about
Membrane remodeling induced by the dynamin-related protein Drp1 stimulates Bax oligomerizationThe cytosolic domain of human Tom22 modulates human Bax mitochondrial translocation and conformation in yeastBH3 domains other than Bim and Bid can directly activate Bax/BakBimL directly neutralizes Bcl-xL to promote Bax activation during UV-induced apoptosisMutation to Bax beyond the BH3 domain disrupts interactions with pro-survival proteins and promotes apoptosisIdentification of a novel topoisomerase inhibitor effective in cells overexpressing drug efflux transportersApoptosis as anticancer mechanism: function and dysfunction of its modulators and targeted therapeutic strategiesControl of adult neurogenesis by programmed cell death in the mammalian brainPotential of apoptotic pathway-targeted cancer therapeutic research: Where do we stand?Regulation of Bim in Health and DiseaseBH3 profiling--measuring integrated function of the mitochondrial apoptotic pathway to predict cell fate decisionsPhotoreceptor cell death and rescue in retinal detachment and degenerationsBAX unleashed: the biochemical transformation of an inactive cytosolic monomer into a toxic mitochondrial poreThe BCL2 Family: Key Mediators of the Apoptotic Response to Targeted Anticancer TherapeuticsIntegration and oligomerization of Bax protein in lipid bilayers characterized by single molecule fluorescence studyThe MCL-1 BH3 helix is an exclusive MCL-1 inhibitor and apoptosis sensitizerEvidence that inhibition of BAX activation by BCL-2 involves its tight and preferential interaction with the BH3 domain of BAXInhibition of oncogenic Wnt signaling through direct targeting of -cateninStructural mechanism of Bax inhibition by cytomegalovirus protein vMIAThe restricted binding repertoire of Bcl-B leaves Bim as the universal BH3-only prosurvival Bcl-2 protein antagonistInhibition of Apoptosis and NF-κB Activation by Vaccinia Protein N1 Occur via Distinct Binding Surfaces and Make Different Contributions to VirulenceBID-induced structural changes in BAK promote apoptosisStructural Insights of tBid, the Caspase-8-activated Bid, and Its BH3 DomainPutting the pieces together: How is the mitochondrial pathway of apoptosis regulated in cancer and chemotherapy?Building blocks of the apoptotic pore: how Bax and Bak are activated and oligomerize during apoptosisRegulation of mitochondrial ceramide distribution by members of the BCL-2 familyCharge profile analysis reveals that activation of pro-apoptotic regulators Bax and Bak relies on charge transfer mediated allosteric regulationBax regulates primary necrosis through mitochondrial dynamicsUpregulation of Bcl2 inhibits apoptosis-driven BAX insertion but favors BAX relocalization in mitochondriaHydrocarbon-stapled peptides: principles, practice, and progressEvidence of conformational selection driving the formation of ligand binding sites in protein-protein interfacesKnockout Serum Replacement Promotes Cell Survival by Preventing BIM from Inducing Mitochondrial Cytochrome C ReleaseActive fragments from pro- and antiapoptotic BCL-2 proteins have distinct membrane behavior reflecting their functional divergenceChemical synthesis of hydrocarbon-stapled peptides for protein interaction research and therapeutic targetingDNA IR-Double Strand Breaks (DSBs) and cellular response via ATMDirect Activation of Bax Protein for Cancer TherapyThe 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.GSDMD membrane pore formation constitutes the mechanism of pyroptotic cell deathSynthetic Antibodies Inhibit Bcl-2-associated X Protein (BAX) through Blockade of the N-terminal Activation Site.The N Terminus of the Vaccinia Virus Protein F1L Is an Intrinsically Unstructured Region That Is Not Involved in Apoptosis Regulation.
