The Crystal Structure of a GroEL/Peptide Complex

Boisvert, 1996, The 2.4 Å crystal structure of the bacterial chaperonin GroEL complexed with ATP gamma S, Nat. Struct. Biol., 3, 170, 10.1038/nsb0296-170

Braig, 1993, A polypeptide bound by the chaperonin GroEL is localized within a central cavity, Proc. Natl. Acad. Sci. USA, 90, 3978, 10.1073/pnas.90.9.3978

Braig, 1994, The crystal structure of the bacterial chaperonin GroEL at 2.8 Å, Nature, 371, 578, 10.1038/371578a0

Braig, 1995, Conformational variability in the refined structure of the chaperonin GroEL at 2.8 Å resolution, Nat. Struct. Biol., 2, 1083, 10.1038/nsb1295-1083

Brünger, 1998, Crystallography and NMR system, Acta Crystallogr. D Biol. Crystallogr., 54, 905, 10.1107/S0907444998003254

Buckle, 1997, A structural model for GroEL-polypeptide recognition, Proc. Natl. Acad. Sci. USA, 94, 3571, 10.1073/pnas.94.8.3571

Chatellier, 1999, GroEL recognises sequential and non-sequential linear structural motifs compatible with extended beta-strands and alpha-helices, J. Mol. Biol., 292, 163, 10.1006/jmbi.1999.3040

Chen, 1994, Location of a folding protein and shape changes in GroEL-GroES complexes imaged by cryo-electron microscopy, Nature, 371, 261, 10.1038/371261a0

Ellis, 1996

Evans, 1993, SETOR, J. Mol. Graph., 11, 134, 10.1016/0263-7855(93)87009-T

Fenton, 1997, GroEL-mediated protein folding, Protein Sci., 6, 743, 10.1002/pro.5560060401

Fenton, 1994, Residues in chaperonin GroEL required for polypeptide binding and release, Nature, 371, 614, 10.1038/371614a0

Fremont, 1992, Crystal structures of two viral peptides in complex with murine MHC class I H-2K, Science, 257, 919, 10.1126/science.1323877

Hartl, 1996, Molecular chaperones in cellular protein folding, Nature, 381, 571, 10.1038/381571a0

Hayer-Hartl, 1994, Conformational specificity of the chaperonin GroEL for the compact folding intermediates of alpha-lactalbumin, EMBO J., 13, 3192, 10.1002/j.1460-2075.1994.tb06618.x

Hlodan, 1995, Binding of defined regions of a polypeptide to GroEL and its implications for chaperonin-mediated protein folding, Nat. Struct. Biol., 2, 587, 10.1038/nsb0795-587

Horwich, 1993, Folding in vivo of bacterial cytoplasmic protiens, Cell, 74, 909, 10.1016/0092-8674(93)90470-B

Hunt, 1996, The crystal structure of the GroES co-chaperonin at 2.8 Å resolution, Nature, 379, 37, 10.1038/379037a0

Itzhaki, 1995, Nature and consequences of GroEL-protein interactions, Biochemistry, 34, 14581, 10.1021/bi00044a037

Jones, 1991, Improved methods for binding protein models in electron density maps and the location of errors in these models, Acta Crystallogr. A, 47, 110, 10.1107/S0108767390010224

Kobayashi, 1999, NMR analysis of the binding of a rhodanese peptide to a minichaperone in solution, J. Mol. Biol., 292, 181, 10.1006/jmbi.1999.3042

Kraulis, 1991, MOLSCRIPT, J. Appl. Crystallogr., 24, 946, 10.1107/S0021889891004399

Landry, 1992, Different conformations for the same polypeptide bound to chaperones DnaK and GroEL, Nature, 355, 455, 10.1038/355455a0

Lin, 1995, The hydrophobic nature of GroEL-substrate binding, J. Biol. Chem., 270, 1011, 10.1074/jbc.270.3.1011

Lippens, 1995, Use of a water flip-back pulse in the homonuclear NOESY experiment, J. Bio. NMR, 5, 327

Ma, 1998, The allosteric mechanism of the chaperonin GroEL, Proc. Natl. Acad. Sci. USA, 95, 8502, 10.1073/pnas.95.15.8502

Madden, 1993, The antigenic identity of peptide-MHC complexes, Cell, 75, 693, 10.1016/0092-8674(93)90490-H

Mande, 1996, Structure of the heat shock protein chaperonin-10 of mycobacterium leprae, Science, 271, 203, 10.1126/science.271.5246.203

Martin, 1991, Chaperonin-mediated protein folding at the surface of groEL through a “molten globule”-like intermediate, Nature, 352, 36, 10.1038/352036a0

Mayhew, 1996, Protein folding in the central cavity of the GroEL-GroES chaperonin complex, Nature, 379, 420, 10.1038/379420a0

Merritt, 1997, RASTER3D, Methods Enzymol., 277, 505, 10.1016/S0076-6879(97)77028-9

Nicholls, 1991, Protein folding and association, Proteins, 11, 281, 10.1002/prot.340110407

Otwinowski, 1997, Processing of X-ray diffraction data collected in oscillation mode, Methods Enzymol., 276, 307, 10.1016/S0076-6879(97)76066-X

Piotto, 1992, Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions, J. Bio. NMR, 2, 661, 10.1007/BF02192855

Schmidt, 1992, Interaction of GroE with an all-beta-protein, J. Biol. Chem., 267, 16829, 10.1016/S0021-9258(18)41858-3

Scott, 1990, Searching for peptide ligands with an epitope library, Science, 249, 386, 10.1126/science.1696028

Sharp, 1991, Reconciling the magnitude of the microscopic and macroscopic hydrophobic effects, Science, 252, 106, 10.1126/science.2011744

Shtilerman, 1999, Chaperonin function, Science, 284, 822, 10.1126/science.284.5415.822

Sigler, 1998, Structure and function in GroEL-mediated protein folding, Annu. Rev. Biochem., 67, 581, 10.1146/annurev.biochem.67.1.581

Tanaka, 1999, Identification of substrate binding site of GroEL minichaperone in solution, J. Mol. Biol., 292, 173, 10.1006/jmbi.1999.3041

Thiyagarajan, 1996, Solution structures of GroEL and its complex with rhodanese from small-angle neutron scattering, Structure, 4, 79, 10.1016/S0969-2126(96)00011-1

Viitanen, 1992, Purified chaperonin 60 (groEL) interacts with the nonnative states of a multitude of Escherichia coli proteins, Protein Sci., 1, 363, 10.1002/pro.5560010308

Weissman, 1995, Mechanism of GroEL action, Cell, 83, 577, 10.1016/0092-8674(95)90098-5

Weissman, 1996, Characterization of the active intermediate of a GroEL-GroES-mediated protein folding reaction, Cell, 84, 481, 10.1016/S0092-8674(00)81293-3

Xu, 1998, GroEL/GroES, J. Struct. Biol., 124, 129, 10.1006/jsbi.1998.4060

Xu, 1997, The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex, Nature, 388, 741, 10.1038/41944

Zahn, 1996, Chaperone activity and structure of monomeric polypeptide binding domains of GroEL, Proc. Natl. Acad. Sci. USA, 93, 15024, 10.1073/pnas.93.26.15024