Bax contains two functional mitochondrial targeting sequences and translocates to mitochondria in a conformational change- and homo-oligomerization-driven process

Journal of Biological Chemistry

Volumn 285, Issue 2, 2010, Pages 1384-1392

  George, Nicholas M ^a   Targy, Natalie ^a   Evans, Jacquelynn J D ^a   Zhang, Liqiang ^a   Luo, Xu ^a  

^a UNIVERSITY OF NEBRASKA MEDICAL CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

APOPTOSIS; CONFORMATIONAL CHANGE; CYTOSOLS; HETEROLOGOUS PROTEINS; HOMO-OLIGOMERS; MITOCHONDRIAL DAMAGE; MITOCHONDRIAL TRANSLOCATION;

CELL DEATH; CONFORMATIONS; OLIGOMERIZATION; OLIGOMERS; PROTEINS;

MITOCHONDRIA;

OLIGOMER; PROLINE; PROTEIN BAX;

ALPHA HELIX; AMINO ACID SEQUENCE; ARTICLE; CONTROLLED STUDY; CYTOSOL; GENE MUTATION; HUMAN; HUMAN CELL; MITOCHONDRION; MUTAGENESIS; NONHUMAN; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN PROCESSING; PROTEIN TARGETING; PROTEIN TRANSPORT; SIGNAL TRANSDUCTION; TARGET CELL;

ANIMALS; APOPTOSIS; BCL-2-ASSOCIATED X PROTEIN; CYTOSOL; HELA CELLS; HUMANS; MICE; MICE, KNOCKOUT; MITOCHONDRIA; PROTEIN MULTIMERIZATION; PROTEIN SORTING SIGNALS; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, SECONDARY; PROTEIN TRANSPORT;

EID: 74049129452     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M109.049924     Document Type: Article

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