메뉴 건너뛰기




Volumn 75, Issue 11-12, 1997, Pages 786-800

DNA topoisomerase I: Customs officer at the border between DNA and RNA worlds?

Author keywords

Alternative splicing; DNA topoisomerase I; mRNA precursor; Nucleus; Protein kinase; Protein phosphorylation; Small nuclear Ribonucleoprotein; Splicing factors

Indexed keywords

ANTINEOPLASTIC AGENT; DNA TOPOISOMERASE; DNA TOPOISOMERASE INHIBITOR; MESSENGER RNA PRECURSOR; PROTEIN KINASE; SMALL NUCLEAR RIBONUCLEOPROTEIN;

EID: 0030828196     PISSN: 09462716     EISSN: None     Source Type: Journal    
DOI: 10.1007/s001090050168     Document Type: Review
Times cited : (35)

References (226)
  • 1
    • 0026034658 scopus 로고
    • Mechanisms of alternative pre-mRNA splicing
    • Maniatis T (1991) Mechanisms of alternative pre-mRNA splicing. Science 251:33-34
    • (1991) Science , vol.251 , pp. 33-34
    • Maniatis, T.1
  • 2
    • 0026477884 scopus 로고
    • RNA binding proteins, splice site selection, and alternative pre-mRNA splicing
    • Rio DC (1992) RNA binding proteins, splice site selection, and alternative pre-mRNA splicing. Gene expression 2:1-15
    • (1992) Gene Expression , vol.2 , pp. 1-15
    • Rio, D.C.1
  • 3
    • 0025993550 scopus 로고
    • Alternative splicing is an efficient mechanism for generation of protein diversity: Contractile protein genes as a model system
    • Nadal-Ginard B, Smith CW, Patton JG, Breitbart RE (1991) Alternative splicing is an efficient mechanism for generation of protein diversity: contractile protein genes as a model system. Adv Enzymol Regul 31:261-286
    • (1991) Adv Enzymol Regul , vol.31 , pp. 261-286
    • Nadal-Ginard, B.1    Smith, C.W.2    Patton, J.G.3    Breitbart, R.E.4
  • 4
    • 0025975057 scopus 로고
    • Pre-mRNA splicing in yeast
    • Ruby SW, Abelson J (1991) Pre-mRNA splicing in yeast. Trends Genet 7:79-83
    • (1991) Trends Genet , vol.7 , pp. 79-83
    • Ruby, S.W.1    Abelson, J.2
  • 5
    • 0000520650 scopus 로고
    • Yeast pre-mRNA splicing
    • Jones EWW, Pringle JR, Broach JR (eds) Cold Spring Harbor Laboratory, Cold Spring Harbor
    • Rymond BC, Rosbash M (1992) Yeast pre-mRNA splicing. In: Jones EWW, Pringle JR, Broach JR (eds) The molecular and cellular biology of yeast saccharomyces, vol 2. Cold Spring Harbor Laboratory, Cold Spring Harbor, pp 143-192
    • (1992) The Molecular and Cellular Biology of Yeast Saccharomyces , vol.2 , pp. 143-192
    • Rymond, B.C.1    Rosbash, M.2
  • 6
    • 0001877802 scopus 로고
    • Splicing of precursors to mRNA by the spliceosome
    • Guesteland RF, Atkins JF (eds) Cold Spring Harbor Laboratory, Cold Spring Harbor
    • Moore MJ, Query CC, Sharp PA (1993) Splicing of precursors to mRNA by the spliceosome. In: Guesteland RF, Atkins JF (eds) RNA world, vol 1. Cold Spring Harbor Laboratory, Cold Spring Harbor, pp 303-357
    • (1993) RNA World , vol.1 , pp. 303-357
    • Moore, M.J.1    Query, C.C.2    Sharp, P.A.3
  • 7
    • 0028307171 scopus 로고
    • Split genes and RNA splicing
    • Sharp PA (1994) Split genes and RNA splicing. Cell 77:805-815
    • (1994) Cell , vol.77 , pp. 805-815
    • Sharp, P.A.1
  • 9
    • 0025787954 scopus 로고
    • Biochemical mechanisms of constitutive and regulated pre-mRNA splicing
    • Green MR (1991) Biochemical mechanisms of constitutive and regulated pre-mRNA splicing. Ann Rev Cell Biol 7:559-599
    • (1991) Ann Rev Cell Biol , vol.7 , pp. 559-599
    • Green, M.R.1
  • 10
    • 0028895417 scopus 로고
    • Exon recognition in vertebrate splicing
    • Berget SM (1995) Exon recognition in vertebrate splicing. J Biol Chem 270:2411-2414
    • (1995) J Biol Chem , vol.270 , pp. 2411-2414
    • Berget, S.M.1
  • 11
    • 0029372979 scopus 로고
    • The superfamily of arginine/serine-rich splicing factors
    • Fu XD (1995) The superfamily of arginine/serine-rich splicing factors. RNA 1:663-680
    • (1995) RNA , vol.1 , pp. 663-680
    • Fu, X.D.1
  • 12
    • 0029767662 scopus 로고    scopus 로고
    • SR proteins and splicing control
    • Manley JL, Tacke R (1996) SR proteins and splicing control. Genes Dev 10:1569-1579
    • (1996) Genes Dev , vol.10 , pp. 1569-1579
    • Manley, J.L.1    Tacke, R.2
  • 13
    • 0028212966 scopus 로고
    • Mechanisms for selecting 5′ splice sites in mammalian pre-mRNA splicing
    • Horowitz DS, Krainer AR (1994) Mechanisms for selecting 5′ splice sites in mammalian pre-mRNA splicing. Trends Genet 10:100-105
    • (1994) Trends Genet , vol.10 , pp. 100-105
    • Horowitz, D.S.1    Krainer, A.R.2
  • 14
    • 0027151934 scopus 로고
    • Modulation of exon skipping and inclusion by heterogeneous nuclear ribonucleoprotein Aland pre-mRNA splicing factor SF2/ASF
    • Mayeda A, Helfman DM, Krainer AR (1993) Modulation of exon skipping and inclusion by heterogeneous nuclear ribonucleoprotein Aland pre-mRNA splicing factor SF2/ASF. Mol Cell Biol 13:2993-3001
    • (1993) Mol Cell Biol , vol.13 , pp. 2993-3001
    • Mayeda, A.1    Helfman, D.M.2    Krainer, A.R.3
  • 15
    • 0026716104 scopus 로고
    • SR proteins: A conserved family of pre-mRNA splicing factors
    • Zahler AM, Lane WS, Stolk JA, Roth MB (1992) SR proteins: a conserved family of pre-mRNA splicing factors. Genes Dev 6:837-847
    • (1992) Genes Dev , vol.6 , pp. 837-847
    • Zahler, A.M.1    Lane, W.S.2    Stolk, J.A.3    Roth, M.B.4
  • 16
    • 0027494389 scopus 로고
    • Functional domains of the human splicing factor ASF/SF2
    • Zuo P, Manley JL (1993) Functional domains of the human splicing factor ASF/SF2. EMBO J 12:4727-4737
    • (1993) EMBO J , vol.12 , pp. 4727-4737
    • Zuo, P.1    Manley, J.L.2
  • 17
    • 0027501327 scopus 로고
    • Functional analysis of premRNA splicing factor SF2/ASF structural domains
    • Càceres JF, Krainer AR (1993) Functional analysis of premRNA splicing factor SF2/ASF structural domains. EMBO J 12:4715-4726
    • (1993) EMBO J , vol.12 , pp. 4715-4726
    • Càceres, J.F.1    Krainer, A.R.2
  • 18
    • 0026569967 scopus 로고
    • Cloning and domain structure of the mammalian splicing factor U2AF
    • Zamore PD, Patton JG, Green MR (1992) Cloning and domain structure of the mammalian splicing factor U2AF. Nature 335:609-614
    • (1992) Nature , vol.335 , pp. 609-614
    • Zamore, P.D.1    Patton, J.G.2    Green, M.R.3
  • 19
    • 0025931225 scopus 로고
    • A conserved family of nuclear phosphoproteins localized to sites of polymerase II transcription
    • Roth MB, Zahler AM, Stolk JA (1991) A conserved family of nuclear phosphoproteins localized to sites of polymerase II transcription. J Cell Biol 115:587-591
    • (1991) J Cell Biol , vol.115 , pp. 587-591
    • Roth, M.B.1    Zahler, A.M.2    Stolk, J.A.3
  • 20
    • 0028286596 scopus 로고
    • A serine kinase regulates intracellular localization of splicing factors in the cell cycle
    • Gui JF, Lane WS, Fu XD (1994) A serine kinase regulates intracellular localization of splicing factors in the cell cycle. Nature 369:678-682
    • (1994) Nature , vol.369 , pp. 678-682
    • Gui, J.F.1    Lane, W.S.2    Fu, X.D.3
  • 21
    • 0030028882 scopus 로고    scopus 로고
    • The Clk/Sty protein kinase phosphorylates SR splicing factors and regulates their intranuclear distribution
    • Colwill K, Pawson T, Andrews B, Prasad J, Manley J, Bell JC, Duncan PI (1996) The Clk/Sty protein kinase phosphorylates SR splicing factors and regulates their intranuclear distribution. EMBO J 15:265-275
    • (1996) EMBO J , vol.15 , pp. 265-275
    • Colwill, K.1    Pawson, T.2    Andrews, B.3    Prasad, J.4    Manley, J.5    Bell, J.C.6    Duncan, P.I.7
  • 22
    • 0029027778 scopus 로고
    • Overexpression of the argenine-rich carboxy-terminal region of U1 snRNP 70 K inhibits both splicing and nucleocytoplasmic transport of mRNA
    • Romac MJ, Keene JD (1995) Overexpression of the argenine-rich carboxy-terminal region of U1 snRNP 70 K inhibits both splicing and nucleocytoplasmic transport of mRNA. Genes Dev 9:1400-1410
    • (1995) Genes Dev , vol.9 , pp. 1400-1410
    • Romac, M.J.1    Keene, J.D.2
  • 24
    • 0022508558 scopus 로고
    • Topoisomerase I interacts with transcribed regions in Drosophila cells
    • Gilmour DS, Pflugfelder G, Wang JC, Lis JT (1986) Topoisomerase I interacts with transcribed regions in Drosophila cells. Cell 44:401-407
