Structural aspects of chaperone-mediated peptide loading in the MHC-I antigen presentation pathway-Reference-Cited by-同舟云学术

Structural aspects of chaperone-mediated peptide loading in the MHC-I antigen presentation pathway

Published:2019-03-04 Issue:2 Volume:54 Page:164-173
ISSN:1040-9238
Container-title:Critical Reviews in Biochemistry and Molecular Biology
language:en
Short-container-title:Critical Reviews in Biochemistry and Molecular Biology

Author:

Natarajan Kannan¹,Jiang Jiansheng¹,Margulies David H.¹

Affiliation:

1. Molecular Biology Section, Laboratory of Immune System Biology, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD, USA

Funder

No potential conflict of interest was reported by the authors

NIAID

NIH

Publisher

Informa UK Limited

Subject

Molecular Biology,Biochemistry

Link

https://www.tandfonline.com/doi/pdf/10.1080/10409238.2019.1610352

Reference63 articles.

1. The quantity of naturally processed peptides stably bound by HLA-A*0201 is significantly reduced in the absence of tapasin

2. Antigen-B Cell Receptor Complexes Associate with Intracellular major histocompatibility complex (MHC) Class II Molecules

3. NMR spectroscopy reveals unexpected structural variation at the protein–protein interface in MHC class I molecules

4. Structure of the human MHC-I peptide-loading complex

5. Pathways of Antigen Processing

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2. Chaperones and Catalysts: How Antigen Presentation Pathways Cope With Biological Necessity;Frontiers in Immunology;2022-04-07

3. MHC I assembly and peptide editing — chaperones, clients, and molecular plasticity in immunity;Current Opinion in Immunology;2021-06

4. Antigenic Peptide Loading into Major Histocompatibility Complex Class I Is Driven by the Substrate N-Terminus;CCS Chemistry;2021-04-16

5. HLA polymorphism and tapasin independence influence outcomes of HIV and dengue virus infection;Proceedings of the National Academy of Sciences;2020-11-25