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Volumn 12, Issue 14, 1998, Pages 1437-1446

Factors regulating the transcriptional elongation activity of RNA polymerase II

Author keywords

ELL associated proteins transcriptional arrest; mRNA synthesis; Negative elongation factor

Indexed keywords

ELONGATION FACTOR; RNA POLYMERASE II;

EID: 0031763366     PISSN: 08926638     EISSN: None     Source Type: Journal    
DOI: 10.1096/fasebj.12.14.1437     Document Type: Review
Times cited : (99)

References (85)
  • 1
    • 0029011873 scopus 로고
    • Purification of P-TEFb, a transcription factor required for the transition into productive elongation
    • Marshall, N. F., and Price, D. H. (1995) Purification of P-TEFb, a transcription factor required for the transition into productive elongation. J. Biol. Chem. 270, 12335-12338
    • (1995) J. Biol. Chem. , vol.270 , pp. 12335-12338
    • Marshall, N.F.1    Price, D.H.2
  • 2
    • 0029942906 scopus 로고    scopus 로고
    • TFIIH functions in regulating transcriptional elongation by Pol II in Xenopus oocytes
    • Yankulov, K. Y., Pandes M., McCracken, S., Bouchard, D., and Bentley, D. L. (1996) TFIIH functions in regulating transcriptional elongation by Pol II in Xenopus oocytes. Mol. Cell Biol. 16, 3291-3299
    • (1996) Mol. Cell Biol. , vol.16 , pp. 3291-3299
    • Yankulov, K.Y.1    Pandes, M.2    McCracken, S.3    Bouchard, D.4    Bentley, D.L.5
  • 3
    • 0029759928 scopus 로고    scopus 로고
    • Activator-dependent regulation of transcriptional pausing on nucleosomal templates
    • Brown, S. A., Imbalzano, A. N., and Kingston, R. E. (1996) Activator-dependent regulation of transcriptional pausing on nucleosomal templates. Genes & Dev. 10, 1479-1490
    • (1996) Genes & Dev. , vol.10 , pp. 1479-1490
    • Brown, S.A.1    Imbalzano, A.N.2    Kingston, R.E.3
  • 4
    • 0029879664 scopus 로고    scopus 로고
    • An RNA polymerasc II elongation factor encoded by the human ELL gene
    • Shilatifard, A., Lane, W. S., Jackson, K. W., Conaway, R. C., and Conaway, J. W. (1996) An RNA polymerasc II elongation factor encoded by the human ELL gene. Science 271, 1873-1876
    • (1996) Science , vol.271 , pp. 1873-1876
    • Shilatifard, A.1    Lane, W.S.2    Jackson, K.W.3    Conaway, R.C.4    Conaway, J.W.5
  • 5
    • 0030772029 scopus 로고    scopus 로고
    • Structure and function of an RNA polymerase II elongation factor ELL. Identification of two overlapping ELL functional domains that govern its interaction with polymerase and the ternary elongation complex
    • Shilatifard, A., Haque, D., Conaway, R. C., and Conaway, J. W. (1997) Structure and function of an RNA polymerase II elongation factor ELL. Identification of two overlapping ELL functional domains that govern its interaction with polymerase and the ternary elongation complex. J. Biol. Chem. 272, 22355-22363
    • (1997) J. Biol. Chem. , vol.272 , pp. 22355-22363
    • Shilatifard, A.1    Haque, D.2    Conaway, R.C.3    Conaway, J.W.4
  • 6
    • 0032080140 scopus 로고    scopus 로고
    • Identification and purification of the Holo-ELL complex
    • Shilatifard, A. (1998) Identification and purification of the Holo-ELL complex. J. Biol. Chem. 273,11212-11217
    • (1998) J. Biol. Chem. , vol.273 , pp. 11212-11217
    • Shilatifard, A.1
  • 7
    • 0027378324 scopus 로고
    • An RNA polymerase II transcription factor SIII. I. Identification, purification, and properties
    • Bradsher, J. N., Jackson, K. W., Conaway, R. C., and Cottaway, J. W. (1993) An RNA polymerase II transcription factor SIII. I. Identification, purification, and properties. J. Biol. Chem. 268, 25587-25593
    • (1993) J. Biol. Chem. , vol.268 , pp. 25587-25593
    • Bradsher, J.N.1    Jackson, K.W.2    Conaway, R.C.3    Cottaway, J.W.4
  • 8
    • 0029834383 scopus 로고    scopus 로고
    • Tat-SF1: Cofactor for stimulation of transcriptional elongation by HIV-1 Tat
