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The N-terminal End of Bax Contains a Mitochondrial-targeting Signal
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What this work says
Outgoing claims: the papers this work cites, builds on, or argues with.
inferredcites →https://doi.org/10.1002/j.1460-2075.1986.tb04364.xopenalex-snapshot
Mitochondrial targeting sequences may form amphiphilic helices.
inferredcites →https://doi.org/10.1006/bbrc.1999.0904openalex-snapshot
The C-Terminus of bax Is Not a Membrane Addressing/Anchoring Signal
inferredcites →https://doi.org/10.1006/excr.2000.4859openalex-snapshot
Cleavage of Bax Enhances Its Cell Death Function
inferredcites →https://doi.org/10.1016/0076-6879(95)60135-xopenalex-snapshot
[10] ATP synthase from Saccharomyces cerevisiae
inferredcites →https://doi.org/10.1016/s0014-5793(00)02330-9openalex-snapshot
The substitution of the C‐terminus of bax by that of bcl‐xL does not affect its subcellular localization but abrogates its pro‐apoptotic properties
inferredcites →https://doi.org/10.1016/s0014-5793(02)02227-5openalex-snapshot
Involvement of the N‐terminus of Bax in its intracellular localization and function
inferredcites →https://doi.org/10.1016/s0014-5793(97)01087-9openalex-snapshot
Release of cytochrome c and decrease of cytochrome c oxidase in Bax‐expressing yeast cells, and prevention of these effects by coexpression of Bcl‐xL
inferredcites →https://doi.org/10.1016/s0014-5793(98)01661-5openalex-snapshot
Role of the C‐terminal domain of Bax and Bcl‐xL in their localization and function in yeast cells
inferredcites →https://doi.org/10.1016/s0021-9258(17)36960-0openalex-snapshot
Assembly of Bcl-2 into microsomal and outer mitochondrial membranes
inferredcites →https://doi.org/10.1016/s0021-9258(18)82073-7openalex-snapshot
Structure-function analysis of the Bcl-2 oncoprotein. Addition of a heterologous transmembrane domain to portions of the Bcl-2 beta protein restores function as a regulator of cell survival
inferredcites →https://doi.org/10.1016/s0021-9258(19)74386-5openalex-snapshot
Targeting of Bcl-2 to the mitochondrial outer membrane by a COOH-terminal signal anchor sequence.
inferredcites →https://doi.org/10.1016/s0960-9822(01)00433-xopenalex-snapshot
Visual neuroscience: Resonating to natural images
inferredcites →https://doi.org/10.1016/s0960-9822(01)00465-1openalex-snapshot
Why do regulators of apoptosis look like bacterial toxins?
inferredcites →https://doi.org/10.1016/s0962-8924(00)01803-1openalex-snapshot
Mitochondria as the central control point of apoptosis
inferredcites →https://doi.org/10.1034/j.1600-0854.2001.20108.xopenalex-snapshot
Targeting of C‐Terminal (Tail)‐Anchored Proteins: Understanding how Cytoplasmic Activities are Anchored to Intracellular Membranes
inferredcites →https://doi.org/10.1038/35048073openalex-snapshot
The mitochondrion in apoptosis: how Pandora's box opens
inferredcites →https://doi.org/10.1074/jbc.273.19.11527openalex-snapshot
An Import Signal in the Cytosolic Domain of theNeurospora Mitochondrial Outer Membrane Protein TOM22
inferredcites →https://doi.org/10.1083/jcb.139.5.1281openalex-snapshot
Movement of Bax from the Cytosol to Mitochondria during Apoptosis
inferredcites →https://doi.org/10.1083/jcb.143.1.207openalex-snapshot
Regulated Targeting of BAX to Mitochondria
