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

Biophysical characterization of ERp29. Evidence for a key structural role of cysteine 125.

The Journal of biological chemistry - 8 Apr 2005

Hermann Veronique M, Cutfield John F, Hubbard Michael J

Abstract excerpt

ERp29 is a major resident of the endoplasmic reticulum (ER) that seemingly plays an important role in most animal cells. Although a protein-folding association is widely supported, ERp29's specific molecular function remains unknown. A chaperone activity was postulated from evidence that ERp29 forms multimers like the classical ER chaperones, but conflicting results have emerged from our recent studies. Here a...

Read the complete abstract on PubMed

Topics

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

Share to Cysteine
Share to Drosophila Proteins
Share to Endoplasmic Reticulum

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

Share to Heat-Shock Proteins

Share to Protein Structure, Quaternary

Share to Protein Subunits

Share to Recombinant Proteins

Share to Solubility

Source

Identifiers

PMID: 15572350
DOI: 10.1074/jbc.M410889200

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.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Biophysical characterization of ERp29. Evidence for a key structural role of cysteine 125.PMID 15572350Read ↗

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

Drosophila SNAP-29 is an essential SNARE that binds multiple proteins involved in membrane traffic.Semantic proximity Read ↗

Site-specific functionality and tryptophan mimicry of lipidation in tetraspanin CD9.Semantic proximity Read ↗

Conserved structural and functional properties of D-domain containing redox-active and -inactive protein disulfide isomerase-related protein chaperones.Semantic proximity Read ↗

The C-terminal tail of tetraspanin protein CD9 contributes to its function and molecular organization.Semantic proximity Read ↗

Dimerization of ERp29, a PDI-like protein, is essential for its diverse functions.Semantic proximity Read ↗

Claudin-3 and claudin-5 protein folding and assembly into the tight junction are controlled by non-conserved residues in the transmembrane 3 (TM3) and extracellular loop 2 (ECL2) segments.Semantic proximity Read ↗

Crystal structure and functional analysis of Drosophila Wind, a protein-disulfide isomerase-related protein.Semantic proximity Read ↗

The role of ERp44 in maturation of serotonin transporter protein.Semantic proximity Read ↗

Characterization of aromatic residue-controlled protein retention in the endoplasmic reticulum of Saccharomyces cerevisiae.Semantic proximity Read ↗

Distinct roles for the cytoplasmic tail sequences of Emp24p and Erv25p in transport between the endoplasmic reticulum and Golgi complex.Semantic proximity Read ↗

An N-terminal 33-amino-acid-deletion variant of hsp25 retains oligomerization and functional properties.Semantic proximity Read ↗

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