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Article

I-Ag7 is subject to post-translational chaperoning by CLIP.

International immunology - 1 Aug 2010

Rinderknecht Cornelia H, Lu Ning, Crespo Oliver, Truong Phi, Hou Tieying, Wang Nan, Rajasekaran Narendiran, Mellins Elizabeth D

Abstract excerpt

Several MHC class II alleles linked with autoimmune diseases form unusually low-stability complexes with class II-associated invariant chain peptides (CLIP), leading us to hypothesize that this is an important feature contributing to autoimmune pathogenesis. We recently demonstrated a novel post-endoplasmic reticulum (ER) chaperoning role of the CLIP peptides for the murine class II allele I-E(d). In the current...

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

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Identifiers

PMID: 20547545
DOI: 10.1093/intimm/dxq056
PMCID: PMC2908477

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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.

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I-Ag7 is subject to post-translational chaperoning by CLIP.PMID 20547545Read ↗

Posttranslational regulation of I-Ed by affinity for CLIP.Semantic proximity Read ↗

Evidence that binding site occupancy is necessary and sufficient for effective major histocompatibility complex (MHC) class II transport through the secretory pathway redefines the primary function of class II-associated invariant chain peptides (CLIP).Semantic proximity Read ↗

Identification of residues in the class II-associated Ii peptide (CLIP) region of invariant chain that affect efficiency of MHC class II-mediated antigen presentation in an allele-dependent manner.Semantic proximity Read ↗

Clip binds to HLA class II using methionine-based, allele-dependent motifs as well as allele-independent supermotifs.Semantic proximity Read ↗

Binding of major histocompatibility complex class II to the invariant chain-derived peptide, CLIP, is regulated by allelic polymorphism in class II.Semantic proximity Read ↗

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