inferredcites →https://doi.org/10.1093/emboj/17.4.1029openalex-snapshot
The conserved N‐terminal BH4 domain of Bcl‐2 homologues is essential for inhibition of apoptosis and interaction with CED‐4
inferredcites →https://doi.org/10.1093/emboj/18.9.2330openalex-snapshot
Conformation of the Bax C‐terminus regulates subcellular location and cell death
inferredcites →https://doi.org/10.1093/emboj/20.22.6306openalex-snapshot
Damage‐induced Bax N‐terminal change, translocation to mitochondria and formation of Bax dimers/complexes occur regardless of cell fate
inferredcites →https://doi.org/10.1093/hmg/11.6.675openalex-snapshot
The expression of a new variant of the pro-apoptotic molecule Bax, Baxpsi, is correlated with an increased survival of glioblastoma multiforme patients
inferredcites →https://doi.org/10.1101/gad.13.15.1899openalex-snapshot
BCL-2 family members and the mitochondria in apoptosis
inferredcites →https://doi.org/10.1111/j.1432-1033.1995.tb20354.xopenalex-snapshot
Import and Insertion of Proteins into the Mitochondrial Outer Membrane
inferredcites →https://doi.org/10.1126/science.281.5381.1322openalex-snapshot
The Bcl-2 Protein Family: Arbiters of Cell Survival
inferredcites →https://doi.org/10.1128/mcb.16.11.6494openalex-snapshot
Structure-Function Comparisons of the Proapoptotic Protein Bax in Yeast and Mammalian Cells
inferredcites →https://doi.org/10.1128/mcb.20.5.1604-1615.2000openalex-snapshot
The Putative Pore-Forming Domain of Bax Regulates Mitochondrial Localization and Interaction with Bcl-XL
What points at this work
Incoming claims: where this work appears in other papers’ reference lists and arguments.
inferred← citeshttps://doi.org/10.1002/med.21379openalex-snapshot
Direct Activation of Bax Protein for Cancer Therapy
inferred← citeshttps://doi.org/10.1002/psc.803openalex-snapshot
Pro‐apoptotic bax‐α1 synthesis and evidence for β‐sheet to α‐helix conformational change as triggered by negatively charged lipid membranes
inferred← citeshttps://doi.org/10.1007/978-1-59745-336-3_18openalex-snapshot
Microtubule Damaging Agents and Apoptosis
inferred← citeshttps://doi.org/10.1007/s10495-006-8882-9openalex-snapshot
Protein tyrosine phosphatase interacting protein 51 (PTPIP51) is a novel mitochondria protein with an N-terminal mitochondrial targeting sequence and induces apoptosis
inferred← citeshttps://doi.org/10.1007/s10495-007-0749-1openalex-snapshot
Bax activation and mitochondrial insertion during apoptosis
inferred← citeshttps://doi.org/10.1007/s10495-007-0758-0openalex-snapshot
The mitochondrial pathway in yeast apoptosis
inferred← citeshttps://doi.org/10.1007/s10495-009-0410-2openalex-snapshot
The Bax carboxy-terminal hydrophobic helix does not determine organelle-specific targeting but is essential for maintaining Bax in an inactive state and for stable mitochondrial membrane insertion
inferred← citeshttps://doi.org/10.1007/s10540-007-9061-0openalex-snapshot
An Artificial Mitochondrial Tail Signal/Anchor Sequence Confirms a Requirement for Moderate Hydrophobicity for Targeting
inferred← citeshttps://doi.org/10.1007/s10695-016-0225-3openalex-snapshot
Cloning and characterization of Bax1 and Bax2 genes of Ctenopharyngodon idellus and evaluation of transcript expression in response to grass carp reovirus infection
inferred← citeshttps://doi.org/10.1007/s10863-005-6570-zopenalex-snapshot
