Identification of an activation site in Bak and mitochondrial Bax triggered by antibodies

Nature Communications

Volumn 7, Issue , 2016, Pages

  Iyer, Sweta ^a   Anwari, Khatira ^a   Alsop, Amber E ^a   Yuen, Wai Shan ^b   Huang, David C S ^a   Carroll, John ^b   Smith, Nicholas A ^c   Smith, Brian J ^c   Dewson, Grant ^a   Kluck, Ruth M ^a  

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

^b MONASH UNIVERSITY   (Australia)

^c LA TROBE UNIVERSITY   (Australia)

Author keywords

[No Author keywords available]

Indexed keywords

CYTOCHROME C; IMMUNOGLOBULIN F(AB) FRAGMENT; MONOCLONAL ANTIBODY; MONOCLONAL ANTIBODY 7D10; PROTEIN BAK; PROTEIN BAX; UNCLASSIFIED DRUG; BAK1 PROTEIN, HUMAN; BAK1 PROTEIN, MOUSE; BAX PROTEIN, HUMAN; BAX PROTEIN, MOUSE; EPITOPE; PROTEIN BINDING;

ANTIBODY; APOPTOSIS; CYTOCHROME; GENE; IDENTIFICATION METHOD; MITOCHONDRIAL DNA; PROTEIN; TRANSLOCATION;

AMINO TERMINAL SEQUENCE; ANIMAL CELL; ANTIGEN BINDING; APOPTOSIS; ARTICLE; CELL PERMEABILIZATION; CHANNEL GATING; CONFORMATIONAL TRANSITION; CYTOSOL; DIMERIZATION; DISULFIDE BOND; EMBRYO; FEMALE; HINGE REGION; HUMAN; HUMAN CELL; MITOCHONDRION; MOLECULAR CLONING; MOLECULAR DOCKING; MOLECULAR DYNAMICS; MOUSE; NONHUMAN; OLIGOMERIZATION; PROTEIN CONFORMATION; PROTEIN UNFOLDING; ALPHA HELIX; ANIMAL; C57BL MOUSE; CELL CULTURE; CHEMISTRY; EPITOPE MAPPING; FIBROBLAST; GENE KNOCKOUT; GENETICS; METABOLISM; OOCYTE; PHYSIOLOGY; PROCEDURES; PROTEIN MULTIMERIZATION; SECRETION (PROCESS); SITE DIRECTED MUTAGENESIS;

ANIMALS; ANTIBODIES, MONOCLONAL; APOPTOSIS; BCL-2 HOMOLOGOUS ANTAGONIST-KILLER PROTEIN; BCL-2-ASSOCIATED X PROTEIN; CELLS, CULTURED; CYTOCHROMES C; CYTOSOL; EPITOPE MAPPING; EPITOPES; FEMALE; FIBROBLASTS; GENE KNOCKOUT TECHNIQUES; HUMANS; MICE; MICE, INBRED C57BL; MITOCHONDRIA; MOLECULAR DOCKING SIMULATION; MOLECULAR DYNAMICS SIMULATION; MUTAGENESIS, SITE-DIRECTED; OOCYTES; PROTEIN BINDING; PROTEIN CONFORMATION, ALPHA-HELICAL; PROTEIN MULTIMERIZATION;

EID: 84970004345     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms11734     Document Type: Article

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