Bax monomers form dimer units in the membrane that further self-assemble into multiple oligomeric species

Nature Communications

Volumn 6, Issue , 2015, Pages

  Subburaj, Yamunadevi ^a   Cosentino, Katia ^a,b   Axmann, Markus ^a,c   Pedrueza Villalmanzo, Esteban ^a,b   Hermann, Eduard ^a,b   Bleicken, Stephanie ^a,b   Spatz, Joachim ^a   García Sáez, Ana J ^a,b  

^a MAX PLANCK INSTITUTE FOR INTELLIGENT SYSTEMS   (Germany)

^b UNIVERSITY OF TÜBINGEN   (Germany)

^c VIENNA UNIVERSITY OF TECHNOLOGY   (Austria)

Author keywords

[No Author keywords available]

Indexed keywords

CYTOCHROME C; DIMER; MONOMER; OLIGOMER; PROTEIN BAX; PROTEIN BCL 2; PROTEIN BCL XL; PROTEIN BID; LIPID BILAYER; PROTEIN BINDING;

APOPTOSIS; CYTOCHROME; EXPERIMENTAL STUDY; MOLECULAR ANALYSIS; MONOCLINE; PROTEIN; STOICHIOMETRY; THEORETICAL STUDY;

APOPTOSIS; ARTICLE; CHANNEL GATING; CYTOSOL; DISSOCIATION; MITOCHONDRIAL MEMBRANE; OLIGOMERIZATION; PROTEIN ASSEMBLY; PROTEIN SECRETION; REGULATORY MECHANISM; STOICHIOMETRY; THEORETICAL MODEL; CHEMISTRY; LIPID BILAYER; METABOLISM; MICROSCOPY; PROCEDURES; SPECTROFLUOROMETRY;

BCL-2-ASSOCIATED X PROTEIN; LIPID BILAYERS; MICROSCOPY; PROTEIN BINDING; SPECTROMETRY, FLUORESCENCE;

EID: 84939448376     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms9042     Document Type: Article

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