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

Cysteines 208 and 241 in Ero1α are required for maximal catalytic turnover.

Redox biology - 1 Apr 2016

Ramming Thomas, Kanemura Shingo, Okumura Masaki, Inaba Kenji, Appenzeller-Herzog Christian

Abstract excerpt

Endoplasmic reticulum (ER) oxidoreductin 1α (Ero1α) is a disulfide producer in the ER of mammalian cells. Besides four catalytic cysteines (Cys(94), Cys(99), Cys(394), Cys(397)), Ero1α harbors four regulatory cysteines (Cys(104), Cys(131), Cys(208), Cys(241)). These cysteines mediate the formation of inhibitory intramolecular disulfide bonds, which adapt the activation state of the enzyme to the redox environment...

Read the complete abstract on PubMed

Topics

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

Share to Catalytic Domain
Share to Cysteine
Share to Disulfides

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Enzyme Stability

Share to HeLa Cells

Share to Membrane Glycoproteins

Share to Oxidation-Reduction

Share to Oxidoreductases

Source

Open in PubMed Open full text

Identifiers

PMID: 26609561
DOI: 10.1016/j.redox.2015.11.004
PMCID: PMC4683387

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

Cysteines 208 and 241 in Ero1α are required for maximal catalytic turnover.PMID 26609561Read ↗

Two conserved cysteine triads in human Ero1alpha cooperate for efficient disulfide bond formation in the endoplasmic reticulum.Semantic proximity Read ↗

Disulfide transfer between two conserved cysteine pairs imparts selectivity to protein oxidation by Ero1.Semantic proximity Read ↗

Domain architecture of protein-disulfide isomerase facilitates its dual role as an oxidase and an isomerase in Ero1p-mediated disulfide formation.Semantic proximity Read ↗

Two pairs of conserved cysteines are required for the oxidative activity of Ero1p in protein disulfide bond formation in the endoplasmic reticulum.Semantic proximity Read ↗

Steps in reductive activation of the disulfide-generating enzyme Ero1p.Semantic proximity Read ↗

Manipulation of oxidative protein folding and PDI redox state in mammalian cells.Semantic proximity Read ↗

Ero1p oxidizes protein disulfide isomerase in a pathway for disulfide bond formation in the endoplasmic reticulum.Semantic proximity Read ↗

Deciphering structural and functional roles of individual disulfide bonds of the mitochondrial sulfhydryl oxidase Erv1p.Semantic proximity Read ↗

Glutathione is required to regulate the formation of native disulfide bonds within proteins entering the secretory pathway.Semantic proximity Read ↗

PRDX4, an endoplasmic reticulum-localized peroxiredoxin at the crossroads between enzymatic oxidative protein folding and nonenzymatic protein oxidation.Semantic proximity Read ↗

Dynamic regulation of Ero1α and peroxiredoxin 4 localization in the secretory pathway.Semantic proximity Read ↗

Oxidative activity of yeast Ero1p on protein disulfide isomerase and related oxidoreductases of the endoplasmic reticulum.Semantic proximity Read ↗

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