    • Zhou, Q., and Sharp, P. A. (1996) Tat-SF1: cofactor for stimulation of transcriptional elongation by HIV-1 Tat. Science 274, 605-610
    • (1996) Science , vol.274 , pp. 605-610
    • Zhou, Q.1    Sharp, P.A.2
  • 9
    • 0032498273 scopus 로고    scopus 로고
    • FACT, a factor that facilitates transcript elongation through nucleosomes
    • Orphanides, G., LeRoy, G., Chang, C. H., Luse, D. S., and Reinberg, D. (1998) FACT, a factor that facilitates transcript elongation through nucleosomes. Cell 92, 105-116
    • (1998) Cell , vol.92 , pp. 105-116
    • Orphanides, G.1    LeRoy, G.2    Chang, C.H.3    Luse, D.S.4    Reinberg, D.5
  • 11
    • 0032004953 scopus 로고    scopus 로고
    • Evidence that Spt4, Spt5, and Spt6 control transcription elongation by RNA polymerasc II in Saccharomyces cerevisiae
    • Hartzog, G. A., Wada, T., Handa, H., and Winston, F. (1998) Evidence that Spt4, Spt5, and Spt6 control transcription elongation by RNA polymerasc II in Saccharomyces cerevisiae. Genes & Dev. 12 357-369
    • (1998) Genes & Dev. , vol.12 , pp. 357-369
    • Hartzog, G.A.1    Wada, T.2    Handa, H.3    Winston, F.4
  • 12
    • 0032031706 scopus 로고    scopus 로고
    • Identification of multiple cyclin subunits of human P-TEFb
    • Peng, J. Zhu, Y., Milton, J. T., and Price, D. H. (1998) Identification of multiple cyclin subunits of human P-TEFb. Genes & Dev. 12, 755-762
    • (1998) Genes & Dev. , vol.12 , pp. 755-762
    • Peng, J.1    Zhu, Y.2    Milton, J.T.3    Price, D.H.4
  • 13
    • 15844396178 scopus 로고    scopus 로고
    • Purification of an RNA polymerase II transcript release factor from Drosophila
    • Xie, Z., and Price, D. H. (1996) Purification of an RNA polymerase II transcript release factor from Drosophila.J. Biol. Chem. 271, 11043-11046
    • (1996) J. Biol. Chem. , vol.271 , pp. 11043-11046
    • Xie, Z.1    Price, D.H.2
  • 14
    • 0030798245 scopus 로고    scopus 로고
    • Histone acetylation in chromatin structure and transcription
    • Grunstein, M. (1997) Histone acetylation in chromatin structure and transcription. Nature (London) 389, 349-352
    • (1997) Nature (London) , vol.389 , pp. 349-352
    • Grunstein, M.1
  • 15
    • 0031009397 scopus 로고    scopus 로고
    • Chromatin remodeling and transcription
    • Tsukiyama, T., and Wu, C. (1997) Chromatin remodeling and transcription. Curr. Opin. Genet. Dev. 7, 182-191
    • (1997) Curr. Opin. Genet. Dev. , vol.7 , pp. 182-191
    • Tsukiyama, T.1    Wu, C.2
  • 16
    • 0029847278 scopus 로고    scopus 로고
    • Chromatin and transcription
    • Edmondson, D., and Roth, S. (1996) Chromatin and transcription. FASEB J. 10,1173-1182
    • (1996) FASEB J. , vol.10 , pp. 1173-1182
    • Edmondson, D.1    Roth, S.2
  • 17
    • 0026641776 scopus 로고
    • Yeast SNF/SWI transcriptional activators and the SPT/SIN chromatin connection
    • Winstion, F., and Carlson, M. (1992) Yeast SNF/SWI transcriptional activators and the SPT/SIN chromatin connection. Trends Genet. 8, 387-391
    • (1992) Trends Genet. , vol.8 , pp. 387-391
    • Winstion, F.1    Carlson, M.2
  • 18
    • 0031460419 scopus 로고    scopus 로고
    • Transcription control: Repressed repeats express themselves
    • Wolffe, A. P. (1997) Transcription control: repressed repeats express themselves. Curr. Biol. 7,796-798
    • (1997) Curr. Biol. , vol.7 , pp. 796-798
    • Wolffe, A.P.1
  • 19
    • 0032488855 scopus 로고    scopus 로고
    • Eukaryotic transcription: An interlaced network of transcription factors and chromatin-modifying machines
    • Kadonaga, J. T. (1998) Eukaryotic transcription: an interlaced network of transcription factors and chromatin-modifying machines. Cell 92, 307-313
    • (1998) Cell , vol.92 , pp. 307-313
    • Kadonaga, J.T.1
  • 20
    • 0029914495 scopus 로고    scopus 로고
    • Multiple switches to turn on chromatin?
