Results 61 to 70 of about 991,885 (339)

RNA elements directing in vivo assembly of the 7SK/MePCE/Larp7 transcriptional regulatory snRNP [PDF]

open access: yes, 2013
Through controlling the nuclear level of active positive transcription elongation factor b (P-TEFb), the 7SK small nuclear RNA (snRNA) functions as a key regulator of RNA polymerase II transcription.
Bayfield   +43 more
core   +2 more sources

ITGAV and SMAD4 influence the progression and clinical outcome of pancreatic ductal adenocarcinoma

open access: yesMolecular Oncology, EarlyView.
In SMAD4‐positive pancreatic ductal adenocarcinoma (PDAC), integrin subunit alpha V (ITGAV) activates latent TGF‐β, which binds to the TGF‐β receptor and phosphorylates SMAD2/3. The activated SMAD2/3 forms a complex with SMAD4, and together they translocate to the nucleus, modulating gene expression to promote proliferation, migration, and invasion. In
Daniel K. C. Lee   +9 more
wiley   +1 more source

Rsp5 promotes Gene Activation mediated by 9aaTAD Transcription Factors Oaf1 and Gal4 [PDF]

open access: yes, 2009
Nine-amino-acid transactivation domain, 9aaTAD, defines a large superfamily of yeast and mammals transcription factors. The transactivation of the 9aaTAD has been addressed to multiple general co-activators TAF9, MED15, CBP and p300.
Joachim Lipp   +2 more
core   +1 more source

Computational Investigations on Polymerase Actions in Gene Transcription and Replication Combining Physical Modeling and Atomistic Simulations

open access: yes, 2015
Polymerases are protein enzymes that move along nucleic acid chains and catalyze template-based polymerization reactions during gene transcription and replication.
Yu, Jin
core   +1 more source

Schizosaccharomyces pombe Pol II transcription elongation factor ELL functions as part of a rudimentary super elongation complex [PDF]

open access: yes, 2018
ELL family transcription factors activate the overall rate of RNA polymerase II (Pol II) transcription elongation by binding directly to Pol II and suppressing its tendency to pause.
Alonso-Nunez   +54 more
core   +1 more source

Comprehensive profiling of lncRNAs and mRNAs enriched in small extracellular vesicles for early noninvasive detection of colorectal cancer: diagnostic panel assembly and extensive validation

open access: yesMolecular Oncology, EarlyView.
Small extracellular vesicles are a promising source of diagnostic molecules. We conducted a comprehensive study, including transcriptome profiling and RT‐qPCR validation on large cohorts of samples. Diagnostic panels enabling sensitive detection of colorectal cancer and precancerous lesions were established. Some molecules were differentially expressed
Petra Vychytilova‐Faltejskova   +26 more
wiley   +1 more source

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

open access: yesGenes & Development, 1998
We report the identification of a transcription elongation factor from HeLa cell nuclear extracts that causes pausing of RNA polymerase II (Pol II) in conjunction with the transcription inhibitor 5,6-dichloro-1-beta-D-ribofuranosylbenzimidazole (DRB ...
T. Wada   +11 more
semanticscholar   +1 more source

A Ribonucleolytic Rat Torpedoes RNA Polymerase II [PDF]

open access: yesCell, 2004
Three recent papers reveal a fascinating link between pol II termination and ribonucleolytic decay of the nascent transcript by a 5'-3' exonuclease (yeast Rat1 and human Xrn2). The exonuclease travels with pol II and gains access to the nascent RNA after endonucleolytic cleavage at the poly(A) site or at a second cotranscriptional cleavage site (CoTC).
David Bentley, Weifei Luo
openaire   +3 more sources

The pause-initiation limit restricts transcription activation in human cells.

open access: yes, 2019
Eukaryotic gene transcription is often controlled at the level of RNA polymerase II (Pol II) pausing in the promoter-proximal region. Pausing Pol II limits the frequency of transcription initiation ('pause-initiation limit'), predicting that the pause ...
Cramer, P., Gressel, S., Schwalb, B.
core   +1 more source

In vivo analysis of NHPX reveals a novel nucleolar localization pathway involving a transient accumulation in splicing speckles [PDF]

open access: yes, 2002
The NHPX protein is a nucleolar factor that binds directly to a conserved RNA target sequence found in nucleolar box C/D snoRNAs and in U4 snRNA. Using enhanced yellow fluorescent protein (EYFP)– and enhanced cyan fluorescent protein–NHPX fusions, we ...
Lamond, Angus I., Leung, Anthony K. L.
core   +5 more sources

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