An evolutionarily conserved U5 snRNP-specific protein is a GTP-binding factor closely related to the ribosomal translocase EF-2.
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The human U5-220kD protein (hPrp8) forms a stable RNA-free complex with several U5-specific proteins, including an RNA unwindase, a homologue of ribosomal elongation factor EF-2, and a novel WD-40 proteinThe product of the mammalian orthologue of the Saccharomyces cerevisiae HBS1 gene is phylogenetically related to eukaryotic release factor 3 (eRF3) but does not carry eRF3-like activityHuman step II splicing factor hSlu7 functions in restructuring the spliceosome between the catalytic steps of splicingProtein 61K, encoded by a gene (PRPF31) linked to autosomal dominant retinitis pigmentosa, is required for U4/U6*U5 tri-snRNP formation and pre-mRNA splicing.Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis.Biochemical analysis of the EJC reveals two new factors and a stable tetrameric protein coreCharacterization of novel SF3b and 17S U2 snRNP proteins, including a human Prp5p homologue and an SF3b DEAD-box proteinHuman homologs of yeast prp16 and prp17 reveal conservation of the mechanism for catalytic step II of pre-mRNA splicingThe human U5-200kD DEXH-box protein unwinds U4/U6 RNA duplices in vitroComparative genomics and evolution of proteins involved in RNA metabolismThe 65 and 110 kDa SR-related proteins of the U4/U6.U5 tri-snRNP are essential for the assembly of mature spliceosomesProteomics analysis reveals stable multiprotein complexes in both fission and budding yeasts containing Myb-related Cdc5p/Cef1p, novel pre-mRNA splicing factors, and snRNAs.Prp8 protein: at the heart of the spliceosomePSF and p54nrb bind a conserved stem in U5 snRNAThe network of protein-protein interactions within the human U4/U6.U5 tri-snRNPFunction of the ski4p (Csl4p) and Ski7p proteins in 3'-to-5' degradation of mRNAA Sm-like protein complex that participates in mRNA degradationHaploinsufficiency of a spliceosomal GTPase encoded by EFTUD2 causes mandibulofacial dysostosis with microcephalyCryoEM structures of two spliceosomal complexes: starter and dessert at the spliceosome feastEvolutionary conservation and expression of human RNA-binding proteins and their role in human genetic diseaseThe architecture of the spliceosomal U4/U6.U5 tri-snRNP.Inhibition of RNA helicase Brr2 by the C-terminal tail of the spliceosomal protein Prp8Structure of a yeast spliceosome at 3.6-angstrom resolutionMolecular architecture of the human U4/U6.U5 tri-snRNPAssembly of Snu114 into U5 snRNP requires Prp8 and a functional GTPase domain.A comprehensive biochemical and genetic analysis of the yeast U1 snRNP reveals five novel proteins.Genetic analysis reveals a role for the C terminus of the Saccharomyces cerevisiae GTPase Snu114 during spliceosome activationThe yeast U5 snRNP coisolated with the U1 snRNP has an unexpected protein composition and includes the splicing factor Aar2pBms1p, a G-domain-containing protein, associates with Rcl1p and is required for 18S rRNA biogenesis in yeast.The identification and characterization of a novel splicing protein, Isy1p, of Saccharomyces cerevisiae.Identification and characterization of two novel components of the Prp19p-associated complex, Ntc30p and Ntc20p.Prp8 retinitis pigmentosa mutants cause defects in the transition between the catalytic steps of splicing.The G-patch protein Spp2 couples the spliceosome-stimulated ATPase activity of the DEAH-box protein Prp2 to catalytic activation of the spliceosomePurification of the yeast U4/U6.U5 small nuclear ribonucleoprotein particle and identification of its proteins.Functional and physical interactions between components of the Prp19p-associated complexCbf5p, a potential pseudouridine synthase, and Nhp2p, a putative RNA-binding protein, are present together with Gar1p in all H BOX/ACA-motif snoRNPs and constitute a common bipartite structure.Proteomic characterization of protein phosphatase complexes of the mammalian nucleusDAP-like kinase interacts with the rat homolog of Schizosaccharomyces pombe CDC5 protein, a factor involved in pre-mRNA splicing and required for G2/M phase transition.The nuclear cap-binding complex interacts with the U4/U6·U5 tri-snRNP and promotes spliceosome assembly in mammalian cellsIdentification of a small molecule inhibitor that stalls splicing at an early step of spliceosome activation.