    • Peterson, C. L. (1996) Multiple switches to turn on chromatin? Curr. Opin. Genet. Dev. 6, 171-175
    • (1996) Curr. Opin. Genet. Dev. , vol.6 , pp. 171-175
    • Peterson, C.L.1
  • 21
    • 0029063189 scopus 로고
    • Interplay between chromatin structure and transcription
    • Kornberg, R. D., and Lorch, Y. (1995) Interplay between chromatin structure and transcription. Curr. Opin. Cell. Biol. 7, 371-375
    • (1995) Curr. Opin. Cell. Biol. , vol.7 , pp. 371-375
    • Kornberg, R.D.1    Lorch, Y.2
  • 22
    • 0031444009 scopus 로고    scopus 로고
    • Protein acetylation: More than chromatin modification to regulate transcription
    • Bayle, J. H., and Crabtree, G. R. (1997) Protein acetylation: more than chromatin modification to regulate transcription. Chem. Biol. 12, 885-888
    • (1997) Chem. Biol. , vol.12 , pp. 885-888
    • Bayle, J.H.1    Crabtree, G.R.2
  • 23
    • 0026629273 scopus 로고
    • Factor-stimulated RNA polymerase II transcribes at physiological elongation rates on naked DNA but very poorly on chromatin templates
    • Izban. M. G., and Luse, D. S. (1992) Factor-stimulated RNA polymerase II transcribes at physiological elongation rates on naked DNA but very poorly on chromatin templates. J. Biol. Chem. 207, 13647-13655
    • (1992) J. Biol. Chem. , vol.207 , pp. 13647-13655
    • Izban, M.G.1    Luse, D.S.2
  • 24
    • 0028837312 scopus 로고
    • The human dystrophin gone requires 16 hours to be transcribed and is cotranscriptionally spliced
    • Tennyson, C. N., Klamut, H. J., and Worton, R. G. (1995) The human dystrophin gone requires 16 hours to be transcribed and is cotranscriptionally spliced. Nat. Genet. 9, 184-190
    • (1995) Nat. Genet. , vol.9 , pp. 184-190
    • Tennyson, C.N.1    Klamut, H.J.2    Worton, R.G.3
  • 25
    • 0021268344 scopus 로고
    • Early events in the stimulation of mammary tumor virus RNA synthesis by glucocorticoids. Novel assays of transcription rates
    • Ucker, D. S., and Yamamoto, K. R. (1984) Early events in the stimulation of mammary tumor virus RNA synthesis by glucocorticoids. Novel assays of transcription rates. J. Biol. Chem. 259, 7416-7420
    • (1984) J. Biol. Chem. , vol.259 , pp. 7416-7420
    • Ucker, D.S.1    Yamamoto, K.R.2
  • 26
    • 0025232290 scopus 로고
    • Spatial and temporal patterns of E74 transcription during Drosophila development
    • Thummel, C. S., Burtis, K. C., and Hogness, D. D. (1990) Spatial and temporal patterns of E74 transcription during Drosophila development. Cell 61, 101-111
    • (1990) Cell , vol.61 , pp. 101-111
    • Thummel, C.S.1    Burtis, K.C.2    Hogness, D.D.3
  • 27
    • 0030249832 scopus 로고    scopus 로고
    • The RNA polymerase II general elongation factors
    • Reines, D., Conaway, J. W., and Conaway, R. C. (1996) The RNA polymerase II general elongation factors. Trends Biochem. Sci. 21, 351-355
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 351-355
    • Reines, D.1    Conaway, J.W.2    Conaway, R.C.3
  • 28
    • 0031008221 scopus 로고    scopus 로고
    • Basic mechanisms of transcript elongation and its regulation
    • Uptain, S., Kane, C. M., and Chamberlin, M. J. (1997) Basic mechanisms of transcript elongation and its regulation. Annu. Rev. Biochem. 66, 117-172
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 117-172
    • Uptain, S.1    Kane, C.M.2    Chamberlin, M.J.3
  • 29
    • 0017172263 scopus 로고
    • Purification of a factor from Ehrlich ascites tumor cells specifically stimulating Pol II
    • Sekimizu, K., Kobayashi, N., Mizuno, D., and Natori, S. (1976) Purification of a factor from Ehrlich ascites tumor cells specifically stimulating Pol II. Biochemistry 15, 5064-5070
    • (1976) Biochemistry , vol.15 , pp. 5064-5070
    • Sekimizu, K.1    Kobayashi, N.2    Mizuno, D.3    Natori, S.4
  • 30
    • 0028059269 scopus 로고
    • The active site of RNA polymerase II participates in transcript cleavage within arrested ternary complexes
    • Rudd, M. D., Izban, M., and Luse, D. S. (1994) The active site of RNA polymerase II participates in transcript cleavage within arrested ternary complexes. Proc. Natl. Acad, Sci. USA 91, 8057-8061