    • (1986) Cell , vol.44 , pp. 401-407
    • Gilmour, D.S.1    Pflugfelder, G.2    Wang, J.C.3    Lis, J.T.4
  • 25
    • 0000266944 scopus 로고
    • Differential expression of DNA topoisomerases I and II during the eukaryotic cell cycle
    • Heck MM, Hittelman WN, Earnshaw WC (1988) Differential expression of DNA topoisomerases I and II during the eukaryotic cell cycle. Proc Natl Acad Sci USA 85:1086-1090
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 1086-1090
    • Heck, M.M.1    Hittelman, W.N.2    Earnshaw, W.C.3
  • 27
    • 0344622123 scopus 로고
    • Spliced segments at the 5′ terminus of adenovirus 2 late mRNA
    • Berget SM, Moore C, Sharp PA (1977) Spliced segments at the 5′ terminus of adenovirus 2 late mRNA. Proc Natl Acad Sci USA 74:3171-3175
    • (1977) Proc Natl Acad Sci USA , vol.74 , pp. 3171-3175
    • Berget, S.M.1    Moore, C.2    Sharp, P.A.3
  • 28
    • 0021223245 scopus 로고
    • Normal and mutant human β-globin pre-mRNAs are faithfully and efficiently spliced in vitro
    • Krainer AR, Maniatis T, Ruskin B, Green MR (1984) Normal and mutant human β-globin pre-mRNAs are faithfully and efficiently spliced in vitro. Cell 36:993-1005
    • (1984) Cell , vol.36 , pp. 993-1005
    • Krainer, A.R.1    Maniatis, T.2    Ruskin, B.3    Green, M.R.4
  • 29
    • 0021719524 scopus 로고
    • Excision of an intact intron as a novel lariat structure during pre-mRNA splicing in vitro
    • Ruskin B, Krainer AR, Maniatis T, Green MR (1984) Excision of an intact intron as a novel lariat structure during pre-mRNA splicing in vitro. Cell 38:317-331
    • (1984) Cell , vol.38 , pp. 317-331
    • Ruskin, B.1    Krainer, A.R.2    Maniatis, T.3    Green, M.R.4
  • 30
    • 0021226996 scopus 로고
    • Messenger RNA splicing in vitro: An excised intervening sequence and a potential intermediate
    • Grabowski PJ, Padgett RA, Sharp PA (1984) Messenger RNA splicing in vitro: an excised intervening sequence and a potential intermediate. Cell 37:415-427
    • (1984) Cell , vol.37 , pp. 415-427
    • Grabowski, P.J.1    Padgett, R.A.2    Sharp, P.A.3
  • 31
    • 0021235185 scopus 로고
    • Lariat RNAs as intermediates and products in the splicing of messenger RNA precursors
    • Padgett RA, Konarska MM, Grabowski PJ, Hardy SF, Sharp PA (1984) Lariat RNAs as intermediates and products in the splicing of messenger RNA precursors. Science 225:898-903
    • (1984) Science , vol.225 , pp. 898-903
    • Padgett, R.A.1    Konarska, M.M.2    Grabowski, P.J.3    Hardy, S.F.4    Sharp, P.A.5
  • 32
    • 0029066770 scopus 로고
    • Structure and activities of group II introns
    • Michel F, Ferat JL (1995) Structure and activities of group II introns. Annu Rev Biochem 64:435-461
    • (1995) Annu Rev Biochem , vol.64 , pp. 435-461
    • Michel, F.1    Ferat, J.L.2
  • 33
    • 0022555857 scopus 로고
    • Biological catalysis by RNA
    • Cech TR, Bass BL (1986) Biological catalysis by RNA. Annu Rev Biochem 55:599-629
    • (1986) Annu Rev Biochem , vol.55 , pp. 599-629
    • Cech, T.R.1    Bass, B.L.2
  • 34
    • 0025173604 scopus 로고
    • Structure of spliceosomal snRNPs and their role in pre-mRNA splicing
    • Lührmann R, Kastner B, Bach M (1990) Structure of spliceosomal snRNPs and their role in pre-mRNA splicing. Biochim Biophys Acta 1087:265-292
    • (1990) Biochim Biophys Acta , vol.1087 , pp. 265-292
    • Lührmann, R.1    Kastner, B.2    Bach, M.3
  • 37
    • 0028556367 scopus 로고
    • Dynamic RNA-RNA interactions in the spliceosome
    • Madhani HD, Guthrie C (1994) Dynamic RNA-RNA interactions in the spliceosome. Annu Rev Genet 28:1-26
    • (1994) Annu Rev Genet , vol.28 , pp. 1-26
    • Madhani, H.D.1    Guthrie, C.2
  • 38
    • 0027739853 scopus 로고
    • The US and U6 small nuclear RNAs as active site components of the spliceosome
    • Sontheimer EJ, Steitz JA (1993) The US and U6 small nuclear RNAs as active site components of the spliceosome. Science 262:1989-1996
    • (1993) Science , vol.262 , pp. 1989-1996
    • Sontheimer, E.J.1    Steitz, J.A.2
  • 39
    • 0027759495 scopus 로고
    • Guides to the heart of the spliceosome
    • Wise JA (1993) Guides to the heart of the spliceosome. Science 262:1978-1979
    • (1993) Science , vol.262 , pp. 1978-1979
    • Wise, J.A.1
  • 40
    • 0023644230 scopus 로고
    • Self-splicing of group II introns in vitro: Lariat formation and 3′ splice site selection in mutant RNAs
    • Schmelzer C, Muller MW (1987) Self-splicing of group II introns in vitro: lariat formation and 3′ splice site selection in mutant RNAs. Cell 51:753-762
    • (1987) Cell , vol.51 , pp. 753-762
    • Schmelzer, C.1    Muller, M.W.2
  • 41
    • 0024428420 scopus 로고
    • Comparative and functional anatomy of group H catalytic introns
    • Michel F, Umesono K, Ozeki H (1989) Comparative and functional anatomy of group H catalytic introns. Gene 8222:5-30
    • (1989) Gene , vol.8222 , pp. 5-30
    • Michel, F.1    Umesono, K.2    Ozeki, H.3
  • 42
    • 0024022167 scopus 로고
    • Group II intron domain 5 facilitates a trans-splicing reaction
    • Jarrell KA, Dietrich RC, Perlman PS (1988) Group II intron domain 5 facilitates a trans-splicing reaction. Mol Cell Biol 8:2361-2366
    • (1988) Mol Cell Biol , vol.8 , pp. 2361-2366
    • Jarrell, K.A.1    Dietrich, R.C.2    Perlman, P.S.3
  • 43
    • 0026695012 scopus 로고
    • Group II introns deleted for multiple substructures retain self-splicing activity
    • Koch JL, Boulanger SC, Dib HS, Hebbar SK, Perlman PS (1992) Group II introns deleted for multiple substructures retain self-splicing activity. Mol Cell Biol 12:1950-1958
    • (1992) Mol Cell Biol , vol.12 , pp. 1950-1958
    • Koch, J.L.1    Boulanger, S.C.2    Dib, H.S.3    Hebbar, S.K.4    Perlman, P.S.5
  • 44
    • 0027263683 scopus 로고
    • Domain 5 interacts with domain 6 and influences the second transesterification reaction of group II intron self-splicing
    • Dib-Hajj SD, Boulanger SC, Hebbar SK, Peebles CL, Franzen JS, Perlman PS (1993) Domain 5 interacts with domain 6 and influences the second transesterification reaction of group II intron self-splicing. Nucleic Acids Res 21:1797-1804
    • (1993) Nucleic Acids Res , vol.21 , pp. 1797-1804
    • Dib-Hajj, S.D.1    Boulanger, S.C.2    Hebbar, S.K.3    Peebles, C.L.4    Franzen, J.S.5    Perlman, P.S.6
  • 45
    • 0026794668 scopus 로고
    • The mutational spectrum of single base-pair substitutions in mRNA splice junctions of human genes: Causes and consequences
    • Krawczak M, Reiss J, Cooper DN (1992) The mutational spectrum of single base-pair substitutions in mRNA splice junctions of human genes: causes and consequences. Hum Genet 90:41-54
    • (1992) Hum Genet , vol.90 , pp. 41-54
    • Krawczak, M.1    Reiss, J.2    Cooper, D.N.3
  • 46
    • 0026543785 scopus 로고
    • Regulation of alternative premRNA splicing by hnRNP A1 and splicing factor SF2
    • Mayeda A, Krainer AR (1992) Regulation of alternative premRNA splicing by hnRNP A1 and splicing factor SF2. Cell 68:365-375
    • (1992) Cell , vol.68 , pp. 365-375
    • Mayeda, A.1    Krainer, A.R.2
  • 47
    • 0029891101 scopus 로고    scopus 로고
    • The sructure and function of proteins involved in mammalian pre-mRNA splicing
    • Krämer A (1996) The sructure and function of proteins involved in mammalian pre-mRNA splicing. Annu Rev Biochem 65:367-409
    • (1996) Annu Rev Biochem , vol.65 , pp. 367-409
    • Krämer, A.1
  • 48
    • 0027440306 scopus 로고
    • Interaction of mammalian splicing factor SF3a with U2 snRNP and relation of its 60-kD subunit to yeast PRP9
    • Brosi R, Gröning K, Behrens SE, Lührmann R, Krämer A (1993) Interaction of mammalian splicing factor SF3a with U2 snRNP and relation of its 60-kD subunit to yeast PRP9. Science 262:102-105
    • (1993) Science , vol.262 , pp. 102-105
    • Brosi, R.1    Gröning, K.2    Behrens, S.E.3    Lührmann, R.4    Krämer, A.5
  • 50
    • 0025906517 scopus 로고
    • Suppressors of a U4 snRNA mutation define a novel U6 snRNP protein with RNA-binding motifs
    • Shannon K, Guthrie C (1991) Suppressors of a U4 snRNA mutation define a novel U6 snRNP protein with RNA-binding motifs. Genes Dev 5:773-785
    • (1991) Genes Dev , vol.5 , pp. 773-785
    • Shannon, K.1    Guthrie, C.2
