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The BCL2 Family: Key Mediators of the Apoptotic Response to Targeted Anticancer TherapeuticsBID-induced structural changes in BAK promote apoptosisThe deubiquitinase Usp27x stabilizes the BH3-only protein Bim and enhances apoptosisBuilding blocks of the apoptotic pore: how Bax and Bak are activated and oligomerize during apoptosisA Maltose-Binding Protein Fusion Construct Yields a Robust Crystallography Platform for MCL1Assembly of Bak homodimers into higher order homooligomers in the mitochondrial apoptotic poreSynthetic 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.Comparative α-helicity of cyclic pentapeptides in water.A phospho-BAD BH3 helix activates glucokinase by a mechanism distinct from that of allosteric activatorsThe rheostat in the membrane: BCL-2 family proteins and apoptosisMaturation stage of T-cell acute lymphoblastic leukemia determines BCL-2 versus BCL-XL dependence and sensitivity to ABT-199BID preferentially activates BAK while BIM preferentially activates BAX, affecting chemotherapy responseBeta-amyloid oligomers activate apoptotic BAK pore for cytochrome c release.Potent and specific peptide inhibitors of human pro-survival protein Bcl-xL.Transformations of the macromolecular landscape at mitochondria during DNA-damage-induced apoptotic cell death.Mitochondria and apoptosis: emerging concepts.Small molecules reveal an alternative mechanism of Bax activation.Allosteric inhibition of antiapoptotic MCL-1.The BCL-2 protein family, BH3-mimetics and cancer therapy.An interconnected hierarchical model of cell death regulation by the BCL-2 familyMitochondria in human pluripotent stem cell apoptosis.Identification of an activation site in Bak and mitochondrial Bax triggered by antibodies.Assembly of the Bak apoptotic pore: a critical role for the Bak protein α6 helix in the multimerization of homodimers during apoptosisMultimodal interaction with BCL-2 family proteins underlies the proapoptotic activity of PUMA BH3Mitochondria: gatekeepers of response to chemotherapyStructural biology of the Bcl-2 family and its mimicry by viral proteinsMantle cell lymphoma in cyclin D1 transgenic mice with Bim-deficient B cells.The C-terminal domain (CTD) in linker histones antagonizes anti-apoptotic proteins to modulate apoptotic outcomes at the mitochondrion.Death upon a kiss: mitochondrial outer membrane composition and organelle communication govern sensitivity to BAK/BAX-dependent apoptosis.Mitochondrial regulation of cell death.Cell death and the mitochondria: therapeutic targeting of the BCL-2 family-driven pathway.Apoptosis regulation at the mitochondrial outer membrane.Many players in BCL-2 family affairs.The Bcl-2 family: structures, interactions and targets for drug discovery.The mystery of BCL2 family: Bcl-2 proteins and apoptosis: an update.An enhanced functional interrogation/manipulation of intracellular signaling pathways with the peptide 'stapling' technology.Emerging understanding of Bcl-2 biology: Implications for neoplastic progression and treatment.New dimension in therapeutic targeting of BCL-2 family proteins.Discoveries and controversies in BCL-2 protein-mediated apoptosis.
P2860
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P2860
description
2013 nî lūn-bûn
@nan
2013年の論文
@ja
2013年論文
@yue
2013年論文
@zh-hant
2013年論文
@zh-hk
2013年論文
@zh-mo
2013年論文
@zh-tw
2013年论文
@wuu
2013年论文
@zh
2013年论文
@zh-cn
name
Direct activation of full-length proapoptotic BAK
@ast
Direct activation of full-length proapoptotic BAK
@en
type
label
Direct activation of full-length proapoptotic BAK
@ast
Direct activation of full-length proapoptotic BAK
@en
prefLabel
Direct activation of full-length proapoptotic BAK
@ast
Direct activation of full-length proapoptotic BAK
@en
P2093
P2860
P356
P1476
Direct activation of full-length proapoptotic BAK
@en
P2093
Craig R Braun
Elizaveta S Leshchiner
Loren D Walensky
P2860
P304
P356
10.1073/PNAS.1214313110
P407
P577
2013-02-12T00:00:00Z