Crossref journal-article
Elsevier BV
Structure (78)
Bibliography

Chen, D.-H., Song, J.-L., Chuang, D. T., Chiu, W., & Ludtke, S. J. (2006). An Expanded Conformation of Single-Ring GroEL-GroES Complex Encapsulates an 86 kDa Substrate. Structure, 14(11), 1711–1722.

Authors 5
  1. Dong-Hua Chen (first)
  2. Jiu-Li Song (additional)
  3. David T. Chuang (additional)
  4. Wah Chiu (additional)
  5. Steven J. Ludtke (additional)
References 46 Referenced 55
  1. 10.1038/386088a0 / Nature / Determination of the fold of the core protein of hepatitis B virus by electron cryomicroscopy by Böttcher (1997)
  2. 10.1038/371578a0 / Nature / The crystal structure of the bacterial chaperonin GroEL at 2.8 A by Braig (1994)
  3. 10.1016/j.str.2004.01.015 / Structure / Experimental verification of conformational variation of human fatty acid synthase as predicted by normal mode analysis by Brink (2004)
  4. 10.1016/S0092-8674(01)00517-7 / Cell / Dual function of protein confinement in chaperonin-assisted protein folding by Brinker (2001)
  5. 10.1016/S0092-8674(01)00523-2 / Cell / GroEL/GroES-mediated folding of a protein too large to be encapsulated by Chaudhuri (2001)
  6. 10.1038/371261a0 / Nature / Location of a folding protein and shape changes in GroEL-GroES complexes imaged by cryo-electron microscopy by Chen (1994)
  7. 10.1074/jbc.274.15.10395 / J. Biol. Chem. / GroEL/GroES-dependent reconstitution of α2β2 tetramers of human mitochondrial branched-chain α-ketoacid decarboxylase. Obligatory interaction of chaperonins with an αβ dimeric intermediate by Chuang (1999)
  8. 10.1016/j.str.2006.05.014 / Structure / An expanded and flexible form of the vacuolar ATPase membrane sector by Clare (2006)
  9. 10.1146/annurev.bi.60.070191.001541 / Annu. Rev. Biochem. / Molecular chaperones by Ellis (1991)
  10. 10.1016/S0092-8674(00)80509-7 / Cell / In vivo observation of polypeptide flux through the bacterial chaperonin system by Ewalt (1997)
  11. 10.1006/jsbi.2001.4354 / J. Struct. Biol. / Classification and reconstruction of a heterogeneous set of electron microscopic images: a case study of GroEL-substrate complexes by Falke (2001)
  12. 10.1006/jmbi.2001.4613 / J. Mol. Biol. / Structural changes in GroEL effected by binding a denatured protein substrate by Falke (2001)
  13. 10.1016/j.jmb.2005.02.027 / J. Mol. Biol. / The 13 angstroms structure of a chaperonin GroEL-protein substrate complex by cryo-electron microscopy by Falke (2005)
  14. 10.1017/S0033583503003883 / Q. Rev. Biophys. / Chaperonin-mediated protein folding: fate of substrate polypeptide by Fenton (2003)
  15. {'key': '10.1016/j.str.2006.09.010_bib15', 'series-title': 'Three Dimensional Electron Microscopy', 'first-page': '145', 'article-title': 'Chapter 2', 'author': 'Frank', 'year': '2006'} / Three Dimensional Electron Microscopy / Chapter 2 by Frank (2006)
  16. 10.1016/j.str.2005.01.006 / Structure / Software extensions to UCSF chimera for interactive visualization of large molecular assemblies by Goddard (2005)
  17. 10.1016/0022-2836(79)90502-3 / J. Mol. Biol. / Purification and properties of groE, a host protein involved in bacteriophage assembly by Hendrix (1979)
  18. 10.1016/0022-2836(79)90501-1 / J. Mol. Biol. / Isolation and characterization of the host protein groE involved in bacteriophage lambda assembly by Hohn (1979)
  19. 10.1016/S0076-6879(98)90013-1 / Methods Enzymol. / Construction of single-ring and two-ring hybrid versions of bacterial chaperonin GroEL by Horwich (1998)
  20. 10.1021/cr040435v / Chem. Rev. / GroEL-GroES-mediated protein folding by Horwich (2006)
  21. 10.1038/45977 / Nature / Identification of in vivo substrates of the chaperonin GroEL by Houry (1999)
  22. 10.1074/jbc.274.15.10405 / J. Biol. Chem. / Mechanisms for GroEL/GroES-mediated folding of a large 86-kDa fusion polypeptide in vitro by Huang (1999)
  23. 10.1006/jmbi.2001.4633 / J. Mol. Biol. / Bridging the information gap: computational tools for intermediate resolution structure interpretation by Jiang (2001)
  24. 10.1016/S0022-2836(03)00555-2 / J. Mol. Biol. / Conformational flexibility of pyruvate dehydrogenase complexes: a computational analysis by quantized elastic deformational model by Kong (2003)
  25. 10.1006/jsbi.1999.4174 / J. Struct. Biol. / EMAN: semiautomated software for high-resolution single-particle reconstructions by Ludtke (1999)
  26. 10.1006/jmbi.2001.5133 / J. Mol. Biol. / A 11.5 Å single particle reconstruction of GroEL using EMAN by Ludtke (2001)