  • 51
    • 0025856790 scopus 로고
    • Characterization and molecular cloning of polypyrimidine tact-binding protein: A component of a complex necessary for pre-mRNA splicing
    • Patton JG, Mayer SA, Tempst P, Nadal-Ginard B (1991) Characterization and molecular cloning of polypyrimidine tact-binding protein: a component of a complex necessary for pre-mRNA splicing. Genes Dev 5:1237-1251
    • (1991) Genes Dev , vol.5 , pp. 1237-1251
    • Patton, J.G.1    Mayer, S.A.2    Tempst, P.3    Nadal-Ginard, B.4
  • 53
    • 0026586528 scopus 로고
    • Isolation of a complementary DNA that encodes the mammalian splicing factor SC35
    • Fu XD, Maniatis T (1992) Isolation of a complementary DNA that encodes the mammalian splicing factor SC35. Science 256:535-538
    • (1992) Science , vol.256 , pp. 535-538
    • Fu, X.D.1    Maniatis, T.2
  • 54
    • 0025743575 scopus 로고
    • Functional expression of cloned human splicing factor SF2: Homology to RNA-binding proteins. U1 70 K, and Drosophila splicing regulators
    • Krainer RK, Mayeda A, Kozak D (1991) Functional expression of cloned human splicing factor SF2: Homology to RNA-binding proteins. U1 70 K, and Drosophila splicing regulators. Cell 66:383-394
    • (1991) Cell , vol.66 , pp. 383-394
    • Krainer, R.K.1    Mayeda, A.2    Kozak, D.3
  • 55
    • 0025827463 scopus 로고
    • Primary structure of the human splicing factor ASF reveals similarities with drosophila regulators
    • Ge H, Zuo P, Manley JL (1991) Primary structure of the human splicing factor ASF reveals similarities with drosophila regulators. Cell 66:373-382
    • (1991) Cell , vol.66 , pp. 373-382
    • Ge, H.1    Zuo, P.2    Manley, J.L.3
  • 56
    • 0024255702 scopus 로고
    • The sex-determining gene tra-2 of Drosophila encodes a putative RNA binding domain
    • Amerein H, Gorman M, Nöthinger R (1988) The sex-determining gene tra-2 of Drosophila encodes a putative RNA binding domain. Cell 55:1025-1035
    • (1988) Cell , vol.55 , pp. 1025-1035
    • Amerein, H.1    Gorman, M.2    Nöthinger, R.3
  • 57
    • 0023667001 scopus 로고
    • Regulation of sexual differentiation in D. melanogaster via alternative splicing of RNA from the transformer gene
    • Boggs RT, Gregor P, Idriss S, Belote JM, McKeown M (1987) Regulation of sexual differentiation in D. melanogaster via alternative splicing of RNA from the transformer gene. Cell 50:739-747
    • (1987) Cell , vol.50 , pp. 739-747
    • Boggs, R.T.1    Gregor, P.2    Idriss, S.3    Belote, J.M.4    McKeown, M.5
  • 58
    • 0024512392 scopus 로고
    • The sex determination locus transformer-2 of drosophila encodes a polypepetide with similarity to RNA binding protein
    • Goralski TJ, Edström JE, Baker BS (1989) The sex determination locus transformer-2 of drosophila encodes a polypepetide with similarity to RNA binding protein. Cell 56:1011-1018
    • (1989) Cell , vol.56 , pp. 1011-1018
    • Goralski, T.J.1    Edström, J.E.2    Baker, B.S.3
  • 59
    • 0026088747 scopus 로고
    • Requirement of the RNA helicase-like protein PRP22 for release of messenger RNA from spliceosomes
    • Company M, Arenas J, Abelson J (1991) Requirement of the RNA helicase-like protein PRP22 for release of messenger RNA from spliceosomes. Nature 349:487-493
    • (1991) Nature , vol.349 , pp. 487-493
    • Company, M.1    Arenas, J.2    Abelson, J.3
  • 60
    • 0025860028 scopus 로고
    • A cold- sensitive mRNA splicing mutant is a member of the RNA helicase gene family
    • Strauss EJ, Guthrie C (1991) A cold- sensitive mRNA splicing mutant is a member of the RNA helicase gene family. Genes Dev 5:629-641
    • (1991) Genes Dev , vol.5 , pp. 629-641
    • Strauss, E.J.1    Guthrie, C.2
  • 61
    • 0025233806 scopus 로고
    • A putative ATP binding protein influences the fidelity of branchpoint recognition in yeast splicing
    • Burgess S, Couto JR, Guthrie C (1990) A putative ATP binding protein influences the fidelity of branchpoint recognition in yeast splicing. Cell 60:705-717
    • (1990) Cell , vol.60 , pp. 705-717
    • Burgess, S.1    Couto, J.R.2    Guthrie, C.3
  • 62
    • 0025165497 scopus 로고
    • The yeast PRP2 protein, a putative RNA-dependent ATPase, shares extensive sequence homology with two other pre-mRNA splicing factors
    • Chen JH, Lin RJ (1990) The yeast PRP2 protein, a putative RNA-dependent ATPase, shares extensive sequence homology with two other pre-mRNA splicing factors. Nucleic Acids Res 18:6447
    • (1990) Nucleic Acids Res , vol.18 , pp. 6447
    • Chen, J.H.1    Lin, R.J.2
  • 63
    • 0025443022 scopus 로고
    • PRP5: A helicase-like protein required for mRNA splicing in yeast
    • Dalbadie-McFarland G, Abelson J (1990) PRP5: A helicase-like protein required for mRNA splicing in yeast. Proc Natl Acad Sci USA 87:4236-4240
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 4236-4240
    • Dalbadie-McFarland, G.1    Abelson, J.2
  • 64
    • 0026019713 scopus 로고
    • PRP16 is an RNA-dependent ATPase that interacts transiently with the spliceosome
    • Schwer B, Guthrie C (1991) PRP16 is an RNA-dependent ATPase that interacts transiently with the spliceosome. Nature 349:494-499
    • (1991) Nature , vol.349 , pp. 494-499
    • Schwer, B.1    Guthrie, C.2
  • 65
    • 0027533005 scopus 로고
    • Pre-mRNA splicing within an assembled yeast spliceosome requires an RNA-dependent ATPase and ATP hydrolysis
    • Kim SH, Lin RJ (1993) Pre-mRNA splicing within an assembled yeast spliceosome requires an RNA-dependent ATPase and ATP hydrolysis. Proc Natl Acad Sci USA 90:888-892
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 888-892
    • Kim, S.H.1    Lin, R.J.2
  • 66
    • 0028096619 scopus 로고
    • PRP28, a 'DEAD-box' protein, is required for the first step of mRNA splicing in vitro
    • Strauss EJ, Guthrie C (1994) PRP28, a 'DEAD-box' protein, is required for the first step of mRNA splicing in vitro. Nucleic Acids Res 22:3187-3193
    • (1994) Nucleic Acids Res , vol.22 , pp. 3187-3193
    • Strauss, E.J.1    Guthrie, C.2
  • 68
    • 0029397324 scopus 로고
    • The second catalytic step of pre-mRNA splicing
    • Umen JG, Guthrie C (1995) The second catalytic step of pre-mRNA splicing. RNA 1:869-885
    • (1995) RNA , vol.1 , pp. 869-885
    • Umen, J.G.1    Guthrie, C.2
  • 69
    • 0026702493 scopus 로고
    • Adenosine phosphorothioates (ATPaS and ATPgS) differentially affect the two steps of mammalian pre-mRNA splicing
    • Tazi J, Daugeron MC, Cathala G, Brunei C, Jeanteur P (1992) Adenosine phosphorothioates (ATPaS and ATPgS) differentially affect the two steps of mammalian pre-mRNA splicing. J Biol Chem 267:4322-4326
    • (1992) J Biol Chem , vol.267 , pp. 4322-4326
    • Tazi, J.1    Daugeron, M.C.2    Cathala, G.3    Brunei, C.4    Jeanteur, P.5
  • 71
    • 0028043718 scopus 로고
    • Regulation of mammalian spliceosome assembly by a protein phosphorylation mechanism
    • Mermoud JE, Cohen PTW, Lamond AI (1994) Regulation of mammalian spliceosome assembly by a protein phosphorylation mechanism. EMBO J 13:5679-56888
    • (1994) EMBO J , vol.13 , pp. 5679-56888
    • Mermoud, J.E.1    Cohen, P.T.W.2    Lamond, A.I.3
  • 72
    • 0001784735 scopus 로고
    • Uncovering the role of Ser/Thr protein phosphorylation in nuclear pre-mRNA splicing
    • Mermoud JE, Calvio C, Lamond AI (1994) Uncovering the role of Ser/Thr protein phosphorylation in nuclear pre-mRNA splicing. Adv Prot Phosphatases 8:99-118
    • (1994) Adv Prot Phosphatases , vol.8 , pp. 99-118
    • Mermoud, J.E.1    Calvio, C.2    Lamond, A.I.3
  • 73
    • 0026731973 scopus 로고
    • Ser/Thr-specific protein phosphatases are required for both catalytic steps of pre-mRNA splicing
    • Mermoud JE, Cohen PTW, Lamond AI (1992) Ser/Thr-specific protein phosphatases are required for both catalytic steps of pre-mRNA splicing. Nucleic Acids Res 20:5263-5269
    • (1992) Nucleic Acids Res , vol.20 , pp. 5263-5269
    • Mermoud, J.E.1    Cohen, P.T.W.2    Lamond, A.I.3
  • 74
    • 0027305702 scopus 로고
    • Identification of an snRNP-associated kinase activity that phosphorylates arginine/serine rich domains typical of splicing factors
