NELFE Antibody

1. define two mutually exclusive complexes CBC-NELF-E and CBC-ARS2-PHAX, which likely act in respectively earlier and later phases of transcription PMID: 29101316
2. novel actions of BRD4 and of NELF-E in GR-controlled gene induction have been uncovered. PMID: 26504077
3. 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. PMID: 24636995
4. 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. PMID: 24453987
5. Multivariate analysis revealed that RDBP protein levels were an independent risk factor for early intrahepatic recurrence of HCC within 2 years of surgery. PMID: 22614758
6. the transcription elongation of KSHV OriLytL-K7 lytic genes is inhibited by NELF during latency, but can also be promptly reactivated in an RTA-independent manner upon external stimuli PMID: 22740393
7. Transient NELF-E knock-down in pituitary increased coincidentally prolactin expression and enhanced transcription of a prolactin-promoter reporter gene. PMID: 20097260
8. Evidence that negative elongation factor represses transcription elongation through binding to a DRB sensitivity-inducing factor/RNA polymerase II complex and RNA PMID: 11940650
9. 5,6-dichloro-1-beta-D-ribofuranosylbenzimidazole sensitivity-inducing factor (DSIF)- and NELF-mediated transcriptional pausing has a dual function in regulating immediate-early expression of the human junB gene. PMID: 16880520
10. NELF E RRM binds to the single-stranded TAR RNAs with K(d) values in the low-micromolar range. PMID: 16898873
11. Negative elongation factor (NELF) is a four subunit transcription factor. Our results point to a surprising role of NELF in the 3' end processing of histone mRNAs and suggest that NELF is a new factor that coordinates mRNA processing in transcription. PMID: 17499042
12. RNA binding to NELF-E RRM induces formation of a helix in the C-terminus. RNA-bound form of NELF-E RRM is very similar to RNA-bound form of U1A RRM, although C-terminus of NELF-E RRM is unstructured in free protein, whereas it is helical in U1A protein. PMID: 18303858
13. Our results do not support any major role of the 4 AMD-associated variants in the risk of developing PCV, but favor a predominant association with the RDBP-SKIV2L variants PMID: 19556007

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HGNC: 13974

OMIM: 154040

KEGG: hsa:7936

STRING: 9606.ENSP00000364578

UniGene: Hs.423935