scholarly article | Q13442814 |
P50 | author | Loren D. Walensky | Q92710996 |
Evripidis Gavathiotis | Q59661942 | ||
P2093 | author name string | Denis E Reyna | |
Marguerite L Davis | |||
Gregory H Bird | |||
P2860 | cites work | tBID, a membrane-targeted death ligand, oligomerizes BAK to release cytochrome c | Q24290118 |
Differential targeting of prosurvival Bcl-2 proteins by their BH3-only ligands allows complementary apoptotic function | Q24293924 | ||
Apoptosis initiated when BH3 ligands engage multiple Bcl-2 homologs, not Bax or Bak | Q24296478 | ||
Proapoptotic Bak is sequestered by Mcl-1 and Bcl-xL, but not Bcl-2, until displaced by BH3-only proteins | Q24302494 | ||
A stapled BID BH3 helix directly binds and activates BAX | Q24307663 | ||
Direct activation of Bax by p53 mediates mitochondrial membrane permeabilization and apoptosis | Q24307994 | ||
Bcl-2 heterodimerizes in vivo with a conserved homolog, Bax, that accelerates programmed cell death | Q24312211 | ||
BID: a novel BH3 domain-only death agonist | Q24320091 | ||
Hematopoietic malignancies demonstrate loss-of-function mutations of BAX | Q24321995 | ||
Membrane binding by tBid initiates an ordered series of events culminating in membrane permeabilization by Bax | Q24323186 | ||
Conformation of the Bax C-terminus regulates subcellular location and cell death | Q24534099 | ||
Activation of apoptosis in vivo by a hydrocarbon-stapled BH3 helix | Q24537504 | ||
Solution structure of BID, an intracellular amplifier of apoptotic signaling | Q27617719 | ||
Solution structure of the proapoptotic molecule BID: a structural basis for apoptotic agonists and antagonists | Q27617723 | ||
Structure of Bax: coregulation of dimer formation and intracellular localization | Q27628839 | ||
Solution structure of the antiapoptotic protein bcl-2 | Q27630598 | ||
The X-ray structure of a BAK homodimer reveals an inhibitory zinc binding site | Q27640443 | ||
Structure of the BH3 domains from the p53-inducible BH3-only proteins Noxa and Puma in complex with Mcl-1 | Q27651003 | ||
BAX activation is initiated at a novel interaction site | Q27652635 | ||
Structure of Bcl-xL-Bak peptide complex: recognition between regulators of apoptosis | Q27734734 | ||
Mass Spectrometric Sequencing of Proteins from Silver-Stained Polyacrylamide Gels | Q27860531 | ||
Using NMRView to visualize and analyze the NMR spectra of macromolecules | Q27860567 | ||
Errors in protein structures | Q27860776 | ||
NMR methods for studying protein-protein interactions involved in translation initiation | Q81390819 | ||
Synthesis and biophysical characterization of stabilized alpha-helices of BCL-2 domains | Q81584715 | ||
NMRPipe: a multidimensional spectral processing system based on UNIX pipes | Q27860859 | ||
GROMACS: fast, flexible, and free | Q27860998 | ||
Proapoptotic BAX and BAK: a requisite gateway to mitochondrial dysfunction and death | Q28363890 | ||
Bim, Bad and Bmf: intrinsically unstructured BH3-only proteins that undergo a localized conformational change upon binding to prosurvival Bcl-2 targets | Q28910218 | ||
Bid, Bax, and lipids cooperate to form supramolecular openings in the outer mitochondrial membrane | Q29616354 | ||
BH3 domains of BH3-only proteins differentially regulate Bax-mediated mitochondrial membrane permeabilization both directly and indirectly | Q29617135 | ||
Distinct BH3 domains either sensitize or activate mitochondrial apoptosis, serving as prototype cancer therapeutics | Q29620467 | ||
Auto-activation of the apoptosis protein Bax increases mitochondrial membrane permeability and is inhibited by Bcl-2 | Q30493313 | ||
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 process | Q33569749 | ||
Bax forms multispanning monomers that oligomerize to permeabilize membranes during apoptosis | Q33854131 | ||
Bax forms an oligomer via separate, yet interdependent, surfaces | Q33885192 | ||
The multidomain proapoptotic molecules Bax and Bak are directly activated by heat | Q34212713 | ||
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, Biophysics | Q36501189 | ||
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 proteins | Q37309119 | ||
BH3-only proteins and their roles in programmed cell death | Q37566201 | ||
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 apoptosis | Q38326924 | ||
Mutagenesis of the BH3 domain of BAX identifies residues critical for dimerization and killing | Q39576297 | ||
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 death | Q40732702 | ||
Bak activation for apoptosis involves oligomerization of dimers via their alpha6 helices | Q43235008 | ||
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 mechanism | Q46159185 | ||
Dissection of the BCL-2 family signaling network with stabilized alpha-helices of BCL-2 domains | Q46500385 | ||
Contributions to Bax insertion and oligomerization of lipids of the mitochondrial outer membrane | Q46765170 | ||
Optimization and use of peptide mass measurement accuracy in shotgun proteomics | Q50232217 | ||
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 19K | Q64380526 | ||
Nonionic detergents induce dimerization among members of the Bcl-2 family | Q73343305 | ||
Hierarchical regulation of mitochondrion-dependent apoptosis by BCL-2 subfamilies | Q79370601 | ||
Complete activation of Bax by a single site mutation | Q80281973 | ||
Impact of pH on Bax alpha conformation, oligomerisation and mitochondrial integration | Q81100878 | ||
P433 | issue | 3 | |
P304 | page(s) | 481-492 | |
P577 | publication date | 2010-11-01 | |
P1433 | published in | Molecular Cell | Q3319468 |
P1476 | title | BH3-triggered structural reorganization drives the activation of proapoptotic BAX | |
P478 | volume | 40 |
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Q39292731 | A unified model of mammalian BCL-2 protein family interactions at the mitochondria. |
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Q36478810 | BH3-in-groove dimerization initiates and helix 9 dimerization expands Bax pore assembly in membranes |
Q39394965 | BH3-only proteins are tail-anchored in the outer mitochondrial membrane and can initiate the activation of Bax |
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