{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nPRPF8 is a central and highly conserved component of the spliceosome that orchestrates the assembly and function of the splicing machinery. It plays a pivotal role in organizing the spliceosome’s active site by interacting with multiple spliceosomal proteins and small nuclear RNAs. Structural studies have revealed that its C‐terminal region contains a Jab1/MPN‐like domain—which, although resembling deubiquitinating enzymes, functions as a platform for protein–protein interactions—and an RNase H–like domain that is critical for assembling and stabilizing the catalytic core. In addition, PRPF8 directly binds key factors such as the DEAD‐box helicase Brr2 and the GTPase Snu114, thereby regulating the RNA unwinding and catalytic activation steps essential for pre‐mRNA splicing."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "4"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its catalytic role, PRPF8 is a key player in the proper assembly and maturation of the U5 small nuclear ribonucleoprotein particle (snRNP). It is involved in quality control mechanisms during spliceosome assembly, including interactions with chaperone complexes and auxiliary factors that help in the stable integration of spliceosomal components. Structural insights into its interaction with proteins such as AAR2 further illuminate how PRPF8 regulates U5 snRNP biogenesis and function in spliceosome activation."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "5", "end_ref": "7"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nPRPF8 also exerts fine control over alternative splicing decisions and splice‐site selection, mechanisms that are critical for tissue‐specific gene expression. Its regulation of 5′ splice‐site recognition and modulation of splicing factor interactions have been linked to the accurate removal of introns in transcripts that govern specialized cellular processes such as mitophagy and cell survival. Defects in these regulatory roles can lead to aberrant splicing patterns, underscoring its importance in maintaining the fidelity of gene expression."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "8", "end_ref": "11"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nOutside its canonical role in splicing, PRPF8 is subject to external modulation that impacts diverse cellular pathways. Viral proteins have been shown to bind its C‐terminal Jab1/MPN domain to disrupt splicing, thereby subverting host gene expression. Furthermore, alterations in specific domains of PRPF8 have been linked to changes in apoptotic signaling and even neurodevelopment, suggesting that PRPF8’s function can extend to the regulation of cellular stress responses and developmental processes."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "12", "end_ref": "15"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nMutations in PRPF8 underscore its critical function in splicing and have been linked to human disease. Numerous studies have identified distinct PRPF8 variants that lead to aberrant splicing and are associated primarily with autosomal dominant retinitis pigmentosa, as well as with other ocular conditions such as primary open angle glaucoma. Detailed genotype–phenotype correlations have further revealed that while widespread splicing defects may be tolerated in many tissues, the exceptionally high splicing demand in retinal cells renders them especially vulnerable to PRPF8 dysfunction. Moreover, emerging evidence also implicates PRPF8 variants in neurodevelopmental disorders, reinforcing the notion that precise control of splicing is essential for cellular homeostasis and organismal development."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "16", "end_ref": "30"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Vladimir Pena, Sunbin Liu, Janusz M Bujnicki, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Structure of a multipartite protein-protein interaction domain in splicing factor prp8 and its link to retinitis pigmentosa."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Cell (2007)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.molcel.2007.01.023"}], "href": "https://doi.org/10.1016/j.molcel.2007.01.023"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "17317632"}], "href": "https://pubmed.ncbi.nlm.nih.gov/17317632"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Vladimir Pena, Alexey Rozov, Patrizia Fabrizio, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Structure and function of an RNase H domain at the heart of the spliceosome."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "EMBO J (2008)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/emboj.2008.209"}], "href": "https://doi.org/10.1038/emboj.2008.209"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "18843295"}], "href": "https://pubmed.ncbi.nlm.nih.gov/18843295"}]}, {"type": "r", "ref": 3, "children": [{"type": "t", "text": "Sina Mozaffari-Jovin, Traudy Wandersleben, Karine F Santos, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Inhibition of RNA helicase Brr2 by the C-terminal tail of the spliceosomal protein Prp8."