snRNP Sm proteins share two evolutionarily conserved sequence motifs which are involved in Sm protein-protein interactions
about
Sm and Sm-like proteins assemble in two related complexes of deep evolutionary origin.Gemin3: A novel DEAD box protein that interacts with SMN, the spinal muscular atrophy gene product, and is a component of gemsPurified U7 snRNPs lack the Sm proteins D1 and D2 but contain Lsm10, a new 14 kDa Sm D1-like proteinStructure of the spliceosomal U4 snRNP core domain and its implication for snRNP biogenesisMutations in SNRPE, which encodes a core protein of the spliceosome, cause autosomal-dominant hypotrichosis simplexThe 20kD protein of human [U4/U6.U5] tri-snRNPs is a novel cyclophilin that forms a complex with the U4/U6-specific 60kD and 90kD proteinsUnique Sm core structure of U7 snRNPs: assembly by a specialized SMN complex and the role of a new component, Lsm11, in histone RNA processingHerpes simplex virus IE63 (ICP27) protein interacts with spliceosome-associated protein 145 and inhibits splicing prior to the first catalytic stepRNA binding in an Sm core domain: X-ray structure and functional analysis of an archaeal Sm protein complex.The 65 and 110 kDa SR-related proteins of the U4/U6.U5 tri-snRNP are essential for the assembly of mature spliceosomesSMNrp is an essential pre-mRNA splicing factor required for the formation of the mature spliceosome.Structures of the pleiotropic translational regulator Hfq and an Hfq-RNA complex: a bacterial Sm-like proteinPredicted structure and phyletic distribution of the RNA-binding protein Hfq.Characterization of U6 snRNA-protein interactions.Symmetrical dimethylation of arginine residues in spliceosomal Sm protein B/B' and the Sm-like protein LSm4, and their interaction with the SMN protein.The human LSm1-7 proteins colocalize with the mRNA-degrading enzymes Dcp1/2 and Xrnl in distinct cytoplasmic foci.Evolutionary conservation of the U7 small nuclear ribonucleoprotein in Drosophila melanogaster.Sm protein-Sm site RNA interactions within the inner ring of the spliceosomal snRNP core structure.Domains in human splicing factors SF3a60 and SF3a66 required for binding to SF3a120, assembly of the 17S U2 snRNP, and prespliceosome formationhnRNP H is a component of a splicing enhancer complex that activates a c-src alternative exon in neuronal cellsThe Sm domain is an ancient RNA-binding motif with oligo(U) specificityA Sm-like protein complex that participates in mRNA degradationStructure of yeast U6 snRNPs: arrangement of Prp24p and the LSm complex as revealed by electron microscopyThe Drosophila U7 snRNP proteins Lsm10 and Lsm11 are required for histone pre-mRNA processing and play an essential role in developmentA divergent Sm fold in EDC3 proteins mediates DCP1 binding and P-body targetingSm-like proteins in Eubacteria: the crystal structure of the Hfq protein from Escherichia coliAn Hfq-like protein in archaea: Crystal structure and functional characterization of the Sm protein from Methanococcus jannaschiiSimilar Modes of Interaction Enable Trailer Hitch and EDC3 To Associate with DCP1 and Me31B in Distinct Protein ComplexesIdentification of the proteins of the yeast U1 small nuclear ribonucleoprotein complex by mass spectrometryYeast pre-mRNA splicing requires a pair of U1 snRNP-associated tetratricopeptide repeat proteins.Multiple functional interactions between components of the Lsm2-Lsm8 complex, U6 snRNA, and the yeast La proteinA role for Q/N-rich aggregation-prone regions in P-body localization.A comprehensive biochemical and genetic analysis of the yeast U1 snRNP reveals five novel proteins.Purification of the yeast U4/U6.U5 small nuclear ribonucleoprotein particle and identification of its proteins.Transcriptional pulse-chase analysis reveals a role for a novel snRNP-associated protein in the manufacture of spliceosomal snRNPs.Purification of Drosophila snRNPs and characterization of two populations of functional U1 particles.Peri-implantation lethality in mice lacking the Sm motif-containing protein Lsm4Formation of the 3' end of histone mRNA: getting closer to the endHfq and its constellation of RNASm and Sm-like proteins belong to a large family: identification of proteins of the U6 as well as the U1, U2, U4 and U5 snRNPs
P2860
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P2860
snRNP Sm proteins share two evolutionarily conserved sequence motifs which are involved in Sm protein-protein interactions
description
1995 nî lūn-bûn
@nan
1995 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
1995 թվականի մայիսին հրատարակված գիտական հոդված
@hy
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
name
snRNP Sm proteins share two ev ...... m protein-protein interactions
@ast
snRNP Sm proteins share two ev ...... m protein-protein interactions
@en
snRNP Sm proteins share two ev ...... m protein-protein interactions
@en-gb
snRNP Sm proteins share two ev ...... m protein-protein interactions
@nl
type
label
snRNP Sm proteins share two ev ...... m protein-protein interactions
@ast
snRNP Sm proteins share two ev ...... m protein-protein interactions
@en
snRNP Sm proteins share two ev ...... m protein-protein interactions
@en-gb
snRNP Sm proteins share two ev ...... m protein-protein interactions
@nl
prefLabel
snRNP Sm proteins share two ev ...... m protein-protein interactions
@ast
snRNP Sm proteins share two ev ...... m protein-protein interactions
@en
snRNP Sm proteins share two ev ...... m protein-protein interactions
@en-gb
snRNP Sm proteins share two ev ...... m protein-protein interactions
@nl
P2093
P2860
P1433
P1476
snRNP Sm proteins share two ev ...... m protein-protein interactions
@en
P2093
P Fabrizio
R Lührmann
P2860
P304
P407
P577
1995-05-01T00:00:00Z