  27. 10.1016/j.str.2004.05.006 / Structure / Seeing GroEL at 6 Å resolution by single particle electron cryomicroscopy by Ludtke (2004)
  28. 10.1016/S0959-440X(97)80006-1 / Curr. Opin. Struct. Biol. / Chaperone-assisted protein folding by Martin (1997)
  29. 10.1073/pnas.0406132101 / Proc. Natl. Acad. Sci. USA / Substrate polypeptide presents a load on the apical domains of the chaperonin GroEL by Motojima (2004)
  30. 10.1016/S1097-2765(00)80117-3 / Mol. Cell / A single ring is sufficient for productive chaperonin-mediated folding in vivo by Nielsen (1998)
  31. 10.1128/JB.181.18.5871-5875.1999 / J. Bacteriol. / A single-ring mitochondrial chaperonin (Hsp60-Hsp10) can substitute for GroEL-GroES in vivo by Nielsen (1999)
  32. 10.1016/S0092-8674(01)00617-1 / Cell / ATP-bound states of GroEL captured by cryo-electron microscopy by Ranson (2001)
  33. 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)
  34. 10.1038/42047 / Nature / Distinct actions of cis and trans ATP within the double ring of the chaperonin GroEL by Rye (1997)
  35. 10.1016/S0092-8674(00)80742-4 / Cell / GroEL-GroES cycling: ATP and nonnative polypeptide direct alternation of folding-active rings by Rye (1999)
  36. 10.1074/jbc.274.30.21251 / J. Biol. Chem. / On the maximum size of proteins to stay and fold in the cavity of GroEL underneath GroES by Sakikawa (1999)
  37. 10.1146/annurev.biochem.67.1.581 / Annu. Rev. Biochem. / Structure and function in GroEL-mediated protein folding by Sigler (1998)
  38. 10.1074/jbc.M002038200 / J. Biol. Chem. / Interactions of GroEL/GroES with a heterodimeric intermediate during α2β2 assembly of mitochondrial branched-chain α-ketoacid dehydrogenase. cis capping of the native-like 86-kDa intermediate by GroES by Song (2000)
  39. 10.1074/jbc.M209705200 / J. Biol. Chem. / Encapsulation of an 86-kDa assembly intermediate inside the cavities of GroEL and its single-ring variant SR1 by GroES by Song (2003)
  40. 10.1016/j.cell.2006.04.027 / Cell / Structural features of the GroEL-GroES nano-cage required for rapid folding of encapsulated protein by Tang (2006)
  41. 10.1016/0304-3991(87)90010-6 / Ultramicroscopy / Similarity measures between images by van Heel (1987)
  42. 10.1016/S0021-9258(18)48338-X / J. Biol. Chem. / Mammalian mitochondrial chaperonin 60 functions as a single toroidal ring by Viitanen (1992)
  43. 10.1016/0092-8674(95)90098-5 / Cell / Mechanism of GroEL action: productive release of polypeptide from a sequestered position under GroES by Weissman (1995)
  44. 10.1074/jbc.275.4.2786 / J. Biol. Chem. / GroEL/GroES promote dissociation/reassociation cycles of a heterodimeric intermediate during alpha(2)beta(2) protein assembly. Iterative annealing at the quaternary structure level by Wynn (2000)
  45. 10.1038/41944 / Nature / The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex by Xu (1997)
  46. 10.1074/jbc.M101765200 / J. Biol. Chem. / Direct evidence for the size and conformational variability of the pyruvate dehydrogenase complex revealed by three-dimensional electron microscopy. The “breathing” core and its functional relationship to protein dynamics by Zhou (2001)
Dates
Type When
Created 18 years, 9 months ago (Nov. 15, 2006, 9:29 p.m.)
Deposited 1 year, 6 months ago (Feb. 10, 2024, 11:57 a.m.)
Indexed 4 days, 8 hours ago (Aug. 20, 2025, 9:07 a.m.)
Issued 18 years, 9 months ago (Nov. 1, 2006)
Published 18 years, 9 months ago (Nov. 1, 2006)
Published Print 18 years, 9 months ago (Nov. 1, 2006)
Funders 2
  1. National Institutes of Health 10.13039/100000002

    Region: Americas

    gov (National government)

    Labels3
    1. Institutos Nacionales de la Salud
    2. US National Institutes of Health
    3. NIH
    Awards4
    1. PN2EY016525
    2. P41RR02250
    3. DK26758
    4. P01GM064692
  2. Welch Foundation 10.13039/100000928

    Region: Americas

    pri (Trusts, charities, foundations (both public and private))

    Labels3
    1. The Welch Foundation
    2. Robert A. Welch Foundation
    3. The Robert A. Welch Foundation
    Awards1
    1. I-1286

@article{Chen_2006, title={An Expanded Conformation of Single-Ring GroEL-GroES Complex Encapsulates an 86 kDa Substrate}, volume={14}, ISSN={0969-2126}, url={http://dx.doi.org/10.1016/j.str.2006.09.010}, DOI={10.1016/j.str.2006.09.010}, number={11}, journal={Structure}, publisher={Elsevier BV}, author={Chen, Dong-Hua and Song, Jiu-Li and Chuang, David T. and Chiu, Wah and Ludtke, Steven J.}, year={2006}, month=nov, pages={1711–1722} }