oxidase with oxygen at low temperatures by optical spectroscopy in the visible region. Biochem. J. 187, 617-622. pubmed PDF
13. Clore, G.M. (1980) The mechanism of reduction of dioxygen by fully reduced cytochrome oxidase: correlation of room and low temperature studies. Rev. Inorg. Chem. 2, 343-360.
14. Clore, G.M. & Chance, E.M. (1980) CO binding to mitochondrial mixed valence state cytochrome oxidase at low temperatures. Biochim. Biophys. Acta 590, 34-49. pubmed PDF
15. Campbell, J.R., Clark, R.J.H., Clore, G.M. & Lane, A.N. (1980) Characterization of the electronic properties and geometric environment of the iron atom in the 'myoglobin-hydrogen peroxide' complex by Soret-excited resonance Raman spectroscopy. Inorg. Chim. Acta 46, 77-84. PDF Inorg. Chim. Acta
16. Clore, G.M., Lane, A.N. & Hollaway, M.R. (1980) The kinetics of the reaction of aquo Fe(III) myoglobin with hydrogen peroxide at pH 8. Inorg. Chim. Acta 46, 139-146. PDF Inorg. Chim. Acta

1981
17. Clore, G.M. (1981) A re-evaluation of the low temperature kinetics of the reaction of fully reduced mitochondrial cytochrome oxidase with carbon monoxide and the spectral characterization of species I_C in the Soret and visible regions. Biochim. Biophys Acta 634, 129-139. pubmed PDF
18. Chance, E.M., Clore, G.M., Curtis, A.R. & Shephard, E.P. (1981) Numerical solution of the Hodgkin-Huxley equations in a moving coordinate system: simulation of nerve impulse transmission over long distances. J. Comp. Phys. 40, 318-326. PDF J. Comp. Phys.
19. Clore, G.M. & Denis, M. (1981) Spectroscopic evidence for an oxygen bridge between the iron atom of cytochrome a₃ and Cu_B in the Class C group of compounds formed in the reaction of mixed valence state cytochrome oxidase with oxygen. Inorg. Chim. Acta 55, L47-L49. PDF Inorg. Chim. Acta
20. Denis, N. & Clore, G.M. (1981) The reaction of mixed valence state cytochrome oxidase with oxygen in plant mitochondria: a study by low temperature flash photolysis and rapid wavelength scanning optical spectroscopy. Plant Physiol. 68, 229-235. Pubmed PDF
21. Clore, G.M. (1981) The mechanism of the reaction of fully reduced cytochrome oxidase with oxygen at low temperatures: a kinetic study by electron paramagnetic resonance and optical spectroscopy. In Oxygen and Life, Royal Society of Chemistry Special Publications No. 39, pp. 189-198, The Royal Society of Chemistry, London.
22. Clore, G.M., Hollaway, M.R., Orengo, C., Peterson, J. & Wilson, M. (1981) The mechanism of the reactions of low spin ferric haem undecapeptide with hydrogen peroxide. Inorg. Chim. Acta 56, 143-148. PDF Inorg. Chim. Acta
23. Birdsall, B., Gronenborn, A.M., Clore, G.M., Roberts, G.C.K., Feeney, J. & Burgen, A.S.V. (1981) ¹³C-NMR evidence for three slowly interconverting conformations of the dihydrofolate reductase-NADP+-folate complex. Biochem. Biophys. Res. Commun. 101, 1139-1141. pubmed PDF
24. Gronenborn, A.M., Clore, G.M. & Davies, R.W. (1981) Modulation of specific binding of Lactobacillus casei dihydrofolate reductase to DNA by folinic acid. FEBS Lett. 133, 92-94. pubmed PDF
25. Clore, G.M., Roberts, G.C.K., Gronenborn, A.M., Birdsall, B & Feeney, J. (1981) Transfer of saturation NMR studies of protein-ligand complexes: the case of three site exchange. J. Magn. Reson. 45,151-161. PDF J. Magn. Reson.
26. Gronenborn, A.M., Clore, G.M., Blazy, B. & Baudras, A. (1981) Conformational selection of syn-cAMP upon binding to the cAMP receptor protein: a ¹H-NMR study. FEBS Lett. 136, 160-164. pubmed PDF

1982
27. Clore, G.M. & Gronenborn, A.M. (1982) Kinetic and structural studies on the intermediates formed in the reactions of 5'-adenosine monophosphate and 5'-guanosine monophosphate with cis-dichlorodiammineplatinum II using ¹H and ¹⁹⁵Pt magnetic resonance spectroscopy. J. Am. Chem. Soc. 104, 1369-1375. PDF ACS
28. Clore, G.M., Gronenborn, A.M. & Davies, R.W. (1982) Theoretical aspects of specific and non-specific equilibrium binding of a protein to DNA as studied by the nitrocellulose filter binding assay: cooperative and non-cooperative binding to a one-dimensional lattice. J. Mol. Biol. 155, 447-466. pubmed PDF
29. Clore, G.M. & Gronenborn, A.M. (1982) Theory and applications of the transferred nuclear Overhauser effect to the study of the conformations of small ligands bound to proteins. J. Magn. Reson. 48, 402-417. PDF J. Magn. Reson.
30. Gronenborn, A.M. & Clore, G.M. (1982) Conformation of NAD+ bound to yeast and horse liver alcohol dehydrogenase in solution: the use of the proton-proton transferred nuclear Overhauser enhancement. J. Mol. Biol. 157, 155-160. pubmed PDF
31. Takahashi, M., Gronenborn, A.M., Clore, G.M., Blazy, B. & Baudras, B. (1982) DNA binding of cAMP receptor protein and its N-terminal core stabilizes the double helix and is modulated by cAMP. FEBS Lett. 139, 37-40. PDF FEBS Lett.
32. Gronenborn, A.M. & Clore, G.M. (1982) Proton nuclear magnetic resonance studies on cyclic nucleotide binding to the Escherichia coli adenosine 3',5'-phosphate receptor protein. Biochemistry 21, 4040-4048. pubmed PDF
33. Clore, G.M. & Gronenborn, A.M. (1982) A proton nuclear magnetic resonance study of the histidine residues of the Escherichia coli adenosine 3',5'-phosphate receptor protein: pH titration behaviour, deuterium exchange and partial assignments. Biochemistry 21, 4048-4053. pubmed PDF
34. Clore, G.M. & Gronenborn, A.M. (1982) Determination of the conformations of cyclic nucleotides bound to the N-terminal core of the cyclic AMP receptor protein of Escherichia coli by ¹H-NMR. FEBS Lett. 145, 197-202. pubmed PDF
35. Clore, G.M., Gronenborn, A.M., Mitchinson, C. & Green, N.M. (1982) 1H-NMR studies on nucleotide binding to the sarcoplasmic reticulum Ca2+ATPase: determination of the conformations of bound nucleotides by the measurement of proton-proton transferred nuclear Overhauser enhancements. Eur. J. Biochem. 128, 113-117. pubmed PDF
36. Birdsall, B., Gronenborn, A.M., Hyde, E.I., Clore, G.M., Roberts, G.C.K., Feeney, J. & Burgen, A.S.V. (1982) ¹H, ¹³C and ³¹P NMR studies of the dihydrofolate reductase-NADP+-folate complex: characterization of three coexisting conformational states. Biochemistry 21, 5831-5838. pubmed PDF

1983
37. Clore, G.M. (1983) Computer analysis of transient kinetic data. In Computing in Biological Science (Geisow, M.J. & Barrett, A.N., eds.) pp. 313-348, Elsevier North-Holland, Amsterdam.
38. Unger, B., Clore, G.M., Gronenborn, A.M. & Hillen, W. (1983) Specific DNA binding of the cyclic AMP receptor protein with the lac operon stabilizes double stranded DNA in the presence of cAMP. EMBO J. 2, 289-293. pubmed PDF
39. Gronenborn, A.M., Clore, G.M. & Gronenborn, B. (1983) Protection against nuclease cleavage of pBR 322 DNA by the cyclic AMP receptor protein of Escherichia coli. J. Mol. Biol. 166, 93-98. pubmed PDF
40. Gronenborn, A.M. & Clore, G.M. (1983) Characterization of the DNA binding region recognized by dihydrofolate reductase from Lactobacillus casei. J. Biol. Chem. 258, 11256-11259. pubmed PDF
41. Clore, G.M. & Gronenborn, A.M. (1983) Theory of the time dependent transferred nuclear Overhauser effect: application to the structural analysis of ligand-protein complexes in solution. J. Magn. Reson. 53, 423-442. PDF J. Magn. Reson.
42. Clore, G.M., Kimber, B.J. & Gronenborn, A.M. (1983) The 1-1 hard pulse: a novel, simple and effective method of water resonance suppression in FT-¹H-NMR. J. Magn. Reson. 54, 170-173. PDF J. Magn. Reson.
43. Barrett, A.N., Roberts, G.C.K., Burgen, A.S.V. & Clore, G.M. (1983) Ab initio molecular orbital calculations of electron distribution in the tetramethylammonium ion. Molec. Pharmacol. 24, 443-448. pubmed PDF
44. Martin, S.R., Gronenborn, A.M. & Clore, G.M. (1983) Specific DNA binding of the cAMP receptor protein to a synthetic oligodeoxyribonucleotide: a circular dichroism study. FEBS Lett. 159, 102-106. pubmed PDF
45. Gronenborn, A.M., Kimber, B.J., Clore, G.M. & McLaughlin, L.W. (1983) A nuclear magnetic resonance study of the ribotrinucleoside diphosphate UpUpC. Nucl. Magn. Res. 11, 5691-5699. pubmed PDF
46. Clore, G.M., Gronenborn, A.M. & Davies, R.W. (1983) Cooperative non-specific DNA binding of the N-terminal core of the cyclic AMP receptor protein of Escherichia coli and its modulation by cyclic AMP. FEBS Lett. 164, 57-612. pubmed PDF
47. Clore, G.M. & Gronenborn, A.M. (1983) Sequence dependent structural variations in two right handed alternating pyrimidine-purine DNA oligomers in solution determined by nuclear Overhauser enhancement measurements. EMBO J. 2, 2109-2115. pubmed PDF

1984
48. Gronenborn, A.M., Clore, G.M., Jones, M.B. & Jiricny, J. (1984) A nuclear Overhauser enhancement study on the imino proton resonances of a DNA pentadecamer comprising the specific target site of the cyclic AMP receptor protein in the ara BAD operon. FEBS Lett. 165, 216-222. pubmed PDF
49. Clore, G.M., Gronenborn, A.M., Birdsall, B.M., Feeney, J. & Roberts, G.C.K. (1984) 19F-NMR studies of 3',5'-difluoromethotrexate binding to Lactobacillus casei dihydrofoate reductase: molecular motion and coenzyme induced conformational changes. Biochem. J. 217, 659-666. pubmed PDF
50. Gronenborn, A.M., Papadopoulos, P. & Clore, G.M. (1984) Immunochemical evidence for extensive ligand induced conformational changes in Lactobacillus casei dihydrofolate reductase. J. Biol. Chem. 259, 1082-1085. pubmed PDF
51. Antonjuk, D.J., Birdsall, B.M., Chang, H.T.A., Clore, G.M., Feeney, J., Gronenborn, A.M., Roberts, G.C.K. & Tran, T.Q. (1984) A 1H-NMR study of the role of the glutamate moiety in the binding of methotrexate to Lactobacillus casei dihydrofolate reductase. Bri. J. Pharmacol. 81, 309-315. pubmed PDF
52. Gronenborn, A.M., Clore, G.M. & Jeffery, J. (1984) An unusual conformation of NAD+ bound to sorbitol dehydrogenase: a time dependent transferred nuclear Overhauser effect study. J. Mol. Biol. 172, 559-572. pubmed PDF
53. Clore, G.M., Gronenborn, A.M. & McLaughlin, L.W. (1984) The structure of the ribotrinucleoside diphosphate codon UpUpC bound to tRNA^Phe from yeast: a time dependent transferred nuclear Overhauser effect study. J. Mol. Biol. 174, 163-173. pubmed PDF
54. Clore, G.M. & Gronenborn, A.M. (1984) A Nuclear Overhauser enhancement study of the solution structure of a double stranded DNA undecamer comprising a portion of the specific target site for the cyclic AMP receptor protein in the gal operon: sequential resonance assignment. Eur. J. Biochem. 141, 119-129. pubmed PDF
55. Gronenborn, A.M., Clore, G.M. & Kimber, B.J. (1984) An investigation into the solution structures of two self-complementary DNA oligonucleotides 5'd-CGTACG and 5'd- ACGCGCGT by means of nuclear Overhauser enhancement measurements. Biochem. J. 221, 723-736. pubmed PDF
56. Clore, G.M., Gronenborn, A.M., Piper, E.A., McLaughlin, L.W., Graeser, E. & van Boom, J.H. (1984) The solution structure of a RNA pentadecamer comprising the anticodon loop and stem of yeast tRNA^Phe: a 500 MHz ¹H-NMR study. Biochem. J. 221, 737-751. pubmed PDF
57. Birdsall, B.M., Bevan, A.W., Pascual, C., Roberts, G.C.K., Feeney, J., Gronenborn, A.M. & Clore, G.M. (1984) Multinuclear NMR characterization of two coexisting conformational states of the Lactobacillus casei dihydrofolate reductase-trimethoprim-NADP⁺ complex. Biochemistry 23, 4733-4742. pubmed PDF
58. Gronenborn, A.M., Clore, G.M., Brunori, M., Giardina, B., Falcioni, G. & Perutz, M.F. (1984) Stereochemistry of ATP and GTP bound to fish haemoglobins: a transferred nuclear Overhauser enhancement, ³¹P-NMR, oxygen equilibrium and molecular modelling study. J. Mol. Biol. 178, 731-742. pubmed PDF
59. Clore, G.M. & Gronenborn, A.M. (1984) An investigation into the solution structure of the single stranded DNA undecamer 5'd- AAGTGTGATAT by means of nuclear Overhauser enhancement measurements. Eur. Biophys. J. 11, 95-102. pubmed PDF
60. Clore, G.M. & Gronenborn, A.M. (1984) Internal mobility in a double stranded B DNA hexamer and undecamer: a time dependent proton-proton nuclear Overhauser enhancement study. FEBS Lett. 172, 219-225. pubmed PDF
61. Clore, G.M. & Gronenborn, A.M. (1984) Interproton distance measurements in solution for a double stranded DNA undecamer comprising a portion of the specific target site for the cyclic AMP receptor protein in the gal operon: a nuclear Overhauser enhancement study. FEBS Lett. 175, 117-123. pubmed PDF
62. Gronenborn, A.M., Clore, G.M., McLaughlin, L.W., Graeser, E., Lorber, B. & Giege, R. (1984) Yeast tRNA^Asp - Codon and wobble codon-anticodon interactions: a transferred nuclear Overhauser enhancement study. Eur. J. Biochem. 145, 359-364. pubmed PDF
63. Gronenborn, A.M., Clore, G.M., Hobbs, L. & Jeffery, J. (1984) Glucose-6-phosphate dehydrogenase: a transferred nuclear Overhauser effect study of NADP⁺ conformations in enzyme-coenzyme binary complexes. Eur. J. Biochem. 145, 365-371. pubmed PDF
64. Clore, G.M., Lauble, H., Frenkiel, T.A. & Gronenborn, A.M. (1984) A two-dimensional NMR study of the solution structure of a DNA dodecamer comprising the consensus sequence for the specific DNA binding sites of the glucocorticoid receptor protein. Eur. J. Biochem. 145, 629-636. pubmed PDF
65. Gronenborn, A.M., Nermut, M.V., Eason, P. & Clore, G.M. (1984) Visualization of cAMP receptor protein induced DNA kinking by electron microscopy. J. Mol. Biol. 179, 751-757. pubmed PDF

1985
66. Clore, G.M. & Gronenborn, A.M. (1985) Assessment of errors involved in the determination of interproton distance ratios and distances by means of one- and two-dimensional NOE measurements. J. Magn. Reson. 61, 158-164. PDF J. Magn. Reson.
67. Clore, G.M. & Gronenborn, A.M. (1985) Probing the three-dimensional structures of DNA and RNA oligonucleotides in solution by nuclear Overhauser enhancement measurements. FEBS Lett. 179, 187-198. pubmed PDF
68. Gronenborn, A.M. & Clore, G.M. (1985) Investigations into the solution structures of short nucleic acid fragments by means of nuclear Overhauser enhancement measurements. Progr. Nucl. Magn. Reson. Spectroscopy 17, 1-32. PDF Progr. NMR Spectr.
69. Andrews, J., Clore, G.M., Davies, R.W., Gronenborn, A.M., Gronenborn, B., Kalderon, D., Papadopoulos, P.C., Schafer, S., Sims, P.F.G. & Stancombe, R. (1985) Nucleotide sequence of the dihydrofolate reductase gene of methotrexate resistant Lactobacillus casei. Gene 35, 217-222. pubmed PDF
70. Perutz, M.F., Gronenborn, A.M., Clore, G.M., Hogg, J.H. & Shi, T. (1985) The pKa's of two histidines in human haemoglobin, the Bohr effect and the dipole moment of a-helices. J. Mol. Biol. 183, 491-498. pubmed PDF
71. Perutz, M.F., Gronenborn, A.M., Clore, G.M., Shi, T. & Craescu, C.T. (1985) Comparison of histidine proton magnetic resonances of human carbonmonoxy haemoglobin in different buffers. J. Mol. Biol. 186, 471-473. pubmed PDF
72. Clore, G.M. & Gronenborn, A.M. (1985) The solution structure of a B-DNA undecamer comprising a portion of the specific target site for the cyclic AMP receptor protein in the gal operon: refinement on the basis of interproton distance data. EMBO J. 4, 829-835. pubmed PDF
73. Clore, G.M., Gronenborn, A.M., Moss, D.S. & Tickle, I.J. (1985) Refinement of the solution structure of the B-DNA hexamer 5'd(CGTACG)₂ on the basis of interproton distance data. J. Mol. Biol. 185, 219-226. pubmed PDF
74. Clore, G.M., Gronenborn, A.M. & McLaughlin, L.W. (1985) The structure of the double stranded RNA pentamer 5'(CACAG).5'(CUGUG) by nuclear Overhauser enhancement measurements: interproton distance determination and structure refinement on the basis of X-ray coordinates. Eur. J. Biochem. 151, 153-165. pubmed PDF
75. Clore, G.M., Gronenborn, A.M., Brunger, A.T. & Karplus, M. (1985) The solution conformation of a heptadecapeptide comprising the DNA binding helix F of the cyclic AMP receptor protein of Escherichia coli: combined use of ¹H-nuclear magnetic resonance and restrained molecular dynamics. J. Mol. Biol. 186, 435-455. pubmed PDF