    • (1994) Proc. Natl. Acad, Sci. USA , vol.91 , pp. 8057-8061
    • Rudd, M.D.1    Izban, M.2    Luse, D.S.3
  • 31
    • 0027447687 scopus 로고
    • Elongation factor SII-dependcnt transcription by an RNA polymerase II through a sequence-specific DNA-binding protein
    • Reines, D., and Mote, J. (1993) Elongation factor SII-dependcnt transcription by an RNA polymerase II through a sequence-specific DNA-binding protein. Proc. Natl. Acad. Sci. USA 90,1917-1921
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 1917-1921
    • Reines, D.1    Mote, J.2
  • 32
    • 0024504832 scopus 로고
    • Dynamic interaction between a Drosophila transcription factor and RNA polymerase II
    • Price, D. H., Sluder, A. E., and Greenleaf, A. L. (1989) Dynamic interaction between a Drosophila transcription factor and RNA polymerase II. Mol. Cell. Biol. 9, 1465-1475
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 1465-1475
    • Price, D.H.1    Sluder, A.E.2    Greenleaf, A.L.3
  • 33
    • 0029055758 scopus 로고
    • Identification of a decay in transcription potential that results in elongation factor dependence of Pol II
    • Gu, W., and Reines, D. (1995) Identification of a decay in transcription potential that results in elongation factor dependence of Pol II.J. Biol. Chem. 270, 11238-11244
    • (1995) J. Biol. Chem. , vol.270 , pp. 11238-11244
    • Gu, W.1    Reines, D.2
  • 40
    • 0024561487 scopus 로고
    • 5,6-Dichloro-1-beta-D-ribofuranosylbenzimidazole inhibits tran- Scription elongation by Pol II in vitro
    • Chodosh, L. A., Fire, A., Samuels, M., and Sharp, P. A. (1989) 5,6-Dichloro-1-beta-D-ribofuranosylbenzimidazole inhibits tran- scription elongation by Pol II in vitro. J. Biol. Chein. 264, 2250-2257
    • (1989) J. Biol. Chein. , vol.264 , pp. 2250-2257
    • Chodosh, L.A.1    Fire, A.2    Samuels, M.3    Sharp, P.A.4
  • 41
    • 37049177936 scopus 로고
    • 5,6-Dichloro-1-beta-D-ribofuranosylbenzimidazole inliibits initiation of nuclear heterogeneous RNA chains in HeLa cells
    • Sehgal, P. B., Derman, E., Molloy, G. R., Tamm, I., and Darnell, J. E. (1976) 5,6-Dichloro-1-beta-D-ribofuranosylbenzimidazole inliibits initiation of nuclear heterogeneous RNA chains in HeLa cells. Science 22, 431-433
    • (1976) Science , vol.22 , pp. 431-433
    • Sehgal, P.B.1    Derman, E.2    Molloy, G.R.3    Tamm, I.4    Darnell, J.E.5
  • 42
    • 0018566872 scopus 로고
    • Early termination of heterogeneous nuclear RNA transcripts in mammalian cells: Accentuation by 5,6-dichloro 1-beta-D-ribofuranosylbenzimidazole
    • Tamm, I., and Kikuchi, T. (1979) Early termination of heterogeneous nuclear RNA transcripts in mammalian cells: accentuation by 5,6-dichloro 1-beta-D-ribofuranosylbenzimidazole.Proc. Natl. Acad. Sci. USA 76, 5750-5754
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 5750-5754
    • Tamm, I.1    Kikuchi, T.2
  • 43
    • 0026641776 scopus 로고
    • Yeast Snf/Swi transcriptional activators and the Spi/Sin chromatin connection
    • Winston, F., and Carlson, M. (1992) Yeast Snf/Swi transcriptional activators and the Spi/Sin chromatin connection. Trends Genet. 8, 387-391
    • (1992) Trends Genet. , vol.8 , pp. 387-391
    • Winston, F.1    Carlson, M.2
  • 44
    • 0025869163 scopus 로고
    • Spt5, an essential gene important for normal transcription in Saccharomyces cerevisiae, encodes an acidic nuclear protein with a carboxyterminal repeat
    • Swanson, M. S., Malone, E. A., and Winston, F. (1991) Spt5, an essential gene important for normal transcription in Saccharomyces cerevisiae, encodes an acidic nuclear protein with a carboxyterminal repeat. Mol. Cell. Biol. 11, 3009-3019
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 3009-3019
    • Swanson, M.S.1    Malone, E.A.2    Winston, F.3
  • 45
    • 0029770436 scopus 로고    scopus 로고
    • Differential intrachromosomal hyper-recombination phenotype of spt4 and spt6 mutants in S. cerevisiae
    • Malagon, F., and Aguilera, A. (1996) Differential intrachromosomal hyper-recombination phenotype of spt4 and spt6 mutants in S. cerevisiae. Curr. Genet. 30, 101-106
    • (1996) Curr. Genet. , vol.30 , pp. 101-106
    • Malagon, F.1    Aguilera, A.2
