Mouse Noxa uses only the C-terminal BH3-domain to inactivate Mcl-1

Apoptosis

Volumn 18, Issue 9, 2013, Pages 1093-1105

  Weber, Arnim ^a,b   Ausländer, David ^b,c   Häcker, Georg ^a  

^a UNIVERSITY OF FREIBURG   (Germany)

^b TECHNICAL UNIVERSITY OF MUNICH   (Germany)

^c ETH ZURICH   (Switzerland)

Author keywords

Apoptosis; BH3 domain; Degradation; Mcl 1; Noxa

Indexed keywords

BH3 PROTEIN; GLYCOGEN SYNTHASE KINASE 3; PROTEIN MCL 1; PROTEIN NOXA; UBIQUITIN; UBIQUITIN SPECIFIC PEPTIDASE 9; UNCLASSIFIED DRUG; MCL1 PROTEIN, MOUSE; MYELOID LEUKEMIA FACTOR 1; PMAIP1 PROTEIN, MOUSE; PROTEIN BCL 2; PROTEIN BINDING;

ALPHA HELIX; ANIMAL CELL; ARTICLE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; FIBROBLAST; MITOCHONDRIAL MEMBRANE; MOUSE; NONHUMAN; POINT MUTATION; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN STRUCTURE; ANIMAL; ANTAGONISTS AND INHIBITORS; CHEMISTRY; GENETICS; HUMAN; METABOLISM; PROTEIN TERTIARY STRUCTURE; PROTEIN TRANSPORT;

ANIMALS; HUMANS; MICE; MITOCHONDRIAL MEMBRANES; MYELOID CELL LEUKEMIA SEQUENCE 1 PROTEIN; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; PROTEIN TRANSPORT; PROTEOLYSIS; PROTO-ONCOGENE PROTEINS C-BCL-2;

EID: 84881476405     PISSN: 13608185     EISSN: 1573675X     Source Type: Journal    
DOI: 10.1007/s10495-013-0868-9     Document Type: Article

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