ArticleCellular and molecular life sciences : CMLS2021
The pro-apoptotic domain of BIM protein forms toxic amyloid fibrils.
Article in Cellular and molecular life sciences : CMLS, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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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.
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Who cites it
4 citing papers in PubMed, 8 citations in OpenAlex.
- Assessing the Catalytic Role of Native Glucagon Amyloid Fibrils.ACS catalysis · 2024Article
- In silico design of potential Mcl-1 peptide-based inhibitors.Journal of molecular modeling · 2024Article
- Article
- Long Non-Coding RNA PNKY Modulates the Development of Choroidal Neovascularization.Frontiers in cell and developmental biology · 2022Article
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
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Abstract
BIM is a key apoptotic protein, participating in diverse cellular processes. Interestingly, recent studies have hypothesized that BIM is associated with the extensive neuronal cell death encountered in protein misfolding diseases, such as Alzheimer's disease. Here, we report that the core pro-apoptotic domain of BIM, the BIM-BH3 motif, forms ubiquitous amyloid fibrils. The BIM-BH3 fibrils exhibit cytotoxicity, disrupt mitochondrial functions, and modulate the structures and dynamics of mitochondrial membrane mimics. Interestingly, a slightly longer peptide in which BIM-BH3 was flanked by four additional residues, widely employed as a model of the pro-apoptotic core domain of BIM, did not form fibrils, nor exhibited cell disruptive properties. The experimental data suggest a new mechanistic role for the BIM-BH3 domain, and demonstrate, for the first time, that an apoptotic peptide forms toxic amyloid fibrils.
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Registered trials
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