{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nPRPF38A (pre‐mRNA processing factor 38A) is an essential spliceosomal factor that plays a critical role during spliceosome activation. Structural analyses using cryo‐electron microscopy have revealed that its conserved amino‐terminal domain is organized around three pairs of antiparallel α‐helices and—unlike classical RNA‐binding domains—serves as a versatile protein–protein interaction platform. Through multiple distinct interaction interfaces, PRPF38A coordinates the sequential exchange of partner proteins that drives the precise folding and assembly of the U2/U6 catalytic RNA core, a prerequisite for forming a catalytically active spliceosome."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "1"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIt is noteworthy that the remainder of the provided literature emphasizes another set of multifunctional proteins—namely, the cytokine interleukin‑11 (IL‑11) and its receptors—which regulate diverse pathophysiological processes such as osteolytic metastasis, gastric inflammation and tumorigenesis, cardiac remodeling, epithelial repair, and fibrotic as well as inflammatory responses in multiple tissues. 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