    • Woppmann A, Will CL, Konstädt U, Zuo P, Manley JM, Lührmann R (1993) Identification of an snRNP-associated kinase activity that phosphorylates arginine/serine rich domains typical of splicing factors. Nucleic Acids Res 21: 2815-2822
    • (1993) Nucleic Acids Res , vol.21 , pp. 2815-2822
    • Woppmann, A.1    Will, C.L.2    Konstädt, U.3    Zuo, P.4    Manley, J.M.5    Lührmann, R.6
  • 75
    • 0027296213 scopus 로고
    • Splicing of pre-mRNA: Mechanism, regulation and role in developement
    • Rio DC (1993) Splicing of pre-mRNA: mechanism, regulation and role in developement. Curr Opin Genet Dev 3:574-584
    • (1993) Curr Opin Genet Dev , vol.3 , pp. 574-584
    • Rio, D.C.1
  • 77
    • 0024565671 scopus 로고
    • A binding consensus: RNA-protein interactions in splicing, snRNPs, and sex
    • Mattaj IW (1989) A binding consensus: RNA-protein interactions in splicing, snRNPs, and sex. Cell 57:1-3
    • (1989) Cell , vol.57 , pp. 1-3
    • Mattaj, I.W.1
  • 78
    • 0027315727 scopus 로고
    • RNA recognition: A family matter?
    • Mattaj IW (1993) RNA recognition: A family matter? Cell 73:837-840
    • (1993) Cell , vol.73 , pp. 837-840
    • Mattaj, I.W.1
  • 80
    • 0028129989 scopus 로고
    • Conserved structures and diversity of functions of RNA-bindina proteins
    • Burd CG, Dreyfuss G (1994) conserved structures and diversity of functions of RNA-bindina proteins. Science 265: 615-620
    • (1994) Science , vol.265 , pp. 615-620
    • Burd, C.G.1    Dreyfuss, G.2
  • 81
    • 0025743575 scopus 로고
    • Functional expression of cloned human splicing factor SF2: Homology to RNA-binding proteins. U1 70 K. and drosophila splicing regulators
    • Krainer RK, Mayeda A, Kozak D (1991) Functional expression of cloned human splicing factor SF2: homology to RNA-binding proteins. U1 70 K. and drosophila splicing regulators. Cell 66:383-394
    • (1991) Cell , vol.66 , pp. 383-394
    • Krainer, R.K.1    Mayeda, A.2    Kozak, D.3
  • 83
    • 0024603237 scopus 로고
    • A common RNA recognition motif identified within a defined U1 RNA binding domain of the 70 K U1 snRNP protein
    • Query CC, Bentley RC, Keene JD (1989) A common RNA recognition motif identified within a defined U1 RNA binding domain of the 70 K U1 snRNP protein. Cell 57:89-101
    • (1989) Cell , vol.57 , pp. 89-101
    • Query, C.C.1    Bentley, R.C.2    Keene, J.D.3
  • 84
    • 0024408832 scopus 로고
    • Identification, purification, and biochemical characterization of U2 small nuclear ribonucleoprotein auxiliary factor
    • Zamore PD, Green MR (1989) Identification, purification, and biochemical characterization of U2 small nuclear ribonucleoprotein auxiliary factor. Proc Natl Acad Sci USA 86: 9243-9247
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 9243-9247
    • Zamore, P.D.1    Green, M.R.2
  • 85
    • 0026026981 scopus 로고
    • Biochemical characterization of U2 snRNP auxiliary factor: An essential pre-mRNA splicing factor with a novel intranuclear distribution
    • Zamore PD, Green MR (1991) Biochemical characterization of U2 snRNP auxiliary factor: an essential pre-mRNA splicing factor with a novel intranuclear distribution. EMBO J 10:207-214
    • (1991) EMBO J , vol.10 , pp. 207-214
    • Zamore, P.D.1    Green, M.R.2
  • 86
    • 0027137934 scopus 로고
    • Specific interactions between proteins implicated in splice site selection and regulated alternative splicing
    • Wu JY, Maniatis T (1993) Specific interactions between proteins implicated in splice site selection and regulated alternative splicing. Cell 75:1061-1070
    • (1993) Cell , vol.75 , pp. 1061-1070
    • Wu, J.Y.1    Maniatis, T.2
  • 87
    • 0028324929 scopus 로고
    • The role of specific protein-RNA and protein-protein interactions in positive and negative control of pre-mRNA splicing by transformer 2
    • Amerein H, Hedley ML, Maniatis T (1994) The role of specific protein-RNA and protein-protein interactions in positive and negative control of pre-mRNA splicing by transformer 2. Cell 76:735-746
    • (1994) Cell , vol.76 , pp. 735-746
    • Amerein, H.1    Hedley, M.L.2    Maniatis, T.3
  • 88
    • 0029665533 scopus 로고    scopus 로고
    • The splicing factor U2AF35 mediates critical protein-protein interactions in constitutive and enhancer-dependent splicing
    • Zuo P, Maniatis T (1996) The splicing factor U2AF35 mediates critical protein-protein interactions in constitutive and enhancer-dependent splicing. Genes Dev 10:1356-1368
    • (1996) Genes Dev , vol.10 , pp. 1356-1368
    • Zuo, P.1    Maniatis, T.2
  • 89
    • 0029933504 scopus 로고    scopus 로고
    • Initial splice-site recognition and pairing during pre-mRNA splicing
    • Reed R (1996) Initial splice-site recognition and pairing during pre-mRNA splicing. Curr Opin Genet Dev 6:215-220
    • (1996) Curr Opin Genet Dev , vol.6 , pp. 215-220
    • Reed, R.1
  • 91
    • 0028077730 scopus 로고
    • Regulation of alternative splicing in vivo by overexpression of antagonistic splicing factors
    • Caceres JF, Stamm S, Helfman DM, Krainer AR (1994) Regulation of alternative splicing in vivo by overexpression of antagonistic splicing factors. Science 265:1706-1709
    • (1994) Science , vol.265 , pp. 1706-1709
    • Caceres, J.F.1    Stamm, S.2    Helfman, D.M.3    Krainer, A.R.4
  • 92
    • 0025324948 scopus 로고
    • A protein factor, ASF, controls cell-specific alternative splicing of SV40 early pre-mRNA in vitro
    • Ge H, Manley JL (1990) A protein factor, ASF, controls cell-specific alternative splicing of SV40 early pre-mRNA in vitro. Cell 62:25-34
    • (1990) Cell , vol.62 , pp. 25-34
    • Ge, H.1    Manley, J.L.2
  • 93
    • 0027185151 scopus 로고
    • A splicing enhancer complex controls alternative splicing of doublesex pre-mRNA
    • Tian M, Maniatis T (1993) A splicing enhancer complex controls alternative splicing of doublesex pre-mRNA. Cell 74: 105-114
    • (1993) Cell , vol.74 , pp. 105-114
    • Tian, M.1    Maniatis, T.2
  • 94
    • 0025367075 scopus 로고
    • The essential premRNA splicing factor SF2 influences 5′ splice site selection by activating proximal sites
    • Krainer AR, Conway GC, Kozak D (1990) The essential premRNA splicing factor SF2 influences 5′ splice site selection by activating proximal sites. Cell 62:35-42
    • (1990) Cell , vol.62 , pp. 35-42
    • Krainer, A.R.1    Conway, G.C.2    Kozak, D.3
  • 95
    • 0026437581 scopus 로고
    • General splicing factors SF2 and SC35 have equivalent activities in vitro, and both affect alternative 5′ and 3′ splice site selection
    • Fu XD, Mayeda A, Maniatis T, Krainer AR (1992) General splicing factors SF2 and SC35 have equivalent activities in vitro, and both affect alternative 5′ and 3′ splice site selection. Proc Natl Acad Sci USA 89:11224-11228
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 11224-11228
    • Fu, X.D.1    Mayeda, A.2    Maniatis, T.3    Krainer, A.R.4
  • 96
    • 0027998643 scopus 로고
    • Protein phosphatase 1 can modulate alternative 5′ splice site selection in a HeLa splicing extract
    • Cardinali B, Cohen PTW, Lamond AI (1994) Protein phosphatase 1 can modulate alternative 5′ splice site selection in a HeLa splicing extract. FEBS Lett 352:276-280
    • (1994) FEBS Lett , vol.352 , pp. 276-280
    • Cardinali, B.1    Cohen, P.T.W.2    Lamond, A.I.3
  • 98
    • 0027478001 scopus 로고
    • In vivo evidence that transcription and splicing are coordinated by a recruiting mechanism
    • Jiménez-Garcia LF, Spector DL (1993) In vivo evidence that transcription and splicing are coordinated by a recruiting mechanism. Cell 73:47-59
    • (1993) Cell , vol.73 , pp. 47-59
    • Jiménez-Garcia, L.F.1    Spector, D.L.2
  • 99
    • 0027957779 scopus 로고
    • Splicing of Balbiani ring 1 gene pre-mRNA occurs simultaneously with transcription
    • Baurén G, Wieslander L (1994) Splicing of Balbiani ring 1 gene pre-mRNA occurs simultaneously with transcription. Cell 76:183-192
    • (1994) Cell , vol.76 , pp. 183-192
    • Baurén, G.1    Wieslander, L.2
  • 100
    • 0027135889 scopus 로고
    • Macromolecular domains within the cell nucleus
    • Spector DL (1993) Macromolecular domains within the cell nucleus. Ann Rev Cell Biol 9:265-315
    • (1993) Ann Rev Cell Biol , vol.9 , pp. 265-315
    • Spector, D.L.1
  • 102
    • 0007362085 scopus 로고
    • Will the real splicing sites please light up?