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Science (2013)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1126/science.1237515"}], "href": "https://doi.org/10.1126/science.1237515"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "23704370"}], "href": "https://pubmed.ncbi.nlm.nih.gov/23704370"}]}, {"type": "r", "ref": 4, "children": [{"type": "t", "text": "Thi Hoang Duong Nguyen, Jade Li, Wojciech P Galej, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Structural basis of Brr2-Prp8 interactions and implications for U5 snRNP biogenesis and the spliceosome active site."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Structure (2013)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.str.2013.04.017"}], "href": "https://doi.org/10.1016/j.str.2013.04.017"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "23727230"}], "href": "https://pubmed.ncbi.nlm.nih.gov/23727230"}]}, {"type": "r", "ref": 5, "children": [{"type": "t", "text": "Vihandha O Wickramasinghe, Mar Gonzàlez-Porta, David Perera, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Regulation of constitutive and alternative mRNA splicing across the human transcriptome by PRPF8 is determined by 5' splice site strength."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Genome Biol (2015)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1186/s13059-015-0749-3"}], "href": "https://doi.org/10.1186/s13059-015-0749-3"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "26392272"}], "href": "https://pubmed.ncbi.nlm.nih.gov/26392272"}]}, {"type": "r", "ref": 6, "children": [{"type": "t", "text": "Anna Malinová, Zuzana Cvačková, Daniel Matějů, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Assembly of the U5 snRNP component PRPF8 is controlled by the HSP90/R2TP chaperones."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Cell Biol (2017)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1083/jcb.201701165"}], "href": "https://doi.org/10.1083/jcb.201701165"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "28515276"}], "href": "https://pubmed.ncbi.nlm.nih.gov/28515276"}]}, {"type": "r", "ref": 7, "children": [{"type": "t", "text": "Marco Preussner, Karine F Santos, Jonathan Alles, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Structural and functional investigation of the human snRNP assembly factor AAR2 in complex with the RNase H-like domain of PRPF8."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Acta Crystallogr D Struct Biol (2022)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1107/S2059798322009755"}], "href": "https://doi.org/10.1107/S2059798322009755"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "36322420"}], "href": "https://pubmed.ncbi.nlm.nih.gov/36322420"}]}, {"type": "r", "ref": 8, "children": [{"type": "t", "text": "Tanuza Das, Joon Kyu Park, Jinyoung Park, et al. "}, {"type": "b", "children": [{"type": "t", "text": "USP15 regulates dynamic protein-protein interactions of the spliceosome through deubiquitination of PRP31."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Nucleic Acids Res (2017)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1093/nar/gkw1365"}], "href": "https://doi.org/10.1093/nar/gkw1365"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "28088760"}], "href": "https://pubmed.ncbi.nlm.nih.gov/28088760"}]}, {"type": "r", "ref": 9, "children": [{"type": "t", "text": "Guang Xu, Ting Li, Jiayi Chen, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Autosomal dominant retinitis pigmentosa-associated gene PRPF8 is essential for hypoxia-induced mitophagy through regulating ULK1 mRNA splicing."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Autophagy (2018)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1080/15548627.2018.1501251"}], "href": "https://doi.org/10.1080/15548627.2018.1501251"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "30103670"}], "href": "https://pubmed.ncbi.nlm.nih.gov/30103670"}]}, {"type": "r", "ref": 10, "children": [{"type": "t", "text": "Robert Atkinson, Maria Georgiou, Chunbo Yang, et al. 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"}, {"type": "b", "children": [{"type": "t", "text": "PRPF8 controls alternative splicing of PIRH2 to modulate the p53 pathway and survival of human ESCs."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Cell Physiol (2023)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1002/jcp.31066"}], "href": "https://doi.org/10.1002/jcp.31066"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "37357506"}], "href": "https://pubmed.ncbi.nlm.nih.gov/37357506"}]}, {"type": "r", "ref": 12, "children": [{"type": "t", "text": "Yen-Chin Liu, Rei-Lin Kuo, Jing-Yi Lin, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Cytoplasmic viral RNA-dependent RNA polymerase disrupts the intracellular splicing machinery by entering the nucleus and interfering with Prp8."