Ubiquitin ligase Smurf1 targets TRAF family proteins for ubiquitination and degradation

Molecular and Cellular Biochemistry

Volumn 338, Issue 1-2, 2010, Pages 11-17

  Li, Shan ^a,b   Lu, Kefeng ^a   Wang, Jian ^a   An, Liguo ^b   Yang, Guiwen ^b   Chen, Hui ^a   Cui, Yu ^a   Yin, Xiushan ^a   Xie, Ping ^a   Xing, Guichun ^a   He, Fuchu ^a,c   Zhang, Lingqiang ^a  

^a BEIJING INSTITUTE OF RADIATION MEDICINE   (China)

^b SHANDONG NORMAL UNIVERSITY   (China)

^c FUDAN UNIVERSITY   (China)

Author keywords

E3 ubiquitin ligase; Protein ubiquitination; Smurf1; TRAF; WW domain

Indexed keywords

IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INTERLEUKIN 1 RECEPTOR; SMAD UBIQUITINATION REGULATION FACTOR 1; TRANSCRIPTION FACTOR AP 1; TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED FACTOR; TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED FACTOR 1; TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED FACTOR 2; TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED FACTOR 3; TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED FACTOR 4; TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED FACTOR 5; TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED FACTOR 6; TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED FACTOR 7; UBIQUITIN PROTEIN LIGASE; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG; SMURF1 PROTEIN, HUMAN; UBIQUITIN;

AMINO ACID SUBSTITUTION; ARTICLE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; EMBRYO; ENZYME ACTIVITY; ENZYME SUBSTRATE; HUMAN; HUMAN CELL; IMMUNOPRECIPITATION; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN MOTIF; PROTEIN PROTEIN INTERACTION; PROTEIN TARGETING; SIGNAL TRANSDUCTION; TWO HYBRID SYSTEM; UBIQUITINATION; CELL LINE; GENETICS; METABOLISM; PROTEIN TERTIARY STRUCTURE;

AMINO ACID MOTIFS; CELL LINE; HUMANS; PROTEIN STRUCTURE, TERTIARY; TNF RECEPTOR-ASSOCIATED FACTOR 4; TUMOR NECROSIS FACTOR RECEPTOR-ASSOCIATED PEPTIDES AND PROTEINS; TWO-HYBRID SYSTEM TECHNIQUES; UBIQUITIN; UBIQUITIN-PROTEIN LIGASES; UBIQUITINATION;

EID: 77951298466     PISSN: 03008177     EISSN: 15734919     Source Type: Journal    
DOI: 10.1007/s11010-009-0315-y     Document Type: Article

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