    • Huang MS, Spector DL (1992) Will the real splicing sites please light up? Curr Biol 2:188-190
    • (1992) Curr Biol , vol.2 , pp. 188-190
    • Huang, M.S.1    Spector, D.L.2
  • 103
    • 0028900584 scopus 로고
    • Transcription dependent redistribution of the large subunit of RNA polymerase II to discrete nuclear domains
    • Bregman DB, Du L, Van derZee S, Warren SL (1995) Transcription dependent redistribution of the large subunit of RNA polymerase II to discrete nuclear domains. J Cell Biol 129:287-298
    • (1995) J Cell Biol , vol.129 , pp. 287-298
    • Bregman, D.B.1    Du, L.2    Van DerZee, S.3    Warren, S.L.4
  • 105
    • 0021334795 scopus 로고
    • Ultrastructural distribution of nuclear ribonucleoproteins as visualized by immunocytochemistry
    • Fakan S, Leser GP, Martin TE (1984) Ultrastructural distribution of nuclear ribonucleoproteins as visualized by immunocytochemistry. J Cell Biol 98:358-363
    • (1984) J Cell Biol , vol.98 , pp. 358-363
    • Fakan, S.1    Leser, G.P.2    Martin, T.E.3
  • 106
    • 0025936626 scopus 로고
    • Associations between distinct pre-mRNA splicing components and the cell nucleus
    • Spector DL, Fu XD, Maniatis T (1991) Associations between distinct pre-mRNA splicing components and the cell nucleus. EMBO J 10:3467-3481
    • (1991) EMBO J , vol.10 , pp. 3467-3481
    • Spector, D.L.1    Fu, X.D.2    Maniatis, T.3
  • 107
    • 0025101714 scopus 로고
    • Higher order nuclear organization: Three-dimensional distribution of small nuclear ribonuicleoprotein particles
    • Spector DL (1990) Higher order nuclear organization: three-dimensional distribution of small nuclear ribonuicleoprotein particles. Proc Natl Acad Sci USA 87:147-151
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 147-151
    • Spector, D.L.1
  • 108
    • 0029798802 scopus 로고    scopus 로고
    • Serine/threonine phosphatase 1 modulates the subnuclear distribution of pre-mRNA splicing factors
    • Misteli T, Spector DL (1996) Serine/threonine phosphatase 1 modulates the subnuclear distribution of pre-mRNA splicing factors. Mol Biol Cell 7:1559-1572
    • (1996) Mol Biol Cell , vol.7 , pp. 1559-1572
    • Misteli, T.1    Spector, D.L.2
  • 109
    • 0025041246 scopus 로고
    • Characterisation of human and murine snRNP proteins by two-dimensional gel electrophoresis and phosphopeptide analysis of U1-specific 70 K protein variants
    • Woppmann A, Patschinsky T, Bringmann P, Godt F, Lührmann R (1990) Characterisation of human and murine snRNP proteins by two-dimensional gel electrophoresis and phosphopeptide analysis of U1-specific 70 K protein variants. Nucleic Acids Res 18:4427-4438
    • (1990) Nucleic Acids Res , vol.18 , pp. 4427-4438
    • Woppmann, A.1    Patschinsky, T.2    Bringmann, P.3    Godt, F.4    Lührmann, R.5
  • 110
    • 0027962510 scopus 로고
    • Purification and characterization of a kinase specific for the serine-and arginine-rich pre-mRNA splicing factors
    • Gui J-F, Tronchère H, Chandler SD, Fu X-D (1994) Purification and characterization of a kinase specific for the serine-and arginine-rich pre-mRNA splicing factors. Proc Natl Acad Sci USA 91:10824-10828
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 10824-10828
    • Gui, J.-F.1    Tronchère, H.2    Chandler, S.D.3    Fu, X.-D.4
  • 111
    • 0027160003 scopus 로고
    • Distinct functions of SR proteins in alternative pre-mRNA splicing
    • Zahler AM, Neugebauer KM, Lane WS, Roth MB (1993) Distinct functions of SR proteins in alternative pre-mRNA splicing. Science 260:219-222
    • (1993) Science , vol.260 , pp. 219-222
    • Zahler, A.M.1    Neugebauer, K.M.2    Lane, W.S.3    Roth, M.B.4
  • 112
    • 0027938872 scopus 로고
    • Characterization by cDNA cloning of two new human protein kinases: Evidence by sequence comparison of a new family of mammalian protein kinases
    • Hanes J, Von der Kammer H, Klaudiny J, Scheit KH (1994) characterization by cDNA cloning of two new human protein kinases: Evidence by sequence comparison of a new family of mammalian protein kinases. J Mol Biol 244:665-672
    • (1994) J Mol Biol , vol.244 , pp. 665-672
    • Hanes, J.1    Von Der Kammer, H.2    Klaudiny, J.3    Scheit, K.H.4
  • 113
    • 0022547813 scopus 로고
    • ATP inhibits nuclear and mithochondrial type I topoisomerases from human leukemia cells
    • Castora FJ, Kelly WG (1986) ATP inhibits nuclear and mithochondrial type I topoisomerases from human leukemia cells. Proc Natl Acad Sci USA 83:1680-1684
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 1680-1684
    • Castora, F.J.1    Kelly, W.G.2
  • 116
    • 0029869828 scopus 로고    scopus 로고
    • The domain organization of human topoisomerase I
    • Stewart L, Ireton GC, Champoux JJ (1996) The domain organization of human topoisomerase I. J Biol Chem 271:7602-7608
    • (1996) J Biol Chem , vol.271 , pp. 7602-7608
    • Stewart, L.1    Ireton, G.C.2    Champoux, J.J.3
  • 117
    • 0026632325 scopus 로고
    • Identification of an N-terminal domain of eukaryotic DNA topoisomerase I dispensable for catalytic activity but essential for in vivo function
    • Alsner J, Svejstrup JQ, Kjeldsen E, Sorensen BS, Westergaard O (1992) Identification of an N-terminal domain of eukaryotic DNA topoisomerase I dispensable for catalytic activity but essential for in vivo function. J Biol Chem 267:12408-12411
    • (1992) J Biol Chem , vol.267 , pp. 12408-12411
    • Alsner, J.1    Svejstrup, J.Q.2    Kjeldsen, E.3    Sorensen, B.S.4    Westergaard, O.5
  • 118
    • 0001498255 scopus 로고
    • Eucaryotic DNA topoisomerases: Two forms of type I DNA topoisomerases from HeLa cell nuclei
    • Liu LF, Miller KG (1981) Eucaryotic DNA topoisomerases: two forms of type I DNA topoisomerases from HeLa cell nuclei. Proc Natl Acad Sci USA 78:3487-3491
    • (1981) Proc Natl Acad Sci USA , vol.78 , pp. 3487-3491
    • Liu, L.F.1    Miller, K.G.2
  • 119
    • 0002827166 scopus 로고
    • Evidence for an intermediate with a single-stand break in the reaction catalyzed by the DNA untwisting enzyme
    • Champoux JJ (1976) Evidence for an intermediate with a single-stand break in the reaction catalyzed by the DNA untwisting enzyme. Proc Natl Acad Sci USA 73:3488-3491
    • (1976) Proc Natl Acad Sci USA , vol.73 , pp. 3488-3491
    • Champoux, J.J.1
  • 120
    • 0002420639 scopus 로고
    • Mechanistic aspects of type-I topoisomerases
    • Wang JC, Cozzarelli NR (eds) Cold Spring Harbor Laboratory, Cold Spring Harbor
    • Champoux JJ (1990) Mechanistic aspects of type-I topoisomerases. In: Wang JC, Cozzarelli NR (eds) DNA topology and its biological effects. Cold Spring Harbor Laboratory, Cold Spring Harbor, pp 217-249
    • (1990) DNA Topology and Its Biological Effects , pp. 217-249
    • Champoux, J.J.1
  • 121
    • 0017708066 scopus 로고
    • Strand breakage by the DNA untwisting enzyme results in covalent attachement of the enzyme to DNA
    • Champoux JJ (1977) Strand breakage by the DNA untwisting enzyme results in covalent attachement of the enzyme to DNA. Proc Natl Acad Sci USA 74:3800-3804
    • (1977) Proc Natl Acad Sci USA , vol.74 , pp. 3800-3804
    • Champoux, J.J.1
  • 122
    • 0018276286 scopus 로고
    • Mechanism of the reaction catalyzed by the DNA untwisting enzyme: Attachment of the enzyme to 3′-terminus of the nicked DNA
