BH3-triggered structural reorganization drives the activation of proapoptotic BAX.

scientific article published on November 2010

BH3-triggered structural reorganization drives the activation of proapoptotic BAX. is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.1016/J.MOLCEL.2010.10.019
P932PMC publication ID3050027
P698PubMed publication ID21070973
P5875ResearchGate publication ID47754920

P50authorLoren D. WalenskyQ92710996
Evripidis GavathiotisQ59661942
P2093author name stringDenis E Reyna
Marguerite L Davis
Gregory H Bird
P2860cites worktBID, a membrane-targeted death ligand, oligomerizes BAK to release cytochrome cQ24290118
Differential targeting of prosurvival Bcl-2 proteins by their BH3-only ligands allows complementary apoptotic functionQ24293924
Apoptosis initiated when BH3 ligands engage multiple Bcl-2 homologs, not Bax or BakQ24296478
Proapoptotic Bak is sequestered by Mcl-1 and Bcl-xL, but not Bcl-2, until displaced by BH3-only proteinsQ24302494
A stapled BID BH3 helix directly binds and activates BAXQ24307663
Direct activation of Bax by p53 mediates mitochondrial membrane permeabilization and apoptosisQ24307994
Bcl-2 heterodimerizes in vivo with a conserved homolog, Bax, that accelerates programmed cell deathQ24312211
BID: a novel BH3 domain-only death agonistQ24320091
Hematopoietic malignancies demonstrate loss-of-function mutations of BAXQ24321995
Membrane binding by tBid initiates an ordered series of events culminating in membrane permeabilization by BaxQ24323186
Conformation of the Bax C-terminus regulates subcellular location and cell deathQ24534099
Activation of apoptosis in vivo by a hydrocarbon-stapled BH3 helixQ24537504
Solution structure of BID, an intracellular amplifier of apoptotic signalingQ27617719
Solution structure of the proapoptotic molecule BID: a structural basis for apoptotic agonists and antagonistsQ27617723
Structure of Bax: coregulation of dimer formation and intracellular localizationQ27628839
Solution structure of the antiapoptotic protein bcl-2Q27630598
The X-ray structure of a BAK homodimer reveals an inhibitory zinc binding siteQ27640443
Structure of the BH3 domains from the p53-inducible BH3-only proteins Noxa and Puma in complex with Mcl-1Q27651003
BAX activation is initiated at a novel interaction siteQ27652635
Structure of Bcl-xL-Bak peptide complex: recognition between regulators of apoptosisQ27734734
Mass Spectrometric Sequencing of Proteins from Silver-Stained Polyacrylamide GelsQ27860531
Using NMRView to visualize and analyze the NMR spectra of macromoleculesQ27860567
Errors in protein structuresQ27860776
NMR methods for studying protein-protein interactions involved in translation initiationQ81390819
Synthesis and biophysical characterization of stabilized alpha-helices of BCL-2 domainsQ81584715
NMRPipe: a multidimensional spectral processing system based on UNIX pipesQ27860859
GROMACS: fast, flexible, and freeQ27860998
Proapoptotic BAX and BAK: a requisite gateway to mitochondrial dysfunction and deathQ28363890
Bim, Bad and Bmf: intrinsically unstructured BH3-only proteins that undergo a localized conformational change upon binding to prosurvival Bcl-2 targetsQ28910218
Bid, Bax, and lipids cooperate to form supramolecular openings in the outer mitochondrial membraneQ29616354
BH3 domains of BH3-only proteins differentially regulate Bax-mediated mitochondrial membrane permeabilization both directly and indirectlyQ29617135
Distinct BH3 domains either sensitize or activate mitochondrial apoptosis, serving as prototype cancer therapeuticsQ29620467
Auto-activation of the apoptosis protein Bax increases mitochondrial membrane permeability and is inhibited by Bcl-2Q30493313
Novel Bcl-2 homology-3 domain-like sequences identified from screening randomized peptide libraries for inhibitors of the pro-survival Bcl-2 proteins.Q33502518
Bax contains two functional mitochondrial targeting sequences and translocates to mitochondria in a conformational change- and homo-oligomerization-driven processQ33569749
Bax forms multispanning monomers that oligomerize to permeabilize membranes during apoptosisQ33854131
Bax forms an oligomer via separate, yet interdependent, surfacesQ33885192
The multidomain proapoptotic molecules Bax and Bak are directly activated by heatQ34212713
A three-helix homo-oligomerization domain containing BH3 and BH1 is responsible for the apoptotic activity of Bax.Q35917067
Mitochondrial permeabilization relies on BH3 ligands engaging multiple prosurvival Bcl-2 relatives, not Bak.Q36118156
Regulated targeting of BAX to mitochondria.Q36255507
Conformational control of Bax localization and apoptotic activity by Pro168.Q36321947
The Bax pore in liposomes, BiophysicsQ36501189
Withdrawal of IL-7 induces Bax translocation from cytosol to mitochondria through a rise in intracellular pH.Q36746298
The role of BH3-only protein Bim extends beyond inhibiting Bcl-2-like prosurvival proteinsQ37309119
BH3-only proteins and their roles in programmed cell deathQ37566201
Survival factor-induced extracellular signal-regulated kinase phosphorylates BIM, inhibiting its association with BAX and proapoptotic activity.Q37593642
Stepwise activation of BAX and BAK by tBID, BIM, and PUMA initiates mitochondrial apoptosis.Q38268983
Bid-induced conformational change of Bax is responsible for mitochondrial cytochrome c release during apoptosisQ38326924
Mutagenesis of the BH3 domain of BAX identifies residues critical for dimerization and killingQ39576297
The first alpha helix of Bax plays a necessary role in its ligand-induced activation by the BH3-only proteins Bid and PUMA.Q40485961
Bcl-2/Bax: a rheostat that regulates an anti-oxidant pathway and cell deathQ40732702
Bak activation for apoptosis involves oligomerization of dimers via their alpha6 helicesQ43235008
Involvement of the N-terminus of Bax in its intracellular localization and function.Q45711449
To trigger apoptosis, Bak exposes its BH3 domain and homodimerizes via BH3:groove interactions.Q46142204
Baxbeta: a constitutively active human Bax isoform that is under tight regulatory control by the proteasomal degradation mechanismQ46159185
Dissection of the BCL-2 family signaling network with stabilized alpha-helices of BCL-2 domainsQ46500385
Contributions to Bax insertion and oligomerization of lipids of the mitochondrial outer membraneQ46765170
Optimization and use of peptide mass measurement accuracy in shotgun proteomicsQ50232217
BH1 and BH2 domains of Bcl-2 are required for inhibition of apoptosis and heterodimerization with Bax.Q52514947
TNF-alpha signals apoptosis through a bid-dependent conformational change in Bax that is inhibited by E1B 19KQ64380526
Nonionic detergents induce dimerization among members of the Bcl-2 familyQ73343305
Hierarchical regulation of mitochondrion-dependent apoptosis by BCL-2 subfamiliesQ79370601
Complete activation of Bax by a single site mutationQ80281973
Impact of pH on Bax alpha conformation, oligomerisation and mitochondrial integrationQ81100878
P433issue3
P304page(s)481-492
P577publication date2010-11-01
P1433published inMolecular CellQ3319468
P1476titleBH3-triggered structural reorganization drives the activation of proapoptotic BAX
P478volume40

Reverse relations

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