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

A di-arginine motif contributes to the ER localization of the type I transmembrane ER oxidoreductase TMX4.

The Biochemical journal - 14 Dec 2009

Roth Doris, Lynes Emily, Riemer Jan, Hansen Henning G, Althaus Nils, Simmen Thomas, Ellgaard Lars

Abstract excerpt

The thiol-disulfide oxidoreductases of the PDI (protein disulfide isomerase) family assist in disulfide-bond formation in the ER (endoplasmic reticulum). In the present study, we have shown that the previously uncharacterized PDI family member TMX4 (thioredoxin-like transmembrane 4) is an N-glycosylated type I membrane protein that localizes to the ER. We also demonstrate that TMX4 contains a single ER-luminal...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Motifs
Share to Arginine

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Blotting, Northern

Share to Chlorocebus aethiops

Share to Endoplasmic Reticulum

Share to Glycosylation

Share to Protein Disulfide-Isomerases

Share to Vero Cells

Source

Identifiers

PMID: 19811453
DOI: 10.1042/BJ20091064

Genes

TMX4

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

A di-arginine motif contributes to the ER localization of the type I transmembrane ER oxidoreductase TMX4.PMID 19811453Read ↗

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

TMX5/TXNDC15, a natural trapping mutant of the PDI family is a client of the proteostatic factor ERp44.Semantic proximity Read ↗

GPX4: old lessons, new featuresSemantic proximity Read ↗

The ER Thioredoxin-Related Transmembrane Protein TMX2 Controls Redox-Mediated Tethering of ER-Mitochondria Contacts (ERMCS)Semantic proximity Read ↗

TMX1, a disulfide oxidoreductase, is necessary for T cell function through regulation of CD3ζSemantic proximity Read ↗

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

Identification of novel nuclear targets of human thioredoxin 1.Semantic proximity Read ↗

Physical and functional interaction of transmembrane thioredoxin-related protein with major histocompatibility complex class I heavy chain: redox-based protein quality control and its potential relevance to immune responses.Semantic proximity Read ↗

The rare TXNRD1_v3 ("v3") splice variant of human thioredoxin reductase 1 protein is targeted to membrane rafts by N-acylation and induces filopodia independently of its redox active site integrity.Semantic proximity Read ↗

The thioredoxin‐like fold: Hidden domains in protein disulfide isomerases and other chaperone proteinsSemantic proximity Read ↗

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

Testis-specific peroxiredoxin 4 variant is not absolutely required for spermatogenesis and fertility in mice.Semantic proximity Read ↗

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