The multidomain proapoptotic molecules Bax and Bak are directly activated by heat

Proceedings of the National Academy of Sciences of the United States of America

Volumn 102, Issue 50, 2005, Pages 17975-17980

  Pagliari, Lisa J ^a   Kuwana, Tomomi ^b   Bonzon, Christine ^a   Newmeyer, Donald D ^a   Tu, Shine ^a   Beere, Helen M ^a,c   Green, Douglas R ^a,c  

^a LA JOLLA INSTITUTE FOR ALLERGY AND IMMUNOLOGY   (United States)

^b UNIVERSITY OF IOWA   (United States)

^c ST JUDE CHILDREN S RESEARCH HOSPITAL   (United States)

Author keywords

Bcl xL; BH3 only; Cytochrome c; Mitochondria; Oligomerization

Indexed keywords

BH3 PROTEIN; CYTOCHROME C; PROTEIN BAK; PROTEIN BAX; PROTEIN BCL XL;

ANIMAL CELL; APOPTOSIS; ARTICLE; CELL MEMBRANE PERMEABILITY; CONTROLLED STUDY; CYTOSOL; EMBRYO; FIBROBLAST; HEAT; HEAT TREATMENT; MITOCHONDRIAL MEMBRANE; MITOCHONDRION; MOUSE; NONHUMAN; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FAMILY; PROTEIN FUNCTION; PROTEIN ISOLATION; TEMPERATURE DEPENDENCE; WILD TYPE;

ANIMALS; APOPTOSIS; BCL-2 HOMOLOGOUS ANTAGONIST-KILLER PROTEIN; BCL-2-ASSOCIATED X PROTEIN; BCL-X PROTEIN; CELLS, CULTURED; CYTOCHROMES C; CYTOSOL; HEAT; MICE; MICE, KNOCKOUT; MITOCHONDRIA, LIVER; MITOCHONDRIAL MEMBRANES; PERMEABILITY;

ANIMALIA;

EID: 29144463145     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.0506712102     Document Type: Article

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