Ca2+/S100 proteins act as upstream regulators of the chaperone-associated ubiquitin ligase chip (c terminus of hsc70-interacting protein)

Journal of Biological Chemistry

Volumn 288, Issue 10, 2013, Pages 7158-7168

  Shimamoto, Seiko ^a   Kubota, Yasuo ^a   Yamaguchi, Fuminori ^a   Tokumitsu, Hiroshi ^a   Kobayashi, Ryoji ^a  

^a KAGAWA UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

C TERMINUS; PROTEASOMAL DEGRADATION; UBIQUITIN LIGASES; UBIQUITINATION;

CALCIUM; SIGNAL TRANSDUCTION;

PROTEINS;

BINDING PROTEIN; C TERMINUS OF HSC70 INTERACTING PROTEIN; CALCYCLIN; CALVASCULIN; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 90; HEAT SHOCK TRANSCRIPTION FACTOR 1; PROTEIN S 100; PROTEIN S100B; S100A1 PROTEIN; S100A10 PROTEIN; S100A11 PROTEIN; S100A12 PROTEIN; S100A2 PROTEIN; SMAD1 PROTEIN; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG; CALCIUM; CALCIUM BINDING PROTEIN; CHEMOTACTIC FACTOR; DNA BINDING PROTEIN; HEAT SHOCK TRANSCRIPTION FACTOR; LYSINE; PROLINE; PROTEASOME; PROTEIN P53; S100A2 PROTEIN, HUMAN; S100P PROTEIN, HUMAN; STUB1 PROTEIN, HUMAN; TRANSCRIPTION FACTOR; TUMOR PROTEIN; UBIQUITIN PROTEIN LIGASE;

ARTICLE; BINDING AFFINITY; BINDING SITE; CALCIUM SIGNALING; CONTROLLED STUDY; ENZYME SUBSTRATE; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; REGULATORY MECHANISM; UBIQUITINATION; GENETICS; HUMAN; METABOLISM; MUTATION; PROTEIN BINDING; SIGNAL TRANSDUCTION; TUMOR CELL LINE; WESTERN BLOTTING;

BINDING SITES; BLOTTING, WESTERN; CALCIUM; CALCIUM-BINDING PROTEINS; CELL LINE, TUMOR; CHEMOTACTIC FACTORS; DNA-BINDING PROTEINS; HSP70 HEAT-SHOCK PROTEINS; HSP90 HEAT-SHOCK PROTEINS; HUMANS; LYSINE; MUTATION; NEOPLASM PROTEINS; PROLINE; PROTEASOME ENDOPEPTIDASE COMPLEX; PROTEIN BINDING; S100 PROTEINS; SIGNAL TRANSDUCTION; SMAD1 PROTEIN; TRANSCRIPTION FACTORS; TUMOR SUPPRESSOR PROTEIN P53; UBIQUITIN-PROTEIN LIGASES; UBIQUITINATION;

MLCS; MLOWN;

EID: 84874906001     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.436758     Document Type: Article

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