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Article

Distinct functions of tapasin revealed by polymorphism in MHC class I peptide loading.

Journal of immunology (Baltimore, Md. : 1950) - 1 Jan 2000

Peh C A, Laham N, Burrows S R, Zhu Y, McCluskey J

Abstract excerpt

Peptide assembly with class I molecules is orchestrated by multiple chaperones including tapasin, which bridges class I molecules with the TAP and is critical for efficient Ag presentation. In this paper, we show that, although constitutive levels of endogenous murine tapasin apparently are sufficient to form stable and long-lived complexes between the human HLA-B*4402 (B*4402) and mouse TAP proteins, this does...

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Source

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PMID: 10605023
DOI: 10.4049/jimmunol.164.1.292

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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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Distinct functions of tapasin revealed by polymorphism in MHC class I peptide loading.PMID 10605023Read ↗

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Critical role for the tapasin-docking site of TAP2 in the functional integrity of the MHC class I-peptide-loading complex.Semantic proximity Read ↗

Soluble tapasin restores MHC class I expression and function in the tapasin-negative cell line .220.Semantic proximity Read ↗

Allele-specific differences in the interaction of MHC class I molecules with transporters associated with antigen processing.Semantic proximity Read ↗

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