  • 46
    • 0029905349 scopus 로고    scopus 로고
    • Faithful chromosome transmission requires Spt4, a putative regulator of chromatin structure in Saccharomyces cerevisiae
    • Basrai, M. A., Kingsbury,J., Koshland, D. Spencer, F., and Hieter, P. (1996) Faithful chromosome transmission requires Spt4, a putative regulator of chromatin structure in Saccharomyces cerevisiae. Mol. Cell. Biol. 16,2838-2847
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 2838-2847
    • Basrai, M.A.1    Kingsbury, J.2    Koshland, D.3    Spencer, F.4    Hieter, P.5
  • 47
    • 0032488913 scopus 로고    scopus 로고
    • Unusual nucleic acid binding properties of factor 2, an Pol II transcript release factor
    • Xie, Z., and Price, D. H. (1998) Unusual nucleic acid binding properties of factor 2, an Pol II transcript release factor. J. Biol. Chem. 273, 3771-3777
    • (1998) J. Biol. Chem. , vol.273 , pp. 3771-3777
    • Xie, Z.1    Price, D.H.2
  • 48
    • 0029959881 scopus 로고    scopus 로고
    • Control of RNA polymerase II elongation potential by a novel carboxylterminal domain kinase
    • Marshall, N. F., Peng J., Xie, Z., and Price, D. H. (1996) Control of RNA polymerase II elongation potential by a novel carboxylterminal domain kinase.J. Biol. Chem. 271, 27176-27183
    • (1996) J. Biol. Chem. , vol.271 , pp. 27176-27183
    • Marshall, N.F.1    Peng, J.2    Xie, Z.3    Price, D.H.4
  • 49
    • 0032548918 scopus 로고    scopus 로고
    • A novel CDK9-associated C-type cyclin interacts directly with HIV-1 Tat and mediates its high-affinity, loop-specific binding to TAR RNA
    • Wei, P., Garber, M. E., Fang, S.-M., Fischer, W. H., and Jones, K. A. (1998) A novel CDK9-associated C-type cyclin interacts directly with HIV-1 Tat and mediates its high-affinity, loop-specific binding to TAR RNA Cell 92, 451-462
    • (1998) Cell , vol.92 , pp. 451-462
    • Wei, P.1    Garber, M.E.2    Fang, S.-M.3    Fischer, W.H.4    Jones, K.A.5
  • 51
    • 0019412155 scopus 로고
    • Pausing and termination of transcription within the early region of bacteriophage T7 DNA in vitro
    • Kassavetis, G. A., and Chamberlin, M.J. (1981) Pausing and termination of transcription within the early region of bacteriophage T7 DNA in vitro. J. Biol. Chem. 256, 2777-2786
    • (1981) J. Biol. Chem. , vol.256 , pp. 2777-2786
    • Kassavetis, G.A.1    Chamberlin, M.J.2
  • 52
    • 0025340514 scopus 로고
    • Transcription elongation and eukaryotic gene regulation
    • Spencer, C. A., and Groudine, M. (1990) Transcription elongation and eukaryotic gene regulation. Oncogene 5, 777-785
    • (1990) Oncogene , vol.5 , pp. 777-785
    • Spencer, C.A.1    Groudine, M.2
  • 53
    • 0027326459 scopus 로고
    • Regulation of eukaryotic gene expression by transcriptional attenuation
    • Wright, S. (1993) Regulation of eukaryotic gene expression by transcriptional attenuation. Mol. Biol. Cell 4, 661-668
    • (1993) Mol. Biol. Cell , vol.4 , pp. 661-668
    • Wright, S.1
  • 54
    • 0028106162 scopus 로고
    • Transcript cleavage by Pol II arrested by a cyclobutane pyrimidine dimer in the DNA template
    • Donahue, B. A., Yin, S., Taylor, J. S., Reines, D., and Hanawalt, P. C. (1994) Transcript cleavage by Pol II arrested by a cyclobutane pyrimidine dimer in the DNA template. Proc. Natl. Acad. Sci. USA 91, 8502-8506
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 8502-8506
    • Donahue, B.A.1    Yin, S.2    Taylor, J.S.3    Reines, D.4    Hanawalt, P.C.5
  • 55
    • 0030584091 scopus 로고    scopus 로고
    • Promoter-proximal sequences modulates Pol II elongation by a novel mechanism
    • Reeder, T. C., and Hawley, D. K., (1996) Promoter-proximal sequences modulates Pol II elongation by a novel mechanism. Cell 87, 767-777
    • (1996) Cell , vol.87 , pp. 767-777
    • Reeder, T.C.1    Hawley, D.K.2
  • 56
    • 0032524661 scopus 로고    scopus 로고
    • Transcriptional fidelity and proofreading by Pol II
    • Thomas, M. J., Platas, A. A., and Hawley, D. K. (1998) Transcriptional fidelity and proofreading by Pol II. Cell 93, 627-637
    • (1998) Cell , vol.93 , pp. 627-637
    • Thomas, M.J.1    Platas, A.A.2    Hawley, D.K.3
  • 57