1986
76. Clore, G.M. & Gronenborn, A.M. (1986) Determination of three-dimensional structures of oligonucleotides in solution: combined use of nuclear Overhauser enhancement measurements and restrained least squares refinement. In Biomolecular Stereodynamics IV (Sarma, R.H., ed.) pp. 139-155, Adenine Press, New York.
77. Gronenborn, A.M. & Clore, G.M. (1986) The solution structure of RNA fragments by nuclear Overhauser enhancement measurements. In Structure and Dynamics of RNA, (van Knippenberg, R.H. & Hilbers, C.W., eds.) pp. 137-150, NATO ASI series, Plenum Press, New York.
78. Gronenborn, A.M. & Clore, G.M. (1986) Overproduction of the cAMP receptor protein of Escherichia coli and expression of the engineered carboxy-terminal DNA binding domain. Biochem. J. 236, 643-649. pubmed PDF
79. Clore, G.M., Gronenborn, A.M., Greipel, J. & Maass, G. (1986) The conformation of the single stranded DNA undecamer 5'd(AAGTGTGATAT) bound to single stranded DNA binding protein of Escherichia coli: a time dependent transferred nuclear Overhauser enhancement study. J. Mol. Biol. 187, 119-124. pubmed PDF
80. Nilsson, L., Clore, G.M., Gronenborn, A.M., Brunger, A.T. & Karplus, M. (1986) Structure refinement of oligonucleotides by molecular dynamics with NOE interproton distance restraints: application to 5'd(CGTACG)₂. J. Mol. Biol. 188, 455-475. pubmed PDF
81. Clore, G.M., Gronenborn, A.M. Carlson, G. & Meyer, E.F. (1986) Stereochemistry of binding of the tetrapeptide Acetyl-Pro-Ala-Pro-TyrNH2 to porcine pancreatic elastase: combined use of two-dimensional transferred nuclear Overhauser enhancement measurements, restrained molecular dynamics, X-ray crystallography and molecular modelling. J. Mol. Biol. 190, 259-267. pubmed PDF
82. Brunger, A.T., Clore, G.M., Gronenborn, A.M. & Karplus, M. (1986) Three-dimensional structures of proteins determined by molecular dynamics with interproton distance restraints: application to crambin. Proc. Natl. Acad. Sci. U.S.A. 83, 3801-3805. pubmed PDF
83. Clore, G.M., Brunger, A.T., Karplus, M. & Gronenborn, A.M. (1986) Application of molecular dynamics with interproton distance restraints to three-dimensional protein structure determination: a model study of crambin. J. Mol. Biol. 191, 523-551. pubmed PDF
84. Clore, G.M., Martin, S.R. & Gronenborn, A.M. (1986) The solution structure of human growth hormone releasing factor: combined use of circular dichroism and nuclear magnetic resonance spectroscopy. J. Mol. Biol. 191, 553-561. pubmed PDF
85. Gronenborn, A.M., Clore, G.M., Schmeissner, U. & Wingfield, P.T. (1986) Sequence specific assignments of aromatic residues in the ¹H-NMR spectrum of human interleukin-1b using site directed mutant proteins. Eur. J. Biochem. 161, 37-43. pubmed PDF
86. Zarbock, J., Clore, G.M. & Gronenborn, A.M. (1986) Nuclear magnetic resonance study of the globular domain of chicken histone H5: resonance assignment and secondary structure. Proc. Natl. Acad. Sci. U.S.A. 23, 7628-7632. pubmed PDF
87. Minter, S.J., Clore, G.M., Gronenborn, A.M. & Davies, R.W. (1986) Cooperative DNA binding by lambda integration protein - a key component of specificity. Eur. J. Biochem. 161, 727-731. pubmed PDF
88. Clore, G.M., Nilges, M., Sukumaran, D.K., Brunger, A.T., Karplus, M. & Gronenborn, A.M. (1986) The three-dimensional structure of a1-purothionin in solution: combined use of nuclear magnetic resonance, distance geometry and restrained molecular dynamics. EMBO J. 5, 2729-2735. Pubmed PDF
89. MacDonald, H.R., Wingfield, P., Schmeissner, U., Shaw, A., Clore, G.M. & Gronenborn, A.M. (1986) Point mutations of human interleukin-1 with decreased receptor binding affinity. FEBS Lett. 209, 295-298. pubmed PDF

1987
90. Clore, G.M., Sukumaran, D.K., Gronenborn, A.M., Teeter, M.M., Whitlow, M. & Jones, B.L. (1987) A nuclear magnetic resonance study of the solution structure of a1-purothionin: sequential resonance assignment, secondary structure and low resolution tertiary structure. J. Mol. Biol. 193, 571-578. pubmed PDF
91. Gent, M., Gronenborn, A.M., Davies, R.W. & Clore, G.M. (1987) Probing the sequence specific interaction of the cAMP receptor protein with DNA by site directed mutagenesis. Biochem. J. 242, 645-653. pubmed PDF
92. Sukumaran, D.K., Clore, G.M., Preuss, A., Zarbock, J. & Gronenborn, A.M. (1987) A proton nuclear magnetic resonance study of hirudin: resonance assignment and secondary structure. Biochemistry 26, 333-338. PDF ACS
93. Clore, G.M., Sukumaran, D.K., Nilges, M. & Gronenborn, A.M. (1987) The three-dimensional structure of phoratoxin in solution: combined use of nuclear magnetic resonance, distance geometry and restrained molecular dynamics. Biochemistry 26, 1732-1745. PDF ACS
94. Brünger, A.T., Campbell, R.L., Clore, G.M., Gronenborn, A.M., Karplus, M., Petsko, G.A. & Teeter, M.M. (1987) Solution of a protein crystal structure with a model obtained from NMR interproton distance restraints. Science 235, 1049-1053. pubmed PDF
95. Clore, G.M., Sukumaran, D.K., Nilges, M., Zarbock, J. & Gronenborn, A.M. (1987) The conformations of hirudin in solution: a study using nuclear magnetic resonance, distance geometry and restrained molecular dynamics. EMBO J. 6, 529-537. pubmed PDF
96. Clore, G.M., Nilges, M., Brünger, A.T., Karplus, M. & Gronenborn, A.M. (1987) A comparison of the restrained molecular dynamics and distance geometry methods for determining three-dimensional structures of proteins on the basis of interproton distance restraints. FEBS Lett. 213, 269-277. pubmed PDF
97. Gronenborn, A.M., Bovermann, G. & Clore, G.M. (1987) A ¹H-NMR study of the solution conformation of secretin: resonance assignment and secondary structure. FEBS Lett. 215, 88-94. pubmed PDF
98. Clore, G.M., Gronenborn, A.M., Nilges, M., Sukumaran, D.K. & Zarbock, J. (1987) The polypeptide fold of the globular domain of histone H5 in solution: a study using nuclear magnetic resonance, distance geometry and restrained molecular dynamics. EMBO J. 6, 1833-1842. pubmed PDF
99. Nilges, M., Clore, G.M., Gronenborn, A.M., Brunger, A.T., Karplus, M. & Nilsson, L. (1987) Refinement of the solution structure of the DNA hexamer 5'd(GCATGC)2: combined use of nuclear magnetic resonance and restrained molecular dynamics. Biochemistry 26, 3718-3733. pubmed PDF
100. Nilges, M., Clore, G.M., Gronenborn, A.M., Piel, N. & McLaughlin, L.W. (1987) Refinement of the solution structure of the DNA decamer 5'd(CTGGATCCAG)₂: combined use of nuclear magnetic resonance and restrained molecular dynamics. Biochemistry 26, 3734-3744. pubmed PDF
101. Gent, M.E., Gartner, S., Gronenborn, A.M., Sandulache, R. & Clore, G.M. (1987) Site-directed mutants of the cAMP receptor protein - DNA binding of five mutant proteins. Protein Engineering 3, 201-203. pubmed
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102. Shih, D.T., Perutz, F., Gronenborn, A.M. & Clore, G.M. (1987) Histidine proton resonances of carbonmonoxyhaemoglobins A and Cowtown in Chloride-free buffer. J. Mol. Biol. 195, 453-455. pubmed PDF
103. Clore, G.M., Gronenborn, A.M., Nilges, M. & Ryan, C.A. (1987) The three-dimensional structure of potato carboxypeptidase inhibitor in solution: a study using nuclear magnetic resonance, distance geometry and restrained molecular dynamics. Biochemistry 26, 8012-8023. pubmed PDF
104. Jansen, C., Gronenborn, A.M. & Clore, G.M. (1987) The binding of the cAMP receptor protein to synthetic DNA sites containing permutations in the concensus sequence TGTGA. Biochem. J. 246, 227-232. pubmed PDF
105. Nilges, M., Clore, G.M. & Gronenborn, A.M. (1987) A simple method for delineating well-defined and variable regions in protein structures determined from interproton distance data. FEBS Lett. 219, 11-16. PDF FEBS Lett.
106. Clore, G.M., Gronenborn, A.M., Kjær, M. & Poulsen, F.M. (1987) The determination of the three-dimensional structure of barley serine proteinase inhibitor 2 by nuclear magnetic resonance, distance geometry and restrained molecular dynamics. Protein Engineering 1, 305-311. pubmed PDF
107. Clore, G.M., Gronenborn, A.M., James, M.N.G., Kjær, M., McPhalen, C.A. & Poulsen, F.M. (1987) Comparison of the solution and X-ray structures of barley serine proteinase inhibitor 2. Protein Engineering 1, 313-318. pubmed PDF
108. Clore, G.M. & Gronenborn, A.M. (1987) Determination of three-dimensional structures of proteins in solution by nuclear magnetic resonance spectroscopy. Protein Engineering 1, 275-288. pubmed PDF
109. Wingfield, P., Mattaliano, R., MacDonald, H.R., Craig, S., Clore, G.M., Gronenborn, A.M. & Schmeissner, U. (1987) Recombinant derived interleukin-1a stabilized against specific deamidation. Protein Engineering 5, 413-417. pubmed PDF
110. Bax, A., Sklenar, V., Clore, G.M. & Gronenborn, A.M. (1987) Water suppression in two-dimensional spin-locked NMR experiments using a novel phase cycling procedure. J. Am. Chem. Soc. 109, 6511-6513. PDF ACS
111. Brünger, A.T., Clore, G.M., Gronenborn, A.M. & Karplus, M. (1987) Solution conformations of human growth hormone releasing factor: comparison of the restrained molecular dynamics and distance geometry methods for a system without long range distance data. Protein Engineering 1, 399-406. pubmed PDF
112. Oschkinat, H., Clore, G.M., Nilges, M. & Gronenborn, A.M. (1987) Application of the z-COSY technique to macromolecules: measuring coupling constants with a modified pulse sequence. J. Magn. Reson. 75, 534-539. PDF J. Magn. Reson.

1988
113. Meyer, E.F., Clore, G.M., Gronenborn, A.M. & Hansen, H.A.S. (1988) Analysis of an enzyme-substrate complex by X-ray crystallography and transferred nuclear Overhauser enhancement measurements: porcine pancreatic elastase and a hexapeptide. Biochemistry 27, 725-730. pubmed PDF
114. Clore, G.M., Nilges, M., Brünger, A.T. & Gronenborn, A.M. (1988) Determination of the backbone conformation of secretin by restrained molecular dynamics on the basis of interproton distance data. Eur. J. Biochem. 171, 479-484. pubmed PDF
115. Scalfi Happ, C., Happ, E., Nilges, M., Gronenborn, A.M. & Clore, G.M. (1988) Refinement of the solution structure of the ribonucleotide 5'r(GCAUGC)₂: combined use of nuclear magnetic resonance and restrained molecular dynamics. Biochemistry 27, 1735-1743. pubmed PDF
116. Clore, G.M., Oschkinat, H., McLaughlin, L.W., Benseler, F., Scalfi Happ, C., Happ, E. & Gronenborn, A.M. (1988) Refinement of the solution structure of the DNA dodecamer 5'd(CGCGPATTCGCG)₂ containing a stable purine-thymine base pair: combined use of nuclear magnetic resonance and restrained molecular dynamics. Biochemistry 27, 4185-4197. pubmed PDF
117. Allet, B., Payton, M., Mattaliano, R.J., Gronenborn, A.M., Clore, G.M. & Wingfield, P.T. (1988) The purification and characterization of the bacteriophage Mu DNA-binding protein ner. Gene 65, 259-268. pubmed PDF
118. Gronenborn, A.M., Sandulache, R., Gärtner, S. & Clore, G.M. (1988) Mutations in the cyclic AMP binding site of the cyclic AMP receptor protein of Escherichia coli. Biochem. J. 253, 801-807. pubmed PDF
119. Cieslar, C., Clore, G.M. & Gronenborn, A.M. (1988) Automatic phasing of pure phase absorption two-dimensional NMR spectra. J. Magn. Reson. 79, 154-157. PDF J. Magn. Reson.

120. Cieslar, C., Clore, G.M. & Gronenborn, A.M. (1988) Computer aided sequential assignment of protein 1H-NMR spectra. J. Magn. Reson. 80, 119-127. PDF J. Magn. Reson.

121. Nilges, M., Clore, G.M. and Gronenborn, A.M. (1988) Determination of three-dimensional structures of proteins from interproton distance data by hybrid distance geometry-dynamical simulated annealing calculations. FEBS Lett 229, 317-324. pubmed PDF
122. Oschkinat, H., Griesinger, C., Kraulis, P.J., Sørensen, O.W., Ernst, R.R., Gronenborn, A.M. & Clore, G.M. (1988) Three-dimensional NMR spectroscopy of a protein in solution. Nature 332, 374-376. pubmed PDF
123. Nilges, M., Gronenborn, A.M., Brünger, A.T. & Clore, G.M. (1988) Determination of three-dimensional structures of proteins by simulated annealing with interproton distance restraints: application to crambin, potato carboxypeptidase inhibitor and barley serine proteinase inhibitor 2. Protein Engineering 2, 27-38. pubmed PDF
124. Oschkinat, H., Clore, G.M. & Gronenborn, A.M. (1988) A two-dimensional nuclear Overhauser enhancement experiment using semiselective soft pulses and its applications to proteins. J. Magn. Reson. 78, 371-375. PDF J. Magn. Reson.
125. Holak, T.A., Engström, Å, Kraulis, P.J., Lindeberg, G., Bennich, H., Jones, T.A., Gronenborn, A.M. & Clore, G.M. (1988) The solution conformation of the antibacterial peptide cecropin A: a nuclear magnetic resonance and dynamical simulated annealing study. Biochemistry 27, 7620-7629. pubmed PDF
126. Holak, T.A., Nilges, M., Prestegard, H., Gronenborn, A.M. & Clore, G.M. (1988) Three-dimensional structure of acyl carrier protein in solution determined by nuclear magnetic resonance and the combined use of dynamical simulated annealing and distance geometry. Eur. J. Biochem. 175, 9-15. pubmed PDF
127. Gronenborn, A.M., Wingfield, P.T., McDonald, H.R., Schmeissner, U. & Clore, G.M. (1988) Site directed mutants of human interleukin-1a: a ¹H-NMR and receptor binding study. FEBS Lett. 231, 135-138. pubmed PDF
128. Scalfi Happ, C., Happ, E., Clore, G.M. & Gronenborn, A.M. (1988) Refinement of the solution structure of the RNA-DNA hybrid 5'[r(GCA)d(TGC)]₂: combined use of nuclear magnetic resonance and restrained molecular dynamics. FEBS Lett. 236, 62-70. pubmed PDF
129. Clore, G.M., Bax, A., Wingfield, P.T. & Gronenborn, A.M. (1988) Long range 15N-1H correlation as an aid to sequential proton resonance assignment of proteins: application to the DNA binding protein ner from phage Mu. FEBS Letters 238, 17-21. pubmed PDF
130. Zarbock, J., Gennaro, R., Romeo, D., Clore, G.M. & Gronenborn, A.M. (1988) A proton nuclear magnetic resonance study of the conformation of bovine anaphylatoxin C5a in solution. FEBS Letters 238, 289-294. pubmed PDF
131. Nilges, M., Clore, G.M. & Gronenborn, A.M. (1988) Determination of three-dimensional structures of proteins from interproton distance data by dynamical simulated annealing from a random array of atoms. FEBS Letters 239, 129-136. pubmed PDF
132. Garin, J., Vignais, P.V., Gronenborn, A.M., Clore, G.M., Gao, Z. & Baeuerlein, E. (1988) ¹H-NMR studies on nucleotide binding to the catalytic sites of bovine mitochondrial F1-ATPase. FEBS Letters 242, 178-182. pubmed PDF

1989
133. Driscoll, P.C., Clore, G.M., Beress, L. & Gronenborn, A.M. (1989) A proton nuclear magnetic resonance study of the anti-hypertensive and anti-viral protein BDS-I from the sea anemone Anemonia sulcata: sequential and stereospecific assignment and secondary structure. Biochemistry 28, 2178-2187. pubmed PDF
134. Driscoll, P.C., Gronenborn, A.M., Beress, L. & Clore, G.M. (1989) Determination of the three-dimensional structure of the anti-hypertensive and anti-viral protein BDS-I from the sea anemone Anemonia sulcata: a study using nuclear magnetic resonance and hybrid distance geometry-dynamical simulated annealing. Biochemistry 28, 2188-2198. pubmed PDF
135. Oschkinat, H., Cieslar, C., Gronenborn, A.M. & Clore, G.M. (1989) Three-dimensional homonuclear Hartmann Hahn-Nuclear Overhauser enhancement spectroscopy in H₂O and its application to proteins. J. Magn. Reson. 81, 212-216. PDF J. Magn. Reson.
136. Folkers, P.J.M., Clore, G.M., Driscoll, P.C., Dodt, J., Köhler, S. & Gronenborn, A.M. (1989) The solution structure of recombinant hirudin and the Lys-47ÆGlu mutant: a nuclear magnetic resonance and hybrid distance geometry-dynamical simulated annealing study. Biochemistry 28, 2601-2617. pubmed PDF
137. Gronenborn, A.M., Bax, A., Wingfield, P.T. & Clore, G.M. (1989) A powerful method of sequential proton resonance assignment in proteins using relayed ¹⁵N-¹H multiple quantum coherence spectroscopy. FEBS Letters 243, 93-98. pubmed PDF
138. Driscoll, P.C., Gronenborn, A.M. & Clore, G.M. (1989) The influence of stereospecific assignments on the determination of three-dimensional structures of proteins by nuclear magnetic resonance spectroscopy: application to the sea anemone protein BDS-I. FEBS Lett. 243, 223-233. pubmed PDF
139. Clore, G.M. & Gronenborn, A.M. (1989) Determination of three-dimensional structures of proteins and nucleic acids in solution by nuclear magnetic resonance spectroscopy. CRC Critical Reviews in Biochemistry and Molecular Biology 24, 479-564. pubmed PDF
140. Clore, G.M., Nilges, M. & Gronenborn, A.M. (1989) Determination of three-dimensional structures of proteins in solution by dynamical simulated annealing with interproton distances derived from nuclear magnetic resonance spectroscopy. In Computer-Aided Molecular Design (Richards, W.G., ed.), pp. 203-219, IBC Technical Services, London.
141. Wingfield, P.T., Graber, P., Shaw, A.R., Gronenborn, A.M., Clore, G.M. & McDonald, H.R. (1989) Preparation, characterization and biochemical application of mutant interleukin-1b's with surface accessible cysteine residues. Eur. J. Biochem. 179, 565-571. pubmed PDF
142. Oschkinat, H., Cieslar, C., Holak, T.A., Clore, G.M. & Gronenborn, A.M. (1989) Practical and theoretical aspects of three-dimensional homonuclear Hartmann Hahn-nuclear Overhauser enhancement spectroscopy of proteins. J. Magn. Reson. 83, 450-472. PDF J. Magn. Reson.
143. Gronenborn, A. M., Wingfield, P. T. & Clore, G. M. (1989) Determination of the secondary structure of the DNA binding protein Ner from phage Mu using ¹H homonuclear and ¹⁵N-¹H heteronuclear NMR spectroscopy. Biochemistry 28, 5081-5089. pubmed PDF
144. Gronenborn, A.M. & Clore, G.M. (1989) Analysis of the relative contributions of the nuclear Overhauser interproton distance restraints and the empirical energy function in the calculation of oligonucleotide structures using restrained molecular dynamics. Biochemistry 28, 5978-5984. pubmed PDF
145. Forman-Kay, J.D., Clore, G.M., Driscoll, P.C., Wingfield, P.T., Richards, F.M. & Gronenborn, A.M. (1989) A proton nuclear magnetic resonance assignment and secondary structure determination of recombinant human thioredoxin. Biochemistry 28, 7088-7097. pubmed PDF
146. Kraulis, P.J., Clore, G.M., Nilges, M., Jones, T.A., Pettersson, G., Knowles, J. & Gronenborn, A.M. (1989) Determination of the three-dimensional solution structure of the C-terminal domain of cellobiohydrolase I from Trichoderma reesei: a study using nuclear magnetic resonance and hybrid distance geometry-dynamical simulated annealing. Biochemistry 28, 7241-7257. pubmed PDF
147. Clore, G.M. & Gronenborn, A.M. (1989) How accurately can interproton distances in macromolecules really be determined by full relaxation matrix analysis of nuclear Overhauser enhancement data? J. Magn. Reson. 84, 398-409. PDF J. Magn. Reson.
148. Marion, D., Driscoll, P.C., Kay, L.E., Wingfield, P.T., Bax, A., Gronenborn, A.M. & Clore, G.M. (1989) Overcoming the overlap problem in the assignment of ¹H-NMR spectra of larger proteins using three-dimensional heteronuclear ¹H-¹⁵N Hartmann-Hahn and nuclear Overhauser - multiple quantum coherence spectroscopy: application to interleukin-1b. Biochemistry 28, 6150-6156. pubmed PDF
149. Clore, G.M., Appella, E., Yamada, M., Matsushima, K. & Gronenborn, A.M. (1989) Determination of the secondary structure of interleukin-8 by nuclear magnetic resonance spectroscopy. J. Biol. Chem. 264, 18907-18911. pubmed PDF

