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Article

Structure and function of the molecular chaperone Trigger Factor.

Biochimica et biophysica acta - 1 Jun 2010

Hoffmann Anja, Bukau Bernd, Kramer Günter

Abstract excerpt

Newly synthesized proteins often require the assistance of molecular chaperones to efficiently fold into functional three-dimensional structures. At first, ribosome-associated chaperones guide the initial folding steps and protect growing polypeptide chains from misfolding and aggregation. After that folding into the native structure may occur spontaneously or require support by additional chaperones which do not...

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Source

Identifiers

PMID: 20132842
DOI: 10.1016/j.bbamcr.2010.01.017

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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Structure and function of the molecular chaperone Trigger Factor.PMID 20132842Read ↗

Trigger factor and DnaK cooperate in folding of newly synthesized proteins.Semantic proximity Read ↗

The C-terminal domain of Escherichia coli trigger factor represents the central module of its chaperone activity.Semantic proximity Read ↗

Identification of nascent chain interaction sites on trigger factor.Semantic proximity Read ↗

L23 protein functions as a chaperone docking site on the ribosome.Semantic proximity Read ↗

Functional dissection of Escherichia coli trigger factor: unraveling the function of individual domains.Semantic proximity Read ↗

PPIase domain of trigger factor acts as auxiliary chaperone site to assist the folding of protein substrates bound to the crevice of trigger factor.Semantic proximity Read ↗

Trigger factor lacking the PPIase domain can enhance the folding of eukaryotic multi-domain proteins in Escherichia coli.Semantic proximity Read ↗

Proteome-wide analysis of chaperonin-dependent protein folding in Escherichia coli.Semantic proximity Read ↗

Interaction of trigger factor with the ribosome.Semantic proximity Read ↗

Trigger factor is a bona fide secretory pathway chaperone that interacts with SecB and the translocaseSemantic proximity Read ↗

Chaperone-mediated assembly of the proteasome core particle – recent developments and structural insightsSemantic proximity Read ↗

Hold 'em and fold 'em: chaperones and signal transduction.Semantic proximity Read ↗

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