Structural basis for GroEL-assisted protein folding from the crystal structure of (GroEL-KMgATP)14 at 2.0A resolution.
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[1] J. Changeux,et al. ON THE NATURE OF ALLOSTERIC TRANSITIONS: A PLAUSIBLE MODEL. , 1965, Journal of molecular biology.
[2] D. Koshland,et al. Comparison of experimental binding data and theoretical models in proteins containing subunits. , 1966, Biochemistry.
[3] R. D. Shannon. Revised effective ionic radii and systematic studies of interatomic distances in halides and chalcogenides , 1976 .
[4] Conrad C. Huang,et al. The MIDAS display system , 1988 .
[5] K. Flaherty,et al. Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate protein , 1990, Nature.
[6] Mike Carson,et al. RIBBONS 2.0 , 1991 .
[7] J. Zou,et al. Improved methods for building protein models in electron density maps and the location of errors in these models. , 1991, Acta crystallographica. Section A, Foundations of crystallography.
[8] J. Rothman,et al. Positive cooperativity in the functioning of molecular chaperone GroEL. , 1992, The Journal of biological chemistry.
[9] G. Lorimer,et al. Hydrolysis of adenosine 5'-triphosphate by Escherichia coli GroEL: effects of GroES and potassium ion. , 1993, Biochemistry.
[10] T. Atkinson,et al. Binding and hydrolysis of nucleotides in the chaperonin catalytic cycle: implications for the mechanism of assisted protein folding. , 1993, Biochemistry.
[11] Yechezkel Kashi,et al. GroEL-mediated protein folding proceeds by multiple rounds of binding and release of nonnative forms , 1994, Cell.
[12] R. Jaenicke,et al. Symmetric complexes of GroE chaperonins as part of the functional cycle. , 1994, Science.
[13] Zbyszek Otwinowski,et al. The crystal structure of the bacterial chaperonln GroEL at 2.8 Å , 1994, Nature.
[14] M. Kessel,et al. Characterization of a functional GroEL14(GroES7)2 chaperonin hetero-oligomer. , 1994, Science.
[15] K. Flaherty,et al. Structural basis of the 70-kilodalton heat shock cognate protein ATP hydrolytic activity. II. Structure of the active site with ADP or ATP bound to wild type and mutant ATPase fragment. , 1994, The Journal of biological chemistry.
[16] Y. Kashi,et al. Residues in chaperonin GroEL required for polypeptide binding and release , 1994, Nature.
[17] G. Lorimer,et al. Dynamics of the chaperonin ATPase cycle: implications for facilitated protein folding. , 1994, Science.
[18] A. Horovitz,et al. Two lines of allosteric communication in the oligomeric chaperonin GroEL are revealed by the single mutation Arg196-->Ala. , 1994, Journal of molecular biology.
[19] A. Brünger,et al. Torsion angle dynamics: Reduced variable conformational sampling enhances crystallographic structure refinement , 1994, Proteins.
[20] A. Clarke,et al. Chaperonins can catalyse the reversal of early aggregation steps when a protein misfolds. , 1995, Journal of molecular biology.
[21] J. Weissman,et al. Mechanism of GroEL action: Productive release of polypeptide from a sequestered position under groes , 1995, Cell.
[22] A. Horovitz,et al. Nested cooperativity in the ATPase activity of the oligomeric chaperonin GroEL. , 1995, Biochemistry.
[23] P. Adams,et al. Conformational variability in the refined structure of the chaperonin GroEL at 2.8 Å resolution , 1995, Nature Structural Biology.
[24] A. Fersht,et al. Conformational states bound by the molecular chaperones GroEL and secB: a hidden unfolding (annealing) activity. , 1996, Journal of molecular biology.
[25] F. Hartl. Molecular chaperones in cellular protein folding , 1996, Nature.
[26] F. Hartl,et al. Significant hydrogen exchange protection in GroEL‐bound DHFR is maintained during iterative rounds of substrate cycling , 1996, Protein science : a publication of the Protein Society.
[27] Helen R Saibil,et al. The Chaperonin ATPase Cycle: Mechanism of Allosteric Switching and Movements of Substrate-Binding Domains in GroEL , 1996, Cell.
[28] A. Plückthun,et al. beta-Lactamase binds to GroEL in a conformation highly protected against hydrogen/deuterium exchange. , 1996, Proceedings of the National Academy of Sciences of the United States of America.
[29] A. Horovitz,et al. Allosteric control by ATP of non-folded protein binding to GroEL. , 1996, Journal of molecular biology.
[30] G. Lorimer,et al. A thermodynamic coupling mechanism for GroEL-mediated unfolding. , 1996, Proceedings of the National Academy of Sciences of the United States of America.
[31] A. Fersht,et al. Catalysis of Amide Proton Exchange by the Molecular Chaperones GroEL and SecB , 1996, Science.
[32] F. Hartl,et al. Mechanism of chaperonin action: GroES binding and release can drive GroEL‐mediated protein folding in the absence of ATP hydrolysis. , 1996, The EMBO journal.
[33] J. Deisenhofer,et al. The crystal structure of the GroES co-chaperonin at 2.8 Å resolution , 1996, Nature.
[34] Zbyszek Otwinowski,et al. The 2.4 Å crystal structure of the bacterial chaperonin GroEL complexed with ATPγS , 1996, Nature Structural Biology.
[35] A. Horovitz,et al. Inter-ring communication is disrupted in the GroEL mutant Arg13 --> Gly; Ala126 --> Val with known crystal structure. , 1996, Journal of molecular biology.