1990
150. Gronenborn, A.M., Nilges, M., Peanasky, R.J. & Clore, G.M. (1990) Sequential resonance assignment and secondary structure determination of the Ascaris trypsin inhibitor, a member of a novel class of proteinases inhibitors. Biochemistry 29, 183-189. pubmed PDF
151. Nilges, M., Clore, G.M. & Gronenborn, A.M. (1990) ¹H-NMR stereospecific assignments by conformational database searches. Biopolymers 29, 813-822. pubmed PDF
152. Clore, G.M. & Gronenborn, A.M. (1990) Extending the limits of protein structure determination by NMR. In Theoretical Biochemistry and Molecular Biophysics: a Comprehensive Survey, (Beveridge, D.L. and Lavery, L., eds.), vol. 2, pp. 1-16, Adenine Press, New York,
153. Forman-Kay, J.D., Gronenborn, A.M., Kay, L.E., Wingfield, P.T. & Clore, G.M. (1990) Studies on the solution conformation of human thioredoxin using heteronuclear ¹⁵N-¹H nuclear magnetic resonance spectroscopy. Biochemistry 29, 1566-1572. pubmed PDF
154. Gronenborn, A.M. & Clore, G.M. (1990) Protein structure determination in solution by two-dimensional and three-dimensional nuclear magnetic resonance spectroscopy. Analytical Chemistry 62, 2-15. pubmed PDF
155. Driscoll, P.C., Clore, G.M., Marion, D., Wingfield, P.T. & Gronenborn, A.M. (1990) Complete resonance assignment for the polypeptide backbone of interleukin-1b using three-dimensional heteronuclear NMR spectroscopy. Biochemistry 29, 3542-3556. pubmed PDF
156. Driscoll, P.C., Gronenborn, A.M., Wingfield, P.T. & Clore, G.M. (1990) Determination of the secondary structure and molecular topology of interleukin-1b using two- and three-dimensional heteronuclear ¹⁵N-¹H NMR spectroscopy. Biochemistry 29, 4468-4682. pubmed PDF
157. Clore, G.M., Appella, E., Yamada, M., Matsushima, K. & Gronenborn, A.M. (1990) The three-dimensional structure of interleukin-8 in solution. Biochemistry 29, 1689-1696. pubmed PDF
158. Bax, A., Clore, G.M., Driscoll, P.C., Gronenborn, A.M., Ikura, M. & Kay, L.E. (1990) Practical aspects of proton-carbon-carbon-proton three-dimensional correlation spectroscopy of ¹³C-labeled proteins. J. Magn. Reson. 87, 620-628. PDF J. Magn. Reson.
159. Bax, A., Clore, G.M. & Gronenborn, A.M. (1990) ¹H-¹H correlation via isotropic mixing of ¹³C magnetization: a new three-dimensional approach for assigning ¹H and ¹³C spectra of ¹³C-enriched proteins. J. Magn. Reson. 88, 425-431. PDF J. Magn. Reson.
160. Clore, G.M., Szabo, A., Bax, A., Kay, L.E., Driscoll, P.C. & Gronenborn, A.M. (1990) Deviations from the simple two parameter model free approach to the interpretation of ¹⁵N nuclear magnetic relaxation of proteins. J. Am. Chem. Soc. 112, 4989-4991. PDF ACS
161. Clore, G.M., Driscoll, P.C., Wingfield, P.T. & Gronenborn, A.M. (1990) Low resolution structure of interleukin-1b in solution derived from ¹H-¹⁵N heteronuclear three-dimensional NMR spectroscopy. J. Mol. Biol. 214, 811-817. pubmed PDF
162. Clore, G.M., Driscoll, P.C., Wingfield, P.T. & Gronenborn, A.M. (1990) Analysis of backbone dynamics of interleukin-1b using two-dimensional inverse detected heteronuclear ¹⁵N-¹H NMR spectroscopy. Biochemistry 29, 7387-7401. pubmed PDF
163. Clore, G.M., Bax, A., Wingfield, P.T. & Gronenborn, A.M. (1990) Identification and localization of bound internal water in the solution structure of interleukin-1b by heteronuclear three-dimensional ¹H rotating frame Overhauser ¹⁵N-¹H multiple quantum coherence NMR spectroscopy. Biochemistry 29, 5671-5676. pubmed PDF
164. Clore, G.M., Bax, A., Driscoll, P.C., Wingfield, P.T. & Gronenborn, A.M. (1990) Assignment of the side chain ¹H and ¹³C resonance of interleukin-1b using double and triple resonance heteronuclear three-dimensional NMR spectroscopy. Biochemistry 29, 8172-8184. pubmed PDF
165. Kay, L.E., Clore, G.M., Bax, A. & Gronenborn, A.M. (1990) Four-dimensional heteronuclear triple resonance NMR spectroscopy of interleukin-1b in solution. Science 249, 411-414. pubmed PDF
166. Omichinski, J., Clore, G.M., Appella, E., Sakaguchi, K. & Gronenborn, A.M. (1990) High resolution three-dimensional solution structure of a single zinc finger from a human enhancer binding protein in solution. Biochemistry 29, 9324-9334. pubmed PDF
167. Becerra, S.P., Clore, G.M., Gronenborn, A.M., Karlström, A., Stahl, S.J., Wilson, S.H. & Wingfield, P.T. (1990) Purification and characterization of the RNase H domain of HIV-1 reverse transcriptase expressed in recombinant Escherichia coli. FEBS Lett. 270, 76-80. pubmed PDF
168. Ikura, M., Bax, A., Clore, G.M. & Gronenborn, A.M. (1990) Detection of nuclear Overhauser effects between degenerate amide proton resonances by heteronuclear three-dimensional NMR spectroscopy. J. Am. Chem. Soc.112, 9020-9022. PDF ACS

1991
169. Clore, G.M., Kay, L.E., Bax, A. & Gronenborn, A.M. (1991) Four dimensional ¹³C/¹³C-edited nuclear Overhauser enhancement spectroscopy of a protein in solution: application to interleukin-1b. Biochemistry 30, 12-18. pubmed PDF
170. Clore, G.M. & Gronenborn, A.M. (1991) Two, three and four dimensional NMR methods for obtaining larger and more precise three-dimensional structures of proteins in solution. Ann. Rev. Biophys. Biophys. Chem. 20, 29-63. pubmed PDF
171. Clore, G.M. & Gronenborn, A.M. (1991) Comparison of NMR and X-ray structures of hirudin. In Computational Aspects of the Study of Biological Macromolecules by Nuclear Magnetic Resonance Spectroscopy, (ed. Hoch, J.C.), pp. 57-66, NATO ASI Series, Plenum Press.
172. Forman-Kay, J.D., Clore, G.M., Wingfield, P.T. & Gronenborn, A.M. (1991) The high resolution three-dimensional structure of reduced recombinant human thioredoxin in solution. Biochemistry 30, 2685-2698. pubmed PDF
173. Baldwin, E.T., Weber, I.T., St. Charles, R., Xuan, J.C., Appella, E., Yamada, M., Matsushima, K., Edwards, B.F.P., Clore, G.M., Gronenborn, A.M. & Wlodawer, A. (1991) Crystal structure of interleukin-8: symbiosis of NMR and crystallography. Proc. Natl. Acad. Sci. U.S.A. 88, 502-506. pubmed PDF
174. Clore, G.M. & Gronenborn, A.M. (1991) Comparison of the solution nuclear magnetic resonance and crystal structures of interleukin-8: possible implications for the mechanism of receptor binding. J. Mol. Biol. 217, 611-620. pubmed PDF
175. Gronenborn, A.M. & Clore, G.M. (1991) Modeling the three-dimensional structure of the monocyte chemoattractant and activating protein MCAF/MCP-1 on the basis of the solution structure of interleukin-8. Protein Engineering 4, 263-269. pubmed PDF
176. Clore, G.M., Bax, A. & Gronenborn, A.M. (1991) Stereospecific assignment of b-methylene protons in larger proteins using three-dimensional ¹⁵N-separated Hartmann-Hahn and ¹³C-separated rotating frame Overhauser spectroscopy. J. Biomol. NMR 1, 13-22. pubmed PDF
177. Clore, G.M., Wingfield, P.T. & Gronenborn, A.M. (1991) High resolution three dimensional structure of interleukin-1b in solution by three and four dimensional nuclear magnetic resonance spectroscopy. Biochemistry 30, 2315-2323. pubmed PDF
178. Clore, G.M. & Gronenborn, A.M. (1991) NMR and X-ray analysis of the three-dimensional structure of interleukin-8. In Neutrophil-Activating Peptides and other Chemotactic Cytokines, (Baggiolini, M. & Sorg, C., eds.) 4, 18-40, S. Karger, Basel
179. Clore, G.M. & Gronenborn, A.M. (1991) Applications of three- and four-dimensional heteronuclear NMR spectroscopy to protein structure determination. Progr. Nucl. Magn. Reson. Spectroscopy 23, 43-92. PDF Progr. NMR Spect.
180. Sakaguchi, K., Appella, E., Omichinski, J.G., Clore, G.M. & Gronenborn, A.M. (1991) Specific DNA binding to an MHC enhancer sequence by a synthetic 57-residue double zinc finger peptide from a human enhancer binding protein. J. Biol. Chem. 266, 7306-7311. pubmed PDF
181. Clore, G.M., Omichinski, J.G. & Gronenborn, A.M. (1991) Slow conformational dynamics at the metal coordination site of a zinc finger. J. Am. Chem. Soc. 113, 4350-4351. PDF ACS
182. Clore, G.M. & Gronenborn, A.M. (1991) Structures of larger proteins in solution: three- and four-dimensional heteronuclear NMR spectroscopy. Science 252, 1390-1399. pubmed PDF
183. Forman-Kay, J.D., Gronenborn, A.M., Wingfield, P.T. & Clore, G.M. (1991) Determination of the positions of bound water in the solution structure of reduced human thioredoxin by heteronuclear three-dimensional nuclear magnetic resonance spectroscopy. J. Mol. Biol. 220, 209-216. pubmed PDF
184. Clore, G.M. & Gronenborn, A.M. (1991) Comparison of the solution nuclear magnetic resonance and X-ray crystal structures of human recombinant interleukin-1b. J. Mol. Biol. 221, 47-53. pubmed PDF
185. Powers, R., Gronenborn, A.M., Clore, G.M. & Bax, A. (1991) Three-dimensional triple resonance NMR of 13C/15N enriched proteins using constant-time evolution. J. Magn. Reson. 94, 209-213. PDF J. Magn. Reson.
186. Gronenborn, A.M., Filpula, D.R., Essig, N.Z., Achari, A., Whitlow, M., Wingfield, P.T. & Clore, G.M. (1991) A novel highly stable fold of the immunoglobulin binding domain of Streptococcal protein G. Science 253, 657-661. pubmed PDF
187. Powers, R., Clore, G.M., Bax, A., Garrett, D.S., Stahl, S.J., Wingfield, P.T. & Gronenborn, A.M. (1991) Secondary structure of the ribonuclease H domain of the human immunodificiency virus reverse transcriptase in solution using three-dimensional double and triple resonance heteronuclear magnetic resonance spectroscopy. J. Mol. Biol. 221, 1081-1090. pubmed PDF
188. Garrett, D.S., Powers, R., Gronenborn, A.M. & Clore, G.M. (1991) A common sense approach to peak picking two-, three- and four-dimensional spectra using automatic computer analysis of contour diagrams. J. Magn. Reson. 95, 214-220. PDF JMR YouTube
189. Omichinski, J.G., Clore, G.M., Sakaguchi, K., Appella, E. & Gronenborn, A.M. (1991) Structural characterization of a 39-residue synthetic peptide containing the two zinc binding domains from the HIV-1 p7 nucleocapsid protein by CD and NMR spectroscopy. FEBS Lett. 292, 25-30. pubmed PDF
190. Gronenborn, A.M. & Clore, G.M. (1991) Similarity of Protein G and Ubiquitin. Science 254, 581-582. PDF Science

1992
191. Clore, G.M. & Gronenborn, A.M. (1992) Localization of bound water in the solution structure of the immunoglobulin binding domain of Streptococcal protein G: evidence for solvent induced helical distortions in solution. J. Mol. Biol. 223, 853-856. pubmed PDF
192. Grzesiek, S., Ikura, M., Clore, G.M., Gronenborn, A.M. & Bax, A. (1992) A 3D triple resonance NMR technique for qualitative measurement of carbonyl-Hb J couplings in isotopically enriched proteins. J. Magn. Reson. 96, 215-221. PDF J. Magn. Reson.
193. Clore, G.M. & Gronenborn, A.M. (1992) Practical aspects of two, three and four-dimensional nuclear magnetic resonance spectroscopy applied to the study of protein structure. In Protein Engineering - a Practical Approach, (eds. Rees, A.R., Wetzel, R. & Sternberg, M.J.E.), pp. 33-56, Oxford University Press.
194. Lozier, R.H., Xie, A., Hofrichter, J. & Clore, G.M. (1992) Reversible steps in the bacteriorhodopsin photocycle. Proc. Natl. Acad. Sci. 89, 3610-3614. pubmed PDF
195. Omichinski, J.G., Clore, G.M., Robien, M., Sakaguchi, K., Appella, E. & Gronenborn, A.M. (1992) High resolution solution structure of the double Cys2His2 zinc finger from the human enhancer binding protein MBP-1. Biochemistry 31, 3907-3917. pubmed PDF
196. Forman-Kay, J.D., Clore, G.M. & Gronenborn, A.M. (1992) The relationship between electrostatics and redox function in human thioredoxin: charaterization of pH titration shifts using two-dimensional homo- and heteronuclear NMR. Biochemistry 31, 3442-3452. pubmed PDF
197. Robien, M.A., Clore, G.M., Omichinski, J.G., Perham, R.N., Appella, E., Sakaguchi, K. & Gronenborn, A.M. (1992) Three-dimensional solution structure of the E3-binding domain of the dihydrolipoamide succinyltransferase core from the 2-oxoglutarate dehydrogenase multienzyme complex of Escherichia coli. Biochemistry 31, 3463-3471. pubmed PDF
198. Powers, R., Garrett, D.S., March, C.J., Frieden, E.A., Gronenborn, A.M. & Clore, G.M. (1992) ¹H, ¹⁵N, ¹³C and ¹³CO assignments of human interleukin-4 using three-dimensional double and triple resonance heteronuclear magnetic resonance spectroscopy. Biochemistry 31, 4334-4347. pubmed PDF
199. Garrett, D.S., Powers, R., March, C.J., Frieden, E.A., Clore, G.M. & Gronenborn, A.M. (1992) Determination of the secondary structure and folding topology of human interleukin-4 using three-dimensional heteronuclear magnetic resonance spectroscopy. Biochemistry 31, 4347-4353. pubmed PDF
200. Chandrasasekhar, I., Clore, G.M., Szabo, A., Gronenborn, A.M. & Brooks, B.R. (1992) A 500 ps molecular dynamics simulation study of interleukin-1b in water: correlation with nuclear magnetic resonance spectroscopy and crystallography. J. Mol. Biol. 226, 239-250. pubmed PDF
201. Ikura, M., Clore, G.M., Gronenborn, A.M., Zhu, G., Klee, C.B. & Bax, A. (1992) Solution structure of a calmodulin-target peptide complex by multi-dimensional NMR. Science 256, 632-638. pubmed PDF
202. Powers, R., Garrett, D.S., March, C.J., Frieden. E.A., Gronenborn, A.M. & Clore, G.M. (1992) Three-dimensional solution structure of human interleukin-4 by multi-dimensional heteronuclear magnetic resonance spectroscopy. Science 256, 1673-1677. pubmed PDF
203. Forman-Kay, J.D., Clore, G.M., Stahl, S.J. & Gronenborn, A.M. (1992) 1H and 15N resonance assignments and secondary structure of the human thioredoxin C62A, C69A, C73A mutant. J. Biomolec. NMR 2, 431-445. pubmed PDF
204. Achari, A., Hale, S.P, Howard, A.J., Clore, G.M., Gronenborn, A.M., Hardman, K.D. & Whitlow, M. (1992) The 1.67 Å X-ray structure of the B2 immunoglobulin domain of streptococcal protein G and comparison to the NMR structure of the B1 domain. Biochemistry 31, 10449-10457. pubmed PDF
205. Shaanan, B., Gronenborn, A.M., Cohen, G.H., Gilliland, G.L., Veerapandian, B., Davies, D.R. & Clore, G.M. (1992) Combining experimental information from crystal and solution studies: joint X-ray and NMR refinement. Science 257, 961-964. pubmed PDF
206. Rose, K., Simona, M.G., Savoy, L.A., Regamey, P.O., Green, B.N., Clore, G.M., Gronenborn, A.M. & Wingfield, P.T. (1992) Pyruvic acid is attached through its central carbon atom to the amino terminus of the recombinant-DNA derived DNA-binding protein Ner of bacteriophage Mu. J. Biol. Chem. 267, 19101-19106. pubmed PDF
207. Powers, R., Clore, G.M., Stahl, S.J., Wingfield, P.T. & Gronenborn, A.M. (1992) Analysis of the backbone dynamics of the ribonuclease H domain of the human immunodeficiency virus reverse transcriptase using ¹⁵N relaxation measurements. Biochemistry 31, 9150-9157. pubmed PDF

