VHL-box and SOCS-box domains determine binding specificity for Cul2-Rbx1 and Cul5-Rbx2 modules of ubiquitin ligases

Genes and Development

Volumn 18, Issue 24, 2004, Pages 3055-3065

  Kamura, Takumi ^a,b   Maenaka, Katsumi ^a   Kotoshiba, Shuhei ^a,b   Matsumoto, Masaki ^a,b   Kohda, Daisuke ^a   Conaway, Ronald C ^c,d   Conaway, Joan Weliky ^c,d   Nakayama, Keiichi I ^a,b  

^a KYUSHU UNIVERSITY   (Japan)

^b JAPAN SCIENCE AND TECHNOLOGY AGENCY   (Japan)

^c STOWERS INSTITUTE FOR MEDICAL RESEARCH   (United States)

^d UNIVERSITY OF KANSAS MEDICAL CENTER   (United States)

Author keywords

Cullin; E3 ubiquitin ligase; SOCS box protein; VHL box protein

Indexed keywords

ISOENZYME; UBIQUITIN PROTEIN LIGASE;

ARTICLE; BINDING AFFINITY; CARBOXY TERMINAL SEQUENCE; DOWN REGULATION; MAMMAL CELL; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FAMILY; PROTEIN LOCALIZATION; PROTEIN PROTEIN INTERACTION;

AMINO ACID SEQUENCE; CARRIER PROTEINS; CELL CYCLE PROTEINS; CELLS, CULTURED; CULLIN PROTEINS; GENE COMPONENTS; HUMANS; IMMUNOBLOTTING; IMMUNOPRECIPITATION; INTRACELLULAR SIGNALING PEPTIDES AND PROTEINS; MASS SPECTROMETRY; MODELS, CHEMICAL; MOLECULAR SEQUENCE DATA; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; PROTEINS; REPRESSOR PROTEINS; RNA INTERFERENCE; SEQUENCE ALIGNMENT; SUPPRESSOR OF CYTOKINE SIGNALING PROTEINS; TUMOR SUPPRESSOR PROTEINS; UBIQUITIN-PROTEIN LIGASES; VON HIPPEL-LINDAU TUMOR SUPPRESSOR PROTEIN;

MAMMALIA;

EID: 10644276385     PISSN: 08909369     EISSN: None     Source Type: Journal    
DOI: 10.1101/gad.1252404     Document Type: Article

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