ELL (gene)

ELL (gene)

Elongation factor RNA polymerase II, also known as ELL, is a human gene.cite web | title = Entrez Gene: ELL elongation factor RNA polymerase II| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8178| accessdate = ]

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Further reading

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*cite journal | author=Thirman MJ, Levitan DA, Kobayashi H, "et al." |title=Cloning of ELL, a gene that fuses to MLL in a t(11;19)(q23;p13.1) in acute myeloid leukemia. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=91 |issue= 25 |pages= 12110–4 |year= 1995 |pmid= 7991593 |doi=
*cite journal | author=Iwabuchi K, Bartel PL, Li B, "et al." |title=Two cellular proteins that bind to wild-type but not mutant p53. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=91 |issue= 13 |pages= 6098–102 |year= 1994 |pmid= 8016121 |doi=
*cite journal | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171–4 |year= 1994 |pmid= 8125298 |doi=
*cite journal | author=Shilatifard A, Lane WS, Jackson KW, "et al." |title=An RNA polymerase II elongation factor encoded by the human ELL gene. |journal=Science |volume=271 |issue= 5257 |pages= 1873–6 |year= 1996 |pmid= 8596958 |doi=
*cite journal | author=Shilatifard A, Haque D, Conaway RC, Conaway JW |title=Structure and function of RNA polymerase II elongation factor ELL. Identification of two overlapping ELL functional domains that govern its interaction with polymerase and the ternary elongation complex. |journal=J. Biol. Chem. |volume=272 |issue= 35 |pages= 22355–63 |year= 1997 |pmid= 9268387 |doi=
*cite journal | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, "et al." |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149–56 |year= 1997 |pmid= 9373149 |doi=
*cite journal | author=Shilatifard A |title=Identification and purification of the Holo-ELL complex. Evidence for the presence of ELL-associated proteins that suppress the transcriptional inhibitory activity of ELL. |journal=J. Biol. Chem. |volume=273 |issue= 18 |pages= 11212–7 |year= 1998 |pmid= 9556611 |doi=
*cite journal | author=Li XY, Green MR |title=The HIV-1 Tat cellular coactivator Tat-SF1 is a general transcription elongation factor. |journal=Genes Dev. |volume=12 |issue= 19 |pages= 2992–6 |year= 1998 |pmid= 9765201 |doi=
*cite journal | author=Shinobu N, Maeda T, Aso T, "et al." |title=Physical interaction and functional antagonism between the RNA polymerase II elongation factor ELL and p53. |journal=J. Biol. Chem. |volume=274 |issue= 24 |pages= 17003–10 |year= 1999 |pmid= 10358050 |doi=
*cite journal | author=Schmidt AE, Miller T, Schmidt SL, "et al." |title=Cloning and characterization of the EAP30 subunit of the ELL complex that confers derepression of transcription by RNA polymerase II. |journal=J. Biol. Chem. |volume=274 |issue= 31 |pages= 21981–5 |year= 1999 |pmid= 10419521 |doi=
*cite journal | author=Kim MK, Nikodem VM |title=hnRNP U inhibits carboxy-terminal domain phosphorylation by TFIIH and represses RNA polymerase II elongation. |journal=Mol. Cell. Biol. |volume=19 |issue= 10 |pages= 6833–44 |year= 2000 |pmid= 10490622 |doi=
*cite journal | author=Lavau C, Luo RT, Du C, Thirman MJ |title=Retrovirus-mediated gene transfer of MLL-ELL transforms primary myeloid progenitors and causes acute myeloid leukemias in mice. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 20 |pages= 10984–9 |year= 2000 |pmid= 10995463 |doi= 10.1073/pnas.190167297
*cite journal | author=Wiemann S, Weil B, Wellenreuther R, "et al." |title=Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. |journal=Genome Res. |volume=11 |issue= 3 |pages= 422–35 |year= 2001 |pmid= 11230166 |doi= 10.1101/gr.154701
*cite journal | author=Simone F, Polak PE, Kaberlein JJ, "et al." |title=EAF1, a novel ELL-associated factor that is delocalized by expression of the MLL-ELL fusion protein. |journal=Blood |volume=98 |issue= 1 |pages= 201–9 |year= 2001 |pmid= 11418481 |doi=
*cite journal | author=Luo RT, Lavau C, Du C, "et al." |title=The elongation domain of ELL is dispensable but its ELL-associated factor 1 interaction domain is essential for MLL-ELL-induced leukemogenesis. |journal=Mol. Cell. Biol. |volume=21 |issue= 16 |pages= 5678–87 |year= 2001 |pmid= 11463848 |doi= 10.1128/MCB.21.16.5678-5687.2001
*cite journal | author=Simone F, Luo RT, Polak PE, "et al." |title=ELL-associated factor 2 (EAF2), a functional homolog of EAF1 with alternative ELL binding properties. |journal=Blood |volume=101 |issue= 6 |pages= 2355–62 |year= 2003 |pmid= 12446457 |doi= 10.1182/blood-2002-06-1664
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899
*cite journal | author=Polak PE, Simone F, Kaberlein JJ, "et al." |title=ELL and EAF1 are Cajal body components that are disrupted in MLL-ELL leukemia. |journal=Mol. Biol. Cell |volume=14 |issue= 4 |pages= 1517–28 |year= 2003 |pmid= 12686606 |doi= 10.1091/mbc.E02-07-0394
*cite journal | author=Wiederschain D, Kawai H, Gu J, "et al." |title=Molecular basis of p53 functional inactivation by the leukemic protein MLL-ELL. |journal=Mol. Cell. Biol. |volume=23 |issue= 12 |pages= 4230–46 |year= 2003 |pmid= 12773566 |doi=
*cite journal | author=Gerhard DS, Wagner L, Feingold EA, "et al." |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504

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