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Journal of Molecular Biology (78)
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Ma, J., Sigler, P. B., Xu, Z., & Karplus, M. (2000). A dynamic model for the allosteric mechanism of GroEL 1 1Edited by A. Fersht. Journal of Molecular Biology, 302(2), 303–313.

Authors 4
  1. Jianpeng Ma (first)
  2. Paul B Sigler (additional)
  3. Zhaohui Xu (additional)
  4. Martin Karplus (additional)
References 61 Referenced 198
  1. {'key': '10.1006/jmbi.2000.4014_BIB1', 'series-title': 'Computer Simulation of Liquids', 'author': 'Allen', 'year': '1980'} / Computer Simulation of Liquids by Allen (1980)
  2. 10.1016/S0263-7855(98)80030-1 / J. Mol. Graph / A fast algorithm for rendering space-filling molecule pictures by Bacon (1988)
  3. 10.1063/1.448118 / J. Chem. Phys / Molecular dynamics with coupling to an external bath by Berendsen (1984)
  4. 10.1016/S0021-9258(19)51017-1 / J. Biol. Chem / ATP induces non-identity of two rings in chaperonin GroEL by Bochkareva (1994)
  5. 10.1038/nsb0296-170 / Nature Struct. Biol / The 2.4 Å crystal structure of the bacterial chaperonin GroEL complexed with ATPγS by Boisvert (1996)
  6. 10.1038/371578a0 / Nature / The crystal structure of the bacterial chaperonin GroEL at 2.8 Å by Braig (1994)
  7. 10.1038/nsb1295-1083 / Nature Struct. Biol / Comformational variability in the refined structure of the chaperonin GroEL at 2.4 Å resolution by Braig (1995)
  8. 10.1002/jcc.540040211 / J. Comput. Chem / CHARMM by Brooks (1983)
  9. 10.1073/pnas.94.8.3571 / Proc. Natl Acad. Sci. USA / A structural model for GroEL-polypeptide recognition by Buckle (1997)
  10. 10.1006/jmbi.1995.0285 / J. Mol. Biol / The origins and consequences of asymmetry in the chaperonin reaction cycle by Burston (1995)
  11. 10.1016/S0021-9258(18)67256-4 / J. Biol. Chem / Purification and properties of the groES morphogenetic protein of Escherichia coli by Chandrasekhar (1986)
  12. 10.1006/jmbi.1999.3040 / J. Mol. Biol / GroEL recognises sequential and non-sequential linear structural motifs compatible with extended beta-strands and alpha-helices by Chatellier (1999)
  13. 10.1016/S0092-8674(00)81673-6 / Cell / The crystal structure of a GroEL/peptide complex by Chen (1999)
  14. 10.1038/371261a0 / Nature / Location of a folding protein and shape changes in GroEL-GroES complexes imaged by cryo-electron microscopy by Chen (1994)
  15. 10.1016/S0959-440X(96)80093-5 / Curr. Opin. Struct. Biol / Molecular chaperonin in protein folding and translocation by Clarke (1996)
  16. 10.1038/10735 / Nature Struct. Biol / GroEL accelerates the refolding of hen lysozyme without changing its folding mechanism by Coyle (1999)
  17. 10.1006/jmbi.1998.2568 / J. Mol. Biol / Conformational changes in the chaperonin GroEL by de Groot (1999)
  18. 10.1146/annurev.bi.60.070191.001541 / Annu. Rev. Biochem / Molecular chaperones by Ellis (1991)
  19. 10.1002/pro.5560060401 / Protein Sci / GroEL-mediated protein folding by Fenton (1997)
  20. 10.1038/371614a0 / Nature / Residues in chaperonin GroEL required for polypeptide binding and release by Fenton (1994)
  21. 10.1073/pnas.74.3.801 / Proc. Natl Acad. Sci. USA / Mechanism of tertiary structural change in hemoglobin by Gelin (1977)
  22. 10.1038/355033a0 / Nature / Protein folding in Cell by Gething (1992)
  23. 10.1016/0014-5793(91)80878-7 / FEBS Letters / Cooperativity in ATP hydrolysis by GroEL is increased by GroES by Gray (1991)
  24. 10.1038/381571a0 / Nature / Molecular chaperones in cellular protein folding by Hartl (1996)
  25. 10.1006/bulm.1999.0150 / Bull. Math. Biol / On the relationship between the hill coefficients for steady-state and transient kinetic data by Horovitz (2000)
  26. 10.1073/pnas.96.6.2682 / Proc. Natl Acad. Sci. USA / GroES in the asymmetric GroEL14-GroES7 complex exchanges via an associated mechanism by Horowitz (1999)
  27. 10.1038/39247 / Nature / Molecular motors by Howard (1997)
  28. 10.1021/bi00061a013 / Biochemistry / Binding and hydrolysis of nucleotides in the chaperonin catalytic cycle by Jackson (1993)
  29. 10.1038/nsb0697-430 / Nature Struct. Biol / Capturing the misfolds by Joachimiak (1997)
  30. 10.1021/ja00392a016 / J. Am. Chem. Soc / Transferable intermolecular potential functions for water, alcohols, and ethers. Application to liquid water by Jorgensen (1981)
  31. 10.1107/S0021889891004399 / J. Appl. Crystallog / MOLSCRIPT by Kraulis (1991)
  32. 10.1006/jsbi.1996.3832 / J. Struct. Biol / Conformational changes in the GroEL oligomer during the functional cycle by Llorca (1997)
  33. 10.1038/41892 / Nature / Protein folding by Lorimer (1997)
