Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Interaction of trigger factor with the ribosome.

Journal of molecular biology - 14 Feb 2003

Maier Raimund, Eckert Barbara, Scholz Christian, Lilie Hauke, Schmid Franz-Xaver

Abstract excerpt

The trigger factor of Escherichia coli is a prolyl isomerase and a chaperone. It interacts with the ribosome and affects the folding of newly formed protein chains. Therefore, the dynamics of the interactions of trigger factor with the ribosome and with unfolded protein chains should be tailored for this function. Previously, we had found that binding of unfolded proteins to trigger factor is fast and that the...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to 2-Naphthylamine
Share to Binding, Competitive
Share to Fluorescence

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Isomerism

Share to Peptidylprolyl Isomerase

Share to Proline

Share to Ribosomes

Share to Ultracentrifugation

Source

Identifiers

PMID: 12559924
DOI: 10.1016/s0022-2836(02)01427-4

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Interaction of trigger factor with the ribosome.PMID 12559924Read ↗

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

Structure and function of the molecular chaperone 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 ↗

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 ↗

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

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 ↗

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

Structural rearrangements and the unfolding mechanism of a Trigger Factor mutant studied by multiple structural probes.Semantic proximity Read ↗

Spatial Distribution and Ribosome-Binding Dynamics of EF-P in Live Escherichia coli.Semantic proximity Read ↗

Multi-Channel smFRET study reveals a Compact conformation of EF-G on the RibosomeSemantic proximity Read ↗

Preparation of ribosomes for smFRET studies: A simplified approach.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.