1993
208. Omichinski, J.G., Trainor, C., Evans, T., Gronenborn, A.M., Clore, G.M. & Felsenfeld, G. (1993) A small single-'finger' peptide from the erythroid factor GATA-1 binds specifically to DNA as a zinc or iron complex. Proc. Natl. Acad. Sci. U.S.A. 90, 1676-1680. pubmed PDF
209. Grasberger, B.L., Gronenborn, A.M. & Clore, G.M. (1993) Analysis of the backbone dynamics of interleukin-8 by ¹⁵N relaxation measurements. J. Mol. Biol. 230, 364-372. pubmed PDF
210. Clore, G.M., Robien, M.A. & Gronenborn, A.M. (1993) Exploring the limits of precision and accuracy of protein structures determined by nuclear magnetic resonance spectroscopy. J. Mol. Biol. 231, 82-102. pubmed PDF
211. Vuister, G.W., Clore, G.M., Gronenborn, A.M., Powers, R., Garrett, D.S., Tschudin, R. & Bax, A. (1993) Increased resolution and improved spectral quality in four-dimensional ¹³C/¹³C-separated HMQC-NOE-HMQC spectra using pulsed field gradients. J. Magn. Reson. Series B 101, 210-213. PDF J. Magn. Reson.
212. Sakaguchi, K., Zambrano, N., Baldwin, E.T., Shapiro, B.A., Erickson, J.W., J.G. Omichinski, G.M. Clore, A.M. Gronenborn & E. Appella (1993) Identification of a binding site for the human immunodeficiency virus type I nucleocapsid protein. Proc. Natl. Acad. Sci. U.S.A. 90, 5219-5223. pubmed PDF
213. Varley, P., Gronenborn, A.M., Christensen, H., Wingfield, P.T., Pain, R.H. & Clore, G.M. (1993) Kinetics of folding of the all b-sheet protein interleukin-1b studied by nuclear magnetic resonance, circular dichroism and fluorescence. Science 240, 1110-1113. pubmed PDF
214. Powers, R., Clore, G.M., Garrett, D.S. & Gronenborn, A.M. (1993) Relationships between the precision of high resolution protein NMR structures, solution order parameters and crystallographic B factors. J. Magn. Reson. Series B 101, 325-327. PDF J. Magn. Reson.
215. Gronenborn, A.M. & Clore, G.M. (1993) Structural studies of immunoglobulin binding domains of Streptococcal Protein G. ImmunoMethods 2, 3-8. PDF Immunomethods
216. Powers, R., Garrett, D.S., March, C.J., Frieden, E.A., Gronenborn, A.M. & Clore, G.M. (1993) The high resolution three-dimensional solution structure of human interleukin-4 determined by multi-dimensional heteronuclear magnetic resonance spectroscopy. Biochemistry 32, 6744-6762. pubmed PDF
217. Gronenborn, A.M. & Clore, G.M. (1993) Identification of the contact surface of a Streptococcal protein G domain complexed with a human Fc fragment. J. Mol. Biol.233, 331-335. pubmed PDF
218. Clore, G.M. & Gronenborn, A.M. (1993) Structural studies of interleukin-1b, interleukin-4 and interleukin-8, ImmunoMethods 3, 56-81. PDF Immunomethods
219. Brünger, A.T., Clore, G.M., Gronenborn, A.M., Saffrich, R. & Nilges, M. (1993) Assessing the quality of solution nuclear magnetic resonance structures by complete cross-validation. Science 261, 328-331. pubmed PDF
220. Omichinski, J.G., Clore, G.M., Schaad, O., Felsenfeld, G., Trainor, C., Appella, E., Stahl, S.J. & Gronenborn, A.M. (1993) NMR structure of a specific DNA complex of Zn-containing DNA binding domain of GATA-1. Science 261, 438-446. pubmed PDF
221. Clore, G.M., Bax, A., Ikura, M. & Gronenborn, A.M. (1993) Structure of calmodulin-target peptide complexes. Curr. Op. Structl. Biol. 3, 838-845. PDF Curr. Op. Struct. Biol.

1994
222. Bax, A., Grzesiek, S., Gronenborn, A.M. & Clore, G.M. (1994) Isotope-filtered 2D HOHAHA spectroscopy of a peptide-protein complex using heteronuclear Hartmann-Hahn dephasing. J. Magn. Reson. 106 Series A, 269-273. PDF J. Magn. Reson.
223. Gronenborn, A.M. & Clore, G.M. (1994) Experimental support for the "hydrophobic zipper" hypothesis of protein folding. Science 263, 536. pubmed PDF
224. Barchi, J.J., Grasberger, B., Gronenborn, A.M. & Clore, G.M. (1994) Investigation of the backbone dynamics of the IgG-binding domain of Streptococcal Protein G by heteronuclear two-dimensional 1H-15N nuclear magnetic resonance spectroscopy. Protein Science 3, 15-21. pubmed PDF
225. Clore, G.M., Bax, A., Omichinski, J.G. & Gronenborn, A.M. (1994) Localization of bound water in the solution structure of the specific complex of the erythroid transcription factor GATA-1 with DNA by water selective two-dimensional heteronuclear magnetic resonance spectroscopy. Structure 2, 89-94. pubmed PDF
226. Clubb, R.T., Omichinski, J.G., Clore, G.M. & Gronenborn, A.M. (1994) Mapping the binding surface of interleukin-8 complexed with an N-terminal fragment of the type I human interleukin-8 receptor. FEBS Lett. 338, 93-97. pubmed PDF
227. Garrett, D.S., Lodi, P.J., Shamoo, Y., Williams, K.R., Clore, G.M. & Gronenborn, A.M. (1994) Determination of the secondary structure and folding topology of a RNA binding domain of the mammalian hnRNP A1 protein using three-dimensional heteronuclear magnetic resonance spectroscopy. Biochemistry 33, 2852-2858. pubmed PDF
228. Clore, G.M. & Gronenborn, A.M. (1994) Structures of larger proteins, protein-ligand and protein-DNA complexes by multi-dimensional heteronuclear NMR. Protein Science 3, 372-390 pubmed PDF; Progr. Biophys. Mol. Biol. 62, 153-184 pubmed PDF; In Encyclopedia of Nuclear Magnetic Resonance, vol. 7, pp. 4602-4622, (eds. Grant, D.M. & Harris, R.K.), John Wiley & Sons, New York (1996). Encyclopedia Magn. Reson.
229. Rozwarski, D.A., Gronenborn, A.M., Clore, G.M., Bazan, J.F., Bohm, A., Wlodawer, A., Hatada, M. & Karplus, P.A. (1994) Structural comparison among the short-chain helical cytokines. Structure 2, 159-173. pubmed PDF
230. Lodi, P.J., Garrett, D.S., Kuszewski, J., Tsang, M.L.S., Weatherbee, J.A., Leonard, W.J., Gronenborn, A.M. & Clore, G.M. (1994) High resolution solution structure of the b chemokine hMIP-1b by multi-dimensional NMR. Science 263, 1762-1767. pubmed PDF
231. Garrett, D.S., Kuszewski, J., Hancock, T.J., Lodi, P.J., Vuister, G.W., Gronenborn, A.M. & Clore, G.M. (1994) The impact of direct refinement against three-bond HN-CaH coupling constants on protein structure determination by NMR. J. Magn. Reson. Series B 104, 99-103. pubmed PDF
232. Gronenborn, A.M. & Clore, G.M. (1994) Identification of N-terminal helix capping boxes by means of 13C chemical shifts. J. Biomol. NMR 4, 455-458. pubmed PDF
233. Smith, L.J., Redfield, C., Smith, R.A.G., Dobson, C.M., Clore, G.M., Gronenborn, A.M., Walter, M.R., Naganbushan, T.L. & Wlodawer, A. (1994) Comparison of four independently determined structures of human recombinant interleukin-4. Nature Struct. Biol. 1, 301-310. pubmed PDF
234. Werner, M.H., Clore, G.M., Gronenborn, A.M., Kondoh, A. & Fisher, R.J. (1994) Refolding proteins by gel filtration chromatography. FEBS Lett. 345, 125-130. pubmed PDF
235. Qin, J., Clore, G.M. & Gronenborn, A.M. (1994) The high resolution three-dimensional solution structure of the oxidized and reduced states of human thioredoxin: delineation of conformational differences between the two redox states. Structure 2, 503-522. pubmed PDF
236. Werner, M.W., Clore, G.M., Gronenborn, A.M. & Nash, H.A. (1994) Symmetry and asymmetry in the function of Escherichia coli integration host factor. Current Biology 4, 477-487. pubmed PDF
237. Grasberger, B.L., Clore, G.M. & Gronenborn, A.M. (1994) High-resolution structure of Ascaris trypsin inhibitor in solution: direct evidence for a pH induced conformational transition in the reactive site. Structure 2, 669-678. pubmed PDF
238. Makhatadze, G.I., Clore, G.M., Gronenborn, A.M. & Privalov, P.L. (1994) Thermodynamics of unfolding of the all b-sheet protein interleukin-1b. Biochemistry 33, 9327-9332. pubmed PDF
239. Clore, G.M. & Gronenborn, A.M. (1994) Multidimensional heteronuclear nuclear magnetic resonance of proteins.Meth. Enzymol. 239, 349-363. pubmed PDF; Spectroscopy 10, 32-38 (1995); In Encyclopedia of Nuclear Magnetic Resonance, vol. 7, pp. 4744-4752, (eds. Grant, D.M. & Harris, R.K.), John Wiley & Sons, New York (1996). pubmed Encyclopedia Magn. Reson.
240. Gronenborn, A.M. & Clore, G.M. (1994) Where is NMR taking us. Proteins: Struct. Funct. Genet. 19, 273-276. pubmed PDF
241. Clore, G.M., Omichinski, J.G., Sakaguchi, K., Zambrano, N., Sakamoto, H., Appella, E. & Gronenborn, A.M. (1994) High-resolution solution structure of the oligomerization domain of p53 by multi-dimensional NMR. Science 265, 386-391. pubmed PDF
242. Wang, A.C., Lodi, P.J., Qin, J., Vuister, G.W., Gronenborn, A.M. & Clore, G.M. (1994) An efficient triple-resonance experiment for proton-directed sequential backbone assignment of medium-sized proteins. J. Magn. Reson. Series B 105, 196-198. pubmed PDF
243. Gronenborn, A.M. & Clore, G.M. (1994) Structural studies of interleukin-8 and interleukin-4. In Structural Biology: The State of the Art, (Sarma, R.H. & Sarma, M.H., eds.) pp. 19-42, Adenine Press, New York.
244. Covell, D.G., Smythers, G.W., Gronenborn, A.M. & Clore, G.M. (1994) Analysis of hydrophobicity in the a and b chemokine families and its relevance to dimerization. Protein Science 3, 2064-2072. pubmed PDF
245. Kuszewski, J., Clore, G.M. & Gronenborn, A.M. (1994) Fast folding of a prototypic polypeptide: the immunoglobulin binding domain of Streptococcal Protein G. Protein Science 3, 1945-1952. pubmed PDF
246. Clubb, R.T., Omichinski, J.G., Savilahti, H., Mizuuchi, K., Gronenborn, A.M. & Clore, G.M. (1994) A novel class of winged helix-turn-helix protein - the DNA binding domain of Mu transposase. Structure 2, 1041-1048. pubmed PDF

1995
247. Clore, G.M. & Gronenborn, A.M. (1995) Three-dimensional structures of a and b chemokines. FASEB Journal 9, 57-62. pubmed PDF
248. Kuszewski, J., Qin, J., Gronenborn, A.M. & Clore, G.M. (1995) The impact of direct refinement against ¹³C^a and ¹³C^b chemical shifts on protein structure determination by NMR. J. Magn. Reson Series B 106, 92-96. pubmed PDF
249. Ernst, J.A., Clubb, R.T., Zhou, H.-X., Gronenborn, A.M. & Clore, G.M. (1995) Demonstration of positionally disordered water within a protein hydrophobic cavity by NMR. Science 267, 1813-1817. pubmed PDF
250. Clore, G.M., Omichinski, J.G., Sakaguchi, K., Zambrano, N., Sakamoto, H., Appella, E. & Gronenborn, A.M. (1995) Interhelical angles in the solution structure of the oligomerization domain of the tumour suppressor p53. Science 267, 1515-1516. pubmed PDF
251. Strzelecka, T.E., Hayes, J.J., Clore, G.M. & Gronenborn, A.M. (1995) DNA binding specificity of the Mu Ner protein. Biochemistry 34, 2946-2955. pubmed PDF
252. Qin, J., Clore, G.M. Kennedy, W.M.P., Huth, J.R. & Gronenborn, A.M. (1995) Solution structure of human thioredoxin in a mixed disulfide intermediate complex with its target peptide from the transcription factor NFkB. Structure 3, 289-297. pubmed PDF
253. Clore, G.M., Ernst, J., Clubb, R.T., Omichinski, J.G., Kennedy, W.M.P., Sakaguchi, K., Appella, E. & Gronenborn, A.M. (1995) Refined solution structure of the oligomerization domain of the tumour suppressor p53. Nature Struct. Biol. 2, 321-332. pubmed PDF
254. Clubb, R.T., Omichinski, J.G., Sakaguchi, K., Appella, E., Gronenborn, A.M. & Clore, G.M. (1995) Backbone dynamics of the oligomerization domain of p53 determined from 15N NMR relaxation measurements. Protein Science 4, 855-862. pubmed PDF
255. Kuszewski, J., Gronenborn, A.M. & Clore, G.M. (1995) The impact of direct refinement against proton chemical shifts in protein structure determination by NMR. J. Magn. Reson. Series B 107, 293-297. pubmed PDF
256. Werner, M.H., Huth, J.R., Gronenborn, A.M. & Clore, G.M. (1995) Molecular basis of human 46X,Y sex reversal revealed from the three-dimensional solution structure of the human SRY-DNA complex. Cell 81, 705-714. pubmed PDF
257. Balagurumoorthy, P., Sakamoto, K., Lewis, M.S., Zambrano, N., Clore, G.M., Gronenborn, A.M., Appella, E. & Harrington, R.E. (1995) Four p53 DNA binding domains bind natural p53 response elements and bend the DNA. Proc. Natl. Acad. Sci. U.S.A. 92, 8591-8585. pubmed PDF
258. Lodi, P.J., Ernst, J.A., Kuszewski, J., Hickman, A.B., Engelman, A., Craigie, R., Clore, G.M. & Gronenborn, A.M. (1995) Solution structure of the DNA binding domain of HIV-1 integrase. Biochemistry 34, 9826-9833. pubmed PDF
259. Makhatadze, G.I., Clore, G.M. & Gronenborn, A.M. (1995) Solvent isotope effect and protein stability. Nature Struct. Biol. 2, 852-855. pubmed PDF
260. Werner, M.H., Bianchi, M.E., Gronenborn, A.M. & Clore, G.M. (1995) NMR spectroscopic analysis of the DNA conformation induced by the human testis determining factor SRY. Biochemistry 34, 11998-12004. pubmed PDF
261. Strzelecka, T.E., Clore, G.M. & Gronenborn, A.M. (1995) The solution structure of the Mu Ner protein reveals a helix-turn-helix DNA recognition motif. Structure 3, 1087-1095. pubmed PDF
262. Gronenborn, A.M. & Clore, G.M. (1995) Structures of protein complexes by multidimensional heteronuclear magnetic resonance spectroscopy. CRC Crit. Rev. Biochem. Mol. Biol. 30, 351-385. pubmed PDF
263. Werner, M.H., Clore, G.M., Fisher, C.L., Fisher, R.J., Trinh, L., Shiloach, J. & Gronenborn, A.M. (1995) The solution structure of the human ETS1/DNA complex reveals a novel mode of binding and true sidechain intercalation. Cell 83, 761-771. Erratum: Cell 87, issue No. 2 (1996). PDF Correction of the NMR structure of the ETS1/DNA complex. J. Biomol. NMR 10, 317-328 (1997). pubmed PDF
264. Frank, M.K., Clore, G.M. & Gronenborn, A.M. (1995) Structural and dynamic characterization of the urea denatured state of the immunoglobulin binding domain of Streptococcal protein G. Protein Science 4, 2605-2615. pubmed PDF

1996
265. Clubb, R.T., Mizuuchi, M., Huth, J.R., Omichinski, J.G., Savilahti, H., Mizuuchi, K., Clore, G.M. & Gronenborn, A.M. (1996) The wing of the enhancer binding domain of Mu phase transposase is flexible and essential for efficient transposition. Proc. Natl. Acad. Sci. U.S.A. 93, 1146-1150. pubmed PDF
266. Qin, J., Clore, G.M. & Gronenborn, A.M. (1996) Ionization equilibria for the side chain carboxyl groups in oxidized and reduced human thioredoxin and in the complex with its target peptide from the transcription factor NFkB. Biochemistry 35, 7-13. pubmed PDF
267. Gronenborn, A.M. & Clore, G.M. (1996) Rapid screening for structural integrity of expressed proteins by heteronuclear NMR spectroscopy. Protein Science 5, 174-177. pubmed PDF
268. Pedone, P.V., Ghirlando, R., Clore, G.M., Gronenborn, A.M., Felsenfeld, G. & Omichinski, J.G. (1996) The single Cys2-His2 zinc finger domain of the GAGA protein flanked by basic residues is sufficient for high affinity DNA binding. Proc. Natl. Acad. Sci. U.S.A. 93, 2822-2826. pubmed PDF
269. Werner, M.H., Gronenborn, A.M. & Clore, G.M. (1996) Intercalation, DNA kinking and the control of transcription. Science 271, 778-784. pubmed PDF
270. Grzesiek, S., Bax, A., Clore, G.M., Gronenborn, A.M., Hu, J.-H., Kaufman, J., Palmer, I., Stahl, S.J. & Wingfield, P.T. (1996) The solution structure of HIV-1 Nef reveals an unexpected fold and permits delineation of the binding surface for the SH3 domain of Hck tyrosine protein kinase. Nature Struct. Biol. 3, 340-345. pubmed PDF
271. Clore, G.M., Werner, M.H., Huth, J.R. & Gronenborn, A.M. (1996) Understanding 46X,Y sex reversal at the atomic level. In Biological Structure and Dynamics, (eds. Sarma, R.H. & Sarma, M.H.), Vol. 1, pp. 35-40, Adenine press, New York. In Mechanisms in Transcription, Nucleic Acids and Molecular Biology, (ed., Ecsktein, F. & Lilley, D.M.J.), vol. 11, pp. 265-273, Springer-Verlag, Berlin.
272. Trainor, C.D., Omichinski, J.G., Vandergon, T.L., Gronenborn, A.M., Clore, G.M. & Felsenfeld, G. (1996) A palyndromic regulatory site with vertebrate GATA-1 promoters requires both zinc fingers of the GATA-1 DNA binding domain for high affinity interaction. Mol. Cell. Biol. 16, 2238-2247. pubmed PDF
273. Qin, J., Clore, G.M., Kennedy W.P., Kuszewski, J. & Gronenborn, A.M. (1996) The solution structure of human thioredoxin complexed with its target from Ref-1 reveals peptide chain reversal. Structure 4, 613-620. pubmed PDF
274. Kuszewski, J., Gronenborn, A.M. & Clore, G.M. (1996) Improving the quality of NMR and crystallographic protein structures by means of a conformational database potential derived from structure databases. Protein Science 5, 1067-1080. pubmed PDF
275. Werner, M.H., Huth, J.R., Gronenborn, A.M. & Clore, G.M. (1996) Molecular determinants of mammalian sex. Trends in Biochem. 21, 302-308. pubmed PDF
276. Kuszewski, J., Gronenborn, A.M. & Clore, G.M. (1996) A potential involving multiple proton chemical shift restraints for non-stereospecifically assigned methyl and methylene protons. J. Magn. Reson. Series B 112, 79-81. pubmed PDF
277. Gronenborn, A.M., Frank, M.K. & Clore, G.M. (1996) Core mutants of the immunoglobulin binding domain of Streptococcal protein G: stability and structural integrity. FEBS Lett. 398, 312-316. pubmed PDF
278. Miller, M., Lubkowski, J., Rao, M.J.K., Danishefsky, A.T., Omichinski, J.G., Sakaguchi, K., Sakamoto, H., Appella, E., Gronenborn, A.M. & Clore, G.M. (1996) The oligomerization domain of p53: crystal structure of the trigonal form. FEBS Lett. 399, 166-170. pubmed PDF

