Crossref journal-article
Elsevier BV
Biophysical Journal (78)
Bibliography

van der Vaart, A., Ma, J., & Karplus, M. (2004). The Unfolding Action of GroEL on a Protein Substrate. Biophysical Journal, 87(1), 562–573.

Authors 3
  1. Arjan van der Vaart (first)
  2. Jianpeng Ma (additional)
  3. Martin Karplus (additional)
References 56 Referenced 46
  1. 10.1126/science.181.4096.223 / Science / Principles that govern the folding of protein chains by Anfinsen (1973)
  2. 10.1006/jmbi.1999.2591 / J. Mol. Biol. / Exploring the kinetic requirements for enhancement of protein folding rates in the GroEL cavity by Betancourt (1999)
  3. {'key': '10.1529/biophysj.103.037333_bib3', 'first-page': '198', 'article-title': 'Nanoseconds molecular dynamics simulation of primary mechanical energy transfer steps in F1-ATP synthase', 'volume': '9', 'author': 'Böckmann', 'year': '2002', 'journal-title': 'Nat. Struct. Biol.'} / Nat. Struct. Biol. / Nanoseconds molecular dynamics simulation of primary mechanical energy transfer steps in F1-ATP synthase by Böckmann (2002)
  4. 10.1038/nsb0296-170 / Nat. Struct. Biol. / The 2.4Å crystal structure of the bacterial chaperonin GroEL complexed with ATPγS by Boisvert (1996)
  5. 10.1016/S0092-8674(01)00517-7 / Cell. / Dual function of protein confinement in chaperonin-assisted protein folding by Brinker (2001)
  6. 10.1002/prot.10139 / Proteins / Stability of macromolecular complexes by Brooijmans (2002)
  7. 10.1002/jcc.540040211 / J. Comput. Chem. / CHARMM: A program for macromolecular energy minimization and dynamics calculations by Brooks (1983)
  8. 10.1073/pnas.94.8.3571 / Proc. Natl. Acad. Sci. USA / A structural model for GroEL-polypeptide recognition by Buckle (1997)
  9. 10.1002/(SICI)1097-0134(199603)24:3<345::AID-PROT7>3.0.CO;2-F / Proteins / A simple model of chaperonin-mediated protein folding by Chan (1996)
  10. 10.1016/S0092-8674(01)00523-2 / Cell. / GroEL/GroES-mediated folding of a protein too large to be encapsulated by Chaudhuri (2001)
  11. 10.1038/90443 / Nat. Struct. Biol. / Folding of malate dehydrogenase inside the GroEL-GroES cavity by Chen (2001)
  12. 10.1016/S0092-8674(00)81673-6 / Cell. / The crystal structure of a GroEL/peptide complex: Plasticity as a basis for substrate diversity by Chen (1999)
  13. 10.1038/371261a0 / Nature / Location of a folding protein and shape changes in GroEL-GroES complexes imaged by cryo-electron microscopy by Chen (1994)
  14. 10.1038/418729a / Nature / Getting out of shape by Dobson (2002)
  15. 10.1016/S0959-440X(99)80013-X / Curr. Opin. Struct. Biol. / Principles of protein folding in the cellular environment by Ellis (1999)
  16. 10.1016/S0092-8674(00)80692-3 / Cell. / Multivalent binding of nonnative substrate proteins by the chaperonin GroEL by Farr (2000)
  17. 10.1038/371614a0 / Nature / Residues in chaperonin GroEL required for polypeptide binding and release by Fenton (1994)
  18. 10.1074/jbc.271.35.21054 / J. Biol. Chem. / Active site structural features for chemically modified forms of rhodanese by Gliubich (1996)
  19. 10.1006/jsbi.2001.4387 / J. Struct. Biol. / Review: A structural view of the GroE chaperone cycle by Grallert (2001)
  20. 10.1002/pro.5560051213 / Prot. Science / Significant hydrogen exchange protection in GroEL-bound DHFR is maintained during iterative rounds of substrate cycling by Groβ (1996)
  21. 10.1074/jbc.M010858200 / J. Biol. Chem. / Protein compactness measured by fluorescence resonance energy transfer by Hammarström (2001)
  22. 10.1074/jbc.M000649200 / J. Biol. Chem. / Protein substrate binding induces conformational changes in the chaperonin GroEL by Hammarström (2000)
  23. 10.1038/381571a0 / Nature / Molecular chaperones in cellular protein folding by Hartl (1996)
  24. 10.1038/45977 / Nature / Identification of in vivo substrates of the chaperonin GroEL by Houry (1999)
  25. 10.1016/0263-7855(96)00018-5 / J. Mol. Graph. / VMD - Visual molecular dynamics by Humphrey (1996)
  26. 10.1016/S0022-2836(03)00087-1 / J. Mol. Biol. / Equilibrium and kinetics of the allosteric transition of GroEL studied by solution X-ray scattering and fluorescence spectroscopy by Inobe (2003)
  27. 10.1016/S0167-4838(00)00274-0 / Biochim. Biophys. Acta / Nucleotide binding to the chaperonin GroEL: non-cooperative binding of ATP analogs and ADP, and cooperative effect of ATP by Inobe (2001)
  28. 10.1002/(SICI)1097-0134(19990501)35:2<133::AID-PROT1>3.0.CO;2-N / Proteins / Effective energy function for proteins in solution by Lazaridis (1999)
  29. 10.1016/0022-2836(71)90324-X / J. Mol. Biol. / The interpretation of protein structures: Estimation of static accessibility by Lee (1971)
  30. 10.1006/jsbi.1996.3832 / J. Struct. Biol. / Conformational changes in the GroEL oligomer during the functional cycle by Llorca (1997)
