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

Distinct patterns of folding and interactions with calnexin and calreticulin in human class I MHC proteins with altered N-glycosylation.

Journal of immunology (Baltimore, Md. : 1950) - 15 Jan 1998

Zhang Q, Salter R D

Abstract excerpt

Calnexin is a lectin-like chaperone that binds to class I MHC molecules soon after their synthesis, retaining unassembled heavy chains and also assisting their folding. Following association with beta2-microglobulin (beta2m) in the endoplasmic reticulum, a large proportion of human class I molecules release from calnexin, whereas mouse class I molecules do not. We asked whether addition of a second N-glycan to...

Read the complete abstract on PubMed

Topics

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

Share to Alleles
Share to Biological Transport
Share to Cell Line

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

Share to Cell Membrane

Share to Glucose

Share to Membrane Proteins

Share to Mutagenesis, Site-Directed

Share to Protein Binding

Source

Identifiers

PMID: 9551918

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

Distinct patterns of folding and interactions with calnexin and calreticulin in human class I MHC proteins with altered N-glycosylation.PMID 9551918Read ↗

Calnexin recognizes carbohydrate and protein determinants of class I major histocompatibility complex molecules.Semantic proximity Read ↗

Calreticulin and calnexin interact with different protein and glycan determinants during the assembly of MHC class I.Semantic proximity Read ↗

Lectin-deficient calnexin is capable of binding class I histocompatibility molecules in vivo and preventing their degradation.Semantic proximity Read ↗

Mutant MHC class I molecules define interactions between components of the peptide-loading complex.Semantic proximity Read ↗

Roles for calreticulin and a novel glycoprotein, tapasin, in the interaction of MHC class I molecules with TAP.Semantic proximity Read ↗

Lectin-deficient calreticulin retains full functionality as a chaperone for class I histocompatibility molecules.Semantic proximity Read ↗

Aglycosylated and phosphatidylinositol-anchored MHC class I molecules are associated with calnexin. Evidence implicating the class I-connecting peptide segment in calnexin association.Semantic proximity Read ↗

Complementation of a pathogenic IFNGR2 misfolding mutation with modifiers of N-glycosylation.Semantic proximity Read ↗

Endoplasmic reticulum-associated degradation of mammalian glycoproteins involves sugar chain trimming to Man6-5GlcNAc2.Semantic proximity Read ↗

N-glycan-dependent quality control of the Na,K-ATPase beta(2) subunit.Semantic proximity Read ↗

Tumor-associated calreticulin variants functionally compromise the peptide loading complex and impair its recruitment of MHC-I.Semantic proximity Read ↗

How N-linked oligosaccharides affect glycoprotein folding in the endoplasmic reticulum.Semantic proximity Read ↗

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