P2860
Q22003972-D49B6F67-DB98-47F0-BC44-564592FC253DQ22008594-58D06484-8247-44CF-AE0F-02CE33BDB6F0Q22009171-56D17CE0-BFB0-41DB-B79C-7D683653386CQ24292373-46B4F2DC-63CA-41DD-8E39-5CC4065FAAACQ24296676-6792A70F-2AA7-447D-A83E-ACC7B29662E4Q24297150-9E47FF43-941B-418B-BC10-ABBA203926F8Q24306748-68EC6C97-03E1-4184-8A3F-3E937FC8B6DFQ24320312-431D7E3F-24A5-43DE-B761-AFE850B0F2C3Q24323409-7071AE42-188B-4C73-A7CA-B4887CF18362Q24515041-E1AE0CE5-5B90-4B46-9814-570A3F6CB22BQ24534416-9BAEC575-13E1-485D-9EE3-91912DA3DCD4Q24537200-BE14CD43-FA2D-4613-B8E6-EF968D70E666Q24537373-FAA4DC4E-BFF2-4755-B5E7-D2FE9E2F6401Q24540146-5A032F9E-F346-4CF0-BEB9-4FA991661F87Q24548787-D8645BD5-8906-4B10-BC8F-05E3D5E7710AQ24551147-740D2F80-A266-4046-92AE-F22979E351E2Q24630673-2E3EB341-7A65-4E8B-8C1C-1F4D2AD3926CQ24633650-27C7A0CA-8DAE-44E8-8D23-54ABBA7D8D39Q26775192-87F4D0D1-3C79-46F0-A14C-2E2636F6841FQ26991754-6DF02F3C-2B6B-4C9E-A3AE-1A129E876D30Q27316447-FA3546F5-EB2A-4080-B039-9CD6AC57E8CCQ27684693-98725214-8781-4A3F-BC59-6EE339728158Q27701867-3E454867-A618-4F78-BD2F-CD329C13ED34Q27704181-504385B2-516A-4E7F-A08B-6850A96B2F7BQ27932833-1D276510-03AD-46A2-BE0A-623FC1A15D9FQ27934040-93FA5FDF-80AC-4E00-A0DD-15A5A7B33E74Q27935130-6455EF03-27BF-4570-96CD-339936EAF29BQ27935715-6F37B8F4-30F0-4E41-89AF-A5F041716E02Q27935958-A11881FE-E66B-4D14-94BC-9C1FE7D3993FQ27937488-6148C492-53C1-47E0-A116-11D77264E9E3Q27937587-A30B3532-CE68-4996-A1DD-1581C81DA174Q27937907-A698A331-A161-40C9-8286-D06114CE9F11Q27938864-7EC8557A-DDAE-46F3-B34B-D2FE08A58F71Q27939063-3F7DE297-AF03-4B36-8331-33408D2DB15DQ27939341-2E870B7A-08C0-454B-A9DC-A8D5FD12CF43Q27940038-D9A57F42-4D10-4061-B458-F41DB39735B4Q28574181-9589FF3D-DFF7-496A-84D2-AC464D88963BQ28575564-AAAFC00B-9E2F-4AA8-AB0D-27A2A063A53AQ28910445-85918A25-6B22-492A-A1BE-73EE68C44708Q30360791-07E0AC1C-6BF7-4954-8EC7-9CCA707E0FFC
P2860
An evolutionarily conserved U5 snRNP-specific protein is a GTP-binding factor closely related to the ribosomal translocase EF-2.
description
1997 nî lūn-bûn
@nan
1997 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
1997 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
1997年の論文
@ja
1997年論文
@yue
1997年論文
@zh-hant
1997年論文
@zh-hk
1997年論文
@zh-mo
1997年論文
@zh-tw
1997年论文
@wuu
name
An evolutionarily conserved U5 ...... the ribosomal translocase EF-2
@nl
An evolutionarily conserved U5 ...... he ribosomal translocase EF-2.
@ast
An evolutionarily conserved U5 ...... he ribosomal translocase EF-2.
@en
An evolutionarily conserved U5 ...... he ribosomal translocase EF-2.
@en-gb
type
label
An evolutionarily conserved U5 ...... the ribosomal translocase EF-2
@nl
An evolutionarily conserved U5 ...... he ribosomal translocase EF-2.
@ast
An evolutionarily conserved U5 ...... he ribosomal translocase EF-2.
@en
An evolutionarily conserved U5 ...... he ribosomal translocase EF-2.
@en-gb
prefLabel
An evolutionarily conserved U5 ...... the ribosomal translocase EF-2
@nl
An evolutionarily conserved U5 ...... he ribosomal translocase EF-2.
@ast
An evolutionarily conserved U5 ...... he ribosomal translocase EF-2.
@en
An evolutionarily conserved U5 ...... he ribosomal translocase EF-2.
@en-gb
P2093
P2860
P3181
P356
P1433
P1476
An evolutionarily conserved U5 ...... he ribosomal translocase EF-2.
@en
P2093
P2860
P304
P3181
P356
10.1093/EMBOJ/16.13.4092
P407
P577
1997-07-01T00:00:00Z