Chaperoning function of stress protein grp170, a member of the hsp70 superfamily, is responsible for its immunoadjuvant activity

Cancer Research

Volumn 66, Issue 2, 2006, Pages 1161-1168

  Park, Jun Eui ^a   Facciponte, John ^a   Chen, Xing ^a   MacDonald, Ian ^a   Repasky, Elizabeth A ^a   Manjili, Masoud H ^b   Wang, Xiang Yang ^a   Subjeck, John R ^a  

^a ROSWELL PARK CANCER INSTITUTE   (United States)

^b VIRGINIA COMMONWEALTH UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; GLYCOPROTEIN GP 100; HEAT SHOCK PROTEIN 110; HEAT SHOCK PROTEIN 70; IMMUNOLOGICAL ADJUVANT; PROTEIN GRP170; UNCLASSIFIED DRUG;

ANIMAL CELL; ANIMAL EXPERIMENT; ANIMAL MODEL; ANTIGEN BINDING; ANTIGEN PRESENTATION; ANTIGEN PRESENTING CELL; ANTINEOPLASTIC ACTIVITY; ARTICLE; COMPLEX FORMATION; CONTROLLED STUDY; CYTOKINE PRODUCTION; DRUG EFFICACY; DRUG RECEPTOR BINDING; FEMALE; IMMUNITY; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; SPLEEN CELL; TUMOR IMMUNITY;

ANIMALS; ANTIBODY FORMATION; ANTIGEN-PRESENTING CELLS; BINDING SITES, ANTIBODY; CANCER VACCINES; FEMALE; GLYCOPROTEINS; HSP70 HEAT-SHOCK PROTEINS; IMMUNOTHERAPY; MEMBRANE GLYCOPROTEINS; MICE; MICE, INBRED C57BL; MOLECULAR CHAPERONES; NEOPLASM PROTEINS;

EID: 31544433928     PISSN: 00085472     EISSN: None     Source Type: Journal    
DOI: 10.1158/0008-5472.CAN-05-2609     Document Type: Article

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