A three-helix homo-oligomerization domain containing BH3 and BH1 is responsible for the apoptotic activity of Bax.
about
Active Bax and Bak are functional holinsBcl-2 family interaction with the mitochondrial morphogenesis machineryBcl-x(L) retrotranslocates Bax from the mitochondria into the cytosolBAX unleashed: the biochemical transformation of an inactive cytosolic monomer into a toxic mitochondrial poreBax and Bak function as the outer membrane component of the mitochondrial permeability pore in regulating necrotic cell death in miceBuilding blocks of the apoptotic pore: how Bax and Bak are activated and oligomerize during apoptosisCharge profile analysis reveals that activation of pro-apoptotic regulators Bax and Bak relies on charge transfer mediated allosteric regulationBax regulates primary necrosis through mitochondrial dynamicsActive fragments from pro- and antiapoptotic BCL-2 proteins have distinct membrane behavior reflecting their functional divergenceThe functional differences between pro-survival and pro-apoptotic B cell lymphoma 2 (Bcl-2) proteins depend on structural differences in their Bcl-2 homology 3 (BH3) domains.Bax contains two functional mitochondrial targeting sequences and translocates to mitochondria in a conformational change- and homo-oligomerization-driven process.Release of Cytochrome C from Bax Pores at the Mitochondrial Membrane.Bortezomib-induced sensitization of malignant human glioma cells to vorinostat-induced apoptosis depends on reactive oxygen species production, mitochondrial dysfunction, Noxa upregulation, Mcl-1 cleavage, and DNA damage.Perturbation of the Bcl-2 network and an induced Noxa/Bcl-xL interaction trigger mitochondrial dysfunction after DNA damageInhibition of apoptotic Bax translocation to the mitochondria is a central function of parkin.The soluble form of Bax regulates mitochondrial fusion via MFN2 homotypic complexes.Mitochondria in apoptosis: Bcl-2 family members and mitochondrial dynamics.Bax forms two types of channels, one of which is voltage-gatedThe BCL-2 family reunion.Mitochondria and apoptosis: emerging concepts.Translocation of a Bak C-terminus mutant from cytosol to mitochondria to mediate cytochrome C release: implications for Bak and Bax apoptotic function.Bax dimerizes via a symmetric BH3:groove interface during apoptosisMechanisms of methicillin-resistant Staphylococcus aureus pneumonia-induced intestinal epithelial apoptosisCellular stress induces Bax-regulated nuclear bubble budding and rupture followed by nuclear protein releaseBax-derived membrane-active peptides act as potent and direct inducers of apoptosis in cancer cells.Molecular control of bacterial death and lysisTransforming growth factor-β directly induces p53-up-regulated modulator of apoptosis (PUMA) during the rapid induction of apoptosis in myc-driven B-cell lymphomas.Where killers meet--permeabilization of the outer mitochondrial membrane during apoptosis.InSite: a computational method for identifying protein-protein interaction binding sites on a proteome-wide scale.Inactivation of prosurvival Bcl-2 proteins activates Bax/Bak through the outer mitochondrial membrane.Mechanisms of action of Bcl-2 family proteinsCleavage by Caspase 8 and Mitochondrial Membrane Association Activate the BH3-only Protein Bid during TRAIL-induced Apoptosis.Apoptosis is triggered when prosurvival Bcl-2 proteins cannot restrain Bax.Assembly of the Bak apoptotic pore: a critical role for the Bak protein α6 helix in the multimerization of homodimers during apoptosisCD4+ lymphocytes control gut epithelial apoptosis and mediate survival in sepsis.Bax/Bak activation in the absence of Bid, Bim, Puma, and p53.Targeting the BCL-2 family in malignancies of germinal centre origin.Apoptosis and oncogenesis: give and take in the BCL-2 family.Inhibition of germinal centre apoptotic programmes by epstein-barr virus.The secrets of the Bcl-2 family.
P2860
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P2860
A three-helix homo-oligomerization domain containing BH3 and BH1 is responsible for the apoptotic activity of Bax.
description
2007 nî lūn-bûn
@nan
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
2007年论文
@zh
2007年论文
@zh-cn
name
A three-helix homo-oligomeriza ...... the apoptotic activity of Bax.
@ast
A three-helix homo-oligomeriza ...... the apoptotic activity of Bax.
@en
type
label
A three-helix homo-oligomeriza ...... the apoptotic activity of Bax.
@ast
A three-helix homo-oligomeriza ...... the apoptotic activity of Bax.
@en
prefLabel
A three-helix homo-oligomeriza ...... the apoptotic activity of Bax.
@ast
A three-helix homo-oligomeriza ...... the apoptotic activity of Bax.
@en
P2093
P2860
P356
P1433
P1476
A three-helix homo-oligomeriza ...... the apoptotic activity of Bax.
@en
P2093
Jacquelynn J D Evans
Nicholas M George
P2860
P304
P356
10.1101/GAD.1553607
P577
2007-08-01T00:00:00Z