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

The role of ERp44 in maturation of serotonin transporter protein.

The Journal of biological chemistry - 18 May 2012

Freyaldenhoven Samuel, Li Yicong, Kocabas Arif M, Ziu Enrit, Ucer Serra, Ramanagoudr-Bhojappa Raman, Miller Grover P, Kilic Fusun

Abstract excerpt

In heterologous and endogenous expression systems, we studied the role of ERp44 and its complex partner endoplasmic reticulum (ER) oxidase 1-α (Ero1-Lα) in mechanisms regulating disulfide bond formation for serotonin transporter (SERT), an oligomeric glycoprotein. ERp44 is an ER lumenal chaperone...

Read the complete abstract on PubMed

Topics

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

Share to Cell Membrane
Share to Disulfides
Share to Gene Silencing

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Membrane Glycoproteins

Share to Molecular Chaperones

Share to Oxidoreductases

Share to Protein Multimerization

Share to Serotonin Plasma Membrane Transport Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 22451649
DOI: 10.1074/jbc.M112.345058
PMCID: PMC3366855

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026. Prepared record publication-22451649-2026-09-04.2. Manifest publication-graph-cohort-2026-09-04.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The role of ERp44 in maturation of serotonin transporter protein.PMID 22451649Read ↗

Participation of the endoplasmic reticulum protein chaperone thio-oxidoreductase in gonadotropin-releasing hormone receptor expression at the plasma membrane.Semantic proximity Read ↗

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

Switching the clientele: a lysine residing in the C terminus of the serotonin transporter specifies its preference for the coat protein complex II component SEC24C.Semantic proximity Read ↗

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

Conserved intramolecular disulfide bond is critical to trafficking and fate of ATP-binding cassette (ABC) transporters ABCB6 and sulfonylurea receptor 1 (SUR1)/ABCC8.Semantic proximity Read ↗

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

[The apoptosis-inducing activity of human selenoprotein P shorter isoform].Semantic proximity Read ↗

Crystal structure and functional analysis of the protein disulfide isomerase-related protein ERp29.Semantic proximity Read ↗

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

Biogenesis of secretory immunoglobulin M requires intermediate non‐native disulfide bonds and engagement of the protein disulfide isomerase ERp44Semantic 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 ↗

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

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