Dual roles for Spt5 in pre-mRNA processing and transcription elongation revealed by identification of Spt5-associated proteins. - Test2 - elhamkhani - TriplyDB

Dual roles for Spt5 in pre-mRNA processing and transcription elongation revealed by identification of Spt5-associated proteins.

Dual roles for Spt5 in pre-mRNA processing and transcription elongation revealed by identification of Spt5-associated proteins.

http://www.wikidata.org/entity/Q27930157

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Network compression as a quality measure for protein interaction networks The Spt6 SH2 domain binds Ser2-P RNAPII to direct Iws1-dependent mRNA splicing and export Evolutionary conservation supports ancient origin for Nudt16, a nuclear-localized, RNA-binding, RNA-decapping enzyme Autosomal dominant retinitis pigmentosa mutations in inosine 5'-monophosphate dehydrogenase type I disrupt nucleic acid binding A sequence motif conserved in diverse nuclear proteins identifies a protein interaction domain utilised for nuclear targeting by human TFIIS Functional interactions of RNA-capping enzyme with factors that positively and negatively regulate promoter escape by RNA polymerase II Human Spt6 stimulates transcription elongation by RNA polymerase II in vitro IMP dehydrogenase: structure, mechanism, and inhibition.Regulation of mRNA cap methylation Shotgun proteomics in neuroscience Analysis of a splice array experiment elucidates roles of chromatin elongation factor Spt4-5 in splicing The Spt4-Spt5 complex: a multi-faceted regulator of transcription elongation Crystal structure of the human transcription elongation factor DSIF hSpt4 subunit in complex with the hSpt5 dimerization interface Spt4/5 stimulates transcription elongation through the RNA polymerase clamp coiled-coil motif The Transcription Factor Spn1 Regulates Gene Expression via a Highly Conserved Novel Structural Motif Noncanonical Tandem SH2 Enables Interaction of Elongation Factor Spt6 with RNA Polymerase II The structure of an Iws1/Spt6 complex reveals an interaction domain conserved in TFIIS, Elongin A and Med26 Structure and Biological Importance of the Spn1-Spt6 Interaction, and Its Regulatory Role in Nucleosome Binding Structural basis for Spt5-mediated recruitment of the Paf1 complex to chromatin The ESS1 prolyl isomerase and its suppressor BYE1 interact with RNA pol II to inhibit transcription elongation in Saccharomyces cerevisiae.Uniform transitions of the general RNA polymerase II transcription complex.Interaction between transcription elongation factors and mRNA 3'-end formation at the Saccharomyces cerevisiae GAL10-GAL7 locus.Tho1, a novel hnRNP, and Sub2 provide alternative pathways for mRNP biogenesis in yeast THO mutants Functional roles for evolutionarily conserved Spt4p at centromeres and heterochromatin in Saccharomyces cerevisiae mRNA capping enzyme activity is coupled to an early transcription elongation Rtr1 is the Saccharomyces cerevisiae homolog of a novel family of RNA polymerase II-binding proteins.Separation of the Saccharomyces cerevisiae Paf1 complex from RNA polymerase II results in changes in its subnuclear localization.Role for the Ssu72 C-terminal domain phosphatase in RNA polymerase II transcription elongation.Identification and characterization of Elf1, a conserved transcription elongation factor in Saccharomyces cerevisiae.Cotranscriptional recruitment of She2p by RNA pol II elongation factor Spt4-Spt5/DSIF promotes mRNA localization to the yeast bud.RNA polymerase II elongation factors Spt4p and Spt5p play roles in transcription elongation by RNA polymerase I and rRNA processing FACT prevents the accumulation of free histones evicted from transcribed chromatin and a subsequent cell cycle delay in G1.The yeast transcription elongation factor Spt4/5 is a sequence-specific RNA binding protein.A Requirement for the Saccharomyces cerevisiae Paf1 complex in snoRNA 3' end formation A functional interface at the rDNA connects rRNA synthesis, pre-rRNA processing and nucleolar surveillance in budding yeast Biochemical Analysis of Yeast Suppressor of Ty 4/5 (Spt4/5) Reveals the Importance of Nucleic Acid Interactions in the Prevention of RNA Polymerase II Arrest Npl3 is an antagonist of mRNA 3' end formation by RNA polymerase II.Histone H2B ubiquitylation is associated with elongating RNA polymerase II The cotranscriptional assembly of snoRNPs controls the biosynthesis of H/ACA snoRNAs in Saccharomyces cerevisiae.Histone H3K4 and K36 methylation, Chd1 and Rpd3S oppose the functions of Saccharomyces cerevisiae Spt4-Spt5 in transcription.

P2860

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P2860

Dual roles for Spt5 in pre-mRNA processing and transcription elongation revealed by identification of Spt5-associated proteins.

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2003 nî lūn-bûn

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2003 թուականի Փետրուարին հրատարակուած գիտական յօդուած

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Dual roles for Spt5 in pre-mRN ...... n of Spt5-associated proteins.

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MCB.23.4.1368-1378.2003

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Molecular and Cellular Biology

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Dual roles for Spt5 in pre-mRN ...... n of Spt5-associated proteins.

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C A Emigh

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D L Lindstrom

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J R Yates

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K C Wachter

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N Muster

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S L Squazzo

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P2860

Tat-SF1 protein associates with RAP30 and human SPT5 proteins

Evidence that P-TEFb alleviates the negative effect of DSIF on RNA polymerase II-dependent transcription in vitro

The chromatin-specific transcription elongation factor FACT comprises human SPT16 and SSRP1 proteins

Functional organization of the yeast proteome by systematic analysis of protein complexes

Participation of the nuclear cap binding complex in pre-mRNA 3' processing

DSIF, a novel transcription elongation factor that regulates RNA polymerase II processivity, is composed of human Spt4 and Spt5 homologs

A novel RNA polymerase II-containing complex potentiates Tat-enhanced HIV-1 transcription

Domains in the SPT5 protein that modulate its transcriptional regulatory properties

Transcription elongation factor hSPT5 stimulates mRNA capping

mRNA capping enzyme is recruited to the transcription complex by phosphorylation of the RNA polymerase II carboxy-terminal domain

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1368-1378

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