Resistance to unfolding by acidic pH and resistance to lysosomal degradation explains disease-association of HLA-B27 subtypes-Reference-Cited by-同舟云学术

Resistance to unfolding by acidic pH and resistance to lysosomal degradation explains disease-association of HLA-B27 subtypes

Published:2022-11 Issue: Volume:112 Page:109226
ISSN:1567-5769
Container-title:International Immunopharmacology
language:en
Short-container-title:International Immunopharmacology

Author:

Thakur Amit Kumar,Rana Manish Kumar,Luthra-Guptasarma Manni^ORCID

Publisher

Elsevier BV

Subject

Pharmacology,Immunology,Immunology and Allergy

Reference41 articles.

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2. Class I HLA oligomerization at the surface of B cells is controlled by exogenous beta (2)-microglobulin: implications in activation of cytotoxic T lymphocytes;Bodnár;Int. Immunol.,2003

3. HLA-B27 in transgenic rats forms disulfide-linked heavy chain oligomers and multimers that bind to thechaperone BiP;Tran;J. Immunol.,2004

4. HLA-B27 lacking associated beta2-microglobulin rearranges to auto-display or cross-display residues 169–181: a novel molecular mechanism for spondyloarthropathies;Luthra-Guptasarma;FEBS Lett.,2004

5. Refolding of HLA-B27 heavy chains in the absence of beta2m yields stable high molecular weight (HMW) protein forms displaying native-like as well as non-native-like conformational features: implications for autoimmune disease;Sharma;BBA,2007

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