DOI: 10.1016/s0092-8674(01)00523-2. GroEL/GroES-Mediated Folding of a Protein Too Large to Be Encapsulated

GroEL/GroES-Mediated Folding of a Protein Too Large to Be Encapsulated

10.1016/s0092-8674(01)00523-2

Crossref journal-article

Elsevier BV

Cell (78)

Bibliography

Chaudhuri, T. K., Farr, G. W., Fenton, W. A., Rospert, S., & Horwich, A. L. (2001). GroEL/GroES-Mediated Folding of a Protein Too Large to Be Encapsulated. Cell, 107(2), 235â246.

Authors 5

Tapan K. Chaudhuri (first)
George W. Farr (additional)
Wayne A. Fenton (additional)
Sabine Rospert (additional)
Arthur L. Horwich (additional)

References 38 Referenced 150

10.1006/jmbi.2000.3648 / J. Mol. Biol. / A thermodynamic coupling mechanism can explain the GroEL-mediated acceleration of the folding of barstar by Bhutani (2000)
10.1016/S0021-9258(18)53840-0 / J. Biol. Chem. / Interactions of phage P22 tailspike protein with GroE molecular chaperones during refolding in vitro by Brunschier (1993)
10.1038/383096a0 / Nature / Release of both native and non-native proteins from a cis-only GroEL ternary complex by Burston (1996)
10.1074/jbc.274.15.10395 / J. Biol. Chem. / GroEL/GroES-dependent reconstitution of α2β2 tetramers of human mitochondrial branched chain α-ketoacid decarboxylase by Chuang (1999)
10.1006/jmbi.1998.2403 / J. Mol. Biol. / The chaperonin GroEL binds to late-folding non-native conformations present in native Escherichia coli and murine dihydrofolate reductases by Clark (1999)
10.1038/10735 / Nat. Struct. Biol. / GroEL accelerates the refolding of hen lysozyme without changing its folding mechanism by Coyle (1999)
10.1093/emboj/17.20.5868 / EMBO J. / Identification of in vivo substrates of the yeast mitochondrial chaperonins reveals overlapping but non-identical requirement for hsp60 and hsp10 by Dubaquié (1998)
10.1016/S0092-8674(00)80509-7 / Cell / In vivo observation of polypeptide flux through the bacterial chaperonin system by Ewalt (1997)
10.1016/S0092-8674(00)80692-3 / Cell / Multivalent binding of nonnative substrate protein by the chaperonin GroEL by Farr (2000)
10.1016/S0092-8674(00)81557-3 / Cell / GroEL-substrate interactions by Feltham (2000)
10.1038/342884a0 / Nature / Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfolded state depends on two chaperonin proteins and MgATP by Goloubinoff (1989)
10.1016/S0021-9258(18)46878-0 / J. Biol. Chem. / Selective in vivo rescue by GroEL/ES of thermolabile folding intermediates to phage P22 structural protein by Gordon (1994)
10.1016/S0959-440X(98)80015-8 / Curr. Opin. Struct. Biol. / Structural aspects of GroEL function by Horovitz (1998)
10.1038/45977 / Nature / Identification of in vivo substrates of the chaperonin GroEL by Houry (1999)
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)
10.1046/j.1432-1327.2001.02130.x / Eur. J. Biochem. / GroEL-assisted refolding of adrenodoxin during chemical cluster insertion by Iametti (2001)
10.1016/S0021-9258(18)68461-3 / J. Biol. Chem. / The state of cluster SH and S2− of aconitase during cluster interconversions and removal by Kennedy (1988)
10.1016/S0021-9258(18)88861-5 / J. Biol. Chem. / Mössbauer studies of aconitase by Kent (1985)
10.1021/bi00125a014 / Biochemistry / Crystal structures of aconitase with isocitrate and nitroisocitrate bound by Lauble (1992)
10.1038/352036a0 / Nature / Chaperonin-mediated protein folding at the surface of groEL through a “molten globule”-like intermediate by Martin (1991)
10.1042/bj0580685 / Biochem. J. / The activation of aconitase by ferrous ions and reducing agents by Morrison (1954)
10.1006/jmbi.1995.0399 / J. Mol. Biol. / Chaperonins can catalyze the reversal of early aggregation steps when a protein misfolds by Ranson (1995)
10.1006/jmbi.1996.0815 / J. Mol. Biol. / Binding, encapsulation, and ejection by Ranson (1997)
10.1073/pnas.101119498 / Proc. Natl. Acad. Sci. USA / The chaperone GroEL is required for the final assembly of the molybdenum-iron protein of nitrogenase by Ribbe (2001)
10.1016/S0092-8674(00)81342-2 / Cell / The chaperonin ATPase cycle by Roseman (1996)
10.1038/42047 / Nature / Distinct actions of cis and trans ATP within the double ring of the chaperonin GroEL by Rye (1997)
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10.1146/annurev.biochem.67.1.581 / Annu. Rev. Biochem. / Structure and function in GroEL-mediated protein folding by Sigler (1998)
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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, 4 months ago (April 15, 2004, 5:36 a.m.)
Deposited	4 years, 2 months ago (June 15, 2021, 12:29 p.m.)
Indexed	3 weeks, 6 days ago (July 30, 2025, 10:08 a.m.)
Issued	23 years, 10 months ago (Oct. 1, 2001)
Published	23 years, 10 months ago (Oct. 1, 2001)
Published Print	23 years, 10 months ago (Oct. 1, 2001)

Funders 0

None

BibTeX

@article{Chaudhuri_2001, title={GroEL/GroES-Mediated Folding of a Protein Too Large to Be Encapsulated}, volume={107}, ISSN={0092-8674}, url={http://dx.doi.org/10.1016/s0092-8674(01)00523-2}, DOI={10.1016/s0092-8674(01)00523-2}, number={2}, journal={Cell}, publisher={Elsevier BV}, author={Chaudhuri, Tapan K. and Farr, George W. and Fenton, Wayne A. and Rospert, Sabine and Horwich, Arthur L.}, year={2001}, month=oct, pages={235–246} }

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