    • Champoux JJ (1978) Mechanism of the reaction catalyzed by the DNA untwisting enzyme: attachment of the enzyme to 3′-terminus of the nicked DNA. J Mol Biol 118:441-446
    • (1978) J Mol Biol , vol.118 , pp. 441-446
    • Champoux, J.J.1
  • 123
    • 0019888076 scopus 로고
    • DNA is linked to the rat liver DNA nick-closing enzyme by a phosphodiester bond to tyrosine
    • Champoux JJ (1981) DNA is linked to the rat liver DNA nick-closing enzyme by a phosphodiester bond to tyrosine. J Biol Chem 256:4805-4809
    • (1981) J Biol Chem , vol.256 , pp. 4805-4809
    • Champoux, J.J.1
  • 124
    • 0024670218 scopus 로고
    • Peptide sequencing and site-directed mutagenesis identify tyrosine-727 as the active site tyrosine of Saccharomyces cerevisiae DNA topoisomerase I
    • Lynn RM, Bjornsti MA, Caron PR, Wang JC (1989) Peptide sequencing and site-directed mutagenesis identify tyrosine-727 as the active site tyrosine of Saccharomyces cerevisiae DNA topoisomerase I. Proc Natl Acad Sci USA 86:3559-3563
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 3559-3563
    • Lynn, R.M.1    Bjornsti, M.A.2    Caron, P.R.3    Wang, J.C.4
  • 125
    • 0026503077 scopus 로고
    • Overexpression of human topoisomerase I in baby hamster kidney cells: Hypersensitivity of clonal isolates to camptothecin
    • Madden KR, Champoux JJ (1992) Overexpression of human topoisomerase I in baby hamster kidney cells: hypersensitivity of clonal isolates to camptothecin. Cancer Res 52:525-532
    • (1992) Cancer Res , vol.52 , pp. 525-532
    • Madden, K.R.1    Champoux, J.J.2
  • 126
    • 0015262632 scopus 로고
    • An activity from mammalian cells that untwists superhelical DNA: A possible swivel for DNA replication
    • Champoux JJ, Dulbecco R (1972) An activity from mammalian cells that untwists superhelical DNA: a possible swivel for DNA replication. Proc Natl Acad Sci USA 69:143-146
    • (1972) Proc Natl Acad Sci USA , vol.69 , pp. 143-146
    • Champoux, J.J.1    Dulbecco, R.2
  • 127
    • 0021891888 scopus 로고
    • DNA Topoisomerases
    • Wang JC (1985) DNA Topoisomerases. Annu Rev Biochem 54:665-697
    • (1985) Annu Rev Biochem , vol.54 , pp. 665-697
    • Wang, J.C.1
  • 128
    • 0025800372 scopus 로고
    • DNA topoisomerases: Why so many?
    • Wang JC (1991) DNA topoisomerases: Why so many? J Biol Chem 266:6659-6662
    • (1991) J Biol Chem , vol.266 , pp. 6659-6662
    • Wang, J.C.1
  • 129
    • 0021272096 scopus 로고
    • Identification of Saccharomyces cerevisiae mutants deficient in DNA topoisomerase I activity
    • Thrash C, Voelkel K, DiNardo S, Sternglanz R (1984) Identification of Saccharomyces cerevisiae mutants deficient in DNA topoisomerase I activity. J Biol Chem 259:1375-1377
    • (1984) J Biol Chem , vol.259 , pp. 1375-1377
    • Thrash, C.1    Voelkel, K.2    Dinardo, S.3    Sternglanz, R.4
  • 130
    • 0021931572 scopus 로고
    • Cloning, characterization, and sequence of the yeast DNA topoisomerase I gene
    • Thrash C, Bankier AT, Barrell BG, Sterglanz R (1985) Cloning, characterization, and sequence of the yeast DNA topoisomerase I gene. Proc Natl Acad Sci USA 82:4374-4378
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 4374-4378
    • Thrash, C.1    Bankier, A.T.2    Barrell, B.G.3    Sterglanz, R.4
  • 131
    • 0009543358 scopus 로고
    • Isolation of type I and II DNA topoisomerase mutants from fission yeast: Single and double mutants show different phenotypes in cell growth and chromatin organization
    • Uemura T, Yanagida M (1984) Isolation of type I and II DNA topoisomerase mutants from fission yeast: single and double mutants show different phenotypes in cell growth and chromatin organization. EMBO J 3:1737-1744
    • (1984) EMBO J , vol.3 , pp. 1737-1744
    • Uemura, T.1    Yanagida, M.2
  • 133
    • 0029897304 scopus 로고    scopus 로고
    • A novel family of TRF (DNA topoisomerase I-related function) genes required for proper nuclear segregation
    • Castano IB, Heath-Pagliuso S, Sadoff BU, Fitzhugh DJ, Christman MF (1996) A novel family of TRF (DNA topoisomerase I-related function) genes required for proper nuclear segregation. Nucleic Acids Res 24:2404-2410
    • (1996) Nucleic Acids Res , vol.24 , pp. 2404-2410
    • Castano, I.B.1    Heath-Pagliuso, S.2    Sadoff, B.U.3    Fitzhugh, D.J.4    Christman, M.F.5
  • 134
  • 135
    • 0024279845 scopus 로고
    • Transcription generates positively and negatively supercoiled domains in the template
    • Wu HY, Shyy S, Wang JC, Liu IF (1988) Transcription generates positively and negatively supercoiled domains in the template. Cell 53:433-440
    • (1988) Cell , vol.53 , pp. 433-440
    • Wu, H.Y.1    Shyy, S.2    Wang, J.C.3    Liu, I.F.4
  • 136
    • 0024968110 scopus 로고
    • Transcription-driven supercoiling of DNA: Direct biochemical evidence from in vitro studies
    • Tsao YP, Wu HY, Liu LF (1989) Transcription-driven supercoiling of DNA: direct biochemical evidence from in vitro studies. Cell 56:111-118
    • (1989) Cell , vol.56 , pp. 111-118
    • Tsao, Y.P.1    Wu, H.Y.2    Liu, L.F.3
  • 137
    • 0023433855 scopus 로고
    • Supercoiling of the DNA template during transcription
    • Liu LF, Wang JC (1987) Supercoiling of the DNA template during transcription. Proc Natl Acad Sci USA 84:7024-7027
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 7024-7027
    • Liu, L.F.1    Wang, J.C.2
  • 138
    • 0025872128 scopus 로고
    • A general topoisomerase I-dependent transcriptional repression in the stationary phase in yeast
    • Choder M (1991) A general topoisomerase I-dependent transcriptional repression in the stationary phase in yeast. Genes Dev 5:2315-2326
    • (1991) Genes Dev , vol.5 , pp. 2315-2326
    • Choder, M.1
  • 139
    • 0023958908 scopus 로고
    • Involvement of DNA topoisomerase I in the transcription of human ribosomal RNA genes
    • Zhang H, Wang JC, Liu LF (1988) Involvement of DNA topoisomerase I in the transcription of human ribosomal RNA genes. Cell 85:1060-1064
    • (1988) Cell , vol.85 , pp. 1060-1064
    • Zhang, H.1    Wang, J.C.2    Liu, L.F.3
  • 140
    • 0024299511 scopus 로고
    • Transcription-dependent DNA supercoiling in yeast DNA topoisomerase mutants
    • Brill SJ, Sternglanz R (1988) Transcription-dependent DNA supercoiling in yeast DNA topoisomerase mutants. Cell 54:403-411
    • (1988) Cell , vol.54 , pp. 403-411
    • Brill, S.J.1    Sternglanz, R.2
  • 141
    • 0023277908 scopus 로고
    • Role of DNA topoisomerase I in the transcription of supercoiled rRNA gene
    • Garg LC, DiAngelo S, Jacob ST (1987) Role of DNA topoisomerase I in the transcription of supercoiled rRNA gene. Proc Natl Acad Sci USA 84:3185-3188
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 3185-3188
    • Garg, L.C.1    DiAngelo, S.2    Jacob, S.T.3
  • 142
    • 0028711871 scopus 로고
    • Roles of DNA topoisomerases in transcription
    • Drolet M, Wu HY, Liu LF (1994) Roles of DNA topoisomerases in transcription. Adv Pharmacol 29:135-146
    • (1994) Adv Pharmacol , vol.29 , pp. 135-146
    • Drolet, M.1    Wu, H.Y.2    Liu, L.F.3
  • 143
    • 0024338961 scopus 로고
    • Function of DNA topoisomerases as replication swivels in S. cerevisiae
    • Kim RA, Wang JC (1989) Function of DNA topoisomerases as replication swivels in S. cerevisiae. J Mol Biol 208:257-267
    • (1989) J Mol Biol , vol.208 , pp. 257-267
