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

Inhibition of virulence-promoting disulfide bond formation enzyme DsbB is blocked by mutating residues in two distinct regions.

The Journal of biological chemistry - 21 Apr 2017

Landeta Cristina, Meehan Brian M, McPartland Laura, Ingendahl Linda, Hatahet Feras, Tran Ngoc Q, Boyd Dana, Beckwith Jon

Abstract excerpt

Disulfide bonds contribute to protein stability, activity, and folding in a variety of proteins, including many involved in bacterial virulence such as toxins, adhesins, flagella, and pili, among others. Therefore, inhibitors of disulfide bond formation enzymes could have profound effects on pathogen virulence. In the Escherichia coli disulfide bond formation pathway, the periplasmic protein DsbA introduces...

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 Disulfides

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

Share to Gene Library

Share to Lipopolysaccharides

Share to Protein Disulfide-Isomerases

Share to Pyridazines

Share to Quinones

Share to Spectrometry, Mass, Electrospray Ionization

Source

Open in PubMed Open full text

Identifiers

PMID: 28232484
DOI: 10.1074/jbc.M116.770891
PMCID: PMC5399105

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

Inhibition of virulence-promoting disulfide bond formation enzyme DsbB is blocked by mutating residues in two distinct regions.PMID 28232484Read ↗

Mutational analysis of the disulfide catalysts DsbA and DsbB.Semantic proximity Read ↗

Mutants in DsbB that appear to redirect oxidation through the disulfide isomerization pathway.Semantic proximity Read ↗

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

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

Converting a Sulfenic Acid Reductase into a Disulfide Bond Isomerase.Semantic proximity Read ↗

Virulence of the Melioidosis Pathogen Burkholderia pseudomallei Requires the Oxidoreductase Membrane Protein DsbBSemantic 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 ↗

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

Conversion of a catalytic into a structural disulfide bond by circular permutation.Semantic proximity Read ↗

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

Identification of a segment of DsbB essential for its respiration-coupled oxidation.Semantic proximity Read ↗

Roles of a conserved arginine residue of DsbB in linking protein disulfide-bond-formation pathway to the respiratory chain of Escherichia coli.Semantic proximity Read ↗

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