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Cited by 395

The DOI matches its Crossref record; 24 of the 24 references it cites were found in a registry or an index.

Characterization of the Active Intermediate of a GroEL–GroES-Mediated Protein Folding Reaction

Open access
Weissman, Jonathan S, Rye, Hays S, Fenton, Wayne A, Beechem, Joseph M, Horwich, Arthur L·1996·Cell

Abstract

Recent studies of GroE-mediated protein folding indicate that substrate proteins are productively released from a cis ternary complex in which the nonnative substrate is sequestered within the GroEL channel underneath GroES. Here, we examine whether protein folding can occur in this space. Stopped-flow fluorescence anisotropy of a pyrene-rhodanese-GroEl complex indicates that addition of GroES and ATP (but not ADP) leads to a rapid change in substrate flexibility at GroEL. Strikingly, when GroES release is blocked by the use of either a nonhydrolyzable ATP analog or a single-ring GroEL mutant, substrates complete folding while remaining associated with chaperonin. We conclude that the cis ternary complex, in the presence of ATP, is the active state intermediate in the GroE-mediated folding reaction: folding is initiated in this state and for some substrates may be completed prior to the timed release of GroES triggered by ATP hydrolysis.

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Metadata

Authors
Weissman, J. S., Rye, H. S., Fenton, W. A., Beechem, J. M., & Horwich, A. L.
Venue
Cell
Publisher
Elsevier BV
Published
1996-02
Volume
84
Issue
3
Pages
481-490
ISSN
0092-8674 (ISSN-L)
OpenAlex
W1965255559
Cited by
395
References
24
FWCI
12.00
Type
journal article
Language
en
Open access
hybrid

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CoChat. (2026). Citation check: Characterization of the Active Intermediate of a GroEL–GroES-Mediated Protein Folding Reaction. https://app.cochat.ai/papers/10.1016/s0092-8674(00)81293-3
The paper
Weissman, J. S., Rye, H. S., Fenton, W. A., Beechem, J. M., & Horwich, A. L. (1996). Characterization of the Active Intermediate of a GroEL–GroES-Mediated Protein Folding Reaction. Cell. https://doi.org/10.1016/s0092-8674(00)81293-3

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