ReviewBiochemical Society transactions2022
Protein-protein and protein-lipid interactions of pore-forming BCL-2 family proteins in apoptosis initiation.
Review in Biochemical Society transactions, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
14 citing papers in PubMed.
- Electron transfer flavoprotein subunit beta suppresses hypoxia/reoxygenation-induced mitochondrial dysfunction and apoptosis in cardiomyocytes.The Journal of international medical research · 2026Article
- Membrane Pore Formation by Peptides Studied by Fluorescence Techniques.Methods in molecular biology (Clifton, N.J.) · 2026Article
- The tumor suppressor LACTB remodels mitochondria to promote cytochrome c release and apoptosis.Science advances · 2025Article
- Uracil derivatives/ursolic acid hybrids - naturally derived compounds as anticancer agents.Scientific reports · 2025Article
- Structural basis of BAK sequestration by MCL-1 in apoptosis.Molecular cell · 2025Article
- Multi-active phlorotannins boost antimicrobial peptide LL-37 to promote periodontal tissue regeneration in diabetic periodontitis.Materials today. Bio · 2025Article
- Deletion of Nrf2 induced severe oxidative stress and apoptosis in mice model of diabetic bladder dysfunction.International urology and nephrology · 2024Article
- Virtual Screening of Small Molecules Targeting BCL2 with Machine Learning, Molecular Docking, and MD Simulation.Biomolecules · 2024Article
- Anti-apoptotic MCL-1 promotes long-chain fatty acid oxidation through interaction with ACSL1.Molecular cell · 2024Article
- Endogenous BAX and BAK form mosaic rings of variable size and composition on apoptotic mitochondria.Cell death and differentiation · 2024Article
- Apoptotic mitochondrial poration by a growing list of pore-forming BCL-2 family proteins.BioEssays : news and reviews in molecular, cellular and developmental biology · 2023Article
- Structure-destabilizing mutations unleash an intrinsic perforation activity of antiapoptotic Bcl-2 in the mitochondrial membrane enabling apoptotic cell death.Mitochondrial communications · 2023Article
- Crosstalk among N6-methyladenosine modification and RNAs in central nervous system injuries.Frontiers in cellular neuroscience · 2022Review
- The dual role of the CD95 and CD95L signaling pathway in glioblastoma.Frontiers in immunology · 2022Review
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
Apoptosis is a common cell death program that is important in human health and disease. Signaling in apoptosis is largely driven through protein-protein interactions. The BCL-2 family proteins function in protein-protein interactions as key regulators of mitochondrial poration, the process that initiates apoptosis through the release of cytochrome c, which activates the apoptotic caspase cascade leading to cellular demolition. The BCL-2 pore-forming proteins BAK and BAX are the key executors of mitochondrial poration. We review the state of knowledge of protein-protein and protein-lipid interactions governing the apoptotic function of BAK and BAX, as determined through X-ray crystallography and NMR spectroscopy studies. BAK and BAX are dormant, globular α-helical proteins that participate in protein-protein interactions with other pro-death BCL-2 family proteins, transforming them into active, partially unfolded proteins that dimerize and associate with and permeabilize mitochondrial membranes. We compare the protein-protein interactions observed in high-resolution structures with those derived in silico by AlphaFold, making predictions based on combining experimental and in silico approaches to delineate the structural basis for novel protein-protein interaction complexes of BCL-2 family proteins.
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Registered trials
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