Thermal‐exchange <scp>HLA‐E</scp> multimers reveal specificity in <scp>HLA‐E</scp> and <scp>NKG2A</scp> / <scp>CD94</scp> complex interactions-Reference-Cited by-同舟云学术

Thermal‐exchange HLA‐E multimers reveal specificity in HLA‐E and NKG2A / CD94 complex interactions

Published:2022-10-20 Issue:3 Volume:168 Page:526-537
ISSN:0019-2805
Container-title:Immunology
language:en
Short-container-title:Immunology

Author:

Ruibal Paula¹^ORCID,Derksen Ian²,van Wolfswinkel Marjolein¹,Voogd Linda¹,Franken Kees L. M. C.¹,El Hebieshy Angela F.²,van Hall Thorbald³,Schoufour Tom A. W.²,Wijdeven Ruud H.²,Ottenhoff Tom H. M.¹,Scheeren Ferenc A.⁴,Joosten Simone A.¹^ORCID

Affiliation:

1. Department of Infectious Diseases Leiden University Medical Center Leiden The Netherlands

2. Department of Cell and Chemical Biology Leiden University Medical Center Leiden The Netherlands

3. Department of Medical Oncology Oncode Institute, Leiden University Medical Center Leiden The Netherlands

4. Department of Dermatology Leiden University Medical Center Leiden The Netherlands

Funder

National Institute of Allergy and Infectious Diseases

Nederlandse Organisatie voor Wetenschappelijk Onderzoek

Publisher

Wiley

Subject

Immunology,Immunology and Allergy

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1111/imm.13591

Reference43 articles.

1. Antigen processing and presentation

2. Mobilizing unconventional T cells

3. The human major histocompatibility complex class Ib molecule HLA-E binds signal sequence-derived peptides with primary anchor residues at positions 2 and 9

4. HLA-E Allelic Variants

5. HLA-E is a major ligand for the natural killer inhibitory receptor CD94/NKG2A

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3. The MHC-E peptide ligands for checkpoint CD94/NKG2A are governed by inflammatory signals, whereas LILRB1/2 receptors are peptide indifferent;Cell Reports;2023-12