Novel Cul3 binding proteins function to remodel E3 ligase complexes

BMC Cell Biology

Volumn 15, Issue 1, 2014, Pages

  Wimuttisuk, Wananit ^b,c   West, Mark ^a   Davidge, Brittney ^a   Yu, Kebing ^b   Salomon, Arthur ^b   Singer, Jeffrey D ^a  

^a PORTLAND STATE UNIVERSITY   (United States)

^b BROWN UNIVERSITY   (United States)

^c NATIONAL SCIENCE AND TECHNOLOGY DEVELOPMENT AGENCY   (Thailand)

Author keywords

BCR ubiquitin ligase complex; BTB domain containing protein; Cullin3; E3 ubiquitin ligase; Mass spectrometry; Protein purification; Tandem affinity purification; Ubiquitin; Ubiquitin ligase

Indexed keywords

BINDING PROTEIN; BTB CULLIN 3 RING BOX PROTEIN 1 UBIQUITIN PROTEIN LIGASE; CELL PROTEIN; COMPLEMENTARY DNA; CULLIN; CULLIN 3; CULLIN 3 BINDING PROTEIN; FMOD PROTEIN; PROTEIN FAZF; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG; CARRIER PROTEIN; CUL3 PROTEIN, HUMAN; PROTEIN BINDING; RBX1 PROTEIN, HUMAN; UBIQUITIN; UBIQUITIN PROTEIN LIGASE;

ALGORITHM; ARTICLE; BINDING SITE; BTB DOMAIN; COMPLEX FORMATION; CONTROLLED STUDY; DELETION MUTANT; ENZYME SUBSTRATE COMPLEX; HEK293 CELL LINE; IN VIVO STUDY; LEUCINE RICH REPEAT DOMAIN; LIQUID CHROMATOGRAPHY; MASS SPECTROMETRY; MOLECULAR DYNAMICS; MOLECULAR MODEL; MULTIDIMENSIONAL PROTEIN IDENTIFICATION TECHNOLOGY MASS SPECTROMETRY; NUCLEOTIDE SEQUENCE; PROTEIN ANALYSIS; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN PROCESSING; PROTEIN PROTEIN INTERACTION; PROTEIN PURIFICATION; SEQUENCE ALIGNMENT; SEQUEST ALGORITHM; STRUCTURE ACTIVITY RELATION; TANDEM AFFINITY PURIFICATION; TANDEM MASS SPECTROMETRY; UBIQUITINATION; WD40 DOMAIN; AMINO ACID SEQUENCE; HUMAN; METABOLISM; MOLECULAR GENETICS; PROTEIN TERTIARY STRUCTURE;

AMINO ACID SEQUENCE; CARRIER PROTEINS; CULLIN PROTEINS; HEK293 CELLS; HUMANS; MOLECULAR SEQUENCE DATA; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; PROTEOLYSIS; UBIQUITIN; UBIQUITIN-PROTEIN LIGASES;

EID: 84903870053     PISSN: None     EISSN: 14712121     Source Type: Journal    
DOI: 10.1186/1471-2121-15-28     Document Type: Article

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