    • 0025720485 scopus 로고
    • Irresistible force meets immovable object: Transcription and the nucleosome
    • Kornberg, R. D., and Lorch, Y. (1991) Irresistible force meets immovable object: transcription and the nucleosome. Cell 67, 833-836
    • (1991) Cell , vol.67 , pp. 833-836
    • Kornberg, R.D.1    Lorch, Y.2
  • 58
    • 0026599021 scopus 로고
    • Chromatin as an essential part of the transcriptional mechanism
    • Felsenfeld, G. (1992) Chromatin as an essential part of the transcriptional mechanism. Nature (London) 355, 219-224
    • (1992) Nature (London) , vol.355 , pp. 219-224
    • Felsenfeld, G.1
  • 59
    • 0030768938 scopus 로고    scopus 로고
    • The H3/H4 tetramer blocks transcript elongation by Pol II in vitro
    • Chang, C.-H., and Luse, D. S. (1997) The H3/H4 tetramer blocks transcript elongation by Pol II in vitro. J. Biol. Chem. 272, 23427-23434
    • (1997) J. Biol. Chem. , vol.272 , pp. 23427-23434
    • Chang, C.-H.1    Luse, D.S.2
  • 60
    • 0026733468 scopus 로고
    • A nucleosome core is transferred out of the path of a transcribing polymerase
    • Clark, D. J., and Felsenfeld, G. (1992) A nucleosome core is transferred out of the path of a transcribing polymerase. Cell 71, 11-22
    • (1992) Cell , vol.71 , pp. 11-22
    • Clark, D.J.1    Felsenfeld, G.2
  • 61
    • 0028125847 scopus 로고
    • A histone octamer can step around a transcribing polymerase without leaving the template
    • Studitsky, V. M., Clark, D. J., and Felsenfeld, G. (1994) A histone octamer can step around a transcribing polymerase without leaving the template. Cell 76, 371-382
    • (1994) Cell , vol.76 , pp. 371-382
    • Studitsky, V.M.1    Clark, D.J.2    Felsenfeld, G.3
  • 62
    • 0031451329 scopus 로고    scopus 로고
    • Mechanism of transcription through the nucleosome by eukaryotic RNA polymerase
    • Studitsky, V. M., Kassavetis, G. A., Geiduschek, E. P., and Felsenfeld, G. (1997) Mechanism of transcription through the nucleosome by eukaryotic RNA polymerase. Science 278, 1960-1963
    • (1997) Science , vol.278 , pp. 1960-1963
    • Studitsky, V.M.1    Kassavetis, G.A.2    Geiduschek, E.P.3    Felsenfeld, G.4
  • 64
  • 65
    • 0032540499 scopus 로고    scopus 로고
    • The Elongin BC complex and the von Hippel-Lindau tumor suppressor protein
    • 64a. Conaway, W. J., Kamura, T., and Conaway, R. C. (1998) The Elongin BC complex and the von Hippel-Lindau tumor suppressor protein. Biochim. Biophys. Acta 1377, M49-M54
    • (1998) Biochim. Biophys. Acta , vol.1377
    • Conaway, W.J.1    Kamura, T.2    Conaway, R.C.3
  • 66
    • 0030953635 scopus 로고    scopus 로고
    • The von Hippel-Lindau tumor-suppressor gene product forms a stable complex with human CUL-2, a member of the Cdc53 family of proteins
    • Pause, A., Lee, S., Worrell, R. A., Chen, D. Y. T., Burgess, W. H., Linehan, W. M., and Klausner, R. D. The von Hippel-Lindau tumor-suppressor gene product forms a stable complex with human CUL-2, a member of the Cdc53 family of proteins (1997) Proc. Natl. Acad. Sci. USA 94, 2156-2161
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 2156-2161
    • Pause, A.1    Lee, S.2    Worrell, R.A.3    Chen, D.Y.T.4    Burgess, W.H.5    Linehan, W.M.6    Klausner, R.D.7
  • 67
    • 0031907152 scopus 로고    scopus 로고
    • Regulation of hypoxia-inducible mRNAs by the von Hippel-Lindau tumor suppressor protein requires binding to complexes containing elongins B/C and Cul2. (1998)
    • Lonergan. K. M., Iliopoulos, O., Ohh, M., Kamura, T., Conaway, R. C., Conaway,J. W., and Kaelin, W. G., Jr. (1998) Regulation of hypoxia-inducible mRNAs by the von Hippel-Lindau tumor suppressor protein requires binding to complexes containing elongins B/C and Cul2. (1998) Mol. Cell. Biol. 18, 732-741
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 732-741
    • Lonergan, K.M.1    Iliopoulos, O.2    Ohh, M.3    Kamura, T.4    Conaway, R.C.5    Conaway, J.W.6    Kaelin Jr., W.G.7
  • 68
    • 0028135353 scopus 로고
    • Cloning of ELL, a gene that fuses to MLL in a t(11;19)(q23'3.1) in acute myeloid leukemia