[36] J. Weissman,et al. Characterization of the Active Intermediate of a GroEL–GroES-Mediated Protein Folding Reaction , 1996, Cell.
[37] S. Mande,et al. Structure of the Heat Shock Protein Chaperonin-10 of Mycobacterium leprae , 1996, Science.
[38] J. Behlke,et al. Nucleotide-dependent complex formation between the Escherichia coli chaperonins GroEL and GroES studied under equilibrium conditions. , 1997, Biochemistry.
[39] K. Wüthrich,et al. Multiple cycles of global unfolding of GroEL-bound cyclophilin A evidenced by NMR. , 1997, Journal of molecular biology.
[40] P. Christen,et al. The power stroke of the DnaK/DnaJ/GrpE molecular chaperone system. , 1997, Journal of molecular biology.
[41] A. Horwich,et al. Distinct actions of cis and trans ATP within the double ring of the chaperonin GroEL , 1997, Nature.
[42] A. Horovitz,et al. Structural basis of allosteric changes in the GroEL mutant Arg197→Ala , 1997, Nature Structural Biology.
[43] A. Horwich,et al. The crystal structure of the asymmetric GroEL–GroES–(ADP)7 chaperonin complex , 1997, Nature.
[44] J. Buchner,et al. Catalysis of protein folding by symmetric chaperone complexes. , 1997, Proceedings of the National Academy of Sciences of the United States of America.
[45] P. Horowitz,et al. ATP Hydrolysis Is Critical for Induction of Conformational Changes in GroEL That Expose Hydrophobic Surfaces* , 1997, The Journal of Biological Chemistry.
[46] A. Fersht,et al. A structural model for GroEL-polypeptide recognition. , 1997, Proceedings of the National Academy of Sciences of the United States of America.
[47] H. Taguchi,et al. Calorimetric Observation of a GroEL-Protein Binding Reaction with Little Contribution of Hydrophobic Interaction* , 1997, The Journal of Biological Chemistry.
[48] A. Horwich,et al. Native-like structure of a protein-folding intermediate bound to the chaperonin GroEL. , 1997, Proceedings of the National Academy of Sciences of the United States of America.
[49] Bernd Bukau,et al. The Hsp70 and Hsp60 Chaperone Machines , 1998, Cell.
[50] P B Sigler,et al. GroEL/GroES: structure and function of a two-stroke folding machine. , 1998, Journal of structural biology.
[51] A. Horwich,et al. Structure and function in GroEL-mediated protein folding. , 1998, Annual review of biochemistry.
[52] R J Read,et al. Crystallography & NMR system: A new software suite for macromolecular structure determination. , 1998, Acta crystallographica. Section D, Biological crystallography.
[53] J. Buchner,et al. Catalysis, commitment and encapsulation during GroE-mediated folding. , 1999, Journal of molecular biology.
[54] K. Kuwajima,et al. Chaperonin-affected refolding of alpha-lactalbumin: effects of nucleotides and the co-chaperonin GroES. , 1999, Journal of molecular biology.
[55] Jun Wang,et al. A computational approach to simplifying the protein folding alphabet , 1999, Nature Structural Biology.
[56] P. Sigler,et al. The Crystal Structure of a GroEL/Peptide Complex Plasticity as a Basis for Substrate Diversity , 1999, Cell.
[57] S W Englander,et al. Chaperonin function: folding by forced unfolding. , 1999, Science.
[58] Helen R. Saibil,et al. GroEL-GroES Cycling ATP and Nonnative Polypeptide Direct Alternation of Folding-Active Rings , 1999, Cell.
[59] J. Weissman,et al. Thinking outside the box: new insights into the mechanism of GroEL-mediated protein folding , 1999, Nature Structural Biology.
[60] A. Fersht,et al. Stabilization of GroEL minichaperones by core and surface mutations. , 2000, Journal of molecular biology.
[61] A. Fersht,et al. From minichaperone to GroEL 1: information on GroEL-polypeptide interactions from crystal packing of minichaperones. , 2000, Journal of molecular biology.
[62] K. Furtak,et al. Multivalent Binding of Nonnative Substrate Proteins by the Chaperonin GroEL , 2000, Cell.
[63] J. Wang,et al. Crystal structures of the HslVU peptidase-ATPase complex reveal an ATP-dependent proteolysis mechanism. , 2001, Structure.
[64] A. Horwich,et al. Folding of malate dehydrogenase inside the GroEL–GroES cavity , 2001, Nature Structural Biology.
[65] G. Farr,et al. GroEL/GroES-Mediated Folding of a Protein Too Large to Be Encapsulated , 2001, Cell.
[66] B. Gowen,et al. ATP-Bound States of GroEL Captured by Cryo-Electron Microscopy , 2001, Cell.
[67] J. Wang,et al. Nucleotide-dependent conformational changes in a protease-associated ATPase HsIU. , 2001, Structure.
[68] A. Horovitz,et al. Review: allostery in chaperonins. , 2001, Journal of structural biology.
[69] D. Thirumalai,et al. Chaperonin-mediated protein folding. , 2001, Annual review of biophysics and biomolecular structure.
[70] B. Gowen,et al. Structures of unliganded and ATP-bound states of the Escherichia coli chaperonin GroEL by cryoelectron microscopy. , 2001, Journal of structural biology.
[71] S. N. Witt,et al. The unfolding story of the Escherichia coli Hsp70 DnaK: is DnaK a holdase or an unfoldase? , 2002, Molecular microbiology.