Structure of Bcl-xL-Bak peptide complex: recognition between regulators of apoptosis
about
Genome-wide prediction and validation of peptides that bind human prosurvival Bcl-2 proteinsDiva, a Bcl-2 homologue that binds directly to Apaf-1 and induces BH3-independent cell deathBax interacts with the permeability transition pore to induce permeability transition and cytochrome c release in isolated mitochondriaBoo, a novel negative regulator of cell death, interacts with Apaf-1.Btf, a novel death-promoting transcriptional repressor that interacts with Bcl-2-related proteins.Bax oligomerization is required for channel-forming activity in liposomes and to trigger cytochrome c release from mitochondriaStructural basis of BFL-1 for its interaction with BAX and its anti-apoptotic action in mammalian and yeast cellstBID, a membrane-targeted death ligand, oligomerizes BAK to release cytochrome cBcl-G, a novel pro-apoptotic member of the Bcl-2 familyMAP-1, a novel proapoptotic protein containing a BH3-like motif that associates with Bax through its Bcl-2 homology domainsTumor necrosis factor-alpha induces Bax-Bak interaction and apoptosis, which is inhibited by adenovirus E1B 19KBcl-x(L) sequesters its C-terminal membrane anchor in soluble, cytosolic homodimersThe novel BH3 α-helix mimetic JY-1-106 induces apoptosis in a subset of cancer cells (lung cancer, colon cancer and mesothelioma) by disrupting Bcl-xL and Mcl-1 protein-protein interactions with BakSiva-1 binds to and inhibits BCL-X(L)-mediated protection against UV radiation-induced apoptosisNoxa/Bcl-2 protein interactions contribute to bortezomib resistance in human lymphoid cellsHuman nuclear clusterin mediates apoptosis by interacting with Bcl-XL through C-terminal coiled coil domainInteraction of F1L with the BH3 domain of Bak is responsible for inhibiting vaccinia-induced apoptosisProapoptotic Bak is sequestered by Mcl-1 and Bcl-xL, but not Bcl-2, until displaced by BH3-only proteins.Functional and structural studies of the vaccinia virus virulence factor N1 reveal a Bcl-2-like anti-apoptotic proteinStructural changes in the BH3 domain of SOUL protein upon interaction with the anti-apoptotic protein Bcl-xLThe conserved N-terminal BH4 domain of Bcl-2 homologues is essential for inhibition of apoptosis and interaction with CED-4Dimerization properties of human BAD. Identification of a BH-3 domain and analysis of its binding to mutant BCL-2 and BCL-XL proteinsThe E1B 19K/Bcl-2-binding protein Nip3 is a dimeric mitochondrial protein that activates apoptosisA short Nur77-derived peptide converts Bcl-2 from a protector to a killerVaccinia virus N1L protein resembles a B cell lymphoma-2 (Bcl-2) family proteinVaccinia virus anti-apoptotic F1L is a novel Bcl-2-like domain-swapped dimer that binds a highly selective subset of BH3-containing death ligandsBcl-xL phosphorylation at Ser49 by polo kinase 3 during cell cycle progression and checkpointsMutation to Bax beyond the BH3 domain disrupts interactions with pro-survival proteins and promotes apoptosisMolecular basis of the interaction between the antiapoptotic Bcl-2 family proteins and the proapoptotic protein ASPP2The structure and interactions of the proline-rich domain of ASPP2MAP-1 is a mitochondrial effector of Bax.Bim: a novel member of the Bcl-2 family that promotes apoptosisEnforced dimerization of BAX results in its translocation, mitochondrial dysfunction and apoptosisActivation of apoptosis in vivo by a hydrocarbon-stapled BH3 helix.Structural conservation of druggable hot spots in protein-protein interfacesThe Bcl-2 apoptotic switch in cancer development and therapySystematic analysis of helical protein interfaces reveals targets for synthetic inhibitorsSmall-molecule Bcl-2 antagonists as targeted therapy in oncologyBok is a pro-apoptotic Bcl-2 protein with restricted expression in reproductive tissues and heterodimerizes with selective anti-apoptotic Bcl-2 family membersBH3 mimetics to improve cancer therapy; mechanisms and examples
P2860
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P2860
Structure of Bcl-xL-Bak peptide complex: recognition between regulators of apoptosis
description
1997 nî lūn-bûn
@nan
1997 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
1997 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
1997年の論文
@ja
1997年論文
@yue
1997年論文
@zh-hant
1997年論文
@zh-hk
1997年論文
@zh-mo
1997年論文
@zh-tw
1997年论文
@wuu
name
Structure of Bcl-xL-Bak peptide complex: recognition between regulators of apoptosis
@ast
Structure of Bcl-xL-Bak peptide complex: recognition between regulators of apoptosis
@en
Structure of Bcl-xL-Bak peptide complex: recognition between regulators of apoptosis
@nl
type
label
Structure of Bcl-xL-Bak peptide complex: recognition between regulators of apoptosis
@ast
Structure of Bcl-xL-Bak peptide complex: recognition between regulators of apoptosis
@en
Structure of Bcl-xL-Bak peptide complex: recognition between regulators of apoptosis
@nl
prefLabel
Structure of Bcl-xL-Bak peptide complex: recognition between regulators of apoptosis
@ast
Structure of Bcl-xL-Bak peptide complex: recognition between regulators of apoptosis
@en
Structure of Bcl-xL-Bak peptide complex: recognition between regulators of apoptosis
@nl
P2093
P921
P3181
P1433
P1476
Structure of Bcl-xL-Bak peptide complex: recognition between regulators of apoptosis
@en
P2093
C B Thompson
D Nettesheim
J E Harlan
M Eberstadt
R P Meadows
S B Shuker
P3181
P356
10.1126/SCIENCE.275.5302.983
P407
P577
1997-02-14T00:00:00Z