BTB proteins are substrate-specific adaptors in an SCF-like modular ubiquitin ligase containing CUL-3

Nature

Volumn 425, Issue 6955, 2003, Pages 316-321

  Xu, Lai ^a   Wei, Yue ^a   Reboul, Jerome ^b,d   Vaglio, Philippe ^b   Shin, Tae Ho ^a   Vidal, Marc ^b   Elledge, Stephen J ^a,c   Harper, J Wade ^a,b  

^a BAYLOR COLLEGE OF MEDICINE   (United States)

^b HARVARD MEDICAL SCHOOL   (United States)

^c HOWARD HUGHES MEDICAL INSTITUTE   (United States)

^d INSTITUT PAOLI CALMETTES   (France)

Author keywords

[No Author keywords available]

Indexed keywords

BINDING ENERGY; GENETIC ENGINEERING; POLYPEPTIDES;

SIGNALLING PATHWAYS;

PROTEINS;

ADAPTOR PROTEIN; BINDING PROTEIN; BTB PROTEIN; CUL 3 UBIQUITIN LIGASE; CUL1 PROTEIN; CUL2 PROTEIN; CUL3 PROTEIN; CUL5 PROTEIN; CULLIN; ELONGIN C; F BOX PROTEIN; LIGASE; POLYPEPTIDE; PROTEASOME; REGULATOR PROTEIN; SKP1 PROTEIN; UBIQUITIN; UBIQUITIN PROTEIN LIGASE; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; BINDING AFFINITY; CAENORHABDITIS ELEGANS; CARBOXY TERMINAL SEQUENCE; COMPLEX FORMATION; EMBRYO DEVELOPMENT; ENZYME ACTIVITY; ENZYME SPECIFICITY; HUMAN; HUMAN CELL; MAMMAL; NONHUMAN; NUCLEOTIDE REPEAT; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN MOTIF; PROTEIN PROTEIN INTERACTION; REGULATORY MECHANISM; SEQUENCE ANALYSIS; SIGNAL TRANSDUCTION;

ADAPTOR PROTEINS, SIGNAL TRANSDUCING; ADENOSINE TRIPHOSPHATASES; AMINO ACID MOTIFS; AMINO ACID SEQUENCE; ANIMALS; CAENORHABDITIS ELEGANS; CAENORHABDITIS ELEGANS PROTEINS; CARRIER PROTEINS; CELL CYCLE PROTEINS; CELL LINE; CULLIN PROTEINS; HUMANS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTATION; PEPTIDE SYNTHASES; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; SKP CULLIN F-BOX PROTEIN LIGASES; SUBSTRATE SPECIFICITY; TWO-HYBRID SYSTEM TECHNIQUES;

CAENORHABDITIS; CAENORHABDITIS ELEGANS; MAMMALIA; NEMATODA;

EID: 0141493447     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/nature01985     Document Type: Article

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