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

Tight hydrophobic contacts with the SecB chaperone prevent folding of substrate proteins.

Biochemistry - 23 Mar 2010

Bechtluft Philipp, Kedrov Alexej, Slotboom Dirk-Jan, Nouwen Nico, Tans Sander J, Driessen Arnold J M

Abstract excerpt

The molecular chaperone SecB binds to hydrophobic sections of unfolded secretory proteins and thereby prevents their premature folding prior to secretion by the translocase of Escherichia coli. Here, we have investigated the effect of the single-residue mutation of leucine 42 to arginine (L42R) c...

Read the complete abstract on PubMed

Topics

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

Share to Hydrophobic and Hydrophilic Interactions
Share to Maltose-Binding Proteins
Share to Molecular Chaperones

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Periplasmic Binding Proteins

Share to Protein Precursors

Share to Protein Structure, Quaternary

Share to SEC Translocation Channels

Share to SecA Proteins

Source

Identifiers

PMID: 20146530
DOI: 10.1021/bi902051e

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-20146530-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Tight hydrophobic contacts with the SecB chaperone prevent folding of substrate proteins.PMID 20146530Read ↗

Characterization of three areas of interactions stabilizing complexes between SecA and SecB, two proteins involved in protein export.Semantic proximity Read ↗

Two alternative binding mechanisms connect the protein translocation Sec71-Sec72 complex with heat shock proteins.Semantic proximity Read ↗

Quaternary dynamics of the SecA motor drive translocase catalysis.Semantic proximity Read ↗

Mutations of the molecular chaperone protein SecB which alter the interaction between SecB and maltose-binding protein.Semantic proximity Read ↗

Dynamic action of the Sec machinery during initiation, protein translocation and termination.Semantic proximity Read ↗

Directed evolution of SecB chaperones toward toxin-antitoxin systems.Semantic proximity Read ↗

Kinetics and energetics of the translocation of maltose binding protein folding mutants.Semantic proximity Read ↗

Dynamics of SecY translocons with translocation-defective mutations.Semantic proximity Read ↗

The molecular mechanisms underlying BiP-mediated gating of the Sec61 translocon of the endoplasmic reticulum.Semantic proximity Read ↗

Interaction of SecB with intermediates along the folding pathway of maltose-binding protein.Semantic proximity Read ↗

A large conformational change couples the ATP binding site of SecA to the SecY protein channel.Semantic proximity Read ↗

Protein translocation functions of Escherichia coli SecY: in vitro characterization of cold-sensitive secY mutants.Semantic proximity Read ↗

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