Mutations in the substrate binding site of human heat-shock protein 70 indicate specific interaction with HLA-DR outside the peptide binding groove-Reference-Cited by-同舟云学术

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Mutations in the substrate binding site of human heat-shock protein 70 indicate specific interaction with HLA-DR outside the peptide binding groove

Published:2014-04-24 Issue:2 Volume:142 Page:237-247
ISSN:0019-2805
Container-title:Immunology
language:en
Short-container-title:Immunology

Author:

Rohrer Karin M.¹,Haug Markus¹²,Schwörer Daniela¹,Kalbacher Hubert³,Holzer Ursula¹

Affiliation:

1. Children's Hospital; University of Tübingen; Tübingen Germany

2. Centre of Molecular Inflammation Research (CEMIR); Department of Cancer Research and Molecular Medicine; NTNU; Trondheim Norway

3. Interfaculty Institute of Biochemistry (IFIB); University of Tübingen; Tübingen Germany

Publisher

Wiley

Subject

Immunology,Immunology and Allergy

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1111/imm.12249/fullpdf

Reference31 articles.

1. Roles of heat-shock proteins in innate and adaptive immunity;Srivastava;Nat Rev Immunol,2002

2. Necrotic but not apoptotic cell death releases heat shock proteins, which deliver a partial maturation signal to dendritic cells and activate the NF-κB pathway;Basu;Int Immunol,2000

3. Structure and function: heat shock proteins and adaptive immunity;Javid;J Immunol,2007

4. HSP70 stimulates cytokine production through a CD14-dependent pathway, demonstrating its dual role as a chaperone and cytokine;Asea;Nat Med,2000

5. The endoplasmic reticulum-resident heat shock protein Gp96 activates dendritic cells via the Toll-like receptor 2/4 pathway;Vabulas;J Biol Chem,2002

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