G. Marius Clore FMedSci, FRS Highly Cited Publications

h-index: 144 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)

 

Greater than 1000 citations

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

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 

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

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

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

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

 

500-1000 citations

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. 

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

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

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

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

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

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

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

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

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

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

Powers, R., Gronenborn, A.M., Clore, G.M. & Bax, A. (1991) Three-dimensional triple resonance NMR of 13C and 15N enriched proteins using constant-time evolution. J. Magn. Reson. 94, 209-213. PDF

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

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

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

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

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

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

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

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

 

200-500 citations

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

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

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

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

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. PDF

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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. Exit Disclaimer

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

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

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

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

Clore, G.M. & Gronenborn, A.M. (1994) Multidimensional heteronuclear nuclear magnetic resonance of proteins. Meth. Enzymol. 239, 349-363. pubmed PDF

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

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-1beta by multi-dimensional NMR. Science 263, 1762-1767. pubmed PDF

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

Clore, G.M. & Gronenborn, A.M. (1995) Three-dimensional structures of alpha and beta chemokines. FASEB Journal 9, 57-62. pubmed PDF

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

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

Makhatadze, G.I., Clore, G.M. & Gronenborn, A.M. (1995) Solvent isotope effect and protein stability. Nature Struct. Biol. 2, 852-855. pubmed PDF

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

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

Werner, M.H., Gronenborn, A.M. & Clore, G.M. (1996) Intercalation, DNA kinking and the control of transcription. Science 271, 778-784. pubmed PDF

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

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

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

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

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

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

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

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

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

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

Clore, G.M. & Gronenborn, A.M. (1997) NMR structures of proteins and protein complexes beyond 20,000 Mr.Nature Struct. Biol. 4, 849-853 pubmed PDF

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

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

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

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

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

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

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

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

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

Cornilescu, G., Ramirez, B.E., Frank, M.K., Clore, G.M., Gronenborn, A.M. & Bax, A. (1999) Correlation between 3hJNC’ and hydrogen bond length in proteins. J. Am. Chem. Soc. 121, 6275-6279. PDF ACS Exit Disclaimer

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 ACS Exit Disclaimer

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 Exit Disclaimer

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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 

 

100-200 Citations

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

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

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

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

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

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. Exit Disclaimer

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

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

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

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

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

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

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. PDF

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

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

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

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

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

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

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

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

Nilges, M., Clore, G.M. & Gronenborn, A.M. (1990) 1H-NMR stereospecific assignments by conformational database searches. Biopolymers 29, 813-822. pubmed PDF

Clore, G.M., Bax, A. & Gronenborn, A.M. (1991) Stereospecific assignment of beta-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

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

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

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

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

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

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

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

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

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

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

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

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-CalphaH coupling constants on protein structure determination by NMR. J. Magn. Reson. Series B 104, 99-103. pubmed PDF

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

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

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

Kuszewski, J., Qin, J., Gronenborn, A.M. & Clore, G.M. (1995) The impact of direct refinement against 13Calpha and 13Cbeta chemical shifts on protein structure determination by NMR. J. Magn. Reson Series B 106, 92-96. pubmed PDF

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

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

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

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

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

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

Clore, G.M. & Gronenborn, A.M. (1997) NMR structures of proteins and protein complexes beyond 20,000 Mr.Nature Struct. Biol. 4, 849-853 (1997), pubmed.

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

Garrett, D.S., Seok, Y.-J., Peterkofsky, A., Gronenborn, A.M. & Clore, G.M. (1999) Solution structure of the 40,000 Mr phosphoryl transfer complex between Enzyme I and HPr. Nature Struct. Biol. 6, 166-173. pubmed PDF

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

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

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

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

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

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

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 IIAGlucose of the Escherichia coli phosphoenolpyruvate:sugar phosphotransferase system. EMBO J. 19, 5635-5649. pubmed PDF

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

Schwieters, C.D. & Clore, G.M. (2001) The VMD-XPLOR visualization package for NMR structure refinement. J. Magn. Reson.149, 239-244. pubmed PDF

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

Louis, J.M., Bewley, C.A. & Clore, G.M. (2001) Design and properties of NCCG-gp41, a chimeric gp41 molecule with nanomolar HIV-fusion inhibitory activity. J. Biol. Chem. 276, 29485-29489. pubmed PDF

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

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

Clore, G.M. & Schwieters, C.D. (2003) Docking of protein-protein complexes on the basis of highly ambiguous intermolecular distance restraints derived from 1HN/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

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

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 IIAGlucose and the cytoplasmic domain of the glucose transporter IICBGlucose of the Escherichia coli glucose phosphotransferase system. J. Biol. Chem. 278, 25191-25206pubmed PDF

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

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

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

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

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

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

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, 404-405pubmed PDF Supplementary Information

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

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

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

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

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

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.

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

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

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

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

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

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 

 

 

 

 

 

 

 

 

 [ Clore Home ]

 

Disclaimer: Dr. Clore created this website in his personal capacity. The information on this site and views expressed are his own and do not necessarily represent the views of the National Institutes of Health or the United States Government