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 in CH1 underlie retention of unassembled Ig heavy chains.

The Journal of biological chemistry - 15 Apr 2005

Elkabetz Yechiel, Argon Yair, Bar-Nun Shoshana

Abstract excerpt

Conformation, structure, and oligomeric state of immunoglobulins not only control quality and functional properties of antibodies but are also critical for immunoglobulins secretion. Unassembled immunoglobulin heavy chains are retained intracellularly by delayed folding of the C(H)1 domain and irreversible interaction of BiP with this domain. Here we show that the three C(H)1 cysteines play a central role in...

Read the complete abstract on PubMed

Topics

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

Share to Papain
Share to Disulfides
Share to Endoplasmic Reticulum Chaperone BiP

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

Share to Glycoside Hydrolases

Share to Immunoglobulin Heavy Chains

Share to Immunoglobulin Light Chains

Share to Immunoprecipitation

Share to Pancreatic Elastase

Source

Identifiers

PMID: 15705573
DOI: 10.1074/jbc.M500161200

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. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Cysteines in CH1 underlie retention of unassembled Ig heavy chains.PMID 15705573Read ↗

Coordination of immunoglobulin chain folding and immunoglobulin chain assembly is essential for the formation of functional IgG.Semantic proximity Read ↗

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

Membrane immunoglobulins are stabilized by interchain disulfide bonds occurring within the extracellular membrane-proximal domain.Semantic proximity Read ↗

Understanding the biosynthesis of human IgM SAM-6 through a combinatorial expression of mutant subunits that affect product assembly and secretion.Semantic proximity Read ↗

Functional Divergence in the Affinity and Stability of Non-Canonical Cysteines and Non-Canonical Disulfide Bonds: Insights from a VHH and VNAR Study.Semantic proximity Read ↗

Structural promiscuity in the human circulatory IgA1 clonal repertoireSemantic proximity Read ↗

A Broad Role for Cysteines in Bovine Antibody DiversitySemantic proximity Read ↗

Structural principles of B-cell antigen receptor assemblySemantic proximity Read ↗

Substituting the Thiol Ester of Human A2M or C3 with a Disulfide Produces Native Proteins with Altered Proteolysis-Induced Conformational Changes.Semantic proximity Read ↗

The short mRNA isoform of the immunoglobulin superfamily, member 1 gene encodes an intracellular glycoprotein.Semantic proximity Read ↗

Disulfide bond introduction for general stabilization of immunoglobulin heavy-chain variable domains.Semantic proximity Read ↗

Removal of a C-terminal serine residue proximal to the inter-chain disulfide bond of a human IgG1 lambda light chain mediates enhanced antibody stability and antibody dependent cell-mediated cytotoxicity.Semantic proximity Read ↗

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