AFF4, a component of the ELL/P-TEFb elongation complex and a shared subunit of MLL chimeras, can link transcription elongation to leukemia.
暂无分享,去创建一个
A. Shilatifard | M. Washburn | L. Florens | R. Conaway | J. Conaway | Edwin R. Smith | Chengqi Lin | Hidehisa Takahashi | Ka Chun Lai | S. Martin-Brown
[1] C. Bach,et al. Misguided Transcriptional Elongation Causes Mixed Lineage Leukemia , 2009, PLoS biology.
[2] Mark Johnston,et al. Linking cell cycle to histone modifications: SBF and H2B monoubiquitination machinery and cell-cycle regulation of H3K79 dimethylation. , 2009, Molecular cell.
[3] Madelaine Gogol,et al. Global Analysis of H3K4 Methylation Defines MLL Family Member Targets and Points to a Role for MLL1-Mediated H3K4 Methylation in the Regulation of Transcriptional Initiation by RNA Polymerase II , 2009, Molecular and Cellular Biology.
[4] Alistair N Boettiger,et al. Synchronous and Stochastic Patterns of Gene Activation in the Drosophila Embryo , 2009, Science.
[5] W. Webb,et al. Spt6 enhances the elongation rate of RNA polymerase II in vivo , 2009, The EMBO journal.
[6] K. Davies,et al. The Robotic Mouse: Understanding the Role of AF4, a Cofactor of Transcriptional Elongation and Chromatin Remodelling, in Purkinje Cell Function , 2009, The Cerebellum.
[7] A. Giordano,et al. Role of the cyclin-dependent kinase 9-related pathway in mammalian gene expression and human diseases , 2008, Cell cycle.
[8] Xiaobo Xia,et al. H3K79 methylation profiles define murine and human MLL-AF4 leukemias. , 2008, Cancer cell.
[9] Peng Fei Wang,et al. Molecular Regulation of H3K4 Trimethylation by Wdr82, a Component of Human Set1/COMPASS , 2008, Molecular and Cellular Biology.
[10] Akihiko Yokoyama,et al. Menin critically links MLL proteins with LEDGF on cancer-associated target genes. , 2008, Cancer cell.
[11] A. Shilatifard,et al. Regulation of the transcriptional activity of poised RNA polymerase II by the elongation factor ELL , 2008, Proceedings of the National Academy of Sciences.
[12] A. Chinnaiyan,et al. A role for the MLL fusion partner ENL in transcriptional elongation and chromatin modification. , 2007, Blood.
[13] Ruchir Shah,et al. RNA polymerase is poised for activation across the genome , 2007, Nature Genetics.
[14] Manolis Kellis,et al. RNA polymerase stalling at developmental control genes in the Drosophila melanogaster embryo , 2007, Nature Genetics.
[15] R. Kornberg. The molecular basis of eukaryotic transcription , 2007, Proceedings of the National Academy of Sciences.
[16] K. Davies,et al. The mixed-lineage leukemia fusion partner AF4 stimulates RNA polymerase II transcriptional elongation and mediates coordinated chromatin remodeling. , 2007, Human molecular genetics.
[17] A. Shilatifard,et al. Cdk9 is an essential kinase in Drosophila that is required for heat shock gene expression, histone methylation and elongation factor recruitment , 2007, Molecular Genetics and Genomics.
[18] A. Shilatifard,et al. Drosophila Rtf1 functions in histone methylation, gene expression, and Notch signaling , 2006, Proceedings of the National Academy of Sciences.
[19] B. Peterlin,et al. Controlling the elongation phase of transcription with P-TEFb. , 2006, Molecular cell.
[20] Wenzheng Zhang,et al. Dot1a-AF9 Complex Mediates Histone H3 Lys-79 Hypermethylation and Repression of ENaCα in an Aldosterone-sensitive Manner* , 2006, Journal of Biological Chemistry.
[21] A. Shilatifard,et al. Mutational Analysis of an RNA Polymerase II Elongation Factor in Drosophila melanogaster , 2005, Molecular and Cellular Biology.
[22] A. Shilatifard,et al. ELL-associated factors 1 and 2 are positive regulators of RNA polymerase II elongation factor ELL. , 2005, Proceedings of the National Academy of Sciences of the United States of America.
[23] A. Shilatifard,et al. A COMPASS in the voyage of defining the role of trithorax/MLL‐containing complexes: Linking leukemogensis to covalent modifications of chromatin , 2005, Journal of cellular biochemistry.
