The cytosolic domain of Bcl-2 forms small pores in model mitochondrial outer membrane after acidic pH-induced membrane association.

Sheng wu yi xue gong cheng xue za zhi = Journal of biomedical engineering = Shengwu yixue gongchengxue zazhi

Volumn 26, Issue 1, 2009, Pages 130-137

  Peng, Jun ^a   Lapolla, Suzanne M ^a   Zhang, Zhi ^a   Lin, Jialing ^a  

^a UNIVERSITY OF OKLAHOMA COLLEGE OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CARRIER PROTEIN; CYTOCHROME C; LIPOSOME; MITOCHONDRIAL PERMEABILITY TRANSITION PORE; PROTEIN BAX; PROTEIN BCL X; PROTEIN BID;

ARTICLE; CELL MEMBRANE PERMEABILITY; HUMAN; METABOLISM; MITOCHONDRIAL MEMBRANE; PH;

BCL-2-ASSOCIATED X PROTEIN; BCL-X PROTEIN; BH3 INTERACTING DOMAIN DEATH AGONIST PROTEIN; CELL MEMBRANE PERMEABILITY; CYTOCHROME C GROUP; HUMANS; HYDROGEN-ION CONCENTRATION; LIPOSOMES; MITOCHONDRIAL MEMBRANE TRANSPORT PROTEINS; MITOCHONDRIAL MEMBRANES;

EID: 75549087784     PISSN: 10015515     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (0)