  34. {'key': '10.1006/jmbi.2000.4014_BIB34', 'first-page': '1083', 'article-title': 'GroE structures galore', 'volume': '2', 'author': 'Lorimer', 'year': '1995', 'journal-title': 'Nature Struct. Biol'} / Nature Struct. Biol / GroE structures galore by Lorimer (1995)
  35. 10.1073/pnas.94.22.11905 / Proc. Natl Acad. Sci. USA / Molecular switch in signal transduction by Ma (1997)
  36. 10.1073/pnas.95.15.8502 / Proc. Natl Acad. Sci. USA / The allosteric mechanism of the chaperonin GroEL by Ma (1998)
  37. 10.1016/S0959-440X(97)80006-1 / Curr. Opin. Struct. Biol / Chaperonin-assisted protein folding by Martin (1997)
  38. 10.1016/S0022-2836(65)80285-6 / J. Mol. Biol / On the nature of allosteric transitions by Monod (1965)
  39. 10.1074/jbc.271.45.28229 / J. Biol. Chem / GroEL locked in a closed conformation by an interdomain cross-link can bind ATP and polypeptide but cannot process further reaction steps by Murai (1996)
  40. 10.1063/1.472061 / J. Chem. Phys / Simulation of activation free energies in molecular systems by Neria (1996)
  41. 10.1006/jmbi.1997.1180 / J. Mol. Biol / Tension in haemoglobin revealed by Fe-His (F8) bond rupture in the fully liganded T-state by Paoli (1997)
  42. 10.1038/372646a0 / Nature / Conformation of GroEL-bound α-lactalbumin probed by mass spectrometry by Robinson (1994)
  43. 10.1016/S0076-6879(98)90026-X / Methods Enzymol / Probing conformations of GroEL-bound substrate proteins by mass spectroscopy by Robinson (1998)
  44. 10.1016/S0092-8674(00)81342-2 / Cell / The chaperonin ATPase cycle by Roseman (1996)
  45. 10.1016/0021-9991(77)90098-5 / J. Comput. Phys / Numerical integration of the cartesian equations of motion of a system with constraints by Ryckaert (1977)
  46. 10.1038/42047 / Nature / Distinct actions of cis and trans ATP within the double ring of the chaperonin GroEL by Rye (1997)
  47. 10.1016/S0092-8674(00)80742-4 / Cell / GroEL-GroES cycling ATP and nonnative polypeptide direct alternation of folding-active rings by Rye (1999)
  48. 10.1080/08927029308022170 / Mol. Sim / Targeted molecular dynamics simulation of conformational change by Schlitter (1993)
  49. 10.1126/science.284.5415.822 / Science / Chaperonin function by Shtilerman (1999)
  50. 10.1146/annurev.biochem.67.1.581 / Annu. Rev. Biochem / Structure and function in GroEL-mediated protein folding by Sigler (1998)
  51. 10.1042/bj3000651 / Biochem. J / Affinity of chaperonin-60 for a protein substrate and its modulation by nucleotides and chaperonin-10 by Staniforth (1994)
  52. 10.1021/bi00084a024 / Biochemistry / Hydrolysis of adenosine 5′-triphosphate by Escherichia coli GroEL by Todd (1993)
  53. 10.1021/bi00476a003 / Biochemistry / Chaperonin-facilitated refolding of ribulosebisphosphate carboxylase and ATP hydrolysis by chaperonin 60 (GroEL) are K+ dependent by Viitanen (1990)
  54. 10.1038/14918 / Nature Struct Biol / Thinking outside the box by Wang (1999)
  55. 10.1038/nsb0997-690 / Nature Struct. Biol / Structural basis of allosteric changes in the GroEL mutant Arg197→Ala by White (1997)
  56. 10.1006/jsbi.1998.4060 / J. Struct. Biol / GroEL/GroES by Xu (1998)
  57. 10.1038/41944 / Nature / The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex by Xu (1997)
  58. 10.1006/jmbi.1994.1667 / J. Mol. Biol / Two lines of allosteric communication in the oligomeric chaperonin GroEL are revealed by the single mutation Arg196 to Ala by Yifrach (1994)
  59. 10.1021/bi00016a001 / Biochemistry / Nested cooperativity in the ATPase activity of the oligomeric chaperonin GroEL by Yifrach (1995)
  60. 10.1021/ja983136u / J. Am. Chem. Soc / Mapping the transition state of the allosteric pathway of GroEL by protein engineering by Yifrach (1998)
  61. 10.1021/bi980370o / Biochemistry / Transient kinetic analysis of adenosine 5′-Triphosphate binding-induced conformational changes in the allosteric chaperonin GroEL by Yifrach (1998)
Dates
Type When
Created 22 years, 11 months ago (Sept. 18, 2002, 3:24 p.m.)
Deposited 4 years, 3 months ago (May 2, 2021, 9:39 p.m.)
Indexed 2 months ago (June 24, 2025, 12:06 p.m.)
Issued 24 years, 11 months ago (Sept. 1, 2000)
Published 24 years, 11 months ago (Sept. 1, 2000)
Published Print 24 years, 11 months ago (Sept. 1, 2000)
Funders 0

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@article{Ma_2000, title={A dynamic model for the allosteric mechanism of GroEL 1 1Edited by A. Fersht}, volume={302}, ISSN={0022-2836}, url={http://dx.doi.org/10.1006/jmbi.2000.4014}, DOI={10.1006/jmbi.2000.4014}, number={2}, journal={Journal of Molecular Biology}, publisher={Elsevier BV}, author={Ma, Jianpeng and Sigler, Paul B and Xu, Zhaohui and Karplus, Martin}, year={2000}, month=sep, pages={303–313} }