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "PLoS Pathog (2014)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1371/journal.ppat.1004199"}], "href": "https://doi.org/10.1371/journal.ppat.1004199"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "24968230"}], "href": "https://pubmed.ncbi.nlm.nih.gov/24968230"}]}, {"type": "r", "ref": 13, "children": [{"type": "t", "text": "Chee-Hing Yang, Hui-Chun Li, Yu-Ling Shiu, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Influenza A virus upregulates PRPF8 gene expression to increase virus production."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Arch Virol (2017)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1007/s00705-016-3210-3"}], "href": "https://doi.org/10.1007/s00705-016-3210-3"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "28110426"}], "href": "https://pubmed.ncbi.nlm.nih.gov/28110426"}]}, {"type": "r", "ref": 14, "children": [{"type": "t", "text": "J V Tapia-Vieyra, R O Arellano, J Mas-Oliva "}, {"type": "b", "children": [{"type": "t", "text": "ARP2 a novel protein involved in apoptosis of LNCaP cells shares a high degree homology with splicing factor Prp8."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Cell Biochem (2005)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1007/s11010-005-3084-2"}], "href": "https://doi.org/10.1007/s11010-005-3084-2"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "15786732"}], "href": "https://pubmed.ncbi.nlm.nih.gov/15786732"}]}, {"type": "r", "ref": 15, "children": [{"type": "t", "text": "Lauren O'Grady, Samantha A Schrier Vergano, Trevor L Hoffman, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Heterozygous variants in PRPF8 are associated with neurodevelopmental disorders."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Am J Med Genet A (2022)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1002/ajmg.a.62772"}], "href": "https://doi.org/10.1002/ajmg.a.62772"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "35543142"}], "href": "https://pubmed.ncbi.nlm.nih.gov/35543142"}]}, {"type": "r", "ref": 16, "children": [{"type": "t", "text": "Goranka Tanackovic, Adriana Ransijn, Philippe Thibault, et al. 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"}, {"type": "b", "children": [{"type": "t", "text": "Autosomal dominant retinitis pigmentosa with intrafamilial variability and incomplete penetrance in two families carrying mutations in PRPF8."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Invest Ophthalmol Vis Sci (2011)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1167/iovs.11-8372"}], "href": "https://doi.org/10.1167/iovs.11-8372"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "22039234"}], "href": "https://pubmed.ncbi.nlm.nih.gov/22039234"}]}, {"type": "r", "ref": 19, "children": [{"type": "t", "text": "Katherine V Towns, Athina Kipioti, Vernon Long, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Prognosis for splicing factor PRPF8 retinitis pigmentosa, novel mutations and correlation between human and yeast phenotypes."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Hum Mutat (2010)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1002/humu.21236"}], "href": "https://doi.org/10.1002/humu.21236"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "20232351"}], "href": "https://pubmed.ncbi.nlm.nih.gov/20232351"}]}, {"type": "r", "ref": 20, "children": [{"type": "t", "text": "Kaylie D Jones, Dianna K Wheaton, Sara J Bowne, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Next-generation sequencing to solve complex inherited retinal dystrophy: A case series of multiple genes contributing to disease in extended families."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Vis (2017)"}]}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "28761320"}], "href": "https://pubmed.ncbi.nlm.nih.gov/28761320"}]}, {"type": "r", "ref": 21, "children": [{"type": "t", "text": "J J C van Lith-Verhoeven, S D van der Velde-Visser, M M Sohocki, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Clinical characterization, linkage analysis, and PRPC8 mutation analysis of a family with autosomal dominant retinitis pigmentosa type 13 (RP13)."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Ophthalmic Genet (2002)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1076/opge.23.1.1.2206"}], "href": "https://doi.org/10.1076/opge.23.1.1.2206"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "11910553"}], "href": "https://pubmed.ncbi.nlm.nih.gov/11910553"}]}, {"type": "r", "ref": 22, "children": [{"type": "t", "text": "Lenka Ivings, Katherine V Towns, M A Matin, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Evaluation of splicing efficiency in lymphoblastoid cell lines from patients with splicing-factor retinitis pigmentosa."