The Role of the Mitochondrial Apoptosis Induced Channel MAC in Cytochrome c Release
inferred← citeshttps://doi.org/10.1007/s10863-009-9202-1openalex-snapshot
Conformational changes and protein stability of the pro-apoptotic protein Bax
inferred← citeshttps://doi.org/10.1007/s11010-010-0631-2openalex-snapshot
Prevention of apoptosis by the interaction between FIH1 and Bax
inferred← citeshttps://doi.org/10.1016/b978-0-12-809633-8.12017-5openalex-snapshot
Mechanisms Controlling the Activity of Localization Signal Sequences
inferred← citeshttps://doi.org/10.1016/j.bbabio.2006.05.032openalex-snapshot
Mitochondria as the target of the pro-apoptotic protein Bax
inferred← citeshttps://doi.org/10.1016/j.bbabio.2011.01.001openalex-snapshot
Microtubule-targeted agents: When mitochondria become essential to chemotherapy
inferred← citeshttps://doi.org/10.1016/j.bbadis.2005.07.002openalex-snapshot
Regulation of the mitochondrial apoptosis-induced channel, MAC, by BCL-2 family proteins
inferred← citeshttps://doi.org/10.1016/j.bbamcr.2003.07.001openalex-snapshot
There is more to life and death than mitochondria: Bcl-2 proteins at the endoplasmic reticulum
inferred← citeshttps://doi.org/10.1016/j.bbamcr.2007.12.013openalex-snapshot
The pleiotropic effects of heterologous Bax expression in yeast
inferred← citeshttps://doi.org/10.1016/j.bbamcr.2008.03.010openalex-snapshot
Mitochondria-dependent apoptosis in yeast
inferred← citeshttps://doi.org/10.1016/j.bbamcr.2010.12.019openalex-snapshot
Molecular biology of Bax and Bak activation and action
inferred← citeshttps://doi.org/10.1016/j.bbamem.2008.12.014openalex-snapshot
How does the Bax-α1 targeting sequence interact with mitochondrial membranes? The role of cardiolipin
inferred← citeshttps://doi.org/10.1016/j.bbamem.2011.10.007openalex-snapshot
Interaction of the full-length Bax protein with biomimetic mitochondrial liposomes: A small-angle neutron scattering and fluorescence study
inferred← citeshttps://doi.org/10.1016/j.bbamem.2017.03.010openalex-snapshot
The substitution of Proline 168 favors Bax oligomerization and stimulates its interaction with LUVs and mitochondria
inferred← citeshttps://doi.org/10.1016/j.bbamem.2022.184075openalex-snapshot
Cell-Free Synthesis and Reconstitution of Bax in Nanodiscs: Comparison between Wild-Type Bax and a Constitutively Active Mutant
inferred← citeshttps://doi.org/10.1016/j.bbrc.2005.10.081openalex-snapshot
Mitochondrial localization of μ-calpain
inferred← citeshttps://doi.org/10.1016/j.bbrc.2017.12.156openalex-snapshot
BaxΔ2 sensitizes colorectal cancer cells to proteasome inhibitor-induced cell death
inferred← citeshttps://doi.org/10.1016/j.biocel.2004.05.018openalex-snapshot
β-Phenylethyl isothiocyanate mediated apoptosis; contribution of Bax and the mitochondrial death pathway
inferred← citeshttps://doi.org/10.1016/j.biocel.2017.12.004openalex-snapshot
N-terminal acetylation modulates Bax targeting to mitochondria
inferred← citeshttps://doi.org/10.1016/j.cellsig.2006.08.019openalex-snapshot
The pro-inflammatory oxidant hypochlorous acid induces Bax-dependent mitochondrial permeabilisation and cell death through AIF-/EndoG-dependent pathways
inferred← citeshttps://doi.org/10.1016/j.cellsig.2018.01.022openalex-snapshot
PNMA family: Protein interaction network and cell signalling pathways implicated in cancer and apoptosis
