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The protein encoded by RDBP is part of a complex termed negative elongation factor (NELF) which represses RNA polymerase II transcript elongation. Additionally we are shipping RD RNA Binding Protein Antibodies (26) and many more products for this protein.
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biochemical analysis reveals that the sequence-specific transcription factor, GAF, orchestrates efficient pausing by recruiting NELF to promoters before transcription initiation and by assisting in loading NELF onto Pol II after initiation
The finding that both phenotypes of arrested embryos are obtained in embryos that lack maternally provided NELF-A as well as in embryos with reduced levels of maternal NELF-E show that these phenotypes result from the reduced activity of the NELF complex.
propose that NELF and DSIF (show SUPT4H1 Proteins) cause polymerase to pause in the promoter proximal region of hsp70
A positively charged face of NELF-AC is involved in RNA binding, whereas the opposite face of the NELF-AC subcomplex binds NELF-B (show COBRA1 Proteins). NELF-B (show COBRA1 Proteins) is predicted to form a HEAT repeat fold, also binds RNA in vivo, and anchors the subunit NELF-E, which is confirmed to bind RNA in vivo.
novel actions of BRD4 (show BRD4 Proteins) and of NELF-E in GR-controlled gene induction have been uncovered.
Following NELF-E knockdown or tumor necrosis factor alpha stimulation, promoter-proximal RNAP II levels increase up to 3-fold, and there is a dramatic increase in RNAP II levels within the HIV genome.
these results describe the RNA binding behavior of NELF-E and supports a biological role for NELF-E in promoter-proximal pausing of both HIV-1 and cellular genes.
Multivariate analysis revealed that RDBP protein levels were an independent risk factor for early intrahepatic recurrence of HCC (show FAM126A Proteins) within 2 years of surgery.
the transcription elongation of KSHV OriLytL-K7 lytic genes is inhibited by NELF during latency, but can also be promptly reactivated in an RTA (show RBM9 Proteins)-independent manner upon external stimuli
data show that NELF subunits exhibit highly specific subcellular localizations, such as in NELF bodies or in midbodies, and some shuttle actively between the nucleus and cytoplasm; loss of NELF from cells can lead to enlarged and/or multiple nuclei
Transient NELF-E knock-down in pituitary increased coincidentally prolactin (show PRL Proteins) expression and enhanced transcription of a prolactin (show PRL Proteins)-promoter reporter gene.
Evidence that negative elongation factor represses transcription elongation through binding to a DRB sensitivity-inducing factor/RNA polymerase II complex and RNA
NELF-C (show TH1L Proteins) and NELF-D (show TH1L Proteins) are highly related or identical to the protein called TH1 (show TH1L Proteins), of unknown function. NELF-B (show COBRA1 Proteins) and NELF-C (show TH1L Proteins) or NELF-D (show TH1L Proteins) are integral subunits that bring NELF-A (show WHSC2 Proteins) and NELF-E together. [NELF-B (show COBRA1 Proteins)] [NELF-C (show TH1L Proteins)]
The protein encoded by this gene is part of a complex termed negative elongation factor (NELF) which represses RNA polymerase II transcript elongation. This protein bears similarity to nuclear RNA-binding proteins\; however, it has not been demonstrated that this protein binds RNA. The protein contains a tract of alternating basic and acidic residues, largely arginine (R) and aspartic acid (D). The gene localizes to the major histocompatibility complex (MHC) class III region on chromosome 6.
, negative elongation factor
, negative elongation factor E
, RD RNA binding protein
, RD RNA-binding protein
, RNA-binding protein RD
, major histocompatibility complex gene RD
, negative elongation factor polypeptide E
, nuclear protein