Title : Bax dimerizes via a symmetric BH3:groove interface during apoptosis.

Pub. Date : 2012 Apr

PMID : 22015607






8 Functional Relationships(s)
Download
Sentence
Compound Name
Protein Name
Organism
1 Bax dimerizes via a symmetric BH3:groove interface during apoptosis. BH 3 BCL2 associated X, apoptosis regulator Homo sapiens
2 We now show that Bax also dimerizes via a BH3:groove interaction after apoptotic signaling in cells and in mitochondrial fractions. BH 3 BCL2 associated X, apoptosis regulator Homo sapiens
3 BH3:groove dimers of Bax were symmetric as dimers but not higher order oligomers could be linked by cysteine residues placed in both the BH3 and groove. BH 3 BCL2 associated X, apoptosis regulator Homo sapiens
4 BH3:groove dimers of Bax were symmetric as dimers but not higher order oligomers could be linked by cysteine residues placed in both the BH3 and groove. BH 3 BCL2 associated X, apoptosis regulator Homo sapiens
5 The BH3:groove interaction was evident in the majority of mitochondrial Bax after apoptotic signaling, and correlated strongly with cytochrome c release, supporting its central role in Bax function. BH 3 BCL2 associated X, apoptosis regulator Homo sapiens
6 The BH3:groove interaction was evident in the majority of mitochondrial Bax after apoptotic signaling, and correlated strongly with cytochrome c release, supporting its central role in Bax function. BH 3 BCL2 associated X, apoptosis regulator Homo sapiens
7 We also found that a population of Bax:Bak heterodimers generated during apoptosis formed via a BH3:groove interaction, further demonstrating that Bax and Bak oligomerize via similar mechanisms. BH 3 BCL2 associated X, apoptosis regulator Homo sapiens
8 We also found that a population of Bax:Bak heterodimers generated during apoptosis formed via a BH3:groove interaction, further demonstrating that Bax and Bak oligomerize via similar mechanisms. BH 3 BCL2 associated X, apoptosis regulator Homo sapiens