P2860
Q24300125-27898E0F-48F1-4D03-A467-190D296EC22DQ24300635-37CCF917-A66F-4BCC-B49D-34DCEFCD9531Q24305138-C711A5AB-E8FA-4340-A729-51B46B73692EQ24309169-984FFE4E-221C-4396-A829-7AAA15831CD0Q24322798-EAD98A1C-B050-4D94-B73D-3EBF78D499C2Q24648348-9C46480F-6533-4DA2-8B18-08CD54BC5C0FQ26750639-C9095E47-826C-4167-934F-F47596CEDA4EQ26751456-16C46259-AD72-4C3F-88A9-CC6EA647C6B1Q26771601-AB694072-A189-42C4-B0E7-98497D3FAE3AQ26781203-E9CDE792-D088-40E7-8B75-A20A42A59139Q26828031-9F7FC998-CB0B-44DB-8146-B6C110E70F03Q26853192-BDEE5F69-0D92-4E95-94E6-51AAF2AD4115Q27002044-8E8703AF-F702-4A35-8257-ABB131E156D4Q27010154-AD50E9CB-9670-44A6-844D-2EC6C0BFF51FQ27314915-37C14AD2-98B2-4329-80C8-45C90E394EA1Q27662487-35BED9EF-2CCA-42E3-AB84-29A7A6E1A6DEQ27665695-46DAD64C-304D-435F-850E-D76C8D7B7722Q27674587-6034EE49-C742-4D32-B67B-A4DE4B7584F6Q27675369-37A5739B-B876-41A2-83C5-7499C556181BQ27675459-1750210C-CD95-401D-BE5D-45ECB58E9C06Q27676390-C32A5599-0302-4F83-9F78-2224BBB32539Q27677468-BF5E487B-6DB3-4742-A73B-28282BF84DECQ27680461-8900AAA5-D4CD-4628-B89D-CB18303C9F8DQ28085240-411E3442-7F00-4A24-AB4E-602966083A86Q28300914-B831C1F3-205F-458D-B896-03175FDBBD06Q28384330-F4252430-6FAF-4FA6-823E-92DFE08D04A3Q28480411-79A45C97-AA37-4E25-B923-D02B55547600Q28506109-47496A28-7DE9-4638-8106-7CED63FDE4F1Q28507255-1A40B02F-3D8A-4CA3-BB26-1195420A0E13Q28542025-6D062D60-420B-4D5B-A626-7F49098E42AAQ28543479-B5346454-A527-43D9-8F51-FA7E53D6E2EDQ28550350-6DEAF635-759E-4944-9136-10EA265CFB7BQ28749082-82D66D24-33B4-417C-B3E5-6BE8217CC998Q28833483-650AA651-1784-481F-BF9F-B273E049C7E2Q30225541-28F82BE9-E9F3-409D-A5C0-0771EA2F1CBCQ30353924-25DCAE2C-C0F6-46C0-8D59-4653D19DA0B6Q30368405-5AF1969E-2504-4FCF-9136-048B892CD1CCQ30370004-AC684E22-ED69-4FA5-816C-17F659EEE8FEQ30381337-E0FDA793-385E-4EE7-8491-4DD158022F2CQ30387749-BF4861FB-507B-4FB8-B250-268741A59C5A
P2860
description
2008 nî lūn-bûn
@nan
2008 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2008 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
name
BAX activation is initiated at a novel interaction site
@ast
BAX activation is initiated at a novel interaction site
@en
BAX activation is initiated at a novel interaction site
@nl
type
label
BAX activation is initiated at a novel interaction site
@ast
BAX activation is initiated at a novel interaction site
@en
BAX activation is initiated at a novel interaction site
@nl
prefLabel
BAX activation is initiated at a novel interaction site
@ast
BAX activation is initiated at a novel interaction site
@en
BAX activation is initiated at a novel interaction site
@nl
P2093
P2860
P50
P3181
P356
P1433
P1476
BAX activation is initiated at a novel interaction site
@en
P2093
Emily H-Y Cheng
Gregory H Bird
Ho-Chou Tu
Hyungjin Kim
Loren D Walensky
Marguerite L Davis
Nico Tjandra
Samuel G Katz
P2860
P2888
P304
P3181
P356
10.1038/NATURE07396
P407
P577
2008-10-01T00:00:00Z
P5875
P6179
1036508338