[24] Yi Zhang,et al. hDOT1L Links Histone Methylation to Leukemogenesis , 2005, Cell.
[25] A. Shilatifard,et al. Regulation of Heat Shock Gene Expression by RNA Polymerase II Elongation Factor, Elongin A* , 2005, Journal of Biological Chemistry.
[26] J. Lis,et al. Transcription Factor and Polymerase Recruitment, Modification, and Movement on dhsp70 In Vivo in the Minutes following Heat Shock , 2003, Molecular and Cellular Biology.
[27] P. Polak,et al. ELL-associated factor 2 (EAF2), a functional homolog of EAF1 with alternative ELL binding properties. , 2003, Blood.
[28] J. Lis,et al. The RNA processing exosome is linked to elongating RNA polymerase II in Drosophila , 2002, Nature.
[29] Philip M Kluin,et al. LAF4, an AF4‐related gene, is fused to MLL in infant acute lymphoblastic leukemia , 2002, Genes, chromosomes & cancer.
[30] A. Shilatifard,et al. dELL is an essential RNA polymerase II elongation factor with a general role in development , 2002, Proceedings of the National Academy of Sciences of the United States of America.
[31] A. Shilatifard,et al. Drosophila ELL is associated with actively elongating RNA polymerase II on transcriptionally active sites in vivo , 2001, The EMBO journal.
[32] P. Polak,et al. EAF1, a novel ELL-associated factor that is delocalized by expression of the MLL-ELL fusion protein. , 2001, Blood.
[33] A. Shilatifard,et al. Functional Analysis of the Leukemia Protein ELL: Evidence for a Role in the Regulation of Cell Growth and Survival , 2001, Molecular and Cellular Biology.
[34] E. Hafen,et al. Lilliputian: an AF4/FMR2-related protein that controls cell identity and cell growth. , 2001, Development.
[35] T. P. Neufeld,et al. Transcriptional regulation of cytoskeletal functions and segmentation by a novel maternal pair-rule gene, lilliputian. , 2001, Development.
[36] S. Newfeld,et al. A screen for modifiers of decapentaplegic mutant phenotypes identifies lilliputian, the only member of the Fragile-X/Burkitt's Lymphoma family of transcription factors in Drosophila melanogaster. , 2001, Genetics.
[37] A. Shilatifard,et al. A carboxy-terminal domain of ELL is required and sufficient for immortalization of myeloid progenitors by MLL-ELL. , 2000, Blood.
[38] A. Shilatifard,et al. Identification, Cloning, Expression, and Biochemical Characterization of the Testis-specific RNA Polymerase II Elongation Factor ELL3* , 2000, The Journal of Biological Chemistry.
[39] A. Shilatifard,et al. Control of elongation by RNA polymerase II. , 2000, Trends in biochemical sciences.
[40] J. Lis,et al. P-TEFb kinase recruitment and function at heat shock loci. , 2000, Genes & development.
[41] G M Rubin,et al. A genetic screen for novel components of the Ras/Mitogen-activated protein kinase signaling pathway that interact with the yan gene of Drosophila identifies split ends, a new RNA recognition motif-containing protein. , 2000, Genetics.
[42] J. Rowley,et al. The critical role of chromosome translocations in human leukemias. , 1998, Annual review of genetics.
[43] T. P. Neufeld,et al. A genetic screen to identify components of the sina signaling pathway in Drosophila eye development. , 1998, Genetics.
[44] A. Shilatifard,et al. ELL2, a new member of an ELL family of RNA polymerase II elongation factors. , 1997, Proceedings of the National Academy of Sciences of the United States of America.
[45] R. Conaway,et al. The RNA polymerase II general elongation factors. , 1996, Trends in biochemical sciences.
[46] A. Shilatifard,et al. An RNA Polymerase II Elongation Factor Encoded by the Human ELL Gene , 1996, Science.
[47] R. Conaway,et al. The RNA polymerase II elongation complex , 1995, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.
[48] J. Rowley,et al. Cloning of ELL, a gene that fuses to MLL in a t(11;19)(q23;p13.1) in acute myeloid leukemia. , 1994, Proceedings of the National Academy of Sciences of the United States of America.
[49] K. Davies,et al. Trinucleotide repeat amplification and hypermethylation of a CpG island in FRAXE mental retardation , 1993, Cell.
[50] R. Conaway,et al. General initiation factors for RNA polymerase II. , 1993, Annual review of biochemistry.