Unphosphorylated SR-like protein Npl3 stimulates RNA polymerase II elongation.
about
SR proteins in vertical integration of gene expression from transcription to RNA processing to translationDynamic integration of splicing within gene regulatory pathwaysGene-specific requirement of RNA polymerase II CTD phosphorylationRSR-2, the Caenorhabditis elegans ortholog of human spliceosomal component SRm300/SRRM2, regulates development by influencing the transcriptional machineryYeast arginine methyltransferase Hmt1p regulates transcription elongation and termination by methylating Npl3p.The shuttling protein Npl3 promotes translation termination accuracy in Saccharomyces cerevisiae.A single SR-like protein, Npl3, promotes pre-mRNA splicing in budding yeast.The yeast SR-like protein Npl3 links chromatin modification to mRNA processingThe Ccr4-Not complex interacts with the mRNA export machineryRNA Polymerase II C-Terminal Domain: Tethering Transcription to Transcript and TemplateTranscription termination by nuclear RNA polymerasesRecruitment of TREX to the transcription machinery by its direct binding to the phospho-CTD of RNA polymerase IIMolecular mechanisms of eukaryotic pre-mRNA 3' end processing regulation.Coupled evolution of transcription and mRNA degradation.The RNA polymerase II CTD coordinates transcription and RNA processing.SR-like RNA-binding protein Slr1 affects Candida albicans filamentation and virulence.Diverse environmental stresses elicit distinct responses at the level of pre-mRNA processing in yeast.Emerging Views on the CTD CodeCo-transcriptional regulation of alternative pre-mRNA splicingThe identification of putative RNA polymerase II C-terminal domain associated proteins in red and green algae.SRSF1 regulates the assembly of pre-mRNA processing factors in nuclear speckles.Specific combinations of SR proteins associate with single pre-messenger RNAs in vivo and contribute different functionsSpecific sequences within arginine-glycine-rich domains affect mRNA-binding protein function.Cotranscriptional recruitment of yeast TRAMP complex to intronic sequences promotes optimal pre-mRNA splicing.H2B ubiquitylation modulates spliceosome assembly and function in budding yeast.Integrating transcription kinetics with alternative polyadenylation and cell cycle control.Protein arginine methylation in Saccharomyces cerevisiae.Co-transcriptional mRNP formation is coordinated within a molecular mRNP packaging station in S. cerevisiaeRestriction of histone gene transcription to S phase by phosphorylation of a chromatin boundary protein.Loss of the Yeast SR Protein Npl3 Alters Gene Expression Due to Transcription Readthrough.Npl3, a new link between RNA-binding proteins and the maintenance of genome integrity.The RNA binding protein Npl3 promotes resection of DNA double-strand breaks by regulating the levels of Exo1.Yeast hnRNP-related proteins contribute to the maintenance of telomeres.The Npl3 hnRNP prevents R-loop-mediated transcription-replication conflicts and genome instabilitymRNA imprinting: Additional level in the regulation of gene expression.Interactions affected by arginine methylation in the yeast protein-protein interaction network.A role for Chk1 in blocking transcriptional elongation of p21 RNA during the S-phase checkpoint.Evolution of protein phosphorylation across 18 fungal species.Post-translational modification directs nuclear and hyphal tip localization of Candida albicans mRNA-binding protein Slr1.
P2860
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P2860
Unphosphorylated SR-like protein Npl3 stimulates RNA polymerase II elongation.
description
2008 nî lūn-bûn
@nan
2008 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2008 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
name
Unphosphorylated SR-like protein Npl3 stimulates RNA polymerase II elongation.
@ast
Unphosphorylated SR-like protein Npl3 stimulates RNA polymerase II elongation.
@en
Unphosphorylated SR-like protein Npl3 stimulates RNA polymerase II elongation.
@nl
type
label
Unphosphorylated SR-like protein Npl3 stimulates RNA polymerase II elongation.
@ast
Unphosphorylated SR-like protein Npl3 stimulates RNA polymerase II elongation.
@en
Unphosphorylated SR-like protein Npl3 stimulates RNA polymerase II elongation.
@nl
prefLabel
Unphosphorylated SR-like protein Npl3 stimulates RNA polymerase II elongation.
@ast
Unphosphorylated SR-like protein Npl3 stimulates RNA polymerase II elongation.
@en
Unphosphorylated SR-like protein Npl3 stimulates RNA polymerase II elongation.
@nl
P2093
P2860
P50
P1433
P1476
Unphosphorylated SR-like protein Npl3 stimulates RNA polymerase II elongation.
@en
P2093
Alfred S Ponticelli
Babatunde Ogundipe
Claire L Moore
Jessica L Dermody
Peter J Park
P2860
P356
10.1371/JOURNAL.PONE.0003273
P407
P577
2008-09-26T00:00:00Z