1997
279. Clore, G.M. & Gronenborn, A.M. (1997) Dissecting intrinsic chaperonin activity. Proc. Natl. Acad. Sci. U.S.A. 94, 7-8. pubmed PDF
280. Omichinski, J.G., Pedone, P.V., Felsenfeld, G., Gronenborn, A.M. & Clore, G.M. (1997) The solution structure of a specific GAGA factor/DNA complex reveals a modular binding mode. Nature Struct. Biol. 4, 122-132. pubmed PDF
281. Garrett, D.S., Seok, Y.J., Liao, D.I., Peterkofsky, A., Gronenborn, A.M. & Clore, G.M. (1997) Solution structure of the 30 kDa N-terminal domain of Enzyme I of the Escherichia coli phosphoenolpyruvate:sugar phosphotransferase system by multidimensional NMR. Biochemistry 36, 2517-2530. pubmed PDF
282. Kuszewski, J., Gronenborn, A.M. & Clore, G.M. (1997) Improvements and extensions in the conformational database potential for the refinement of NMR and X-ray structures of proteins and nucleic acids. J. Magn. Reson. 125, 171-177. pubmed PDF
283. Pedone, P.V., Omichinski, J.G., Nony, P., Trainor, C., Gronenborn, A.M., Clore, G.M. & Felsenfeld, G. (1997) The N-terminal fingers of cGATA-2 and cGATA-3 are independent sequence-specific DNA binding domains. EMBO J. 16, 2874-2882. pubmed PDF
284. Garrett, D.S., Seok, Y.J., Peterkofsky, A., Clore, G.M. & Gronenborn, A.M. (1997) Identification by NMR of the binding surface for the histidine-containing phosphocarrier protein HPr on the N-terminal domain of enzyme I of the Escherichia coli phosphotransferase system. Biochemistry 36, 4393-4398. pubmed PDF
285. Gronenborn, A.M. & Clore, G.M. (1997) Water in and around proteins. The Biochemist 19, issue 3, 18-21.
286. Tjandra, N., Garrett, D.S., Gronenborn, A.M., Bax, A. & Clore, G.M. (1997) Defining long range order in NMR structure determination from the dependence of heteronuclear relaxation times on rotational diffusion anisotropy. Nature Struct. Biol.4, 443-449. pubmed PDF
287. Nagaich, A.K., Zhurkin, V.B., Sakamoto, H., Gorin, A.A., Clore, G.M., Gronenborn, A.M., Appella, E. & Harrington, R.E. (1997) Architectural accomodation in the complex of four p53 DNA binding domain peptides with the p21/Waf1/Cip1 DNA response element. J. Biol. Chem. 272, 14830-14841. pubmed PDF
288. Wingfield, P.T., Stahl, S.J., Kaufman, J., Zlotnick, A., Hyde, C.C., Gronenborn, A.M. & Clore, G.M. (1997) The extracellular domain of immunodeficiency virus gp41 protein: expression in Escherichia coli, purification and crystallization. Protein Sci.6, 1653-1660. pubmed PDF
289. Cai, M., Zheng, R., Caffrey, M., Craigie, R., Clore, G.M. & Gronenborn, A.M. (1997) Solution structure of the N-terminal zinc binding domain of HIV-1 integrase. Nature Struct. Biol. 4, 567-577. pubmed PDF
290. Tjandra, N., Omichinski, J.G., Gronenborn, A.M., Clore, G.M. & Bax, A. (1997) Use of dipolar ¹⁵N-¹H and ¹³C-¹H couplings in the structure determination of magnetically oriented macromolecules in solution. Nature Struct. Biol. 4, 732-738. pubmed PDF
291. Huth, J.R., Bewley, C.A., Nissen, M.S., Evans, J.N.S., Reeves, R., Gronenborn, A.M. & Clore, G.M. (1997) The solution structure of an HMG-I(Y)/DNA complex defines a new architectural minor groove binding motif. Nature Sruct. Biol. 4, 657-665. pubmed PDF
292. Caffrey, M., Cai, M., Kaufman, J., Stahl, S.J., Wingfield, P.T., Gronenborn, A.M. & Clore, G.M. (1997) Determination of the secondary structure and global topology of the 44 kDa ectodomain of gp41 of the simian immunodeficiency virus by multidimensional nuclear magnetic resonance spectroscopy. J. Mol. Biol. 271, 819-826. pubmed PDF
293. Clore, G.M. & Gronenborn, A.M. (1997) NMR structures of proteins and protein complexes beyond 20,000 M_r.Nature Struct. Biol. 4, 849-853 (1997), pubmed. Current Opinions in Chemical Biology 2, 564-570 (1998). pubmed PDF
294. Clubb, R.T., Schumaker, S., Mizuuchi, K., Gronenborn, A.M. & Clore, G.M. (1997) Solution structure of the Ig subdomain of the Mu end DNA binding domain of Mu phage transposase. J. Mol. Biol. 273, 19-25. pubmed PDF
295. Huth, J.R., Bewley, C.A., Jackson, B.M., Hinnebusch, A.G., Clore, G.M. & Gronenborn, A.M. (1997) Design of an expression system for detecting folded protein domains and mapping macromolecular interactions by NMR. Protein Sci. 6, 2359-2364. pubmed PDF
296. Schumacher, S., Clubb, R.T., Cai. M., Mizuuchi, K., Clore, G.M. & Gronenborn, A.M. (1997) Solution structure of the Mu end DNA binding Ib subdomain of phage Mu transposase: modular DNA recognition by two tethered domains. EMBO J. 16, 7532-7541. pubmed PDF

1998
297. Clore, G.M. & Gronenborn, A.M. (1998) Determining structures of large proteins and protein complexes by NMR. Trends in Biotechnology 16, 22-34. pubmed PDF
298. Bewley, C.A., Gronenborn, A.M. & Clore, G.M. (1998) Minor-groove binding architectural proteins: structure, function and DNA recognition. Ann. Rev. Biophys. Biomolec. Struct. 27, 105-131. pubmed PDF
299. Cai, M., Huang, Y., Sakaguchi, K., Clore, G.M., Gronenborn, A.M. & Craigie, R. (1998) An efficient and cost-effective isotope labeling protocol for proteins expressed in Escherichia coli. J. Biomol. NMR 11, 97-102. pubmed PDF
300. Louis, J.M., Martin, R., Clore, G.M. & Gronenborn, A.M. (1998) Preparation of uniformly isotope labeled DNA oligonucleotides for NMR spectroscopy. J. Biol. Chem. 273, 2374-2378. pubmed PDF
301. Clore, G.M. & Gronenborn, A. M. (1998) New methods of structure refinement for macromolecular structure determination by NMR. Proc. Natl. Acad. Sci. U.S.A. 95, 5891-5898. pubmed PDF
302. Clore, G.M., Gronenborn, A.M. & Tjandra, N. (1998) Direct refinement against residual dipolar couplings in the presence of rhombicity of unknown magnitude. J. Magn. Reson. 131, 159-162. pubmed PDF
303. Garrett, D.S., Seok, Y.-J., Peterkofsky, A., Clore, G.M. & Gronenborn, A.M. (1998) Tautomeric state and pK_a of the phosphorylated active site histidine in the N-terminal domain of Enzyme I of the Escherichia coli phosphoenolpyruvate:sugar phosphotransferase system. Protein Science 7, 789-793. pubmed PDF
304. Starich, M.R., Wikström, M., Arst, H.N., Clore, G.M. & Gronenborn, A.M. (1998) The solution structure of a fungal AREA protein-DNA complex: an alternative binding mode for the basic carboxyl tail of GATA factors. J. Mol. Biol. 277, 605-620. pubmed PDF
305. Starich, M.R., Wikström, M., Schumacher, S., Arst, H.N., Gronenborn, A.M. & Clore, G.M. (1998) The solution structure of the Leu22ÆVal mutant of the AREA DNA binding domain complexed with a TGATA core element defines a role for hydrophobic packing in the determination of specificity. J. Mol. Biol. 277, 621-634. pubmed PDF
306. Brünger, A.T., Adams, P.D., Clore, G.M., DeLano, W.L., Gros, P., Grosse-Kunsteleve, R.W., Jiang, J.-S., Kuszewski, J., Nilges, M., Pannu, N.S., Read, R.J., Rice, L.M., Simonson, T. & Warren, G.L. (1998) Crystallography and NMR system (CNS): a new software suite for macromolecular structure determination. Acta Cryst. Series D 54, 901-921. pubmed PDF
307. Clore, G.M., Gronenborn, A.M. & Bax, A. (1998) A robust method for determining the magnitude of the fully asymmetric alignment tensor of oriented macromolecules in the absence of structural information. J. Magn. Reson. 133, 216-221. pubmed PDF
308. Clore, G.M., Gronenborn, A.M., Szabo, A. & Tjandra, N. (1998) Determining the magnitude of the fully asymmetric diffusion tensor from heteronuclear relaxation data in the absence of structural information. J. Am. Chem. Soc. 120, 4889-4890. PDF ACS
309. Clore, G.M., Murphy, E.C., Gronenborn, A.M. & Bax, A. (1998) Determination of three-bond ¹H3’-³¹P couplings in nucleic acids and protein-nucleic acid complexes by quantitative J correlation spectroscopy. J. Magn. Reson. 134, 164-167. pubmed PDF
310. Bewley, C.A., Gustafson, K.R., Boyd, M.R., Covell, D.G., Bax, A., Clore, G.M. & Gronenborn, A.M. (1998) Solution structure of cyanovirin-N, a potent HIV-inactivating protein. Nature Struct. Biol. 5, 571-578. pubmed PDF
311. Caffrey, M., Cai, M., Kaufman, J., Stahl, S.J., Wingfield, P.T., Covell, D.G., Gronenborn, A.M. & Clore, G.M. (1998) Three-dimensional solution structure of the 44 kDa ectodomain of SIV gp41. EMBO J. 17, 4572-4584. pubmed PDF
312. Caffrey, M., Kaufman, J., Stahl, S.J., Wingfield, P.T., Gronenborn, A.M. & Clore, G.M. (1998) 3D NMR experiments for measuring ¹⁵N relaxation data of large proteins: application to the 44 kDa ectodomain of SIV gp41. J. Magn. Reson. 135, 368-372. pubmed PDF
313. Cai, M., Huang, Y., Zheng, R., Wei, S.-Q., Ghirlando, R., Lee, M.S., Craigie, R., Gronenborn, A.M. & Clore, G.M. (1998) Solution structure of the cellular factor BAF responsible for protecting retroviral DNA from autointegration. Nature Struct. Biol. 5, 903-909. pubmed PDF
314. Cai, M., Huang, Y., Caffrey, M., Zheng, R., Craigie, R., Clore, G.M. & Gronenborn, A.M. (1998) Solution structure of the His12ÆCys mutant of the N-terminal zinc binding domain of HIV-1 integrase complexed to cadmium. Protein Sci.7, 2669-2674. pubmed PDF
315. Clore, G.M., Starich, M.R., Gronenborn, A.M. (1998) Measurement of residual dipolar couplings of macromolecules aligned in the nematic phase of a colloidal suspension of rod-shaped viruses. J. Am. Chem. Soc. 120, 10571-10572. PDF ACS

1999
316. Yu, B., Blaber, M., Gronenborn, A.M., Clore, G.M. & Caspar, D.L.D. (1999) Disordered water within a hydrophobic cavity visualized by X-ray crystallography. Proc. Natl. Acad. Sci. U.S.A. 96, 103-108. pubmed PDF
317. Gronenborn, A.M., Clore, G.M., Louis, J.M. & Wingfield, P.T. (1999) Is human thioredoxin monomeric or dimeric? Protein Sci. 8, 426-429. pubmed PDF
318. Garrett, D.S., Seok, Y.-J., Peterkofsky, A., Gronenborn, A.M. & Clore, G.M. (1999) Solution structure of the 40,000 M_r phosphoryl transfer complex between Enzyme I and HPr. Nature Struct. Biol. 6, 166-173. pubmed PDF
319. Kuszewski, J., Gronenborn, A.M. & Clore, G.M. (1999) Improving the packing and accuracy of NMR structures with a pseudopotential for the radius of gyration. J. Am. Chem. Soc. 121, 2337-2338. PDF Supporting Information ACS
320. Yang, F., Bewley, C.A., Louis, J.M., Gustafson, K.R., Boyd, M.R., Gronenborn, A.M., Clore, G.M. & Wlodawer, A. (1999) Crystal structure of cyanovirin-N, a potent HIV-inactivating protein, shows unexpected domain swapping. J. Mol. Biol. 288, 403-412. pubmed PDF
321. Cornilescu, G., Ramirez, B.E., Frank, M.K., Clore, G.M., Gronenborn, A.M. & Bax, A. (1999) Correlation between ^3hJ_NC’ and hydrogen bond length in proteins. J. Am. Chem. Soc. 121, 6275-6279. PDF ACS
322. Caffrey, M., Kaufman, J., Stahl, S.J., Wingfield, P.T., Gronenborn, A.M. & Clore, G.M. (1999) Monomer-trimer equilibrium of the ectodomain of SIV gp41: insight into the mechanism of peptide inhibition of HIV infection. Protein Sci. 8, 1904-1907. pubmed PDF
323. Louis, J.M., Clore, G.M. & Gronenborn, A.M. (1999) Regulation of HIV-1 protease: autoprocessing is tightly coupled to protein folding. Nature Struct. Biol. 6, 868-875. pubmed PDF
324. Clore, G.M., Starich, M.R., Bewley, C.A., Cai, M. & Kuszewski, J. (1999) Impact of residual dipolar couplings on the accuracy of NMR structures determined from a minimal number of NOE restraints. J. Am. Chem. Soc. 121, 6513-6514. PDF ACS
325. Clore, G.M. & Garrett, D.S. (1999) R-factor, Free R and complete cross-validation for dipolar coupling refinement of NMR structures. J. Am. Chem. Soc. 121, 9008-9012. PDF ACS

2000
326. Kontaxis, G., Clore, G.M. & Bax, A. (2000) Evaluation of cross-relaxation effects and measurement of one-bond couplings in proteins with short transverse relaxation times. J. Magn. Reson. 143, 184-196. pubmed PDF
327. Tjandra, N., J. Marquardt, J. & Clore, G.M. (2000) Direct refinement against proton-proton dipolar couplings in NMR structure determination of macromolecules. J. Magn. Reson. 142, 393-396. pubmed PDF
328. Louis, J.M., Weber, I.T., Tözser, J., Clore, G.M. & Gronenborn, A.M. (2000) HIV-1 protease: maturation, enzyme specificity and drug resistance. Adv. Pharmacol. 49, 111-146. pubmed PDF
329. Caffrey, M., Braddock, D.T., Louis, J.M., Abu-Asab, M.A., Kingma, D., Liotta, L., Tsokos, M., Tresser, N., Pannell, L.K., Watts, N., Steven, A.C., Simon, M.N., Stahl, S.J., Wingfield, P.T. & Clore, G.M. (2000) Biophysical characterization of gp41 aggregates suggests a model for the molecular mechanism of HIV-associated neurological damage and dementia. J. Biol. Chem. 275, 19877-19882. pubmed PDF
330. Wang, G., Sondej, M., Garret, D.S., Peterkovsky, A. & Clore, G.M. (2000) A common interface on HPr for interaction with its partner proteins. J. Biol. Chem. 275, 16401-16403. pubmed PDF
331. Huang, K., Louis, J.M., Donaldson, L., Lim, F,-L., Sharrocks, A.D. & Clore, G.M. (2000) Solution structure of the MEF2A-DNA complex: structural basis for the modulation of DNA bending and specificity by MADS-box transcription factors. EMBO J. 19, 2615-2628. pubmed PDF
332. Clore, G.M. (2000) Accurate and rapid docking of protein-protein complexes on the basis of intermolecular nuclear Overhauser enhancement data and dipolar couplings by rigid body minimization. Proc. Natl. Acad. Sci. U.S.A. 97, 9021-9025. pubmed PDF
333. Bewley, C.A. & Clore, G.M. (2000) Determination of the relative orientation of the two halves of the domain-swapped dimer of cyanovirin-N in solution using dipolar couplings and rigid body minimization. J. Am. Chem. Soc. 122, 6009-6016. PDF ACS
334. Kuszewski, J. & Clore, G.M. (2000) Source of and solutions to problems in the refinement of protein NMR structures against torsion angle potentials of mean force. J. Magn. Reson. 146, 249-254. pubmed PDF
335. Chen, Y.W. & Clore, G.M. (2000) A systematic case study on using NMR models for molecular replacement: p53 tetramerization domain revisited. Acta Cryst. D56, 1535-1540. pubmed PDF
336. Wang, G., Louis, J.M., Sondej, M., Seok, Y.-J., Peterkofsky, A. & Clore, G.M. (2000) Solution structure of the phosphoryl transfer complex between the signal transducing protein HPr and IIA^Glucose of the Escherichia coli phosphoenolpyruvate:sugar phosphotransferase system. EMBO J. 19, 5635-5649. pubmed PDF
337. Wang, G., Peterkofsky, A. & Clore, G.M. (2000) A novel membrane anchor function for the N-terminal amphipathic sequence of the signal transducing protein IIA^Glucose of the Escherichia coli phosphotransferase system. J. Biol. Chem.275, 39811-39814. pubmed PDF

