{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Tang SX"],"funding":["Ludwig Center at Harvard","NICHD NIH HHS","NIA NIH HHS","NHLBI NIH HHS","Alex's Lemonade Stand Foundation for Childhood Cancer","Nihon Kohden America","Wood Family Foundation","NCI NIH HHS","National Institutes of Health","Cook Family Foundation","Abell Foundation"],"pagination":["1815-1826.e5"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11490406"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["31(10)"],"pubmed_abstract":["BCL-w is a BCL-2 family protein that promotes cell survival in tissue- and disease-specific contexts. The canonical anti-apoptotic functionality of BCL-w is mediated by a surface groove that traps the BCL-2 homology 3 (BH3) α-helices of pro-apoptotic members, blocking cell death. A distinct N-terminal portion of BCL-w, termed the BCL-2 homology 4 (BH4) domain, selectively protects axons from paclitaxel-induced degeneration by modulating IP3 receptors, a noncanonical BCL-2 family target. Given the potential of BCL-w BH4 mimetics to prevent or mitigate chemotherapy-induced peripheral neuropathy, we sought to characterize the interaction between BCL-w BH4 and the IP3 receptor, combining \"staple\" and alanine scanning approaches with molecular dynamics simulations. We generated and identified s"],"journal":["Cell chemical biology"],"pubmed_title":["Dissecting the neuroprotective interaction between the BH4 domain of BCL-w and the IP3 receptor."],"pmcid":["PMC11490406"],"funding_grant_id":["R50 CA211399","K00AG078230","R50CA211399","T32 HL007574","K00 AG078230","5T32HL007574","R35 CA197583","P50 HD105351","R01 CA205255","R01CA205255","R35CA197583"],"pubmed_authors":["Tang SX","Franco JA","Camara CM","Li Y","Godes M","Bird GH","Walensky LD","Moyer BM","Segal RA","Pazyra-Murphy MF"],"additional_accession":[]},"is_claimable":false,"name":"Dissecting the neuroprotective interaction between the BH4 domain of BCL-w and the IP3 receptor.","description":"BCL-w is a BCL-2 family protein that promotes cell survival in tissue- and disease-specific contexts. The canonical anti-apoptotic functionality of BCL-w is mediated by a surface groove that traps the BCL-2 homology 3 (BH3) α-helices of pro-apoptotic members, blocking cell death. A distinct N-terminal portion of BCL-w, termed the BCL-2 homology 4 (BH4) domain, selectively protects axons from paclitaxel-induced degeneration by modulating IP3 receptors, a noncanonical BCL-2 family target. Given the potential of BCL-w BH4 mimetics to prevent or mitigate chemotherapy-induced peripheral neuropathy, we sought to characterize the interaction between BCL-w BH4 and the IP3 receptor, combining \"staple\" and alanine scanning approaches with molecular dynamics simulations. We generated and identified s","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Oct","modification":"2026-06-04T13:56:33.184Z","creation":"2026-05-10T03:11:22.797Z"},"accession":"S-EPMC11490406","cross_references":{"pubmed":["39067448"],"doi":["10.1016/j.chembiol.2024.06.016"]}}