    • Thirman, M. J., Levitan, D. A., Kobayashi, H., Simon, M. C., and Rowley, J. D. Cloning of ELL, a gene that fuses to MLL in a t(11;19)(q23'3.1) in acute myeloid leukemia (1994) Proc. Natl. Acad. Sci. USA 91, 12110-12114
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 12110-12114
    • Thirman, M.J.1    Levitan, D.A.2    Kobayashi, H.3    Simon, M.C.4    Rowley, J.D.5
  • 69
    • 0028939520 scopus 로고
    • Cloning of several species of MLL/MEN chimeric cDNAs in myeloid leukemia with t(11;19)(q23;p13.l) translocation
    • Mitani, K. Kanda, Y., Ogawa, S., Tanaka, T., Inazawa, J., Yazaki, Y.,and Hirai, H. (1995) Cloning of several species of MLL/MEN chimeric cDNAs in myeloid leukemia with t(11;19)(q23;p13.l) translocation. Blood 85, 2017-2024
    • (1995) Blood , vol.85 , pp. 2017-2024
    • Mitani, K.1    Kanda, Y.2    Ogawa, S.3    Tanaka, T.4    Inazawa, J.5    Yazaki, Y.6    Hirai, H.7
  • 70
    • 0026454451 scopus 로고
    • Involvement of a homolog of Drosophila trithorax by 11q23 chromosomal translocations in acute leukemias
    • Tkachuk, D. C., Kohler, S., and Cleary, M. L. (1992) Involvement of a homolog of Drosophila trithorax by 11q23 chromosomal translocations in acute leukemias. Cell 71, 691-700
    • (1992) Cell , vol.71 , pp. 691-700
    • Tkachuk, D.C.1    Kohler, S.2    Cleary, M.L.3
  • 71
    • 0026496887 scopus 로고
    • The t(4;11) chromosome translocation of human acute leukemias fuses the ALL-1 gene, related to Drosophila trithorax, to the AF-4 gene
    • Gu,Y., Nakamura, T., Alder, H., Prasad, R., Canaani, O., Cimino, G., Croce, C. M., and Canaani, E. (1992) The t(4;11) chromosome translocation of human acute leukemias fuses the ALL-1 gene, related to Drosophila trithorax, to the AF-4 gene. Cell 71, 701-708
    • (1992) Cell , vol.71 , pp. 701-708
    • Gu, Y.1    Nakamura, T.2    Alder, H.3    Prasad, R.4    Canaani, O.5    Cimino, G.6    Croce, C.M.7    Canaani, E.8
  • 72
    • 0027970838 scopus 로고
    • Chromosomal translocations in human cancer
    • Rabbitts T. H. (1994) Chromosomal translocations in human cancer. Nature (London) 372, 143-149
    • (1994) Nature (London) , vol.372 , pp. 143-149
    • Rabbitts, T.H.1
  • 73
  • 74
    • 0000778884 scopus 로고    scopus 로고
    • EEN encodes for a member of a new family of proteins containing an Src homology 3 domain and is the third gene located on chromosome 19p13 that fuses to MLL in human leukemia
    • So C. W., Caldas, C., Liu, M. M., Chen, S. J., Huang, Q. H., Gu, L. J., Sham, M. H., Wiedemann, L. M., and Chan, L. C. (1997) EEN encodes for a member of a new family of proteins containing an Src homology 3 domain and is the third gene located on chromosome 19p13 that fuses to MLL in human leukemia. Proc. Natl. Acad. Sci. USA 94, 2563-2568
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 2563-2568
    • So, C.W.1    Caldas, C.2    Liu, M.M.3    Chen, S.J.4    Huang, Q.H.5    Gu, L.J.6    Sham, M.H.7    Wiedemann, L.M.8    Chan, L.C.9
  • 76
    • 0028169259 scopus 로고
    • ENL, the gene fused with HRX in t(11;19) leukemias, encodes a nuclear protein with transcriptional activation potential in lymphoid and myeloid cells
    • Rubnitz, J. E., Morrissey, J., Savage, P. A., and Cleary, M. L. (1994) ENL, the gene fused with HRX in t(11;19) leukemias, encodes a nuclear protein with transcriptional activation potential in lymphoid and myeloid cells. Blood 84,1747-1752
    • (1994) Blood , vol.84 , pp. 1747-1752
    • Rubnitz, J.E.1    Morrissey, J.2    Savage, P.A.3    Cleary, M.L.4
  • 77
    • 9844268506 scopus 로고    scopus 로고
    • Chimeric MLL products with a Ras binding cytoplasmic protein AF6 involved in t(6;11) (q27;q23) leukemia localize in the nucleus
    • Joh, T., Yamamoto, K., Kagami, Y., Kakuda, H., Sato, T., Yamamoto, T., Takahashi, T., Ueda, R., Kaibuchi, K., and Seto, M. (1997) Chimeric MLL products with a Ras binding cytoplasmic protein AF6 involved in t(6;11) (q27;q23) leukemia localize in the nucleus. Oncogene 15,1681-1687
    • (1997) Oncogene , vol.15 , pp. 1681-1687
    • Joh, T.1    Yamamoto, K.2    Kagami, Y.3    Kakuda, H.4    Sato, T.5    Yamamoto, T.6    Takahashi, T.7    Ueda, R.8    Kaibuchi, K.9    Seto, M.10
  • 79
    • 0030772567 scopus 로고    scopus 로고