2001
338. Schwieters, C.D. & Clore, G.M. (2001) The VMD-XPLOR visualization package for NMR structure refinement. J. Magn. Reson.149, 239-244. pubmed PDF
339. Peterkofsky, A., Wang, G., Garrett, D.S., Lee, B.R. & Clore, G.M. (2001) Three-dimensional structures of protein-protein complexes in the E. coli PTS. J. Mol. Microbiol. Biotechnol.3, 347-354. (Symposium on PTS). pubmed PDF
340. Kuszewski, J., Schwieters, C.D. & Clore, G.M. (2001) Improving the accuracy of NMR structures of DNA by means of a database potential of mean force describing base-base positional interactions. J. Am. Chem. Soc. 123, 3903-3918. pubmed PDF
341. Louis, J.M., Bewley, C.A. & Clore, G.M. (2001) Design and properties of N_CCG-gp41, a chimeric gp41 molecule with nanomolar HIV-fusion inhibitory activity. J. Biol. Chem. 276, 29485-29489. pubmed PDF
342. Cai, M., Huang, Y., Ghirlando, R., Wilson, K.L., Craigie, R. and Clore, G.M. (2001) Solution structure of the constant region of nuclear envelope protein LAP2 reveals two LEM-domain structures: one binds BAF and the other binds DNA. EMBO J. 20, 4399-4407. pubmed PDF
343. Braddock, D.T., Cai, M., Baber, J.L., Huang, Y. & Clore, G.M. (2001) Rapid identification of medium to large scale interdomain motion in modular proteins using dipolar couplings. J. Am. Chem. Soc. 123, 8634-8635. pubmed PDF
344. Cai, M., Huang, Y. & Clore, G.M. (2001) Accurate orientation of the functional groups of asparagine and glutamine side-chains using one- and two-bond dipolar couplings. J. Am. Chem. Soc. 123, 8642-8643. pubmed PDF
345. Schwieters, C.D. & Clore, G.M. (2001) Internal coordinates for molecular dynamics and minimization in structure determination and refinement. J. Magn. Reson. 152, 288-302. pubmed PDF
346. Murphy, E.C., Zhurkin, V.B., Louis, J.M., Cornilescu, G. and Clore, G.M. (2001) Structural basis for SRY-dependent 46-X,Y sex reversal: modulation of DNA bending by a naturally occuring point mutation. J. Mol. Biol. 312, 481-499. pubmed PDF

2002
347. Clore, G.M. & Bewley, C.A. (2002) Using conjoined rigid body / torsion angle simulated annealing to determine the relative orientation of covalently linked protein domains from dipolar couplings. J. Magn. Reson. 154, 329-335. pubmed PDF
348. Braddock, D.T., Louis, J.M., Baber, J.L., Levens, D. & Clore, G.M. (2002) Structure and dynamics of KH domains from FBP bound to single stranded DNA. Nature 415, 1051-1056. pubmed PDF Supplementary
349. Clore, G.M. & Schwieters, C.D. (2002) Theoretical and computational advances in biomolecular NMR spectroscopy. Curr. Op. Struct. Biol. 12, 146-153. pubmed PDF
350. Clore, G.M. & Kuszewski, J. (2002) c1 rotamer populations and angles of mobile surface side chains are accurately predicted by a torsion angle database potential of mean force. J. Am. Chem. Soc. 124, 2866-2867. pubmed PDF
351. Bewley, C.A., Louis, J.M., Ghirlando, R. & Clore, G.M. (2002) Design of a novel peptide inhibitor of HIV fusion that disrupts the internal trimeric coiled-coil of gp41. J. Biol. Chem. 277, 14238-14245. pubmed PDF
352. Braddock, D.T., Baber, J.L., Levens, D. & Clore, G.M. (2002) Molecular basis of sequence specific single-stranded DNA recognition by KH domains: solution structure of a complex between hnRNP K KH3 and single-stranded DNA. EMBO J. 21, 3476-3485. pubmed PDF Supplementary
353. Schwieters, C.D. & Clore, G.M. (2002) Reweighted atomic densities to represent ensembles of NMR structures. J. Biomol. NMR 23, 221-225. pubmed PDF
354. Cornilescu, G., Lee, B.R., Cornilescu, C.C., Wang, G., Peterkofsky, A. & Clore, G.M. (2002) Solution structure of the phosphoryl transfer complex between the cytoplasmic A domain of the mannitol transporter II^Mannitol and HPr of the Escherichia coli phosphotransferase system. J. Biol. Chem. 277, 42289-42298. pubmed PDF

2003
355. Schwieters, C.D., Kuszewski, J., Tjandra, N. & Clore, G.M. (2003) The Xplor-NIH NMR molecular structure determination package. J. Magn. Reson. 160, 66-74. pubmed PDF

356. Clore, G.M. & Kuszewski, J. (2003) Improving the accuracy of NMR structures of RNA by means of conformational database potentials of mean force as assessed by complete dipolar coupling cross-validation. J. Am. Chem. Soc. 125, 1518-1525. pubmed PDF
357. Clore, G.M. & Schwieters, C.D. (2003) Docking of protein-protein complexes on the basis of highly ambiguous intermolecular distance restraints derived from ¹H_N/¹⁵N chemical shift mapping and backbone ¹⁵N-¹H residual dipolar couplings using conjoined rigid body/torsion angle dynamics. J. Am. Chem. Soc. 125, 2902-2912. pubmed PDF
358. Louis, J.M., Nesheiwat, I., Chang, L.C., Clore, G.M. & Bewley, C.A. (2003) Covalent trimers of the internal N-terminal trimeric coiled-coil of gp41 and antibodies directed against them are potent inhibitors of HIV envelope-mediated cell fusion. J. Biol. Chem. 278, 20278-20285. pubmed PDF
359. Iwahara, J., Anderson, D.E., Murphy, E.C. & Clore, G.M. (2003) EDTA-derivatized deoxythymidine as a tool for rapid determination of protein binding polarity to DNA by intermolecular paramagnetic relaxation enhancement. J. Am. Chem. Soc. 125, 6634-6635. pubmed PDF Supplementary Information
360. Cai, M., Williams, D.C., Wang, G., Lee, B.R., Peterkofsky, A. & Clore, G.M. (2003) Solution structure of the phosphoryl transfer complex between the signal transducing protein IIA^Glucose and the cytoplasmic domain of the glucose transporter IICB^Glucose of the Escherichia coli glucose phosphotransferase system. J. Biol. Chem. 278, 25191-25206. pubmed PDF

2004
361. Williams, D.C., Cai, M. & Clore, G.M. (2004) Molecular basis for synergistic activation by Oct1 and Sox2 revealed from the solution structure of the 42 kDa Oct1·Sox2·Hoxb1-DNA ternary transcription factor complex. J. Biol. Chem. 279, 1449-1457. pubmed PDF
362. Clore, G.M. & Schwieters, C.D. (2004) How much backbone motion in ubiquitin is required to be consistent with dipolar coupling data measured in multiple alignment media as assessed by independent cross-validation. J. Am. Chem. Soc. 126, 2923-2938. pubmed PDF Supplementary Information

363. Schulz, D.M., Ihling, C., Clore, G.M. & Sinz, A. (2004) Mapping the topology and determination of a low resolution three-dimensional structure of the calmodulin-mellitin complex by chemical cross-linking and high resolution FTICR mass spectrometry. Biochemistry 43, 4703-4715. pubmed PDF

364. Iwahara, J., Schwieters, C. D., Clore, G. M. (2004) Ensemble approach for NMR structure refinement against ¹H paramagnetic relaxation enhancement data arising from a flexible paramagnetic group attached to a macromolecule. J. Am. Chem. Soc. 126, 5879-5896. pubmed PDF Supplementary Information

365. Kuszewski, J., Schwieters, C.D., Garrett, D.S., Byrd, R.A., Tjandra, N. & Clore, G. M. (2004) Completely automated, highly error tolerant macromolecular structure determination from multidimensional nuclear Overhauser enhancement spectra and chemical shift assignments. J. Am. Chem. Soc. 126, 6258-6273. pubmed PDF

366. Gallo, S.A., Clore, G.M., Louis, J.M., Bewley, C.A. & Blumenthal, R. (2004) Temperature-dependent intermediates in HIV-1 envelope glycoprotein-mediated fusion revealed by inhibitors that target N-terminal and C-terminal helical regions of HIV-1 gp41. Biochemistry 43, 8230-8233. pubmed PDF

367. Miclet, E., Williams, D.C., Clore, G.M., Boisbouvier, J. & Bax, A. (2004) Relaxation-optimized NMR spectroscopy of methylene groups in proteins and nucleic acids. J. Am. Chem. Soc. 126, 10560-10570. pubmed PDF Supplementary Information

368. Clore, G.M. & Schwieters, C. D. (2004) Amplitudes of protein backbone dynamics and correlated motions in a small a/b protein: correspondence of dipolar coupling and heteronuclear relaxation measurements. Biochemistry 43, 10678-10691. pubmed PDF Supplementary Information

369. Huth, J.R., Yu, L., Collins, I., Mack, J., Mendoza, R., Isaac, B., Braddock, D.T., Muchmore, S.W., Comess, K.M., Fesik, S.W., Clore, G.M., Levens, D. & Hajduk, P.J. (2004) Benzoylanthranilic acid inhibitors of FBP binding to the c-myc promoter. J. Med. Chem. 47, 4851-4857. pubmed PDF

370. Legler, P. M., Cai, M., Peterkofsky, A. & Clore, G. M. (2004) Three-dimensional solution structure of the cytoplasmic B domain of the mannitol transporter II^Mannitol of the Escherichia coli phosphotransferase system. J. Biol. Chem. 279, 39115-39121. pubmed PDF

371. Iwahara, J., Schwieters, C.D. & Clore, G.M. (2004) Characterization of non-specific protein-DNA interactions by ¹H paramagnetic relaxation enhancement. J. Am. Chem. Soc. 126, 12800-12808. pubmed PDF

2005

372. Gozansky, E. K., Louis, J. M., Caffrey, M. & Clore, G. M. (2005) Mapping the binding of the N-terminal extracellular tail of the CXCR4 receptor to stromal cell-derived factor-1a. J. Mol. Biol. 345, 651-658. pubmed PDF

373. Gustchina, E., Hummer, G., Bewley, C.A & Clore, G. M. (2005) Differential inhibition of HIV-1 and SIV envelope-mediated cell fusion by C34 peptides derived from the C-terminal heptad repeat of gp41 from diverse strains of HIV-1, HIV-2 and SIV. J. Med. Chem. 48, 3036-3044. pubmed PDF

374. Tang, C., Williams, D.C., Ghirlando, R. & Clore, G.M. (2005) Solution structure of enzyme IIA^Chitobiose from the N,N'-diacetylchitobiose branch of the Escherichia coli phosphotransferase system. J. Biol. Chem. 280, 11770-11780. pubmed PDF

375. Williams, D.C., Cai, M., Suh, J.-Y., Peterkofsky, A. & Clore, G. M. (2005) Solution NMR structure of the 48 kDa IIA^Mannose-HPr complex of the Escherichia coli mannose phosphotransferase system. J. Biol. Chem. 280, 20775-20784. pubmed PDF

376. Williams, D.C., Lee, J. Y., Cai, M., Bewley, C.A. & Clore, G.M. (2005) Crystal structures of the HIV-1 inhibitory cyanobacterial protein MVL free and bound to Man₃GlcNac₂: structural basis for specificity and high-affinity binding to the core pentasaccharide from N-linked oligomannoside. J. Biol. Chem. 280, 29269-29276. pubmed PDF

377. Tang, C., Iwahara, J. & Clore, G.M. (2005) Accurate determination of leucine and valine side-chain conformations using U-[¹⁵N/¹³C/²H]/[¹H-methyl/methine)-Leu/Val] isotope labeling, NOE pattern recognition and methine CgHg/CbHb residual dipolar couplings: application to the 34 kDa enzyme IIA^Chitobiose. J. Biomol. NMR. 33, 105-121. pubmed PDF

378. Dimitrov, A.S., Louis, J.M., Bewley, C.A., Clore, G.M. & Blumenthal, R. (2005) Conformational changes in HIV-1 gp41 in the course of HIV-1 Env-mediated fusion and inactivation. Biochemistry 44, 12471-12479. pubmed PDF

379. Suh, J.-Y., Tang, C., Cai, M. & Clore, G.M. (2005) Visualization of the phosphorylated active site loop of the cytoplasmic B domain of the mannitol transporter II^Mannitol of the Escherichia coli phosphotransferase system by NMR spectroscopy and residual dipolar coplings. J. Mol. Biol. 353, 1129-1136. pubmed PDF

380. Louis, J.M., Bewley, C.A., Gustchina, E., Aniana, A. & Clore, G.M. (2005) Characterization and HIV-1 fusion inhibitory properties of monoclonal Fabs obtained from a human non-immune phage library selected against diverse epitopes of the ectodomain of HIV-1 gp41. J.Mol. Biol. 353, 945-951. pubmed PDF

2006

381. Schwieters, C.D., Kuszewski, J. & Clore, G.M. (2006) Using Xplor-NIH for NMR molecular structure determination. Progr. NMR Spectroscopy 48, 47-62. PDF Progr. NMR Spectr

382. Clore, G.M. & Schwieters, C.D. (2006) Concordance of residual dipolar couplings, backbone order parameters and crystallographic B-factors for a small a/b protein: a unified picture of high probability, fast atomic motions in proteins. J. Mol. Biol. 355, 879-886. pubmed PDF Coordinates for N=8 ensemble

383. Iwahara, J. & Clore, G.M. (2006) Direct observation of enhanced translocation of a homeodomain between DNA cognate sites by NMR exchange spectroscopy. J. Am. Chem. Soc. 128, 404-405. pubmed PDF Supplementary Information

384. Suh, J.-Y., Cai, M., Williams, D.C. & Clore, G.M. (2006) Solution structure of a post-transition state analog of the phoshotransfer reaction between the A and B cytoplasmic domains of the mannitol transporter II^Mannitol of the Escherichia coli phosphotransferase system. J. Biol. Chem. 281, 8939-8949. pubmed PDF

385. Clore, G.M. (2006) Structural proteomics by NMR. In Proteomics for Biological Discovery (Veenstra, T.D. & Yates, J.R., eds.), pp. 171-185, John Wiley & Sons, New York. PDF

386. Iwahara, J. & Clore, G.M. (2006) Detecting transient intermediates in macromolecular binding by paramagnetic NMR. Nature 440, 1227-1230. pubmed PDF Supplementary Information

387. Hu, K., Vögeli, B & Clore, G.M. (2006) Interference between transverse cross-correlated relaxation and longitudinal relaxation affects apparent J-coupling and transverse cross-correlated relaxation. Chem. Phys. Lett. 423, 123-125. PDF Chem. Phys. Lett.

388. Tang, C. & Clore, G.M. (2006) A simple and reliable approach to docking protein-protein complexes from very sparse NOE-derived intermolecular distance restraints. J. Biomol. NMR 36, 37-44. pubmed PDF

389. Iwahara, J., Zweckstetter, M. & Clore, G.M. (2006) NMR structural and kinetic characterization of a homeodomain diffusing and hopping on non-specific DNA. Proc. Natl. Acad. Sci. U.S.A. 103, 15062-15067. Pubmed PDF Supplementary Material

390. Tang, C., Iwahara, J. & Clore, G.M. (2006) Visualization of transient encounter complexes in protein-protein association. Nature 444, 383-386. pubmed PDF Supplementary Material Movie1 Movie2
News & Views (Blundell & Fernandez-Recio, Nature 444, 279-280)
Leading Edge Molecular Biology Selects, Cell 127, 653 (2006)

391. Gustchina, E., Louis, J.M., Bewley, C.A. & Clore, G.M. (2006) Synergistic inhibition of HIV-1 envelope-mediated membrane fusion by inhibitors targeting the N- and C-terminal heptad repeats of gp41. J. Mol. Biol. 364, 283-289. pubmed PDF

392. Iwahara, J. & Clore, G.M. (2006) Sensitivity improvement for correlations involving arginine side-chain Ne/He resonances in multi-dimensional NMR experiments using broadband ¹⁵N 180° pulses. J. Biomol. NMR 36, 251-257. pubmed PDF

393. Hu, K., Vögeli, B. & Clore, G.M. (2006) ¹³C-detected HN(CA)C and HMCMC experiments using a single methyl-reprotonated sample for unambiguous methyl resonance assignment. J. Biomol. NMR 36, 259-266. pubmed PDF

2007

394. Iwahara, J., Tang, C. & Clore, G.M. (2007) Practical aspects of ¹H transverse paramagnetic relaxation enhancement measurements on macromolecules. J. Magn. Reson. 184, 185-195. pubmed PDF

395. Schwieters, C.D. & Clore, G.M. (2007) A physical picture of atomic motions within the Dickerson DNA dodecamer in solution derived from joint ensemble refinement against NMR and large angle X-ray scattering data. Biochemistry 46, 1152-1166. pubmed PDF Supplementary Material Coordinates for N=4 ensemble

396. Suh, J.-Y., Iwahara, J. & Clore, G.M. (2007) Intramolecular domain-domain association/dissociation and phosphoryl transfer in the mannitol transporter of Escherichia coli are not coupled. Proc. Natl. Acad. Sci. U.S.A. 104, 3153-3158. pubmed PDF Supplementary Material

397. Iwahara, J., Jung, Y.-S., & Clore, G.M. (2007) Heteronuclear NMR spectroscopy for lysine NH₃ groups in proteins: unique effect of water-exchange on ¹⁵N transverse relaxation. J. Am. Chem. Soc. 129, 2971-2980. pubmed PDF

398. Hu, K., Vögeli, B. & Clore, G.M. (2007) Spin state selective carbon-detected HNCO with TROSY optimization in all dimensions and double echo-antiecho sensitivity enhancement in both indirect dimensions. J. Am. Chem. Soc. 129, 5484-5489. pubmed PDF Supplementary Material

399. Cai, M., Huang, Y., Suh, J.-Y., Louis, J.M., Ghirlando, R., Craigie, R. & Clore, G.M. (2007) Solution NMR struture of the Barrier-to-Autointegration Factor/Emerin complex. J. Biol. Chem. 282, 14525-14535. pubmed PDF

400. Tang, C., Schwieters, C.D. & Clore, G.M. (2007) Open-to-closed transition in apo maltose-binding protein visualized by paramagnetic NMR. Nature 449, 1078-1082. pubmed PDF Supplementary Material

401. Clore, G.M., Tang, C. & Iwahara, J. (2007) Elucidating transient macromolecular interactions using paramagnetic relaxation enhancement. Curr. Op. Struct. Biol. 17, 603-616. pubmed PDF

402. Gustchina, E., Louis, J. M., Lam, S.N., Bewley, C.A. & Clore, G.M. (2007) A monoclonal Fab derived from a human non-immune phage library reveals a new epitope on gp41 and neutralizes diverse HIV-1 strains. J. Virol. 81, 12946-12953. pubmed PDF

403. Sahu, D., Clore, G.M. & Iwahara, J. (2007) TROSY-based z-exchange spectroscopy: application to the determination of the activation energy for intermolecular protein translocation between specific sites on different DNA molecules. J. Am. Chem. Soc. 129, 13232-13237. pubmed PDF

404. Suh, J.-Y., Tang, C. & Clore, G.M. (2007) Role of electrostatic interactions in transient encounter complexes in protein-protein association investigated by paramagnetic relaxation enhancement. J. Am. Chem. Soc 129, 12954-12955. pubmed PDF Supplementary Material

2008

405. Schwieters, C.D. & Clore, G.M. (2008) A pseudopotential for improving the packing of ellipsoidal protein structures determined by NMR. J. Phys. Chem. B 112, 6070-6073. pubmed PDF

406. Tang, C., Ghirlando, R. & Clore, G. M. (2008) Visualization of transient ultra-weak protein self-association in solution using paramagnetic relaxation enhancement. J. Am. Chem. Soc. 130, 4048-4056. pubmed PDF

407. Hu, J., Hu, K., Williams, D.C., Komlosh, M., Cai, M. & Clore, G.M. (2008) Solution NMR structures of productive and non-productive complexes between the A and B domains of the cytoplasmic subunit of the mannose transporter of the Escherichia coli phosphotransferase system. J. Biol. Chem. 283, 11024-11037. pubmed PDF

408. Nelson, J.D., Kinkead, H., Brunel, F.M., Leaman, D., Jensen, R., Louis, J.M., Maruyama, T., Bewley, C.A., Bowdish, K., Clore, G.M., Dawson, P.E., Frederickson, S., Mage, R.G., Richman, D.D., Burton, D.R. & Zwick, M.B. (2008) Antibody elicited against the gp41 N-heptad repeat (NHR) coiled-coil can neutralize HIV-1 with modest potency but non-neutralizing antibodies also bind to NHR mimetics. Virology 377, 170-183. pubmed PDF

409. Suh, J.-Y., Cai, M. & Clore, G.M. (2008) Impact of phosphorylation on the structure and thermodynamics of the interaction between the N-terminal domain of Enzyme I and the histidine phosphocarrier protein of the bacterial phosphotransferase system. J. Biol. Chem. 283, 18980-18989. pubmed PDF

410. Kim, Y.C., Tang, C., Clore, G.M. & Hummer, G. (2008) Replica exchange simulations of transient encounter complexes in protein-protein association. Proc. Natl. Acad. Sci. U. S. A. 105, 12855-12860. pubmed PDF Supplementary Appendix

411. Kuszewski, J., Thottungal, R.A., Clore, G.M. & Schwieters, C.D. (2008) Automated error-tolerant macromolecular structure determination from multidimensional nuclear Overhauser enhancement spectra and chemical shift assignments: improved robustness and performance of the PASD algorithm. J. Biomol. NMR, 41, 221-239. pubmed PDF Supplementary

412. Clore, G.M. (2008) Visualizing lowly-populated regions of the free energy landscape of macromolecular complexes by paramagnetic relaxation enhancement. Molecular BioSystems 4, 1058-1069. pubmed PDF

413. Doucleff, M. & Clore, G.M. (2008) Global jumping and domain-specific intersegment transfer between DNA cognate sites of the multi-domain transcription factor Oct-1. Proc. Natl. Acad. Sci. U. S. A. 105, 13871-13876. pubmed PDF Supplementary.