inferred← citeshttps://doi.org/10.1016/j.chemphyslip.2014.05.003openalex-snapshot
Functions of the C-terminal domains of apoptosis-related proteins of the Bcl-2 family
inferred← citeshttps://doi.org/10.1016/j.febslet.2004.10.080openalex-snapshot
Impact of pH on Bax α conformation, oligomerisation and mitochondrial integration
inferred← citeshttps://doi.org/10.1016/j.febslet.2008.07.047openalex-snapshot
Bax inserts into the mitochondrial outer membrane by different mechanisms
inferred← citeshttps://doi.org/10.1016/j.jsb.2008.07.004openalex-snapshot
The interaction of the Bax C-terminal domain with negatively charged lipids modifies the secondary structure and changes its way of insertion into membranes
inferred← citeshttps://doi.org/10.1016/j.micpath.2019.103892openalex-snapshot
The role of Bax in the apoptosis of Leishmania-infected macrophages
inferred← citeshttps://doi.org/10.1016/j.mito.2013.01.004openalex-snapshot
The N-terminal helix of Bcl-xL targets mitochondria
inferred← citeshttps://doi.org/10.1016/j.molcel.2004.10.028openalex-snapshot
The First α Helix of Bax Plays a Necessary Role in Its Ligand-Induced Activation by the BH3-Only Proteins Bid and PUMA
inferred← citeshttps://doi.org/10.1016/j.molcel.2009.09.030openalex-snapshot
Stepwise Activation of BAX and BAK by tBID, BIM, and PUMA Initiates Mitochondrial Apoptosis
inferred← citeshttps://doi.org/10.1016/j.neuro.2009.06.001openalex-snapshot
Cadmium exposure induces mitochondria-dependent apoptosis in oligodendrocytes
inferred← citeshttps://doi.org/10.1016/j.yexcr.2017.08.016openalex-snapshot
The functional domains for Bax∆2 aggregate-mediated caspase 8-dependent cell death
inferred← citeshttps://doi.org/10.1016/j.ymeth.2013.03.030openalex-snapshot
BAK/BAX activation and cytochrome c release assays using isolated mitochondria
inferred← citeshttps://doi.org/10.1016/s1567-1356(03)00143-0openalex-snapshot
Yeast as a tool to study Bax/mitochondrial interactions in cell death
inferred← citeshttps://doi.org/10.1021/bi035348wopenalex-snapshot
Transbilayer Lipid Diffusion Promoted by Bax: Implications for Apoptosis
inferred← citeshttps://doi.org/10.1021/bi036044copenalex-snapshot
Membrane-Insertion Fragments of Bcl-xL, Bax, and Bid
inferred← citeshttps://doi.org/10.1038/cdd.2008.39openalex-snapshot
Bax targeting to mitochondria occurs via both tail anchor-dependent and -independent mechanisms
inferred← citeshttps://doi.org/10.1038/cddis.2014.410openalex-snapshot
Synergistic anti-tumor activity and inhibition of angiogenesis by cotargeting of oncogenic and death receptor pathways in human melanoma
inferred← citeshttps://doi.org/10.1038/embor.2012.19openalex-snapshot
Non‐apoptotic functions of apoptosis‐regulatory proteins
inferred← citeshttps://doi.org/10.1038/s41418-018-0184-6openalex-snapshot
Topology of active, membrane-embedded Bax in the context of a toroidal pore
inferred← citeshttps://doi.org/10.1038/s41420-024-02108-xopenalex-snapshot
The membrane insertion of the pro-apoptotic protein Bax is a Tom22-dependent multi-step process: a study in nanodiscs
inferred← citeshttps://doi.org/10.1038/s41420-026-03066-2openalex-snapshot
A unified therapeutic theory for treating cancer via master regulators of the universal apoptosis network
inferred← citeshttps://doi.org/10.1038/sj.cdd.4401270openalex-snapshot