    • Kim, R.A.1    Wang, J.C.2
  • 144
  • 145
    • 0023127037 scopus 로고
    • Need for DNA topoisomerase activity as a swivel for DNA replication and for transcription of ribosomal DNA
    • Brill SJ, DiNardo S, Voelkel-Meiman K, Sternglanz R (1987) Need for DNA topoisomerase activity as a swivel for DNA replication and for transcription of ribosomal DNA. Nature 326:414-416
    • (1987) Nature , vol.326 , pp. 414-416
    • Brill, S.J.1    DiNardo, S.2    Voelkel-Meiman, K.3    Sternglanz, R.4
  • 146
    • 0027139317 scopus 로고
    • Interaction between replication forks and topoisomerase I-DNA cleavable complexes: Studies in a cell-free SV40 DNA replication system
    • Tsao YP, Russo A, Nyamuswa G, Silber R, Liu LF (1993) Interaction between replication forks and topoisomerase I-DNA cleavable complexes: studies in a cell-free SV40 DNA replication system. Cancer Res 53:5908-5914
    • (1993) Cancer Res , vol.53 , pp. 5908-5914
    • Tsao, Y.P.1    Russo, A.2    Nyamuswa, G.3    Silber, R.4    Liu, L.F.5
  • 147
    • 0023002286 scopus 로고
    • Topoisomerase inhibitors can selectively interfere with different stages of simian virus 40 DNA replication
    • Snapka RM (1986) Topoisomerase inhibitors can selectively interfere with different stages of simian virus 40 DNA replication. Mol Cell Biol 6:4221-4227
    • (1986) Mol Cell Biol , vol.6 , pp. 4221-4227
    • Snapka, R.M.1
  • 148
    • 0023811784 scopus 로고
    • Topoisomerase I is preferentially associated with isolated replicating simian virus 40 molecules after treatment of infected cells with camptothecin
    • Champoux JJ (1988) Topoisomerase I is preferentially associated with isolated replicating simian virus 40 molecules after treatment of infected cells with camptothecin. J Virol 62:3675-3683
    • (1988) J Virol , vol.62 , pp. 3675-3683
    • Champoux, J.J.1
  • 149
    • 0024420685 scopus 로고
    • Arrest of replication forks by drug-stabilized topoisomerase I-DNA cleavable complexes as a mechanism of cell killing by camptothecin
    • Hsiang YH, Lihou MG, Liu LF (1989) Arrest of replication forks by drug-stabilized topoisomerase I-DNA cleavable complexes as a mechanism of cell killing by camptothecin. Cancer Res 49:5077-5082
    • (1989) Cancer Res , vol.49 , pp. 5077-5082
    • Hsiang, Y.H.1    Lihou, M.G.2    Liu, L.F.3
  • 150
    • 0024277974 scopus 로고
    • Mitotic recombination in the rDNA of S. cerevisiae is suppressed by the combined action of DNA topoisomerase I and II
    • Christman MF, Dietrich FS, Fink GR (1993) Mitotic recombination in the rDNA of S. cerevisiae is suppressed by the combined action of DNA topoisomerase I and II. Cell 55:413-425
    • (1993) Cell , vol.55 , pp. 413-425
    • Christman, M.F.1    Dietrich, F.S.2    Fink, G.R.3
  • 151
    • 0024997668 scopus 로고
    • The role of DNA topoisomerases in recombination and genomic stability: A double-edged sword?
    • Wang JC, Caron PR, Kim RA (1990) The role of DNA topoisomerases in recombination and genomic stability: a double-edged sword? Cell 62:403-406
    • (1990) Cell , vol.62 , pp. 403-406
    • Wang, J.C.1    Caron, P.R.2    Kim, R.A.3
  • 152
    • 0024392077 scopus 로고
    • A subthreshold level of DNA topoisomerases leads to the excision of yeast rDNA as extrachromosomal rings
    • Kim RA, Wang JC (1989) A subthreshold level of DNA topoisomerases leads to the excision of yeast rDNA as extrachromosomal rings. Cell 57:975-985
    • (1989) Cell , vol.57 , pp. 975-985
    • Kim, R.A.1    Wang, J.C.2
  • 153
    • 0029960067 scopus 로고    scopus 로고
    • Topoisomerase I involvement in illegitimate recombination in Saccharomyces cerevisiae
    • Zhu J, Schiestl RH (1996) Topoisomerase I involvement in illegitimate recombination in Saccharomyces cerevisiae. Mol Cell Biol 16:1805-1812
    • (1996) Mol Cell Biol , vol.16 , pp. 1805-1812
    • Zhu, J.1    Schiestl, R.H.2
  • 154
    • 0030040266 scopus 로고    scopus 로고
    • Effects of DNA topoisomerase inhibitors on nonhomologous and homologous recombination in mammalian cells
    • Aratani Y, Andoh T, Koyama H (1996) Effects of DNA topoisomerase inhibitors on nonhomologous and homologous recombination in mammalian cells. Mutat Res 362:181-191
    • (1996) Mutat Res , vol.362 , pp. 181-191
    • Aratani, Y.1    Andoh, T.2    Koyama, H.3
  • 155
    • 0024324482 scopus 로고
    • A hyper-recombination mutation in S. cerevisiae identifies a novel eukaryotic topoisomerase
    • Wallis JW, Chrebet G, Brodsky G, Rolfe M, Rothstein R (1989) A hyper-recombination mutation in S. cerevisiae identifies a novel eukaryotic topoisomerase. Cell 58:409-419
    • (1989) Cell , vol.58 , pp. 409-419
    • Wallis, J.W.1    Chrebet, G.2    Brodsky, G.3    Rolfe, M.4    Rothstein, R.5
  • 156
    • 0022409106 scopus 로고
    • Association of crossover points with topoisomerase I cleavage sites: A model for nonhomologous recombination
    • Bullock P, Champoux JJ, Botchan M (1985) Association of crossover points with topoisomerase I cleavage sites: a model for nonhomologous recombination. Science 230:954-958
    • (1985) Science , vol.230 , pp. 954-958
    • Bullock, P.1    Champoux, J.J.2    Botchan, M.3
  • 157
    • 0021111554 scopus 로고
    • Association of eukaryotic DNA topoisomerase I with nucleosomes and chromosomal proteins
    • Javaherian K, Liu LF (1983) Association of eukaryotic DNA topoisomerase I with nucleosomes and chromosomal proteins. Nucleic Acids Res 11:461-472
    • (1983) Nucleic Acids Res , vol.11 , pp. 461-472
    • Javaherian, K.1    Liu, L.F.2
  • 158
    • 0027250337 scopus 로고
    • The rRNA-encoding DNA array has an altered structure in topoisomerase I mutants of S. cerevisiae
    • Christman MF, Dietrich FS, Levin NA, Sadoff BU, Fink GR (1993) The rRNA-encoding DNA array has an altered structure in topoisomerase I mutants of S. cerevisiae. Proc Natl Acad Sci USA 90:7637-7641
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 7637-7641
    • Christman, M.F.1    Dietrich, F.S.2    Levin, N.A.3    Sadoff, B.U.4    Fink, G.R.5
  • 159
    • 0029986401 scopus 로고    scopus 로고
    • Human TOP3: A single-copy gene encoding DNA topoisomerase III
    • Hanai R, Caron PR, Wang JC (1996) Human TOP3: a single-copy gene encoding DNA topoisomerase III. Proc Natl Acad Sci USA 93:3653-3657
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 3653-3657
    • Hanai, R.1    Caron, P.R.2    Wang, J.C.3
  • 160
    • 0023650299 scopus 로고
    • Cloning and sequencing of Schizosaccharomyces pombe DNA topoisomerase I gene, and effect of gene disruption
    • Uemura T, Morino K, Uzawa S, Shiozaki K, Yanagida M (1987) Cloning and sequencing of Schizosaccharomyces pombe DNA topoisomerase I gene, and effect of gene disruption. Nucleic Acids Res 15:9727-9739
    • (1987) Nucleic Acids Res , vol.15 , pp. 9727-9739
    • Uemura, T.1    Morino, K.2    Uzawa, S.3    Shiozaki, K.4    Yanagida, M.5
  • 161
    • 0022780331 scopus 로고
    • The nucleotide sequence of the fission yeast DNA topoisomerase II gene: Structural and functional relationships to other DNA topoisomerases
    • Uemura T, Morikawa K, Yanagida M (1986) The nucleotide sequence of the fission yeast DNA topoisomerase II gene: structural and functional relationships to other DNA topoisomerases. EMBO J 5:2355-2361
    • (1986) EMBO J , vol.5 , pp. 2355-2361
