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 |