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Article

Characterization of the active intermediate of a GroEL-GroES-mediated protein folding reaction.

Cell - 9 Feb 1996

Weissman J S, Rye H S, Fenton W A, Beechem J M, Horwich A L

Abstract excerpt

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. Stoppe...

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Identifiers

PMID: 8608602
DOI: 10.1016/s0092-8674(00)81293-3

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026. Prepared record publication-8608602-2026-09-04.2. Manifest publication-graph-cohort-2026-09-04.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 4 Sept 2026.

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Characterization of the active intermediate of a GroEL-GroES-mediated protein folding reaction.PMID 8608602Read ↗

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Active cage mechanism of chaperonin-assisted protein folding demonstrated at single-molecule level.Semantic proximity Read ↗

A dynamic model of long-range conformational adaptations triggered by nucleotide binding in GroEL-GroES.Semantic proximity Read ↗

Characterisation of a GroEL single-ring mutant that supports growth of Escherichia coli and has GroES-dependent ATPase activity.Semantic proximity Read ↗

Dynamics of the GroEL-protein complex: effects of nucleotides and folding mutants.Semantic proximity Read ↗

Stimulating the substrate folding activity of a single ring GroEL variant by modulating the cochaperonin GroES.Semantic proximity Read ↗

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