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Vis (2008)"}]}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "19096719"}], "href": "https://pubmed.ncbi.nlm.nih.gov/19096719"}]}, {"type": "r", "ref": 23, "children": [{"type": "t", "text": "Shazia Micheal, Barend F Hogewind, Muhammad Imran Khan, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Variants in the PRPF8 Gene are Associated with Glaucoma."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Neurobiol (2018)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1007/s12035-017-0673-5"}], "href": "https://doi.org/10.1007/s12035-017-0673-5"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "28707069"}], "href": "https://pubmed.ncbi.nlm.nih.gov/28707069"}]}, {"type": "r", "ref": 24, "children": [{"type": "t", "text": "Juan L López-Cánovas, Natalia Hermán-Sánchez, Mercedes Del Rio-Moreno, et al. "}, {"type": "b", "children": [{"type": "t", "text": "PRPF8 increases the aggressiveness of hepatocellular carcinoma by regulating FAK/AKT pathway via fibronectin 1 splicing."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Exp Mol Med (2023)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/s12276-022-00917-7"}], "href": "https://doi.org/10.1038/s12276-022-00917-7"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "36609600"}], "href": "https://pubmed.ncbi.nlm.nih.gov/36609600"}]}, {"type": "r", "ref": 25, "children": [{"type": "t", "text": "Pascal Escher, Olga Passarin, Francis L Munier, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Variability in clinical phenotypes of PRPF8-linked autosomal dominant retinitis pigmentosa correlates with differential PRPF8/SNRNP200 interactions."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Ophthalmic Genet (2018)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1080/13816810.2017.1393825"}], "href": "https://doi.org/10.1080/13816810.2017.1393825"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "29087248"}], "href": "https://pubmed.ncbi.nlm.nih.gov/29087248"}]}, {"type": "r", "ref": 26, "children": [{"type": "t", "text": "Saloni Walia, Gerald A Fishman, Jana Zernant-Rajang, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Phenotypic expression of a PRPF8 gene mutation in a Large African American family."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Arch Ophthalmol (2008)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1001/archopht.126.8.1127"}], "href": "https://doi.org/10.1001/archopht.126.8.1127"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "18695108"}], "href": "https://pubmed.ncbi.nlm.nih.gov/18695108"}]}, {"type": "r", "ref": 27, "children": [{"type": "t", "text": "Difei Cao, Jiaying Xue, Guoqing Huang, et al. "}, {"type": "b", "children": [{"type": "t", "text": "The role of splicing factor PRPF8 in breast cancer."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Technol Health Care (2022)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.3233/THC-THC228028"}], "href": "https://doi.org/10.3233/THC-THC228028"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "35124606"}], "href": "https://pubmed.ncbi.nlm.nih.gov/35124606"}]}, {"type": "r", "ref": 28, "children": [{"type": "t", "text": "F Testa, C Ziviello, M Rinaldi, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Clinical phenotype of an Italian family with a new mutation in the PRPF8 gene."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Eur J Ophthalmol (2006)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1177/112067210601600524"}], "href": "https://doi.org/10.1177/112067210601600524"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "17061239"}], "href": "https://pubmed.ncbi.nlm.nih.gov/17061239"}]}, {"type": "r", "ref": 29, "children": [{"type": "t", "text": "Z Wu, M Zhong, M Li, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Mutation Analysis of Pre-mRNA Splicing Genes PRPF31, PRPF8, and SNRNP200 in Chinese Families with Autosomal Dominant Retinitis Pigmentosa."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Curr Mol Med (2018)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.2174/1566524018666181024160452"}], "href": "https://doi.org/10.2174/1566524018666181024160452"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "30360737"}], "href": "https://pubmed.ncbi.nlm.nih.gov/30360737"}]}, {"type": "r", "ref": 30, "children": [{"type": "t", "text": "Paul K Korir, Lisa Roberts, Raj Ramesar, et al. "}, {"type": "b", "children": [{"type": "t", "text": "A mutation in a splicing factor that causes retinitis pigmentosa has a transcriptome-wide effect on mRNA splicing."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "BMC Res Notes (2014)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1186/1756-0500-7-401"}], "href": "https://doi.org/10.1186/1756-0500-7-401"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "24969741"}], "href": "https://pubmed.ncbi.nlm.nih.gov/24969741"}]}]}]}