A Novel N-Terminal <i>PRPF6</i> Variant in Autosomal Dominant Retinitis Pigmentosa. [PDF]
Clin Case RepABSTRACT This report identifies the first N‐terminal PRPF6 variant (c.514C>T) as a cause of autosomal dominant Retinitis Pigmentosa. This novel variant is associated with progressive peripheral vision loss but notably preserved central visual acuity, suggesting a distinct phenotypic expression compared to C‐terminal variants.
Li N, Dang Y.
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Liquid-Liquid Phase Separation: Mechanisms, Roles, and Implications in Cellular Function and Disease. [PDF]
FASEB BioadvLiquid–liquid phase separation (LLPS) is a fundamental biophysical process responsible for forming membraneless organelles involved in key cellular functions like chromatin organization and gene expression. Dysregulation of LLPS contributes to various diseases, including neurodegenerative disorders.
Thakur DK +4 more
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Identification of a 35S U4/U6.U5 tri-small nuclear ribonucleoprotein (tri-snRNP) complex intermediate in spliceosome assembly [PDF]
Journal of Biological Chemistry, 2017 The de novo assembly and post-splicing reassembly of the U4/U6.U5 tri-snRNP remain to be investigated. We report here that ZIP, a protein containing a CCCH-type zinc finger and a G-patch domain, as characterized by us previously, regulates pre-mRNA splicing independent of RNA binding.
Zhe, Chen +14 more
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Structural basis for dual roles of Aar2p in U5 snRNP assembly [PDF]
, 2013 Yeast U5 small nuclear ribonucleoprotein particle (snRNP) is assembled via a cytoplasmic precursor that contains the U5-specific Prp8 protein but lacks the U5-specific Brr2 helicase.
Beggs, J.D. +8 more
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Association of U2, U4, U5, and U6 small nuclear ribonucleoproteins in a spliceosome-type complex in absence of precursor RNA. [PDF]
Proceedings of the National Academy of Sciences, 1988 Small nuclear ribonucleoprotein particles (snRNPs) associate to form multi-snRNP complexes during splicing of mRNA precursors. A vast majority of the three snRNPs U4, U5, and U6 are present in a nuclear extract in a single complex, while U1 and U2 snRNPs exist as separate particles.
M M, Konarska, P A, Sharp
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Cloning and molecular characterization of Trypanosoma cruzi U2, U4, U5, and U6 small nuclear RNAs
Memorias do Instituto Oswaldo Cruz, 2007 Small nuclear RNAs (snRNAs) are important factors in the functioning of eukaryotic cells that form several small complexes with proteins; these ribonucleoprotein particles (U snRNPs) have an essential role in the pre-mRNA processing, particularly in ...
DL Ambrósio, MTA Silva, RMB Cicarelli
doaj +1 more source
PRP4: a protein of the yeast U4/U6 small nuclear ribonucleoprotein particle [PDF]
, 1989 The Saccharomyces cerevisiae prp mutants (prp2 through prp11) are known to be defective in pre-mRNA splicing at nonpermissive temperatures. We have sequenced the PRP4 gene and shown that it encodes a 52-kilodalton protein.
Abelson, John N., Banroques, Josette
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A U5 Small Nuclear Ribonucleoprotein Particle Protein Involved Only in the Second Step of Pre-mRNA Splicing in Saccharomyces cerevisiae [PDF]
Molecular and Cellular Biology, 1993 The PRP18 gene, which had been identified in a screen for pre-mRNA splicing mutants in Saccharomyces cerevisiae, has been cloned and sequenced. Yeast strains bearing only a disrupted copy of PRP18 are temperature sensitive for growth; even at a low temperature, they grow extremely slowly and do not splice pre-mRNA efficiently.
Horowitz, David S., Abelson, John
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A Block in Mammalian Splicing Occurring after Formation of Large Complexes Containing U1, U2, U4, U5, and U6 Small Nuclear Ribonucleoproteins [PDF]
Molecular and Cellular Biology, 1989 The assembly of mammalian pre-mRNAs into large 50S to 60S complexes, or spliceosomes, containing small nuclear ribonucleoproteins (snRNPs) leads to the production of splicing intermediates, 5' exon and lariat-3' exon, and the subsequent production of spliced products.
C H, Agris, M E, Nemeroff, R M, Krug
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Structural investigation of human U6 snRNA recognition by spliceosomal recycling factor SART3 RNA recognition motifs. [PDF]
FEBS JHuman SART3 has two RRM domains to engage with U6 snRNA for spliceosome recycling. This study reports solution structures of SART3 RRM domains and investigates the interaction between RRM and U6 snRNA. SART3 binds to the asymmetric bulge of U6 snRNA as a dimer via conserved positively charged surfaces.
Kim I +8 more
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