414. Gustchina, E., Bewley, C.A. & Clore, G.M. (2008) Sequestering the pre-hairpin intermediate of gp41 by peptide N36^Mut(e,g)potentiates the human immunodeficiency virus type 1 neutralizing activity of monoclonal antibodies directed against the N-terminal helical repeat of gp41. J. Virol. 82, 10032-10041. pubmed PDF

415. Tang, C., Louis, J.M., Aniana, A., Suh, J.-Y. & Clore, G.M (2008) Visualizing transient events in amino-terminal auto-processing of HIV-1 protease. Nature 455, 693-696. pubmed PDF Supplementary

2009

416. Clore, G.M. (2009) NMR in Structural Biology, in Imaging Life: Biological Systems from Atoms to Tissues, pp. 51-73 ed. G.C. Howard, W.E. Brown & M. Auer, Oxford University Press (published 2014).

417. Clore, G.M. & Iwahara, J. (2009) Theory, practice and applications of paramagnetic relaxation enhancement for the characterization of transient low-population states of biological macromolecules and their complexes. Chem. Rev. 109, 4108-4139. pubmed PDF

418. Ryabov, Y., Suh, J.-Y., Grishaev, A., Clore, G.M. & Schwieters, C.D. (2009) Using the experimentally determined components of the overall rotational diffusion tensor to restrain molecular shape and size in NMR structure determination of globular proteins and protein-protein complexes. J. Am. Chem. Soc. 131, 9522-9531. pubmed PDF Supplementary

419. Hu, K., Doucleff, M. & Clore, G.M. (2009) Using multiple quantum coherence to increase the ¹⁵N resolution in a three-dimensional TROSY HNCO experiment for accurate PRE and RDC measurements. J. Magn. Reson. 200, 173-177. pubmed PDF

420. Gustchina, E., Louis, J.M., Frisch, C., Ylera, F., Lechner, A., Bewley, C.A. & Clore, G.M. (2009) Affinity maturation by targeted diversification of the CDR-H2 loop of a monoclonal Fab derived from a synthetic naïve human antibody library and directed against the internal trimeric coiled-coil of gp41 yields a set of Fabs with improved HIV-1 neutralization potency and breadth. Virology 393, 112-119. pubmed PDF

2010

421. Fawzi, N.L., Doucleff, M., Suh, J.-Y. & Clore, G.M. (2010) Mechanistic details of a protein-protein association pathway revealed by paramagnetic relaxation enhancement titration measurements. Proc. Natl. Acad. Sci. U. S. A. 121, 1379-1384. pubmed PDF Supplementary

422. Yung, Y.-S., Cai, M. & Clore, G.M. (2010) Solution structure of the IIA^Chitobiose-IIB^Chitobiose complex of the N,N'-diacetylchitobiose branch of the Eschrichia coli phosphotransferase system. J. Biol. Chem. 285, 4173-4184. pubmed PDF

423. Ryabov, Y., Clore, G.M. & Schwieters, C.D. (2010) Direct use of ¹⁵N relaxation rates as experimental restraints on molecular shape and orientation for docking of protein-protein complexes. J. Am. Chem. Soc. 132, 5987-5989 pubmed PDF Supplementary

424. Fawzi, N., Ying, J., Torchia, D, A., Clore, G. M. (2010) Kinetics of amyloid b monomer to oligomer exchange by NMR relaxation. J. Am. Chem. Soc. 132, 9948-9951 pubmed PDF Supplementary

425. Schwieters, C.D., Suh, J.-Y., Grishaev, A., Ghirlando, R., Takayama, Y. & Clore, G.M. (2010) Solution structure of the 128 kDa Enzyme I dimer from Escherichia coli and its 146 kDa complex with HPr using residual dipolar couplings and small and wide angle X-ray scattering. J. Am. Chem. Soc. 132, 13026-13045. pubmed PDF Supplementary

426. Iwahara, J. & Clore, G.M. (2010) Structure-independent analysis of the breadth of the positional distribution of disordered groups in macromolecules from order parameters for long variable-length vectors using NMR paramagnetic relaxation enhancement. J. Am. Chem. Soc. 132, 13346-13356. pubmed PDF

427. Gustchina, E., Li, M., Louis, J.M., Anderson, D.E., Lloyd, J., Frisch, C., Bewley, C.A., Gustchina, A., Wlodawer, A. & Clore, G.M. (2010) Structural basis of HIV-1 neutralization by affinity matured Fabs directed against the internal trimeric coiled-coil of gp41. PLoS Pathogens 6, e1001182. pubmed PDF Supplementary

428. Yin, H., Feng, G., Clore, G.M., Hummer, G. & Rasaiah, J.C. (2010) Water in the polar and non-polar cavities of the protein interleukin-1b. J. Phys. Chem. 114, 16290-16297 pubmed PDF

429. Cai, M., Huang, Y., Craigie, R. & Clore, G.M. (2010) Structural basis of the association of HIV-1 matrix protein with DNA. PloS One 5, e15675. pubmed PDF

2011

430. Clore, G.M. (2011) Exploring sparsely-populated states of macromolecules by diamagnetic and paramagnetic NMR relaxation. Protein Sci. 20, 229-246. pubmed PDF

431. Takayama, Y., Schwieters, C. D., Grishaev, A., Ghirlando, R. & Clore, G.M. (2011) Combined use of residual dipolar couplings and solution X-ray scattering to rapidly probe rigid body conformational transitions in a non-phosphorylatable active site mutant of the 128 kDa enzyme I dimer. J. Am. Chem. Soc. 133, 424-427. pubmed PDF Supplementary

432. Clore, G.M. (2011) Adventures in biomolecular NMR, in Encyclopedia of Magnetic Resonance, Historical Perspectives, (Becker, E.D., ed.; Harris, R.K. & Wasylishen, R.E., editors-in-chief) John Wiley & Sons (Chichester), doi:10.1002/9780470034590.emrhp1008. PDF Encyclopedia Magn. Reson.

433. Shahzad-ul-Hussan, S., Gustchina, E., Ghirlando, R., Clore, G.M. & Bewley, C.A. (2011) Solution structure of the monovalent lectin microvirin in complex with Mana(1-2)Man provides a basis for anti-HIV activity with low toxicity. J. Biol. Chem. 286, 20788-20796. pubmed PDF Supplementary

434. Takayama, Y. & Clore, G.M. (2011) Intra- and intermolecular translocation of the bi-domain transcription factor Oct1 characterized by liquid crystal and paramagnetic NMR. Proc. Natl Acad. Sci. U. S. A. 108, E169-E176. pubmed PDF Supplementary Author summary

435. Ryabov, Y., Schwieters, C.D. & Clore, G.M. (2011) Impact of ¹⁵N R₂/R₁ relaxation restraints on molecular size, shape and bond vector orientation for NMR protein structure determination with sparse distance restraints. J. Am. Chem. Soc. 133, 6154-6157. pubmed PDF Supplementary

436. Fawzi, N.L., Fleissner, M.R., Anthis, N.J., Kalai, T., Hideg, K., Hubbell, W.L. & Clore, G.M. (2011) A rigid disulfide-linked nitroxide side chain simplifies the quantitative analysis of PRE data. J. Biomol. NMR 51, 105-114. pubmed PDF

437. Clore, G.M. (2011) Exploring translocation of proteins on DNA by NMR. J. Biomol. NMR 51, 209-219. pubmed PDF

438. Venditti, V., Fawzi, N.L. & Clore, G.M. (2011) Automated sequence- and stereo-specific assignment of methyl-labeled proteins by paramagnetic relaxation and methyl-methyl nuclear Overhauser enhancement spectroscopy. J. Biomol. NMR 51, 319-328. pubmed PDF Supplementary

439. Huang, Y., Cai, M., Clore, G.M. & Craigie, R. (2011) No interaction of barrier-to-autointegration factor (BAF) with HIV-1 MA, cone-rode homeobox (Crx or MAN1-C in absence of DNA. PloS ONE 6, e25123. pubmed PDF

440. Fawzi, N.L., Ying, J., Ghirlando, R, Torchia, D.A. & Clore, G.M. (2011) Atomic resolution dynamics on the surface of amyloid ß protofibrils probed by solution NMR. Nature 480, 268-272. pubmed PDF Supplementary Software for fitting DEST data

441. Anthis, N.J., Doucleff, M. & Clore, G.M. (2011) Transient sparsely-populated compact states of apo and calcium-loaded calmodulin probed by paramagnetic relaxation enhancement: interplay of conformational selection and induced fit. J. Am. Chem. Soc. 133, 18976-18974. pubmed PDF Supplementary

2012

442. Ryabov, Y., Clore, G.M. & Schwieters, C.D. (2012) Coupling between internal dynamics and rotational diffusion in the presence of exchange between discrete molecular conformations. J. Chem. Phys. 136, 034108. pubmed PDF Supplementary

443. Venditti, V., Fawzi, N.L. & Clore, G.M. (2012) An efficient protocol for incorporation of an unnatural amino acid in perdeutrated recombinant proteins using glucose-based media. J. Biomol. NMR 52, 191-195. pubmed PDF

444. Dogo-Isonagie, C., Lam, S., Gustchina, E., Acharya, P., Yang, Y., Shahzad-ul-Hussan, S., Clore, G.M., Kwong, P.D. & Bewley, C.A. (2012) Peptides from the second extracellular loop of the C-C chemokine receptor type 5 (CCR5) inhibit diverse strains of HIV-1. J. Biol. Chem. 287, 15076-15086. pubmed PDF

445. Takayama, Y. & Clore, G.M. (2012) Interplay between minor and major groove-binding transcription factors Sox2 and Oct1 in translocation on DNA studied by paramagnetic and diamagnetic NMR. J. Biol. Chem. 287, 14349-14363. pubmed PDF

446. Arredondo, S.A., Cai, M., Takayama, Y., MacDonald, N.J., Anderson, D.E., Aravind, L., Clore, G.M. & Miller, L.H. (2012) Structure of the Plasmodium 6-cysteine s48/s46 domain. Proc. Natl. Acad. Sci. U.S.A. 109, 6692-6697. pubmed PDF

447. Fawzi, N.L., Ying, J., Torchia, D.A. & Clore, G.M. (2012) Probing exchange kinetics and atomic resolution dynamics in high molecular weight complexes: dark-state exchange saturation transfer NMR spectroscopy. Nature Protocol 7, 1523-1533. pubmed PDF

448. Jung, Y.-S., Cai, M. & Clore, G.M. (2012) Solution structure of the IIA^Chitobiose-HPr complex of the N,N’-diacetylchitobiose branch of the Escherichia coli phosphotransferase system. J. Biol. Chem. 287, 23819-23829. pubmed PDF

449. Takayama, Y. & Clore, G.M. (2012) Impact of protein-protein interactions on global intermolecular translocation rates of the transcription factors Sox2 and Oct1 between DNA cognate sites studied by z-exchange NMR spectroscopy. J. Biol. Chem. 287, 26962-26970. Pubmed PDF

450. Venditti, V. & Clore, G.M. (2012) Conformational selection and substrate binding regulate the monomer/dimer equilibrium of the C-terminal domain of Escherichia coli Enzyme I. J. Biol. Chem. 287, 26989-26998. Pubmed PDF

451. Grishaev, A., Anthis, N.J. & Clore, G.M. (2012) Contrast-matched small angle X-ray scattering from a heavy atom-labeled protein in structure determination: application to a lead-substituted calmodulin-peptide complex. J. Am. Chem. Soc. 134, 14686-14689. Pubmed PDF Supplementary

452. Bermejo, G. A., Clore, G.M. & Schwieters, C.D. (2012) Smooth statistical torsion angle potential derived from a large conformational database via adaptive kernel density estimation improves the quality of NMR protein structures. Protein Sci. 21, 1824-1836. Pubmed PDF

2013

453. Anthis, N.J. & Clore, G.M. (2013) Sequence-specific determination of protein and peptide concentrations by absorbance at 205 nm, Protein Science, 22, 851-858. Pubmed PDF Software

454. Venditti, V., Ghirlando, R. & Clore, G.M. (2013) Structural basis for Enzyme I inhibition by a-ketoglutarate. ACS Chem. Biol. 8, 1232-1240. Pubmed PDF Supplementary

455. Clore, G.M. (2013) Generating accurate contact maps of transient long-range interactions in intrinsically disordered proteins by paramagnetic relaxation enhancement. Biophys. J. 104, 1635-1636. Pubmed PDF

456. Libich, D.S., Fawzi, N.L., Ying, J. & Clore, G.M. (2013) Probing the transient ‘dark-state’ of substrate binding to GroEL by relaxation-based solution NMR. Proc. Natl. Acad. Sci. U.S.A. 110, 11361-11366. Pubmed PDF

457. Anthis, N.J. & Clore, G.M. (2013) The length of the calmodulin linker determines the extent of transient interdomain association and target affinity. J. Am. Chem. Soc. 135, 9648-9651. Pubmed PDF Supplementary

458. Clore, G.M. & Venditti, V. (2013) Structure, dynamics and biophysics of the cytoplasmic protein-protein complexes of the bacterial phosphoenolpyruvate:sugar phosphotransferase system. Trends Biochem. 38, 515-530. Pubmed PDF

459. Gustchina, E., Ghirlando, R., Schuck, P., Louis, J.M., Pierson, J., Rao, P., Subramaniam, S., Gustchina, A., Clore, G.M. & Wlodawer, A. (2013) Complexes of neutralizing and non-neutralizing affinity matured Fabs with a mimetic of the internal trimeric coiled-coil of HIV-1 gp41. PloS One 8, e78187. Pubmed PDF Supplementary

460. Deshmukh, L., Schwieters, C.D., Grishaev, A., Ghirlando, R., Baber, J.L. & Clore, G.M. (2013) Structure and dynamics of full length HIV-1 capsid protein in solution. J. Am. Chem. Soc. 133, 16133-16147. Pubmed PDF Supplementary

461. Clore, G.M. (2013) Seeing the invisible by paramagnetic and diamagnetic NMR. Centenary Award and Frederick Gowland Hopkins Memorial Lecture. Biochem. Soc. Trans. 41, 1343-1354. Pubmed PDF

2014

462. Clore, G.M. (2014) Interplay between conformational selection and induced fit in multidomain protein-ligand binding probed by paramagnetic relaxation enhancement. Biophysical Chemistry. 186, 3-12. Pubmed PDF

463. Deshmukh, L., Ghirlando, R. & Clore, G.M. (2014) Investigation of the structure and dynamics of the capsid-spacer peptide 1-nucleocapsid fragment of the HIV-1 Gag polyprotein by solution NMR spectroscopy. Angwandte Chemie Int. Ed. 53, 1025-1028. Pubmed PDF Supplementary

464. Tugarinov, V., Venditti, V. & Clore, G.M. (2014) A NMR experiment for simultaneous correlations of valine and leucine/isoleucine methyls with carbonyl chemical shifts in proteins. J. Biomol. NMR 58, 1-8. Pubmed PDF Supplementary

465. Kozakov, D., Lee, K., Hall, D.R., Beglov, D., Zheng, J., Vakili, P., Schueler-Furman, O., Paschalidis, I.C., Clore, G.M. & Vajda, S. (2014) Encounter complexes and dimensionality reduction in protein-protein association. eLife 3:e01370 (doi:10.7554/eLife.01370) Pubmed PDF Supplementary

466. Schwieters, C.D. & Clore, G.M. (2014) Using small angle solution scattering data in Xplor-NIH structure calculations. Progr. Nucl. Magn. Reson. Spectroscopy 80, 1-11 Pubmed PDF

467. Louis, J.M., Aniana, A., Lohith, K., Sayer, J.M., Roche, J., Bewley, C.A. & Clore, G.M. (2014) Binding of HIV-1 gp41-directed neutralizing and non-neutralizing fragment antibody binding domain (Fab) and single chain variable fragment (ScFv) antibodies to the ectodomain of gp41 in the pre-hairpin and six-helix bundle conformations. Plos One 9, e104683. Pubmed PDF Supplementary

468. Fawzi, N.L., Libich, D.S., Ying, J., Tugarinov, V. & Clore, G.M. (2014) Characterizing methyl-bearing side chain contacts and dynamics mediating amyloid beta protofibril interactions using ¹³C_methyl-DEST and lifetime line broadening. Angewandte Chemie Int. Ed. 53, 10345-10349. Pubmed PDF Supplementary

469. Ryu, K.-S., Tugarinov, V. & Clore, G.M. (2014) Probing the rate limiting step for intramolecular transfer of a transcription factor between specific sites on the same DNA molecule by ¹⁵N_z-exchange NMR spectroscopy. J. Am. Chem. Soc. 136, 14369-14372. Pubmed PDF Supplementary

2015

470. Venditti, V., Tugarinov, V., Schwieters, C.D., Grishaev, A. & Clore, G.M. (2015) Large interdomain rearrangement triggered by suppression of micro- to millisecond dynamics in bacterial Enzyme I. Nature Communications 6, 5960. Pubmed PDF Supplementary

471. Anthis, N.J. & Clore, G.M. (2015) Visualizing transient dark states by NMR spectroscopy. Q. Rev. Biophys. 48, 35-116. Pubmed PDF

472. Clore, G.M. (2015) Dynamics of Sox2 interactions with DNA. In Sox2: Biology and Role in Development and Disease, pp. 25-41. eds. Kondoh, H. & Lovell-Badge, R., Elsevier, Amsterdam. PDF

