A single amino acid change makes the peptide specificity of B*3910 unrelated to B*3901 and closer to a group of HLA-B proteins including the malaria-protecting allotype HLA-B53-Reference-Cited by-同舟云学术

A single amino acid change makes the peptide specificity of B*3910 unrelated to B*3901 and closer to a group of HLA-B proteins including the malaria-protecting allotype HLA-B53

Published:1998-11 Issue:5 Volume:52 Page:416-421
ISSN:0001-2815
Container-title:Tissue Antigens
language:en
Short-container-title:

Author:

Yagüe J.,Vázquez J.,Castro J.A. López

Publisher

Wiley

Subject

Genetics,Biochemistry,Immunology,General Medicine,Immunology and Allergy

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1399-0039.1998.tb03067.x/fullpdf

Reference28 articles.

1. HLA-B27 subtypes in Asian patients with ankylosing spondylitis. Evidence for new associations;Lopez-Larrea;Tissue Antigens,1995

2. Relevance of residue 116 of HLA-B27 in determining susceptibility to ankylosing spondylitis;D'Amato;Eur J Immunol,1995

3. HLA-B27 and HLA-A2 subtypes: structure, evolution and function;Lopez de Castro;Immunol Today,1989

4. Peptide motifs of closely related HLA class I molecules encompass substantial differences;Rotzschke;Eur J Immunol,1992

5. The pathogenetdc role of HLA-B27 in chronic arthritis;López de Castro;Curr Opin Immunol,1998

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3. Homology, similarity, and identity in peptide epitope immunodefinition;Journal of Peptide Science;2012-06-14

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