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Coiled-coil-helix-coiled-coil-helix domain-containing protein 10 (CHCHD10) is a mitochondrial protein characterized by the presence of a CHCH domain, which consists of two pairs of cysteine residues involved in disulfide bond formation upon import into the mitochondria[3][4]. These structural domains support the protein's role in maintaining mitochondrial ultrastructure and are involved in the assembly, function, and structural integrity of electron transport chain complexes, particularly in the stabilization of protein complexes that are essential for normal mitochondrial morphology and respiration[3][4][7][6]. Proteins in this family are generally not classical therapeutic targets such as receptors, transporters, or enzymes, but rather are considered structural or scaffolding proteins crucial for organelle stability and cellular energy metabolism[4][7]. Mutations in CHCHD10 are implicated in some neurodegenerative diseases and mitochondrial disorders, underscoring its importance in cellular physiology, although no known drugs act directly on this protein and it is not currently considered a direct therapeutic target[4][7].
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