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

Two protein disulfide isomerase subgroups work synergistically in catalyzing oxidative protein folding.

Plant physiology - 20 Jan 2022

Fan Fenggui, Zhang Qiao, Zhang Yini, Huang Guozhong, Liang Xuelian, Wang Chih-Chen, Wang Lei, Lu Dongping

Abstract excerpt

Disulfide bonds play essential roles in the folding of secretory and plasma membrane proteins in the endoplasmic reticulum (ER). In eukaryotes, protein disulfide isomerase (PDI) is an enzyme catalyzing the disulfide bond formation and isomerization in substrates. The Arabidopsis (Arabidopsis thaliana) genome encodes diverse PDIs including structurally distinct subgroups PDI-L and PDI-M/S. It remains unclear how...

Read the complete abstract on PubMed

Topics

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

Share to Arabidopsis
Share to Catalysis
Share to Disulfides

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Genetic Variation

Share to Genotype

Share to Oxidation-Reduction

Share to Protein Disulfide-Isomerases

Share to Protein Folding

Source

Open in PubMed Open full text

Identifiers

PMID: 34609517
DOI: 10.1093/plphys/kiab457
PMCID: PMC8774737

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

Two protein disulfide isomerase subgroups work synergistically in catalyzing oxidative protein folding.PMID 34609517Read ↗

Endoplasmic reticulum stress activates the expression of a sub-group of protein disulfide isomerase genes and AtbZIP60 modulates the response in Arabidopsis thaliana.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 ↗

Phylogenetic Analyses Identify 10 Classes of the Protein Disulfide Isomerase Family in Plants, Including Single-Domain Protein Disulfide Isomerase-Related ProteinsSemantic proximity Read ↗

Biochemical basis of oxidative protein folding in the endoplasmic reticulum.Semantic proximity Read ↗

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

The thiol-disulfide exchange activity of AtPDI1 is involved in the response to abiotic stresses.Semantic proximity Read ↗

Decoding PDI diversity: insights into structure, domains, and functionality in sorghumSemantic proximity Read ↗

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

Genome-Wide Identification and Expression Profiling of the PDI Gene Family Reveals Their Probable Involvement in Abiotic Stress Tolerance in Tomato (Solanum lycopersicum L.)Semantic proximity Read ↗

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

Radically different thioredoxin domain arrangement of ERp46, an efficient disulfide bond introducer of the mammalian PDI family.Semantic proximity Read ↗

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