473. Deshmukh, L., Ghirlando, R. & Clore, G.M. (2015) Conformation and dynamics of the Gag polyprotein of the human immunodeficiency virus 1 studied by NMR spectroscopy. Proc. Natl. Acad. Sci. U. S. A. 112, 3374-3379. Pubmed PDF

474. Baber, J. L., Louis, J. M. & Clore, G. M. (2015) Dependence of distance distributions derived from double electron-electron resonance pulsed EPR spectroscopy on pulse-sequence time. Angewandte Chemie Int. Ed. 54. 5336-5339. Pubmed PDF Supplementary

475. Libich, D.S., Tugarinov, V. & Clore, G.M. (2015) Intrinsic unfoldase/foldase activity of the chaperonin GroEL directly demonstrated using multinuclear relaxation-based NMR. Proc. Natl. Acad. Sci. U. S. A. 112, 8817-8823. Pubmed PDF

476. Clore, G.M. (2015) Practical aspects of paramagnetic relaxation enhancement in biological macromolecules. Meth. Enzymol. 564, 485-497. Pubmed PDF

477. Tugarinov, V., Libich, D.S., Meyer, V., Roche, J. & Clore, G.M. (2015) The energetics of a three-state protein folding system probed by high-pressure relaxation dispersion NMR spectroscopy. Angewandte Chemie Int. Ed. 54,11157-11161. Pubmed PDF Supplementary

478. Venditti, V., Schwieters, C.D., Grishaev, A. & Clore, G.M. (2015) Dynamic equilibrium between closed and partially-closed states of the bacterial Enzyme I unveiled by solution NMR and X-ray scattering. Proc. Natl. Acad. Sci. U. S. A. 112, 11565-11570. Pubmed PDF

479. Louis, J.M., Deshmukh, L., Sayer, J., Aniania, A. & Clore, G.M. (2015) Mutations proximal to sites of autoproteolysis and the alpha-helix which co-evolve under drug pressure modulate autoprocessing and vitality of HIV-1 protease. Biochemistry 54, 5414-5424. Pubmed PDF Supplementary

480. Clore, G.M. (2015) NMR in structural and cell biology. In Encyclopedia of Cell Biology (eds. Bradshaw, R.A. and Stahl, P.D.), Vol. 1, pp. 98-107, Academic Press, Waltham, MA. doi:10.1016/B978-0-12-394447-4.10019-7. Pubmed PDF

481. Louis, J.M., Baber, J.L. & Clore, G.M. (2015) The C34 peptide fusion inhibitor binds to the 6-helix bundle core domain of HIV-1 gp41 by displacement of the C-terminal helical repeat region. Biochemistry 54, 6796-6805. Pubmed PDF Supplementary

482. Libich, D.S., Tugarinov, V & Clore, G.M. (2015) Flux analysis of GroEL-assisted folding/unfolding. Proc. Natl. Acad. Sci. U. S. A. 112, E6833-6844. Pubmed PDF

2016

483. Clore, G.M. (2016) Structure determination of large macromolecular complexes using NMR. In Encyclopedia of Spectroscopy and Spectrometry, 3rd ed., (ed. Lindon, J.C., Tranter G.E. & Koppenaal, D.W.), vol. 4, pp. 316-318, Oxford, Elsevier. https://dx/doi.org/10.1016/B978-0-12-409547-2.12131-6. PDF

484. Venditti, V., Egner, T.K. & Clore, G.M. (2016) Hybrid approaches to structural characterization of conformational ensembles of complex macromolecular systems combining NMR residual dipolar couplings and solution X-ray scattering. Chem. Rev. 11, 6305-6322. Pubmed PDF

485. Bermejo, G., Clore, G.M. & Schwieters, C.D. (2016) Improving NMR structures of RNA. Structure 24, 806-815. Pubmed PDF Supplementary

486. Deshmukh, L., Schweiters, C.D.Grishaev, A. & Clore, G.M. (2016) Quantitative characterization of configurational space sampled by HIV-1 nucleocapsid using solution NMR, X-ray scattering and protein engineering. ChemPhysChem, 17, 1548-1552. Pubmed PDF Supplementary

487. Ceccon, A., Tugarinov, V., Bax, A. & Clore, G.M. (2016) Global dynamics and exchange kinetics of a protein on the surface of nanoparticles revealed by relaxation-based solution NMR spectroscopy. J. Am. Chem. Soc. 138, 5789-5792. Pubmed PDF Supplementary
C&E News (Borman S., vol 94, issue 20, p.11)
J. Am. Chem. Soc. Spotlight (2016, 138, 7199)

488. Schmidt, T., Ghirlando, R., Baber, J. & Clore, G.M. (2016) Quantitative resolution of monomer-dimer populations by inversion modulated DEER EPR spectroscopy. ChemPhysChem 17, 2987-2991. Pubmed PDF Supplementary

489. Cai, M., Huang, Y., Yang, R., Craigie, R. & Clore, G.M. (2016) A simple and robust protocol for high-yield expression of perdeuterated proteins in Escherichia coli grown in shaker flasks. J. Biomol. NMR 66, 85-91. Pubmed PDF

490. Ceccon, A., Clore, G.M. & Tugarinov, V. (2016) Towards interpretation of intermolecular paramagnetic relaxation enhancement outside the fast exchange limit. J. Biomol. NMR 66, 1-7. Pubmed PDF Supplementary

491. Deshmukh, L., Louis, J.M., Ghirlando, R. & Clore, G.M. (2016) Transient Gag-protease interactions revealed by paramagnetic NMR suggest origins of compensatory drug resistance mutations in HIV-1. Proc. Natl. Acad. Sci. U. S. A. 113, 12456-12461. Pubmed PDF

492. Schmidt, T., Walti, M.A., Baber, J.L., Hustedt, E.J. & Clore, G.M. (2016) Long distance measurements up to 160 A in the GroEL tetradecamer using Q-band DEER EPR spectroscopy. Angewandte Chemie Int. Ed.55, 15905-15909. Pubmed PDF Supplementary

2017

493. Libich, D.S., Tugarinov, V., Ghirlando, R. & Clore, G.M. (2017) Confinement and stabilization of Fyn SH3 folding intermediate mimetics within the cavity of the chaperonin GroEL by relaxation-based NMR. Biochemistry 56, 903-906. Pubmed PDF Supplementary

494. Ceccon, A., Tugarinov, V., Boughton, A. J., Fushman, D. & Clore, G.M. (2017) Probing the binding modes of a multidomain protein to lipid-based nanoparticles by relaxation-based NMR. J. Chem. Phys. Lett. 8, 2535-2540. Pubmed PDF Supplementary

495. Walti, M. A., Schmidt, T., Murray, D.T., Wang, H., Hinshaw, J.E. & Clore, G.M. (2017) The chaperonin GroEL accelerates protofibril formation and decorates fibrils in the Het-s prion protein. Proc. Natl. Acad. Sci. U. S. A. 114, 9104-9109. Pubmed PDF

496. Walti, M.A. & Clore, G.M. (2017) Disassembly/reassembly strategy for the production of highly pure GroEL, a tetradecameric supramolecular machine, suitable for quantitative NMR, EPR and mutational studies. Protein Expression and Purification 142, 8-15. Pubmed PDF Supplementary

497. Deshmukh, L., Tugarinov, V., Louis, J.M. & Clore, G.M. (2017) Binding kinetics and substrate selectivity in HIV-1 protease-Gag interactions probed at atomic resolution by chemical exchange NMR. Proc. Natl. Acad. Sci. U. S. A. 114,E9855-E9862. Pubmed PDF

2018

498. Schwieters, C.D., Bermejo, G.A. & Clore, G.M. (2018) Xplor-NIH for molecular structure determination from NMR and other data sources. Protein Sci. 27, 26-40. Pubmed PDF

499. Schmidt, T., Tian, L. & Clore, G.M. (2017) Probing conformational states of the finger and thumb subdomains of HIV-1 reverse transcriptase using double electron-electron resonance electron paramagnetic resonance spectroscopy. Biochemistry 55, 489-493. Pubmed PDF Supplementary

500. Deshmukh, L., Tugarinov, V., Appella, D.H. & Clore, G.M. (2018) Targeting a dark excited state of HIV-1 nucleocapsid by anti-retoviral thioesters revealed by NMR. Angewandte Chemie Int. Ed. 57, 2687-2691. Pubmed PDF Supplementary

501. Ceccon, A., Schmidt., T., Tugarinov, V., Kotler, S.A. Schieters, C.D. & Clore, G.M. (2018) Interaction of Huntingtin Exon-1 peptides with lipid-based micellar nanoparticles probed by solution NMR and Q-band pulsed EPR. J. Am. Chem. Soc. 140, 6199-6202. Pubmed PDF Supplementary

502. Walti, M., Libich, D.S. & Clore, G.M. (2018) Extensive sampling of the cavity of the GroEL nanomachine by protein substrates probed by paramagnetic relaxation enhancement. J. Phys. Chem. Lett. 9, 3368-3371. Pubmed PDF Supplementary

503. Ceccon, A., Clore, G.M. & Tugarinov, V. (2018) Decorrelating kinetic and relaxation parameters in exchange saturation transfer NMR: a case study of N-terminal huntingtin peptides binding to unilamellar vesicles. J. Phys. Chem. B. 122, 11271-11278. Pubmed PDF

504. Walti, M.A., Steiner, J., Meng, F., Chung, H. S., Louis, J.M., Ghirlando, R., Tugarinov, V., Nath, A. & Clore, G.M. (2018) Probing the mechanism of inhibition of amyloid b(1-42) induced neurotoxicity by the chaperonin GroEL. Proc. Natl. Acad. Sci. U. S. A. 115, E11924-E11932. Pubmed PDF Supplementary

2019

505. Ceccon, A., Tugarinov, V. & Clore, G.M. (2019) TiO2 nanoparticles catalyze oxidation of huntingtin exon 1-derived peptides impeding aggregation: a quantitative NMR study of binding and kinetics. J. Am. Chem. Soc. 141, 94-97. Pubmed PDF Supplementary

506. Kotler, S.A, Tugarinov, V., Schmidt, T., Ceccon, A., Libich, D.S., Ghirlando, R., Schwieters, C.D. and Clore, G.M. (2019) Probing initial transient oligomerization events facilitating Huntingtin fibril nucleation at atomic resolution by relaxation-based NMR. Proc. Natl. Acad. Sci. U. S. A. 116, 3562-3571. Pubmed PDF Supplementary

507. Tugarinov, V. & Clore, G.M. (2019) Exchange saturation transfer and associated NMR techniques for studies of protein interactions involving high molecular weight systems. J. Biomol. NMR 73, 461-469. Pubmed PDF

508. Miller-Henkins, L., Paine, E.L., Deshmukh, L., Nikolayesvkiy, H., Lyons, G.C., Scerba, M.T., Gorge-Rosenker, K., Luecke, H., Louis, J.M. Chertova, E., Gorelick, R.J., Ott, D.E., Clore, G.M. & Appella, D.H. (2019) Inhibition of HIV maturation via selective unfolding and crosslinking of Gag polyprotein by a mercaptobenamide acetylator. J. Am. Chem. Soc. 121, 8327-8338. Pubmed PDF Supplementary

509. Bax, A. & Clore, G.M. (2019) Protein NMR: boundless opportunities. J. Magn. Reson. 306, 187-191. Pubmed PDF

510. Schmidt, T., Schwieters, C.D. & Clore, G.M. 92019) Spatial domain organization in the HIV-1 reverse transcriptase p66 homodimer precursor probed by double electron-electron resonance EPR. Proc. Natl. Acad. Sci. U. S. A. 116, 17809-17816. Pubmed PDF Supplementary
PNAS Commentary [Varney, Cook & Weber (2019) An asymmetry that leads to activity. Proc. Natl. Acad. Sci. U.S.A.116, 17614-17615.

511. Karamanos, T.K., Tugarinov, V. & Clore, G.M. (2019) Unraveling the structure and dynamics of the human DNAJB6b chaperone by NMR reveals insights into Hsp40-mediated proteostasis. Proc. Natl. Acad. Sci. U.S.A. 116, 21529-21538. Pubmed PDF Supplementary

512. Cai, M., Huang, Y., Craigie, R. & Clore, G.M. (2019) A simple protocol for expression of isotope-labeled proteins in Escherichia coli grown in shaker flasks at high cell density. J. Biomol. NMR 73 ,743-748. Pubmed PDF

513. Cai, M., Juang, Y., Shen, Y., Li, M., Mizuuchi, M., Ghirlando, R., Mizuuchi, K. & Clore, G.M. (2019) Probing transient excited states of the bacterial cell devision regulator MinE by relaxation dispersion NMR spectroscopy. Proc. Natl. Acad. Sci. U.S.A. 116, 25446-25455 Pubmed PDF Supplementary

2020

514. Schwieters, C.D., Bermejo, G.A. & Clore, G.M. (2020) A three-dimensional potential of mean force to improve backbone and sidechain hydrogen bond geometry in protein structure determination. Protein Sci. 21, 100-110. Pubmed PDF

515. Garrett, D.S., Cai., M. & Clore, G.M. (2020) XIPP – Multi-Dimensional NMR analysis software. J. Biomol. NMR 74, 9-25. Pubmed PDF

516. Tugarinov, V., Karamanos, T.K., Ceccon, A. & Clore, G.M. (2020) Optimized NMR experiments for the isolation of I = 1/2 manifold transitions in methyl groups of proteins. ChemPhysChem 21, 13-19 Pubmed PDF Supplementary

517. Karamanos, T.K., Tugarinov, V. & Clore, G.M. (2020) Determining methyl sidechain conformations in a CS-ROSETTA model using 1H-13C residual dipolar couplings. J. Biomol. NMR 74, 111-118. Pubmed PDF Supplementary

518. Ceccon, A., Tugarinov, V., Ghirlando, R. & Clore, G.M. (2020) Abrogation of pre-nucleation, transient oligomerization of the Huntingtin exon-1 protein by human profilin-I. Proc. Natl. Acad. Sci. U.S.A. 117, 5844-5852. Pubmed PDF Supplementary

519. Tugarinov, V., Karamanos, T. & Clore, G.M. (2020) Magic-angle-pulse driven separation of degenerate ¹H transitions in methyl groups of proteins: application to studies of methyl axis dynamics. ChemPhysChem. 21, 13-19. Pubmed PDF Supplementary

520. Okuno, Y., Szabo, A. & Clore, G.M. (2020) On the quantitative interpretation of solvent paramagnetic relaxation for probing protein-cosolute interactions. J. Am. Chem. Soc. 142, 8281-8290. Pubmed PDF Supplementary

521. Schmidt, T., Jeon, J., Okuno, Y., Chiliveri, S.C. & Clore, G.M. (2020) Submillisecond freezing permits cryoprotectant-free EPR double electron-electron resonance spectroscopy. ChemPhysChem 21, 1224-1229. Pubmed PDF Supplementary

522. Schmidt, T., Louis, J.M. & Clore, G.M. (2020) Probing the interaction between HIV-1 protease and the homodimeric p66/p66' reverse transcriptase precursor by double electron-electron resonance EPR spectroscopy. ChemBioChem. 21, 3051-3055. Pubmed PDF Supplementary

523. Ceccon, A., Tugarinov, V. & Clore, G.M. (2020) Kinetics of fast tetramerization of the huntingtin exon 1 protein probed by concentration-dependent on-resonance R1rho measurements. J. Phys. Chem. Lett. 11, 5643-5648. Pubmed PDF Supplementary

524. Schmidt, T. & Clore, G.M. (2020) Tm filtering by 1H-methyl labeling in a deuterated protein for pulsed double electron-electron resonance EPR. Chem. Commun. 56, 10890-10893. Pubmed PDF Supplementary

525. Tugarinov, V., Karamanos, T.K. & Clore, G.M. (2020) Optimized selection of slow-relaxating 13C transitions in methyl groups of proteins: application to relaxation dispersion. J. Biomol.NMR 74, 673-680. Pubmed PDF Supplementary

526. Karamanos, T.K., Tugarinov, V. & Clore, G.M. (2020) An S/T motif controls reversible oligomerization of the Hsp40 chaperone DNAJB6b through subtle reorganization of a b-sheet backbone. Proc. Natl. Acad. Sci. U.S.A. 117, 30441-30450. Pubmed PDF Supplementary

2021

527. Cai, M., Huang, Y., Lloyd, J., Craigie, R. & Clore, G.M. (2021) A simple and cost-effective protocol for high-yield expression of deuterated and selectively isoleucine/leucine/valine methyl protonated proeins in Escherichia coli in shaker flasks. J. Biomol. NMR 75 83-87. Pubmed PDF

528. Walti, M.A., Kotler, S.A. & Clore, G.M. (2021) Probing the interacttion of huntingtin exon-1 polypeptides with the chaperonin nanomachine GroEL. ChemBioChem epub ahead of print doi:10.1002/cbic.202100055. Pubmed PDF Supplementary

529. Tugarinov, V., Ceccon, A. & Clore, G.M. (2021) Probing side-chain dynamics in proteins by NMR relaxation of ¹³C magnetization modes in ¹³CH₃ methyl groups J. Phys. Chem. B 125 3343-3352. Pubmed PDF Supplementary

Books

Clore, G.M. & Gronenborn, A.M. (1993) NMR of Proteins, Topics in Molecular and Structural Biology, MacMillan Press, Ltd. (London).

Clore, G.M. & Potts, J. (2012) Recent Development in Biomolecular NMR, RSC Biomolecular Sciences Series, Royal Society of Chemistry Publishing, Cambridge. doi:10.1039/9781849735391

Patents
1. Clore, G.M., Bewley-Clore, C. A. & Medabalimi, J.L. GP41 inhibitors. US Provisional Application No. 60/339,751 (filed Dec 17, 2001); International Application No. PCT/US02/40684 (filed Dec 17, 2002)
2. Clore, G.M., Bewley-Clore, C. A. & Medabalimi, J.L. Novel peptide inhibitor of HIV fusion that disrupts the internal trimeric coiled-coil of gp41. US Provisional Patent Application No. 60/480,070 (filed February 11, 2003). PCT Patent application No. PCT/US04/003794 (filed February 10, 2004)
3. Clore, G.M., Bewley-Clore, C. A. & Medabalimi, J.L. Tightly binding antibodies directed against the internal trimeric coiled-coil of gp41 inhibit HIV-envelope mediated cell fusion. US Provisional Patent Application No. 60/480,070 (filed June 20, 2003).

Miscellaneous articles
Clore, G.M. (2006) The ins and outs of HID lighting: 18/21 watt HID lights. NACD Journal vol. 39, 1st Quarter, pp. 37-40. (National Association for Cave Diving).
Bauer, J., Carmichael, R., Clore, G.M., Green, D., Green, L., Hurley, J., Murcar, R., O'Leary, M., Richards, J., Schmid, J. & Wyatt, J. (2006) Cavern/Cave Diver Workbook, First edition, revised April 2006, National Association for Cave Diving, Gainesville, FL.
Clore, G.M. (2006) High quality LED backup lights. NACD Journal vol. 39, 3rd Quarter, pp. 33-35 (National Association for Cave Diving).

Clore, G.M. and Green, L. (2007) Exploring Peacock. NACD Journal vol 40, 1st Quarter, pp. 10-12 (National Association for Cave Diving). PDF
Clore, G.M. (2007) Update on primary and backup lights. NACD Journal vol 40, 4th quarter, p. 13
Clore, G.M. (2007) Doubles wings reviewed. NACD Journal vol. 40, 4th quarter, pp. 25-27.

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