Investigation of the role of the C-terminus of Bax and of tc-Bid on Bax interaction with yeast mitochondria
inferred← citeshttps://doi.org/10.1038/sj.cdd.4401992openalex-snapshot
BCL-2 in the crosshairs: tipping the balance of life and death
inferred← citeshttps://doi.org/10.1038/sj.cdd.4402025openalex-snapshot
Elucidation of some Bax conformational changes through crystallization of an antibody–peptide complex
inferred← citeshttps://doi.org/10.1038/sj.cdd.4402055openalex-snapshot
TOM22, a core component of the mitochondria outer membrane protein translocation pore, is a mitochondrial receptor for the proapoptotic protein Bax
inferred← citeshttps://doi.org/10.1038/sj.emboj.7600675openalex-snapshot
Bax forms multispanning monomers that oligomerize to permeabilize membranes during apoptosis
inferred← citeshttps://doi.org/10.1038/sj.jid.5700533openalex-snapshot
AKT Delays the Early-Activated Apoptotic Pathway in UVB-Irradiated Keratinocytes Via BAD Translocation
inferred← citeshttps://doi.org/10.1038/sj.onc.1210044openalex-snapshot
Nucleophosmin is a novel Bax chaperone that regulates apoptotic cell death
inferred← citeshttps://doi.org/10.1038/sj.onc.1210303openalex-snapshot
Increase in PGE2 biosynthesis induces a Bax dependent apoptosis correlated to patients’ survival in glioblastoma multiforme
inferred← citeshttps://doi.org/10.1038/sj.onc.1210439openalex-snapshot
Arsenic trioxide-induced neuroblastoma cell death is accompanied by proteolytic activation of nuclear Bax
inferred← citeshttps://doi.org/10.1038/sj.onc.1210517openalex-snapshot
Complete activation of Bax by a single site mutation
inferred← citeshttps://doi.org/10.1042/bj20031152openalex-snapshot
Bax-induced cytochrome c release from mitochondria depends on alpha-helices-5 and -6
inferred← citeshttps://doi.org/10.1073/pnas.0402293101openalex-snapshot
Constitutive association of the proapoptotic protein Bim with Bcl-2-related proteins on mitochondria in T cells
inferred← citeshttps://doi.org/10.1073/pnas.0500676102openalex-snapshot
Dual targeting of the protein disulfide isomerase RB60 to the chloroplast and the endoplasmic reticulum
inferred← citeshttps://doi.org/10.1074/jbc.m109.049924openalex-snapshot
Bax Contains Two Functional Mitochondrial Targeting Sequences and Translocates to Mitochondria in a Conformational Change- and Homo-oligomerization-driven Process
inferred← citeshttps://doi.org/10.1074/jbc.m112.374785openalex-snapshot
BaxΔ2 Is a Novel Bax Isoform Unique to Microsatellite Unstable Tumors
inferred← citeshttps://doi.org/10.1074/jbc.m308408200openalex-snapshot
An Anti-apoptotic Viral Protein That Recruits Bax to Mitochondria
inferred← citeshttps://doi.org/10.1074/jbc.m308436200openalex-snapshot
Mmm1p Spans Both the Outer and Inner Mitochondrial Membranes and Contains Distinct Domains for Targeting and Foci Formation
inferred← citeshttps://doi.org/10.1074/jbc.m311922200openalex-snapshot
The p18 Truncated Form of Bax Behaves Like a Bcl-2 Homology Domain 3-only Protein
inferred← citeshttps://doi.org/10.1074/jbc.m408373200openalex-snapshot
Studies of the Interaction of Substituted Mutants of BAX with Yeast Mitochondria Reveal That the C-terminal Hydrophobic α-Helix Is a Second ART Sequence and Plays a Role in the Interaction with Anti-apoptotic BCL-xL
inferred← citeshttps://doi.org/10.1074/jbc.m409714200openalex-snapshot
