Spt4/5 stimulates transcription elongation through the RNA polymerase clamp coiled-coil motif - Wikidata - wikimedia - TriplyDB

Spt4/5 stimulates transcription elongation through the RNA polymerase clamp coiled-coil motif

Spt4/5 stimulates transcription elongation through the RNA polymerase clamp coiled-coil motif

http://www.wikidata.org/entity/Q27660089

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Termination and antitermination: RNA polymerase runs a stop sign New Insights into the Functions of Transcription Factors that Bind the RNA Polymerase Secondary Channel NusG/Spt5: are there common functions of this ubiquitous transcription elongation factor?The Spt4-Spt5 complex: a multi-faceted regulator of transcription elongation RNA polymerase and transcription elongation factor Spt4/5 complex structure.Architecture of the RNA polymerase-Spt4/5 complex and basis of universal transcription processivity An α Helix to β Barrel Domain Switch Transforms the Transcription Factor RfaH into a Translation Factor Structural basis for Spt5-mediated recruitment of the Paf1 complex to chromatin Structure of transcribing mammalian RNA polymerase II The transcription elongation factor Spt5 influences transcription by RNA polymerase I positively and negatively.Uniform transitions of the general RNA polymerase II transcription complex.The yeast transcription elongation factor Spt4/5 is a sequence-specific RNA binding protein.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 Yeast transcription elongation factor Spt5 associates with RNA polymerase I and RNA polymerase II directly.Ubiquitous transcription factors display structural plasticity and diverse functions: NusG proteins - Shifting shapes and paradigms Pleiohomeotic interacts with the core transcription elongation factor Spt5 to regulate gene expression in Drosophila Sub1 associates with Spt5 and influences RNA polymerase II transcription elongation rate A meiosis-specific Spt5 homolog involved in non-coding transcription.Insights into how Spt5 functions in transcription elongation and repressing transcription coupled DNA repair.The interactome of the atypical phosphatase Rtr1 in Saccharomyces cerevisiae RNA polymerase II transcription elongation and Pol II CTD Ser2 phosphorylation: A tail of two kinases.Simulation vs. reality: a comparison of in silico distance predictions with DEER and FRET measurements Functional analysis of Thermus thermophilus transcription factor NusG Transcription elongation. Heterogeneous tracking of RNA polymerase and its biological implications.Pol II waiting in the starting gates: Regulating the transition from transcription initiation into productive elongation.Mutations in the transcription elongation factor SPT5 disrupt a reporter for dosage compensation in Drosophila Highly reproducible label free quantitative proteomic analysis of RNA polymerase complexes.The β subunit gate loop is required for RNA polymerase modification by RfaH and NusG.The initiation factor TFE and the elongation factor Spt4/5 compete for the RNAP clamp during transcription initiation and elongation RNA polymerase I activity is regulated at multiple steps in the transcription cycle: recent insights into factors that influence transcription elongation.The spt5 C-terminal region recruits yeast 3' RNA cleavage factor I.Structures and Functions of the Multiple KOW Domains of Transcription Elongation Factor Spt5 Rho and NusG suppress pervasive antisense transcription in Escherichia coli.TFE and Spt4/5 open and close the RNA polymerase clamp during the transcription cycle Pausing for thought: disrupting the early transcription elongation checkpoint leads to developmental defects and tumourigenesis.Structural insights into NusG regulating transcription elongation.Hold on!: RNA polymerase interactions with the nascent RNA modulate transcription elongation and termination.A nexus for gene expression-molecular mechanisms of Spt5 and NusG in the three domains of life.Archaeology of RNA polymerase: factor swapping during the transcription cycle.The transcript elongation factor SPT4/SPT5 is involved in auxin-related gene expression in Arabidopsis

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Spt4/5 stimulates transcription elongation through the RNA polymerase clamp coiled-coil motif

http://www.wikidata.org/entity/Q27660089

description

2010 nî lūn-bûn

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2010 թուականի Յուլիսին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի հուլիսին հրատարակված գիտական հոդված

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2010年の論文

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2010年学术文章

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2010年学术文章

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2010年学术文章

@zh-hans

2010年学术文章

@zh-my

2010年学术文章

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2010年學術文章

@yue

name

Spt4/5 stimulates transcriptio ...... merase clamp coiled-coil motif

@ast

Spt4/5 stimulates transcriptio ...... merase clamp coiled-coil motif

@en

Spt4/5 stimulates transcriptio ...... merase clamp coiled-coil motif

@nl

type

label

Spt4/5 stimulates transcriptio ...... merase clamp coiled-coil motif

@ast

Spt4/5 stimulates transcriptio ...... merase clamp coiled-coil motif

@en

Spt4/5 stimulates transcriptio ...... merase clamp coiled-coil motif

@nl

prefLabel

Spt4/5 stimulates transcriptio ...... merase clamp coiled-coil motif

@ast

Spt4/5 stimulates transcriptio ...... merase clamp coiled-coil motif

@en

Spt4/5 stimulates transcriptio ...... merase clamp coiled-coil motif

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Nucleic Acids Research

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Spt4/5 stimulates transcriptio ...... merase clamp coiled-coil motif

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Angela Hirtreiter

http://www.w3.org/2001/XMLSchema#string

Dina Grohmann

http://www.w3.org/2001/XMLSchema#string

Erika Vojnic

http://www.w3.org/2001/XMLSchema#string

Gerke E Damsma

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Patrick Cramer

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P2860

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

Domains in the SPT5 protein that modulate its transcriptional regulatory properties

Crystal structure and RNA binding of the Rpb4/Rpb7 subunits of human RNA polymerase II

Structure of an archaeal homolog of the eukaryotic RNA polymerase II RPB4/RPB7 complex

Crystal structures of transcription factor NusG in light of its nucleic acid- and protein-binding activities

Structural Basis for Converting a General Transcription Factor into an Operon-Specific Virulence Regulator

Crystal structure of NusG N-terminal (NGN) domain from Methanocaldococcus jannaschii and its interaction with rpoE''

Two Structurally Independent Domains of E. coli NusG Create Regulatory Plasticity via Distinct Interactions with RNA Polymerase and Regulators

Crystal structure of the human transcription elongation factor DSIF hSpt4 subunit in complex with the hSpt5 dimerization interface

Coot: model-building tools for molecular graphics

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4040-4051

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scholarly article

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3163764

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10.1093/NAR/GKQ135

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12

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38

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2010-03-02T00:00:00Z

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41669142

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20197319

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2896526

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