{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nAmong the provided abstracts, only one (PMID"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "1"}]}, {"type": "t", "text": "describes a protein belonging to the Ups1/PRELI‐like family, which includes PRELID3A. This study reveals that members of this protein family function in mitochondrial phospholipid transfer. In partnership with their chaperones (such as TRIAP1/Mdm35), these proteins facilitate the trafficking of phospholipids within mitochondria—a process essential for maintaining mitochondrial membrane composition, structural integrity, and proper organelle function. Structural analysis of the PRELI domain shows a remarkable resemblance to mammalian phosphatidylinositol transfer proteins; this similarity suggests that the PRELI-like proteins regulate access to a buried lipid‐binding cavity via conformationally adaptable loops, thereby ensuring efficient and regulated lipid transfer during mitochondrial import.\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Xeni Miliara, James A Garnett, Takashi Tatsuta, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Structural insight into the TRIAP1/PRELI-like domain family of mitochondrial phospholipid transfer complexes."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "EMBO Rep (2015)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.15252/embr.201540229"}], "href": "https://doi.org/10.15252/embr.201540229"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "26071602"}], "href": "https://pubmed.ncbi.nlm.nih.gov/26071602"}]}]}]}