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ProteomicsDynamic re-configuration of pro-apoptotic BAK on membranes
BAK and BAX, the effectors of intrinsic apoptosis, undergo major reconfiguration to an activated conformer that self-associates to damage mitochondria and cause cell death. However, the dynamic structural mechanisms that describe this reconfiguration in the presence of a membrane have yet to be full...
ORGANISM(S): Homo sapiens (Human) 
2021-08-09 | PXD027288 | Pride
Bak Apoptosis Hdx 
TranscriptomicsWild type mouse embryonic fibroblasts (MEF) vs Bax/BAK double knock out MEF treated with and without Nocodazole
MEF WT, MEF DKO(Bax/Bak), MEF DKO(Bax/Bak) expressing rabbit Serca2a, MEF DKO(Bax/Bak) expressing Bak at the endoplasmic reticulum both control and treated with Noco 100 nM for 48h
ORGANISM(S): Mus musculus 
2023-06-12 | E-MTAB-10997 | biostudies-arrayexpress
ProteomicsIdentification of proteins that interact with the latch domain of BAK
Previous results show that the latch domain of BAK is able to trigger an autophagic response that has atypical features. Identification of a mutant form that lacks the activity (including 5 mutations, 5M version) allowed the design of a proteomics project directed to find proteins that specifically ...
ORGANISM(S): Homo sapiens (Human) 
2025-03-10 | PXD045985 | Pride
Autophagy Apoptosis Bak 
ProteomicsThe bacterial porin OmpA is an inhibitor of Bak-activation at mitochondria and blocks apoptosis of human cells infected with Chlamydia trachomatis
Many infectious agents have the need to inhibit host apoptosis, and various strategies are known. Chlamydia trachomatis is an obligate intracellular bacterium replicating in a vacuole in the human cytosol. Chlamydia-infected human cells are strongly protected against apoptosis. We here mapped this a...
ORGANISM(S): Homo sapiens (Human) 
2026-01-26 | PXD011848 | Pride
Ompa Mitochondria Chlamydia trachomatis Apoptosis Bcl-2 
GenomicsComputational design of potent and selective BAK and BAX binders
Computational design of potent and selective BAK and BAX binders
PRJNA1107244 | ENA
ProteomicsMitochondrial E3 ubiquitin ligase MARCHF5 controls BAK function independently of BH3-only proteins
Intrinsic apoptosis is principally regulated by the BCL-2 family of proteins, but some non-BCL-2 proteins also serve as important regulators. To identify novel apoptosis regulators, we performed a genome-wide CRISPR-Cas9 library screen, and it identified the mitochondrial E3 ubiquitin ligase MARCHF5...
ORGANISM(S): Mus musculus (Mouse) 
2022-09-25 | PXD030246 | Pride
Apoptosis  bak  bcl-2  marchf5/mitol  e3 ubiquitin ligase  mitochondria  bh3 mimetic 
GenomicsVDAC2 primes Myeloma cells for BAK-dependent apoptosis by stabilizing BAK and not BAX and represents a novel therapeutic target
VDAC2 primes Myeloma cells for BAK-dependent apoptosis by stabilizing BAK and not BAX and represents a novel therapeutic target
PRJNA1168568 | ENA
ProteomicsVDAC2 promotes BAX apoptotic activity
Intrinsic apoptosis is critical for normal physiology including the prevention of tumor formation. BAX and BAK, which are essential for mediating this process and for the cytotoxic action of many anti-cancer drugs, are thought to be regulated through similar mechanisms and act redundantly to drive a...
ORGANISM(S): Mus musculus (Mouse) 
2018-10-29 | PXD011195 | Pride
Cancer Bak Bax Mitochondria Voltage-dependent anion channel. Bcl-2 Apoptosis 
ProteomicsAPEX2 of BAX, BAK and DRP1 in healthy and apoptotic cells
To identify components of mitochondrial apoptotic foci, Flag-APEX2-tagged constructs targeting Bax, Bak, and Drp1 were generated. These constructs are designed to localize to foci at the mitochondrial outer membrane (MOM) during apoptosis. Following biotinylation with BP and H2O2, quantitative mass ...
ORGANISM(S): Homo sapiens (Human) 
2026-03-27 | PXD055201 | Pride
Bak Apex2 Bax Apoptotic foci Drp1 
OtherComputational design of potent and selective BAK and BAX binders
There are numerous binders of the pro-survival BCL2 family proteins such as BCL2, MCL1, and BCL-XL, but development of potent and selective binders of their pro-apoptotic counterparts BAK and BAX has remained a major unsolved challenge. We use computational protein design to generate 13 kDa binders ...
ORGANISM(S): Saccharomyces cerevisiae 
2025-05-01 | GSE266473 | GEO
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