  31. 10.1073/pnas.95.15.8502 / Proc. Natl. Acad. Sci. USA / The allosteric mechanism of the chaperonin GroEL: A dynamic analysis by Ma (1998)
  32. 10.1006/jmbi.2000.4014 / J. Mol. Biol. / A dynamic model for the allosteric mechanism of GroEL by Ma (2000)
  33. 10.1016/S0092-8674(01)00617-1 / Cell. / ATP-bound states of GroEL captured by cryo-electron microscopy by Ranson (2001)
  34. 10.1016/S0092-8674(00)81342-2 / Cell. / The chaperonin ATPase cycle: Mechanism of allosteric switching and movements of substrate-binding domains in GroEL by Roseman (1996)
  35. 10.1016/0021-9991(77)90098-5 / J. Comput. Phys. / Numerical integration of the Cartesian equations of motion of a system with constraints: Molecular dynamics of n-alkanes by Ryckaert (1977)
  36. 10.1038/42047 / Nature / Distinct actions of cis and trans ATP within the double ring of the chaperonin GroEL by Rye (1997)
  37. 10.1016/S0092-8674(00)80742-4 / Cell. / GroEL-GroES cycling: ATP and nonnative polypeptide direct alternation of folding-active rings by Rye (1999)
  38. 10.1016/S0959-440X(00)00074-9 / Curr. Opin. Struct. Biol. / Molecular chaperones: Containers and surfaces for folding, stabilising or unfolding proteins by Saibil (2000)
  39. {'key': '10.1529/biophysj.103.037333_bib39', 'first-page': '45', 'article-title': 'Allostery and protein substrate conformational change during GroEL/GroES-mediated protein folding', 'volume': '59', 'author': 'Saibil', 'year': '2002', 'journal-title': 'Adv. Prot. Chem.'} / Adv. Prot. Chem. / Allostery and protein substrate conformational change during GroEL/GroES-mediated protein folding by Saibil (2002)
  40. 10.1080/08927029308022170 / Mol. Simulat. / Targeted molecular dynamics simulation of conformational change-application to the T↔R transition in insulin by Schlitter (1993)
  41. 10.1021/bi952033a / Biochemistry / Simulations of chaperone-assisted folding by Sfatos (1996)
  42. 10.1126/science.284.5415.822 / Science / Chaperonin function: Folding by forced unfolding by Shtilerman (1999)
  43. 10.1016/S0301-4622(02)00298-3 / Biophys. Chem. / Annealing function of GroEL: Structural and bioinformatic analysis by Stan (2003)
  44. 10.1146/annurev.biophys.30.1.245 / Annu. Rev. Biophys. Biomol. Struct. / Chaperonin-mediated protein folding by Thirumalai (2001)
  45. 10.1073/pnas.93.9.4030 / Proc. Natl. Acad. Sci. USA / Chaperonin-facilitated protein folding: Optimization of rate and yield by an iterative annealing mechanism by Todd (1996)
  46. 10.1126/science.7913555 / Science / Dynamics of the chaperonin ATPase cycle: Implications for facilitated protein folding by Todd (1994)
  47. 10.1002/jmr.597 / J. Mol. Recognit. / Protein-protein interactions: Mechanisms and modification by drugs by Veselovsky (2002)
  48. 10.1073/pnas.93.18.9425 / Proc. Natl. Acad. Sci. USA / A thermodynamic coupling mechanism for GroEL-mediated unfolding by Walter (1996)
  49. 10.1016/S0022-2836(03)00184-0 / J. Mol. Biol. / Structural basis for GroEL-assisted protein folding from the crystal structure of (GroEL-KMgATP)14 at 2.0Å resolution by Wang (2003)
  50. 10.1016/0092-8674(94)90533-9 / Cell. / GroEL-mediated protein folding proceeds by multiple rounds of binding and release of nonnative forms by Weissman (1994)
  51. 10.1016/S0092-8674(00)81293-3 / Cell. / Characterization of the active intermediate of a GroEL-GroES-mediated protein folding reaction by Weissman (1996)
  52. 10.1038/41944 / Nature / The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex by Xu (1997)
  53. 10.1073/pnas.0337432100 / Proc. Natl. Acad. Sci. USA / The missing link between thermodynamics and structure in F1-ATPase by Yang (2003)
  54. 10.1006/jmbi.1996.0028 / J. Mol. Biol. / Allosteric control by ATP of non-folded protein binding to GroEL by Yifrach (1996)
  55. 10.1006/jmbi.1996.0440 / J. Mol. Biol. / Conformational states bound by the molecular chaperones GroEL and SecB: A hidden unfolding (annealing) activity by Zahn (1996)
  56. 10.1126/science.271.5249.642 / Science / Catalysis of amide proton exchange by the molecular chaperones GroEL and SecB by Zahn (1996)
Dates
Type When
Created 21 years, 2 months ago (July 6, 2004, 9:29 p.m.)
Deposited 2 years, 7 months ago (Jan. 25, 2023, 8:22 a.m.)
Indexed 1 year ago (Aug. 12, 2024, 9:12 a.m.)
Issued 21 years, 2 months ago (July 1, 2004)
Published 21 years, 2 months ago (July 1, 2004)
Published Print 21 years, 2 months ago (July 1, 2004)
Funders 0

None

@article{van_der_Vaart_2004, title={The Unfolding Action of GroEL on a Protein Substrate}, volume={87}, ISSN={0006-3495}, url={http://dx.doi.org/10.1529/biophysj.103.037333}, DOI={10.1529/biophysj.103.037333}, number={1}, journal={Biophysical Journal}, publisher={Elsevier BV}, author={van der Vaart, Arjan and Ma, Jianpeng and Karplus, Martin}, year={2004}, month=jul, pages={562–573} }