Distinct Domains Control the Addressing and the Insertion of Bax into Mitochondria
inferred← citeshttps://doi.org/10.1074/jbc.m511182200openalex-snapshot
Mitochondrial and Nuclear Forms of Wnt13 Are Generated via Alternative Promoters, Alternative RNA Splicing, and Alternative Translation Start Sites
inferred← citeshttps://doi.org/10.1074/jbc.m607444200openalex-snapshot
Evaluation of the Roles of Apoptosis, Autophagy, and Mitophagy in the Loss of Plating Efficiency Induced by Bax Expression in Yeast
inferred← citeshttps://doi.org/10.1074/jbc.m703155200openalex-snapshot
The Mitochondrial TOM Complex Is Required for tBid/Bax-induced Cytochrome c Release
inferred← citeshttps://doi.org/10.1074/jbc.m703823200openalex-snapshot
Control of Bax Homodimerization by Its Carboxyl Terminus
inferred← citeshttps://doi.org/10.1074/jbc.m704891200openalex-snapshot
Substitutions of Potentially Phosphorylatable Serine Residues of Bax Reveal How They May Regulate Its Interaction with Mitochondria
inferred← citeshttps://doi.org/10.1083/jcb.200309013openalex-snapshot
Conformational control of Bax localization and apoptotic activity by Pro168
inferred← citeshttps://doi.org/10.1089/152308604322899323openalex-snapshot
Utilization of Yeast To Investigate the Role of Lipid Oxidation in Cell Death
inferred← citeshttps://doi.org/10.1111/j.1471-4159.2004.02572.xopenalex-snapshot
Mitochondrial mechanisms of neural cell apoptosis
inferred← citeshttps://doi.org/10.1111/j.1600-0854.2007.00661.xopenalex-snapshot
A Bioinformatics Approach to Identifying Tail‐Anchored Proteins in the Human Genome
inferred← citeshttps://doi.org/10.1128/jvi.02710-07openalex-snapshot
Cytomegalovirus Proteins vMIA and m38.5 Link Mitochondrial Morphogenesis to Bcl-2 Family Proteins
inferred← citeshttps://doi.org/10.1128/mcb.00161-10openalex-snapshot
Bax Activation by Engagement with, Then Release from, the BH3 Binding Site of Bcl-x L
inferred← citeshttps://doi.org/10.1158/0008-5472.can-05-2097openalex-snapshot
The Small Organic Compound HA14-1 Prevents Bcl-2 Interaction with Bax to Sensitize Malignant Glioma Cells to Induction of Cell Death
inferred← citeshttps://doi.org/10.1158/1541-7786.mcr-14-0162openalex-snapshot
BaxΔ2 Promotes Apoptosis through Caspase-8 Activation in Microsatellite-Unstable Colon Cancer
inferred← citeshttps://doi.org/10.1186/1471-2121-10-50openalex-snapshot
Evidence for a mitochondrial localization of the retinoblastoma protein
inferred← citeshttps://doi.org/10.1186/1471-2121-8-16openalex-snapshot
The N-terminus and alpha-5, alpha-6 helices of the pro-apoptotic protein Bax, modulate functional interactions with the anti-apoptotic protein Bcl-xL
inferred← citeshttps://doi.org/10.1371/journal.pone.0009066openalex-snapshot
Active Fragments from Pro- and Antiapoptotic BCL-2 Proteins Have Distinct Membrane Behavior Reflecting Their Functional Divergence
inferred← citeshttps://doi.org/10.15698/mic2015.03.193openalex-snapshot
Yeast as a tool for studying proteins of the Bcl-2 family
inferred← citeshttps://doi.org/10.15698/mic2016.12.547openalex-snapshot
Bax mitochondrial relocation is linked to its phosphorylation and its interaction with Bcl-xL
inferred← citeshttps://doi.org/10.18297/etd/155openalex-snapshot
Mitochondrial targeting of the pro-apoptotic protein Bax : Role of the Bax carboxy-terminal tail.
