Results 161 to 170 of about 30,416 (203)
Knockdown of the fly spliceosome component Rbp1 (orthologue of SRSF1 ) extends lifespan
Hayman DJ, Simons MJP.
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Architecture of the Spliceosome
Biochemistry, 2012Precursor-mRNA splicing is catalyzed by an extraordinarily large and highly dynamic macromolecular assemblage termed the spliceosome. Detailed biochemical and structural study of the spliceosome presents a formidable challenge, but there has recently been significant progress made on this front highlighted by the crystal structure of a 10-subunit human
Clarisse, van der Feltz +3 more
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RNA Splicing by the Spliceosome
Annual Review of Biochemistry, 2020The spliceosome removes introns from messenger RNA precursors (pre-mRNA). Decades of biochemistry and genetics combined with recent structural studies of the spliceosome have produced a detailed view of the mechanism of splicing. In this review, we aim to make this mechanism understandable and provide several videos of the spliceosome in action to ...
Clement Charenton +2 more
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Seminars in Cell and Developmental Biology, 2018 The U12-dependent (minor) spliceosome excises a rare group of introns that are characterized by a highly conserved 5' splice site and branch point sequence. Several new congenital or somatic diseases have recently been associated with mutations in components of the minor spliceosome.
Antto Norppa +2 more
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BioEssays, 1993
AbstractThe spliceosome is a large RNA‐protein complex that catalyses the removal of introns from nuclear pre‐mRNA. A wide range of biochemical and genetical studies shows that the spliceosome comprises three major RNA‐protein subunits, the U1, U2 and [U4/U6.U5] small nuclear ribonucleoprotein particles (snRNPs), and an additional group of non‐snRNP ...
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AbstractThe spliceosome is a large RNA‐protein complex that catalyses the removal of introns from nuclear pre‐mRNA. A wide range of biochemical and genetical studies shows that the spliceosome comprises three major RNA‐protein subunits, the U1, U2 and [U4/U6.U5] small nuclear ribonucleoprotein particles (snRNPs), and an additional group of non‐snRNP ...
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Science, 1991
In cell extracts, the snRNAs exist associated with proteins as small nuclear ribonucleoproteins (snRNPs, pronounced «snurps»). In an in vitro splicing reaction, the snRNPs, other essential protein factors, and the pre-mRNA form a macromolecular complex known as a spliceosome.
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In cell extracts, the snRNAs exist associated with proteins as small nuclear ribonucleoproteins (snRNPs, pronounced «snurps»). In an in vitro splicing reaction, the snRNPs, other essential protein factors, and the pre-mRNA form a macromolecular complex known as a spliceosome.
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A glimpse into the spliceosome
Current Biology, 1993The removal of introns from mRNA precursors (premRNA) is a complex process that takes place in the nucleus in a multi-component structure known as the spliceosome. The spliceosome is comparable in size and complexity to the ribosome and is mainly comprised of four RNA-protein complexes, the Ul, U2, U4/U6 and U5 small nuclear ribonucleoprotein particles
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Science, 1996
In this issue of Science , Tarn and Steitz ( p. 1824 ) report the identification of two new RNAs that reside in the special spliceosome that acts on the rare AT-AC class of introns. In his Perspective, Nilsen describes why the now complete description of the RNA components of this spliceosome
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In this issue of Science , Tarn and Steitz ( p. 1824 ) report the identification of two new RNAs that reside in the special spliceosome that acts on the rare AT-AC class of introns. In his Perspective, Nilsen describes why the now complete description of the RNA components of this spliceosome
openaire +2 more sources
Structures of the human pre-catalytic spliceosome and its precursor spliceosome [PDF]
Cell Research, 2018 The pre-catalytic spliceosome (B complex) is preceded by its precursor spliceosome (pre-B complex) and followed by the activated spliceosome (Bact complex). The pre-B-to-B and B-to-Bact transitions are driven by the ATPase/helicases Prp28 and Brr2, respectively. In this study, we report the cryo-electron microscopy structures of the human pre-B complex
Xiechao Zhan +2 more
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