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https://doi.org/10.2139/ssrn.4143267

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inferredcites →https://doi.org/10.1002/1873-3468.12030openalex-extracted
Regulation of Bax/mitochondria interaction by AKT
inferredcites →https://doi.org/10.1002/bip.1981.360201209openalex-extracted
Nmr studies of the rates of proline cis – trans isomerization in oligopeptides
inferredcites →https://doi.org/10.1006/bbrc.1999.0904openalex-extracted
The C-Terminus of bax Is Not a Membrane Addressing/Anchoring Signal
inferredcites →https://doi.org/10.1006/prep.1998.1010openalex-extracted
Expression and Purification of Full-Length Human Bax α
inferredcites →https://doi.org/10.1007/s10495-007-0749-1openalex-extracted
Bax activation and mitochondrial insertion during apoptosis
inferredcites →https://doi.org/10.1016/0003-2697(86)90241-1openalex-extracted
Analysis of protein circular dichroism spectra for secondary structure using a simple matrix multiplication
inferredcites →https://doi.org/10.1016/bs.mie.2021.02.003openalex-extracted
Combining in vitro translation with nanodisc technology and functional reconstitution of channels in planar lipid bilayers
inferredcites →https://doi.org/10.1016/j.bbamem.2017.03.010openalex-extracted
The substitution of Proline 168 favors Bax oligomerization and stimulates its interaction with LUVs and mitochondria
inferredcites →https://doi.org/10.1016/j.biocel.2015.03.020openalex-extracted
Bcl-xL stimulates Bax relocation to mitochondria and primes cells to ABT-737
inferredcites →https://doi.org/10.1016/j.cell.2011.02.034openalex-extracted
Bcl-xL Retrotranslocates Bax from the Mitochondria into the Cytosol
inferredcites →https://doi.org/10.1016/j.cell.2012.12.031openalex-extracted
Bax Crystal Structures Reveal How BH3 Domains Activate Bax and Nucleate Its Oligomerization to Induce Apoptosis
inferredcites →https://doi.org/10.1016/j.febslet.2008.07.047openalex-extracted
Bax inserts into the mitochondrial outer membrane by different mechanisms
inferredcites →https://doi.org/10.1016/j.febslet.2011.12.003openalex-extracted
The cytosolic domain of human Tom22 modulates human Bax mitochondrial translocation and conformation in yeast
inferredcites →https://doi.org/10.1016/j.molcel.2012.12.022openalex-extracted
Bax Exists in a Dynamic Equilibrium between the Cytosol and Mitochondria to Control Apoptotic Priming
inferredcites →https://doi.org/10.1016/j.molcel.2014.10.028openalex-extracted
Mitochondrial Shape Governs BAX-Induced Membrane Permeabilization and Apoptosis
inferredcites →https://doi.org/10.1016/j.molcel.2016.06.010openalex-extracted
An Autoinhibited Dimeric Form of BAX Regulates the BAX Activation Pathway
inferredcites →https://doi.org/10.1016/j.pep.2016.02.010openalex-extracted
Characterization of the membrane-inserted C-terminus of cytoprotective BCL-XL
inferredcites →https://doi.org/10.1016/j.str.2019.03.013openalex-extracted
Biophysical Characterization of a Nanodisc with and without BAX: An Integrative Study Using Molecular Dynamics Simulations and Cryo-EM
inferredcites →https://doi.org/10.1016/j.tibtech.2009.05.005openalex-extracted
Membrane protein expression: no cells required
inferredcites →https://doi.org/10.1016/j.tips.2021.11.001openalex-extracted
Physiological and pharmacological modulation of BAX
inferredcites →https://doi.org/10.1016/s0014-5793(00)01404-6openalex-extracted
