The RTP site shared by the HIV-1 Tat protein and the 11 S regulator subunit α is crucial for their effects on proteasome function including antigen processing

Journal of Molecular Biology

Volumn 323, Issue 4, 2002, Pages 771-782

  Huang, Xiaohua ^a   Seifert, Ulrike ^a   Salzmann, Ulrike ^a   Henklein, Peter ^a   Preissner, Robert ^a   Henke, Wolfgang ^a   Sijts, Alice J ^a   Kloetzel, Peter Michael ^a   Dubiel, Wolfgang ^a  

^a HUMBOLDT UNIVERSITY   (Germany)

Author keywords

11 S regulator; 20 S proteasome; Antigen processing; HIV 1; Tat

Indexed keywords

11 S REGULATOR SUBUNIT ALPHA; 20 S PROTEOSOME; ALANINE; AMINO ACID; ARGININE; ASPARTIC ACID; EPITOPE; GLUTAMINE; LYSINE; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 1; MUTANT PROTEIN; PEPTIDASE; PP89 PROTEIN; PROTEASOME; PROTEIN SUBUNIT; TRANSACTIVATOR PROTEIN; UNCLASSIFIED DRUG; VIRUS PROTEIN;

ANIMAL CELL; ANTIGEN PRESENTATION; ARTICLE; COMPLEX FORMATION; CONTROLLED STUDY; CYTOMEGALOVIRUS; ENZYME KINETICS; FIBROBLAST; HUMAN IMMUNODEFICIENCY VIRUS 1; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN FUNCTION; PROTEIN INTERACTION; PROTEIN STRUCTURE;

CYTOMEGALOVIRUS; HUMAN IMMUNODEFICIENCY VIRUS; HUMAN IMMUNODEFICIENCY VIRUS 1;

EID: 0036979090     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(02)00998-1     Document Type: Article

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