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

Nonconsecutive disulfide bond formation in an essential integral outer membrane protein.

Proceedings of the National Academy of Sciences of the United States of America - 6 Jul 2010

Ruiz Natividad, Chng Shu-Sin, Hiniker Annie, Kahne Daniel, Silhavy Thomas J

Abstract excerpt

The Gram-negative bacterial envelope is bounded by two membranes. Disulfide bond formation and isomerization in this oxidizing environment are catalyzed by DsbA and DsbC, respectively. It remains unknown when and how the Dsb proteins participate in the biogenesis of outer membrane proteins, which are transported across the cell envelope after their synthesis. The Escherichia coli protein LptD is an integral outer...

Read the complete abstract on PubMed

Topics

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

Share to Bacterial Outer Membrane Proteins
Share to Cysteine

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Disulfides

Share to Electrophoresis, Polyacrylamide Gel

Share to Escherichia coli Proteins

Share to Immunoblotting

Share to Oxidation-Reduction

Share to Protein Disulfide-Isomerases

Source

Open in PubMed Open full text

Identifiers

PMID: 20566849
DOI: 10.1073/pnas.1007319107
PMCID: PMC2901483

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Nonconsecutive disulfide bond formation in an essential integral outer membrane protein.PMID 20566849Read ↗

The protein-disulfide isomerase DsbC cooperates with SurA and DsbA in the assembly of the essential β-barrel protein LptD.Semantic proximity Read ↗

The disulphide isomerase DsbC cooperates with the oxidase DsbA in a DsbD-independent manner.Semantic proximity Read ↗

Transmembrane electron transfer by the membrane protein DsbD occurs via a disulfide bond cascade.Semantic proximity Read ↗

Six conserved cysteines of the membrane protein DsbD are required for the transfer of electrons from the cytoplasm to the periplasm of Escherichia coli.Semantic proximity Read ↗

Legionella pneumophila utilizes a single-player disulfide-bond oxidoreductase system to manage disulfide bond formation and isomerization.Semantic proximity Read ↗

An in vivo pathway for disulfide bond isomerization in Escherichia coli.Semantic proximity Read ↗

Reduction of the periplasmic disulfide bond isomerase, DsbC, occurs by passage of electrons from cytoplasmic thioredoxin.Semantic proximity Read ↗

Functional analysis of paralogous thiol-disulfide oxidoreductases in Bacillus subtilis.Semantic proximity Read ↗

Engineered pathways for correct disulfide bond oxidation.Semantic proximity Read ↗

Respiratory chain strongly oxidizes the CXXC motif of DsbB in the Escherichia coli disulfide bond formation pathway.Semantic proximity Read ↗

Identification and characterization of a new disulfide isomerase-like protein (DsbD) in Escherichia coli.Semantic proximity Read ↗

Staphylococcus aureus DsbA Does Not Have a Destabilizing DisulfideSemantic proximity Read ↗

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