Site-Dependent Cysteine Lipidation Potentiates the Activation of Proapoptotic BAX

scientific article published on 01 March 2020

Site-Dependent Cysteine Lipidation Potentiates the Activation of Proapoptotic BAX is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.1016/J.CELREP.2020.02.057
P932PMC publication ID7343539
P698PubMed publication ID32160532

P50authorJohn R. EngenQ50420861
Loren D. WalenskyQ92710996
P2093author name stringThomas E Wales
Daniel T Cohen
Matthew W McHenry
P2860cites workStructural model of active Bax at the membrane.Q42166522
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Mule/ARF-BP1, a BH3-only E3 ubiquitin ligase, catalyzes the polyubiquitination of Mcl-1 and regulates apoptosisQ24306444
A stapled BID BH3 helix directly binds and activates BAXQ24307663
Bax crystal structures reveal how BH3 domains activate Bax and nucleate its oligomerization to induce apoptosisQ24313049
Membrane binding by tBid initiates an ordered series of events culminating in membrane permeabilization by BaxQ24323186
BAX unleashed: the biochemical transformation of an inactive cytosolic monomer into a toxic mitochondrial poreQ27002044
Structure of Bax: coregulation of dimer formation and intracellular localizationQ27628839
BAX activation is initiated at a novel interaction siteQ27652635
Structure of Bcl-xL-Bak peptide complex: recognition between regulators of apoptosisQ27734734
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Dual role of proapoptotic BAD in insulin secretion and beta cell survivalQ28586275
Posttranslational N-myristoylation of BID as a molecular switch for targeting mitochondria and apoptosisQ28647600
An inhibitor of Bcl-2 family proteins induces regression of solid tumoursQ29547595
Auto-activation of the apoptosis protein Bax increases mitochondrial membrane permeability and is inhibited by Bcl-2Q30493313
The multidomain proapoptotic molecules Bax and Bak are directly activated by heatQ34212713
Conformational rearrangements in the pro-apoptotic protein, Bax, as it inserts into mitochondria: a cellular death switchQ34552749
Evidence for the presence of hydrogen-bonded secondary structure in angiotensin II in aqueous solutionQ34688172
The BCL-2 family reunionQ35568029
Cysteine 62 of Bax is critical for its conformational activation and its proapoptotic activity in response to H2O2-induced apoptosisQ35674492
Small molecules reveal an alternative mechanism of Bax activation.Q35936239
Allosteric inhibition of antiapoptotic MCL-1.Q36012325
Sphingolipid metabolism cooperates with BAK and BAX to promote the mitochondrial pathway of apoptosisQ36422392
Hydrogen exchange-mass spectrometry measures stapled peptide conformational dynamics and predicts pharmacokinetic propertiesQ37442733
Chemoproteomic profiling and discovery of protein electrophiles in human cellsQ37664926
Stepwise activation of BAX and BAK by tBID, BIM, and PUMA initiates mitochondrial apoptosis.Q38268983
The MCL1 inhibitor S63845 is tolerable and effective in diverse cancer modelsQ38736457
Revealing oxidative damage to enzymes of carbohydrate metabolism in yeast: An integration of 2D DIGE, quantitative proteomics, and bioinformaticsQ39755679
Bcl-2/Bax: a rheostat that regulates an anti-oxidant pathway and cell deathQ40732702
Selective Covalent Targeting of Anti-Apoptotic BFL-1 by Cysteine-Reactive Stapled Peptide Inhibitors.Q41374031
Inhibition of Pro-apoptotic BAX by a noncanonical interaction mechanism.Q41432708
BH3-triggered structural reorganization drives the activation of proapoptotic BAX.Q41884328
Analysis of protein conformation and dynamics by hydrogen/deuterium exchange MS.Q41910169
S-palmitoylation represents a novel mechanism regulating the mitochondrial targeting of BAX and initiation of apoptosisQ42003162
P433issue10
P304page(s)3229-3239.e6
P577publication date2020-03-01
P1433published inCell ReportsQ5058165
P1476titleSite-Dependent Cysteine Lipidation Potentiates the Activation of Proapoptotic BAX
P478volume30

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Q97531409A redox switch regulates the structure and function of anti-apoptotic BFL-1cites workP2860

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