Dissociation of Bak α 1 helix from the core and latch domains is required for apoptosis

Nature Communications

Volumn 6, Issue , 2015, Pages

  Alsop, Amber E ^a,b   Fennell, Stephanie C ^a   Bartolo, Ray C ^a   Tan, Iris K L ^a   Dewson, Grant ^a,b   Kluck, Ruth M ^a,b  

^a WALTER AND ELIZA HALL INSTITUTE OF MEDICAL RESEARCH   (Australia)

^b UNIVERSITY OF MELBOURNE   (Australia)

Author keywords

[No Author keywords available]

Indexed keywords

CYTOCHROME C; DISULFIDE; EPITOPE; PROTEIN BAK; PROTEIN BID;

ANTIBODY; APOPTOSIS; ARRAY; MITOCHONDRION; MUTAGENICITY; PERMEABILITY; SULFIDE;

ALPHA HELIX; ANIMAL CELL; APOPTOSIS; ARTICLE; CHANNEL GATING; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; DIMERIZATION; DISSOCIATION; ENZYME RELEASE; EPITOPE MAPPING; FLUORESCENCE ACTIVATED CELL SORTING; MOUSE; MUTAGENESIS; NONHUMAN; PROTEIN DOMAIN; PROTEIN STABILITY; ANIMAL; CELL LINE; HUMAN; METABOLISM; PROTEIN MICROARRAY; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; SITE DIRECTED MUTAGENESIS; TRANSFORMED CELL LINE;

ANIMALS; APOPTOSIS; BCL-2 HOMOLOGOUS ANTAGONIST-KILLER PROTEIN; BH3 INTERACTING DOMAIN DEATH AGONIST PROTEIN; CELL LINE; CELL LINE, TRANSFORMED; EPITOPE MAPPING; HUMANS; MICE; MUTAGENESIS, SITE-DIRECTED; PROTEIN ARRAY ANALYSIS; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY;

EID: 84928036799     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms7841     Document Type: Article

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