{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\n Recent structure‐ and data‐driven analyses of the human proteome have revealed that BNIP5 harbors a BH3‐like motif capable of mediating direct interactions with multiple anti‐apoptotic Bcl-2 family proteins, including Bcl-xL, Bcl-w, Bcl-2, Mcl-1, and Bfl-1."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "1"}]}, {"type": "t", "text": " Biochemical characterization using peptide SPOT arrays and solution binding assays demonstrated that peptides derived from BNIP5 and similar candidates bind these prosurvival receptors with nanomolar affinities, delineating unique specificity profiles not observed with previously characterized BH3 motifs. This evidence supports a model in which BNIP5, by virtue of its BH3-like sequence, functions as a pro-apoptotic factor that can antagonize anti-apoptotic proteins, thereby modulating the cellular commitment to programmed cell death. The findings underscore the utility of combining structure-based prediction with experimental screening to uncover novel regulators of apoptosis.\n "}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Joe DeBartolo, Mikko Taipale, Amy E Keating "}, {"type": "b", "children": [{"type": "t", "text": "Genome-wide prediction and validation of peptides that bind human prosurvival Bcl-2 proteins."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "PLoS Comput Biol (2014)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1371/journal.pcbi.1003693"}], "href": "https://doi.org/10.1371/journal.pcbi.1003693"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "24967846"}], "href": "https://pubmed.ncbi.nlm.nih.gov/24967846"}]}]}]}