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

Immunology

Volumn 142, Issue 2, 2014, Pages 237-247

  Rohrer, Karin M ^a   Haug, Markus ^a,b   Schwörer, Daniela ^a   Kalbacher, Hubert ^a   Holzer, Ursula ^a  

^a UNIVERSITY OF TÜBINGEN   (Germany)

^b NORWEGIAN UNIVERSITY OF SCIENCE AND TECHNOLOGY   (Norway)

Author keywords

Dissociation enhanced lanthanide fluorescent immunoassay; Heat shock proteins 70; HLA DR binding; Point mutations

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ALANINE; HEAT SHOCK COGNATE PROTEIN 70; HEAT SHOCK PROTEIN 70; HLA DR ANTIGEN; HLA DRB1 ANTIGEN; MONOCLONAL ANTIBODY; VALINE;

ANTIGEN PRESENTATION; ARTICLE; BINDING AFFINITY; BINDING SITE; CELL PROLIFERATION; CIRCULAR DICHROISM; CONTROLLED STUDY; IN VITRO STUDY; LYMPHOCYTE PROLIFERATION; POINT MUTATION; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN EXPRESSION; PROTEIN PROTEIN INTERACTION;

CD4+ T-CELL PROLIFERATION; DISSOCIATION-ENHANCED LANTHANIDE FLUORESCENT IMMUNOASSAY; HEAT-SHOCK PROTEINS 70; HLA-DR BINDING; POINT MUTATIONS;

BINDING SITES; CD4-POSITIVE T-LYMPHOCYTES; CELL PROLIFERATION; CELLS, CULTURED; HLA-DR ANTIGENS; HSP70 HEAT-SHOCK PROTEINS; HUMANS; MUTATION; PEPTIDES; SUBSTRATE SPECIFICITY;

EID: 84899069290     PISSN: 00192805     EISSN: 13652567     Source Type: Journal    
DOI: 10.1111/imm.12249     Document Type: Article

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