    • A novel MLL-AF10 fusion mRNA variant in a patient with acute myeloid leukemia detected by a new asymmetric reverse transcription PCR method
    • Hjorth-Sorensen, B., Pallisgaard, N., Gronholm, M., Hokland, P., Clausen, N., and Jorgensen, P. (1997) A novel MLL-AF10 fusion mRNA variant in a patient with acute myeloid leukemia detected by a new asymmetric reverse transcription PCR method. Leukemia 11, 1588-1593
    • (1997) Leukemia , vol.11 , pp. 1588-1593
    • Hjorth-Sorensen, B.1    Pallisgaard, N.2    Gronholm, M.3    Hokland, P.4    Clausen, N.5    Jorgensen, P.6
  • 80
    • 0031031378 scopus 로고    scopus 로고
    • Cloning and characterization of AFX, the gene that fuses to MLL in acute leukemia with a t(X;11) (q13;q23)
    • Borkhardt, A., Repp, R., Haas, O. A., Leis, T., Harbott, J., Kreuder, J., Hammermann, J., Henn, T., and Lampert, F. (1997) Cloning and characterization of AFX, the gene that fuses to MLL in acute leukemia with a t(X;11) (q13;q23). Oncogene 14, 195-202
    • (1997) Oncogene , vol.14 , pp. 195-202
    • Borkhardt, A.1    Repp, R.2    Haas, O.A.3    Leis, T.4    Harbott, J.5    Kreuder, J.6    Hammermann, J.7    Henn, T.8    Lampert, F.9
  • 81
    • 15844394270 scopus 로고    scopus 로고
    • An M11-AF9 fusion gene made by homologous recombination causes acute leukemia in chimeric mice: A method to create fusion oncogenes
    • Corral, J., Lavenir, I., Impey, H., Warren, A. J., Forster, A., Larson, T. A., Bell, S., McKenzie, A. N.J., King, G., and Rabbitts, T. H. (1996) An M11-AF9 fusion gene made by homologous recombination causes acute leukemia in chimeric mice: A method to create fusion oncogenes. Cell 85, 853-861
    • (1996) Cell , vol.85 , pp. 853-861
    • Corral, J.1    Lavenir, I.2    Impey, H.3    Warren, A.J.4    Forster, A.5    Larson, T.A.6    Bell, S.7    McKenzie, A.N.J.8    King, G.9    Rabbitts, T.H.10
  • 82
    • 0027240084 scopus 로고
    • The tight junction protein ZO-1 is homologous to the Drosophila discs-large tumor suppressor protein of septate junctions
    • Willott, E., Balda, M. S., Fanning, A. S., Jameson, B., van Itallie, C., and Anderson J. M. (1993) The tight junction protein ZO-1 is homologous to the Drosophila discs-large tumor suppressor protein of septate junctions. Proc. Natl. Acad. Sci. USA 90, 7834-7838
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 7834-7838
    • Willott, E.1    Balda, M.S.2    Fanning, A.S.3    Jameson, B.4    Van Itallie, C.5    Anderson, J.M.6
  • 83
    • 0028110309 scopus 로고
    • Direct association of occludin with ZO-1 and its possible involvement in the localization of occludin at tight junctions
    • Furuse, M., Itoh, M., Hirase, T., Nagafuchi, A., Yonemura, Tsukita, S., and Tsukita, S. (1994) Direct association of occludin with ZO-1 and its possible involvement in the localization of occludin at tight junctions. J. Cell Biol. 127, 1617-1626
    • (1994) J. Cell Biol. , vol.127 , pp. 1617-1626
    • Furuse, M.1    Itoh, M.2    Hirase, T.3    Nagafuchi, A.4    Yonemura5    Tsukita, S.6    Tsukita, S.7
  • 84
    • 0027744129 scopus 로고
    • Occludin: A novel integral membrane protein localizing at tight junctions
    • Furuse, M., Hirase, T., Itoh, M., Nagafuchi, A., Yonemura, S., and Tsukita, S. (1993) Occludin: A novel integral membrane protein localizing at tight junctions. J. Cell Biol. 123, 1777-1788
    • (1993) J. Cell Biol. , vol.123 , pp. 1777-1788
    • Furuse, M.1    Hirase, T.2    Itoh, M.3    Nagafuchi, A.4    Yonemura, S.5    Tsukita, S.6
  • 85
    • 0029744106 scopus 로고    scopus 로고
    • The junction-associated protein zonula occludens-1, localizes to the nucleus before the maturation and during the remodeling of cell-cell contacts
    • Gottardi, C. J., Arpin, M., Fanning, A. S., and Louvard, D. (1996) The junction-associated protein zonula occludens-1, localizes to the nucleus before the maturation and during the remodeling of cell-cell contacts. Proc. Natl. Acad. Sci. USA 93,10779-10784
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 10779-10784
    • Gottardi, C.J.1    Arpin, M.2    Fanning, A.S.3    Louvard, D.4


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