inferred← citeshttps://doi.org/10.2174/138161211795049651openalex-snapshot
The Importance of Humanized Yeast to Better Understand the Role of Bcl-2 Family in Apoptosis: Finding of Novel Therapeutic Opportunities
inferred← citeshttps://doi.org/10.2174/187152612798994948openalex-snapshot
Viral Product Trafficking to Mitochondria, Mechanisms and Roles in Pathogenesis
inferred← citeshttps://doi.org/10.22159/ajpcr.2017.v10i7.19063openalex-snapshot
THE BIOPHYSICAL CHARACTERISTICS AND STRUCTURAL EXPLORATION OF PROGRAMMED CELL DEATH REGULATOR B-CELL LYMPHOMA 2-ASSOCIATED X PROTEIN OF CHINESE LIVER FLUKE (CLONORCHIS SINENSIS)
inferred← citeshttps://doi.org/10.2741/3471openalex-snapshot
The mitochondrial outer membrane protein import machinery: a new player in apoptosis?
inferred← citeshttps://doi.org/10.3389/fcell.2018.00013openalex-snapshot
Subcellular Localization and Dynamics of the Bcl-2 Family of Proteins
inferred← citeshttps://doi.org/10.3389/fonc.2022.1068994openalex-snapshot
Non-phosphorylatable mutants of Ser184 lead to incomplete activation of Bax
inferred← citeshttps://doi.org/10.3390/biom12020162openalex-snapshot
Bcl-2 Family Members and the Mitochondrial Import Machineries: The Roads to Death
inferred← citeshttps://doi.org/10.3390/genes11020145openalex-snapshot
Reconstituting the Mammalian Apoptotic Switch in Yeast
inferred← citeshttps://doi.org/10.3410/f.732787375.793565300openalex-snapshot
Faculty Opinions recommendation of Subcellular Localization and Dynamics of the Bcl-2 Family of Proteins.
inferred← citeshttps://doi.org/10.37349/etat.2022.00076openalex-snapshot
Yeast as a tool to decipher the molecular mechanisms underlying the functions of Bcl-2 family
inferred← citeshttps://doi.org/10.3969/j.issn.1673-5374.2012.17.006openalex-snapshot
Apoptosis-related protein expression in rabbits with blast brain injury following early hyperbaric oxygen therapy.
inferred← citeshttps://doi.org/10.4049/jimmunol.173.10.6220openalex-snapshot
The Bax N Terminus Is Required for Negative Regulation by the Mitogen-Activated Protein Kinase Kinase and Akt Signaling Pathways in T Cells
inferred← citeshttps://doi.org/10.4161/cc.4.5.1671openalex-snapshot
Activation of Bax by BH3 Domains during Apoptosis:The zunfolding of a Deadly Plot
inferred← citeshttps://doi.org/10.70675/0e2f7ca1z6260z4fc4zb883z94ab06e6c670openalex-snapshot
Etude des régions d'insertion membranaire des protéines de la famille Bcl-2 et conception de "poropetides" anticancéreux
inferred← citeshttps://doi.org/10.70675/1f03460cze5d6z42c6za18ez352e34a4dee4openalex-snapshot
Rôles des régulateurs de l’apoptose Bcl-wav et Nrz, au cours du développement embryonnaire du poisson zèbre
inferred← citeshttps://doi.org/10.70675/21fc59dcz18e1z4490z8916zceb56eb3779copenalex-snapshot
Régulations de la protéine proapoptotique Bax : rôle des kinases Akt et GSK-3β et de la protéine antiapoptotique Bcl-xL
inferred← citeshttps://doi.org/10.70675/5ffd7262za032z4230zbbaaz9d8a596af7fcopenalex-snapshot
L'insertion membranaire de la protéine pro-apoptotique Bax est un processus muti-étapes dépendant de TOM22
inferred← citeshttps://doi.org/10.70675/d1fa4100z5c50z4a30z9f26z0ee43285ce5fopenalex-snapshot
Involvements of Bcl-2 family of proteins during early zebrafish development
inferred← citeshttps://doi.org/10.7936/k7rb72m2openalex-snapshot
Regulation of BAX/BAK-Dependent Cell Death Program
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