A cytochrome c–GFP fusion is not released from mitochondria into the cytoplasm upon expression of Bax in yeast cells
inferredcites →https://doi.org/10.1016/s0014-5793(00)02330-9openalex-extracted
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-extracted
Involvement of the N‐terminus of Bax in its intracellular localization and function
inferredcites →https://doi.org/10.1016/s0092-8674(00)00167-7openalex-extracted
Structure of Bax
inferredcites →https://doi.org/10.1016/s0092-8674(02)01036-xopenalex-extracted
Bid, Bax, and Lipids Cooperate to Form Supramolecular Openings in the Outer Mitochondrial Membrane
inferredcites →https://doi.org/10.1017/s0033583521000044openalex-extracted
Amphipathic environments for determining the structure of membrane proteins by single-particle electron cryo-microscopy
inferredcites →https://doi.org/10.1021/acs.jpcb.0c03374openalex-extracted
Confinement in Nanodiscs Anisotropically Modifies Lipid Bilayer Elastic Properties
inferredcites →https://doi.org/10.1021/ja0393574openalex-extracted
Directed Self-Assembly of Monodisperse Phospholipid Bilayer Nanodiscs with Controlled Size
inferredcites →https://doi.org/10.1021/ja1030613openalex-extracted
Elliptical Structure of Phospholipid Bilayer Nanodiscs Encapsulated by Scaffold Proteins: Casting the Roles of the Lipids and the Protein
inferredcites →https://doi.org/10.1038/35019596openalex-extracted
BAX-dependent transport of cytochrome c reconstituted in pure liposomes
inferredcites →https://doi.org/10.1038/cdd.2008.39openalex-extracted
Bax targeting to mitochondria occurs via both tail anchor-dependent and -independent mechanisms
inferredcites →https://doi.org/10.1038/cdd.2013.153openalex-extracted
The rheostat in the membrane: BCL-2 family proteins and apoptosis
inferredcites →https://doi.org/10.1038/cdd.2017.161openalex-extracted
The BCL-2 arbiters of apoptosis and their growing role as cancer targets
inferredcites →https://doi.org/10.1038/cddis.2013.210openalex-extracted
Three-dimensional structure of Bax-mediated pores in membrane bilayers
inferredcites →https://doi.org/10.1038/ncomms10731openalex-extracted
Tripartite assembly of RND multidrug efflux pumps
inferredcites →https://doi.org/10.1038/ncomms5935openalex-extracted
Small-molecule Bax agonists for cancer therapy
inferredcites →https://doi.org/10.1038/ni.1697openalex-extracted
The peptidyl-prolyl isomerase Pin1 facilitates cytokine-induced survival of eosinophils by suppressing Bax activation
inferredcites →https://doi.org/10.1038/nprot.2007.426openalex-extracted
Preparative scale expression of membrane proteins in Escherichia coli-based continuous exchange cell-free systems
inferredcites →https://doi.org/10.1038/nsmb.3195openalex-extracted
Nanodiscs for structural and functional studies of membrane proteins
inferredcites →https://doi.org/10.1038/s41418-018-0184-6openalex-extracted
Topology of active, membrane-embedded Bax in the context of a toroidal pore
inferredcites →https://doi.org/10.1038/sj.cdd.4402055openalex-extracted
TOM22, a core component of the mitochondria outer membrane protein translocation pore, is a mitochondrial receptor for the proapoptotic protein Bax
inferredcites →https://doi.org/10.1042/bj3450271openalex-extracted
Bax oligomerization is required for channel-forming activity in liposomes and to trigger cytochrome c release from mitochondria
inferredcites →https://doi.org/10.1073/pnas.81.7.2035openalex-extracted
Cloning and expression of the gene for bacteriophage T7 RNA polymerase.
