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dc.contributor.authorRenault, Thibaud T
dc.contributor.authorDejean, Laurent M
dc.contributor.authorManon, Stéphen
dc.date.accessioned2017-11-06T15:12:15Z
dc.date.available2017-11-06T15:12:15Z
dc.date.issued2017-01
dc.identifier.citationA brewing understanding of the regulation of Bax function by Bcl-xL and Bcl-2. 2017, 161 (Pt B):201-210 Mech. Ageing Dev.en
dc.identifier.issn1872-6216
dc.identifier.pmid27112371
dc.identifier.doi10.1016/j.mad.2016.04.007
dc.identifier.urihttp://hdl.handle.net/10033/621163
dc.description.abstractBcl-2 family members form a network of protein-protein interactions that regulate apoptosis through permeabilization of the mitochondrial outer membrane. Deciphering this intricate network requires streamlined experimental models, including the heterologous expression in yeast. This approach had previously enabled researchers to identify domains and residues that underlie the conformational changes driving the translocation, the insertion and the oligomerization of the pro-apoptotic protein Bax at the level of the mitochondrial outer membrane. Recent studies that combine experiments in yeast and in mammalian cells have shown the unexpected effect of the anti-apoptotic protein Bcl-xL on the priming of Bax. As demonstrated with the BH3-mimetic molecule ABT-737, this property of Bcl-xL, and of Bcl-2, is crucial to elaborate about how apoptosis could be reactivated in tumoral cells.
dc.language.isoenen
dc.rights.urihttp://creativecommons.org/licenses/by-nc-sa/4.0/*
dc.subject.meshAnimalsen
dc.subject.meshBiphenyl Compoundsen
dc.subject.meshHumansen
dc.subject.meshMitochondrial Membranesen
dc.subject.meshNeoplasmsen
dc.subject.meshNitrophenolsen
dc.subject.meshPiperazinesen
dc.subject.meshProto-Oncogene Proteins c-bcl-2en
dc.subject.meshSaccharomyces cerevisiaeen
dc.subject.meshSulfonamidesen
dc.subject.meshbcl-2-Associated X Proteinen
dc.subject.meshbcl-X Proteinen
dc.titleA brewing understanding of the regulation of Bax function by Bcl-xL and Bcl-2.en
dc.typeArticleen
dc.contributor.departmentHelmholtz-Zentrum für Infektionsforschung GmbH. Inhoffenstr.7, 38124 Braunschweig, Germany.en
dc.identifier.journalMechanisms of ageing and developmenten
refterms.dateFOA2018-01-01T00:00:00Z
html.description.abstractBcl-2 family members form a network of protein-protein interactions that regulate apoptosis through permeabilization of the mitochondrial outer membrane. Deciphering this intricate network requires streamlined experimental models, including the heterologous expression in yeast. This approach had previously enabled researchers to identify domains and residues that underlie the conformational changes driving the translocation, the insertion and the oligomerization of the pro-apoptotic protein Bax at the level of the mitochondrial outer membrane. Recent studies that combine experiments in yeast and in mammalian cells have shown the unexpected effect of the anti-apoptotic protein Bcl-xL on the priming of Bax. As demonstrated with the BH3-mimetic molecule ABT-737, this property of Bcl-xL, and of Bcl-2, is crucial to elaborate about how apoptosis could be reactivated in tumoral cells.


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