inferredcites →https://doi.org/10.1074/jbc.272.21.13829openalex-extracted
Nonionic Detergents Induce Dimerization among Members of the Bcl-2 Family
inferredcites →https://doi.org/10.1074/jbc.c200524200openalex-extracted
The Kinetics of Translocation of Smac/DIABLO from the Mitochondria to the Cytosol in HeLa Cells
inferredcites →https://doi.org/10.1074/jbc.m003807200openalex-extracted
The Destabilization of Lipid Membranes Induced by the C-terminal Fragment of Caspase 8-cleaved Bid Is Inhibited by the N-terminal Fragment
inferredcites →https://doi.org/10.1074/jbc.m208955200openalex-extracted
The N-terminal End of Bax Contains a Mitochondrial-targeting Signal
inferredcites →https://doi.org/10.1074/jbc.m400063200openalex-extracted
×Phosphorylation of Bax Ser184 by Akt Regulates Its Activity and Apoptosis in Neutrophils
inferredcites →https://doi.org/10.1074/jbc.m405153200openalex-extracted
The Mitochondrial Apoptosis-induced Channel (MAC) Corresponds to a Late Apoptotic Event
inferredcites →https://doi.org/10.1074/jbc.m408373200openalex-extracted
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
inferredcites →https://doi.org/10.1074/jbc.m409714200openalex-extracted
Distinct Domains Control the Addressing and the Insertion of Bax into Mitochondria
inferredcites →https://doi.org/10.1074/jbc.m500084200openalex-extracted
Nicotine Inactivation of the Proapoptotic Function of Bax through Phosphorylation
inferredcites →https://doi.org/10.1074/jbc.m703155200openalex-extracted
The Mitochondrial TOM Complex Is Required for tBid/Bax-induced Cytochrome c Release
inferredcites →https://doi.org/10.1074/jbc.m704891200openalex-extracted
Substitutions of Potentially Phosphorylatable Serine Residues of Bax Reveal How They May Regulate Its Interaction with Mitochondria
inferredcites →https://doi.org/10.1074/jbc.m708426200openalex-extracted
Differential Regulation of Bax and Bak by Anti-apoptotic Bcl-2 Family Proteins Bcl-B and Mcl-1
inferredcites →https://doi.org/10.1074/jbc.m806610200openalex-extracted
Assembly of the Mitochondrial Apoptosis-induced Channel, MAC
inferredcites →https://doi.org/10.1083/jcb.143.1.207openalex-extracted
Regulated Targeting of BAX to Mitochondria
inferredcites →https://doi.org/10.1083/jcb.200107057openalex-extracted
A novel, high conductance channel of mitochondria linked to apoptosis in mammalian cells and Bax expression in yeast
inferredcites →https://doi.org/10.1083/jcb.200210084openalex-extracted
Characterization of the signal that directs Bcl-xL, but not Bcl-2, to the mitochondrial outer membrane
inferredcites →https://doi.org/10.1083/jcb.200309013openalex-extracted
Conformational control of Bax localization and apoptotic activity by Pro168
inferredcites →https://doi.org/10.1091/mbc.e04-12-1111openalex-extracted
Oligomeric Bax Is a Component of the Putative Cytochrome c Release Channel MAC, Mitochondrial Apoptosis-induced Channel
inferredcites →https://doi.org/10.1093/bioinformatics/btl327openalex-extracted
A reference database for circular dichroism spectroscopy covering fold and secondary structure space
inferredcites →https://doi.org/10.1093/emboj/20.23.6627openalex-extracted
Apoptosis‐associated release of Smac/DIABLO from mitochondria requires active caspases and is blocked by Bcl‐2
inferredcites →https://doi.org/10.1093/hmg/11.6.675openalex-extracted
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/10.15252/embj.201592789openalex-extracted
Bax assembles into large ring‐like structures remodeling the mitochondrial outer membrane in apoptosis
inferredcites →https://doi.org/10.15252/embj.201593384openalex-extracted
Bax assembly into rings and arcs in apoptotic mitochondria is linked to membrane pores
inferredcites →https://doi.org/10.15252/embr.201745235openalex-extracted
Phosphorylation switches Bax from promoting to inhibiting apoptosis thereby increasing drug resistance
inferredcites →https://doi.org/10.1529/biophysj.104.046896openalex-extracted
Molecular Dynamics Simulations of Discoidal Bilayers Assembled from Truncated Human Lipoproteins
inferredcites →https://doi.org/10.15698/mic2016.12.547openalex-extracted
Bax mitochondrial relocation is linked to its phosphorylation and its interaction with Bcl-xL
inferredcites →https://doi.org/10.3109/09687688.2012.762125openalex-extracted
Close allies in membrane protein research: Cell-free synthesis and nanotechnology
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