    • Uemura, T.1    Morikawa, K.2    Yanagida, M.3
  • 162
    • 0021185946 scopus 로고
    • Yeast DNA topoisomerase II is encoded by a single-copy, essential gene
    • Goto T, Wang JC (1984) Yeast DNA topoisomerase II is encoded by a single-copy, essential gene. Cell 36:1073-1080
    • (1984) Cell , vol.36 , pp. 1073-1080
    • Goto, T.1    Wang, J.C.2
  • 163
    • 0023651332 scopus 로고
    • DNA topoisomerase II is required for condensation and separation of mitotic chromosomes in S. pombe
    • Uemura T, Ohkura H, Adachi Y, Morino K, Shiozaki K, Yanagida M (1987) DNA topoisomerase II is required for condensation and separation of mitotic chromosomes in S. pombe. Cell 50:917-925
    • (1987) Cell , vol.50 , pp. 917-925
    • Uemura, T.1    Ohkura, H.2    Adachi, Y.3    Morino, K.4    Shiozaki, K.5    Yanagida, M.6
  • 164
    • 0011173714 scopus 로고
    • DNA topoisomerase II mutant of Sacchammvces cerevisiae: Topoisomerase II is required for segregation of daughter molecules at the termination of DNA replication
    • DiNardo S, Voelkel K, Sternglanz R (1984) DNA topoisomerase II mutant of Sacchammvces cerevisiae: topoisomerase II is required for segregation of daughter molecules at the termination of DNA replication. Proc Natl Acad Sci USA 81:2616-5620
    • (1984) Proc Natl Acad Sci USA , vol.81 , pp. 2616-5620
    • DiNardo, S.1    Voelkel, K.2    Sternglanz, R.3
  • 165
    • 0022400533 scopus 로고
    • DNA topoisomerase II is required at the time of mitosis in yeast
    • Holm C, Goto T, Wang JC, Botstein D (1985) DNA topoisomerase II is required at the time of mitosis in yeast. Cell 41:553-563
    • (1985) Cell , vol.41 , pp. 553-563
    • Holm, C.1    Goto, T.2    Wang, J.C.3    Botstein, D.4
  • 166
    • 0022067647 scopus 로고
    • Eukaryotic type I topoisomerase is enriched in the nucleolus and catalytically active on ribosomal DNA
    • Muller MT, Pfund WP, Mehta VB, Trask DK (1985) Eukaryotic type I topoisomerase is enriched in the nucleolus and catalytically active on ribosomal DNA. EMBO J 4:1237-1243
    • (1985) EMBO J , vol.4 , pp. 1237-1243
    • Muller, M.T.1    Pfund, W.P.2    Mehta, V.B.3    Trask, D.K.4
  • 168
    • 0029960812 scopus 로고    scopus 로고
    • Eukaryotic DNA topoisomerase I: Genome gatekeeper and its intruders, camptothecins
    • Pommier Y (1996) Eukaryotic DNA topoisomerase I: genome gatekeeper and its intruders, camptothecins. Semin Oncol 23:3-10
    • (1996) Semin Oncol , vol.23 , pp. 3-10
    • Pommier, Y.1
  • 169
    • 0024853052 scopus 로고
    • Topoisomerase-targeting antitumor drugs
    • D'Arpa P, Liu LF (1989) Topoisomerase-targeting antitumor drugs. Biochim Biophys Acta 989:163-177
    • (1989) Biochim Biophys Acta , vol.989 , pp. 163-177
    • D'Arpa, P.1    Liu, L.F.2
  • 170
    • 0025190947 scopus 로고
    • Rapid induction of c-fos transcription reveals quantitative linkage of RNA polymerase II and DNA topoisomerase I enzyme activities
    • Stewart AF, Herrera RE, Nordheim A (1990) Rapid induction of c-fos transcription reveals quantitative linkage of RNA polymerase II and DNA topoisomerase I enzyme activities. Cell 60:141-149
    • (1990) Cell , vol.60 , pp. 141-149
    • Stewart, A.F.1    Herrera, R.E.2    Nordheim, A.3
  • 171
    • 0024431084 scopus 로고
    • Interaction of topoisomerase I with the transcribed region of the Drosophila HSP 70 heat shock gene
    • Kroeger PE, Rowe TC (1989) Interaction of topoisomerase I with the transcribed region of the Drosophila HSP 70 heat shock gene. Nucleic Acids Res 17:8495-8509
    • (1989) Nucleic Acids Res , vol.17 , pp. 8495-8509
    • Kroeger, P.E.1    Rowe, T.C.2
  • 172
    • 0030042250 scopus 로고    scopus 로고
    • Inactivation of topoisomerases affects transcription-dependent chromatin transitions in rDNA but not in a gene transcribed by RNA polymerase II
    • Cavalli G, Bachmann D, Thoma F (1996) Inactivation of topoisomerases affects transcription-dependent chromatin transitions in rDNA but not in a gene transcribed by RNA polymerase II. EMBO J 15:590-597
    • (1996) EMBO J , vol.15 , pp. 590-597
    • Cavalli, G.1    Bachmann, D.2    Thoma, F.3
  • 173
    • 0023805882 scopus 로고
    • Association of DNA topoisomerase I and RNA polymerase I: A possible role for topoisomerase I in ribosomal gene transcription
    • Rose KM, Szopa J, Han FS, Cheng YC, Richter A, Scheer U (1988) Association of DNA topoisomerase I and RNA polymerase I: a possible role for topoisomerase I in ribosomal gene transcription. Chromosoma 96:411-416
    • (1988) Chromosoma , vol.96 , pp. 411-416
    • Rose, K.M.1    Szopa, J.2    Han, F.S.3    Cheng, Y.C.4    Richter, A.5    Scheer, U.6
  • 174
    • 0030047434 scopus 로고    scopus 로고
    • Identification of a Nucleolin binding site in human topoisomerase I
    • Bharti AK, Olson MOJ, Kufe DW, Rubin EH (1996) Identification of a Nucleolin binding site in human topoisomerase I. J Biol Chem 271:1993-1996
    • (1996) J Biol Chem , vol.271 , pp. 1993-1996
    • Bharti, A.K.1    Olson, M.O.J.2    Kufe, D.W.3    Rubin, E.H.4
  • 176
    • 0027186443 scopus 로고
    • DNA topoisomerase I is involved in both repression and activation of transcription
    • Merino A, Madden KR, Lane WS, Champoux JJ, Reinberg D (1993) DNA topoisomerase I is involved in both repression and activation of transcription. Nature 365:227-232
    • (1993) Nature , vol.365 , pp. 227-232
    • Merino, A.1    Madden, K.R.2    Lane, W.S.3    Champoux, J.J.4    Reinberg, D.5
  • 177
    • 0027138674 scopus 로고
    • Identification of human DNA topoisomerase I as a cofactor for activator-dependent transcription by RNA polymerase II
    • Kretzschmar M, Meisterernst M, Roeder RG (1993) Identification of human DNA topoisomerase I as a cofactor for activator-dependent transcription by RNA polymerase II. Proc Natl Acad Sci USA 90:11508-11512
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 11508-11512
    • Kretzschmar, M.1    Meisterernst, M.2    Roeder, R.G.3
  • 178
    • 0027436353 scopus 로고
    • Transcription and DNA supercoiling
    • Wang JC, Lynch AS (1993) Transcription and DNA supercoiling. Curr Opin Genet Dev 3:764-768
    • (1993) Curr Opin Genet Dev , vol.3 , pp. 764-768
    • Wang, J.C.1    Lynch, A.S.2
  • 179
    • 0028787255 scopus 로고
    • Preferential binding of human topoisomerase I to superhelical DNA
    • Madden KR, Stewart L, Champoux JJ (1995) Preferential binding of human topoisomerase I to superhelical DNA. EMBO J 14:5399-5409
    • (1995) EMBO J , vol.14 , pp. 5399-5409
    • Madden, K.R.1    Stewart, L.2    Champoux, J.J.3
  • 180
    • 0026654950 scopus 로고
    • Topoisomerase I is preferentially associated with normal SV40 replicative intermediates, but is associated with both replicating and nonreplicating SV40 DNAs which are deficient in histones
    • Champoux JJ (1992) Topoisomerase I is preferentially associated with normal SV40 replicative intermediates, but is associated with both replicating and nonreplicating SV40 DNAs which are deficient in histones. Nucleic Acids Res 20:3347-3352
    • (1992) Nucleic Acids Res , vol.20 , pp. 3347-3352
    • Champoux, J.J.1
  • 181
  • 183
    • 0024316466 scopus 로고
    • DNA topoisomerase poisons as antitumor drugs
    • Liu LF (1989) DNA topoisomerase poisons as antitumor drugs. Annu Rev Biochem 58:351-375
    • (1989) Annu Rev Biochem , vol.58 , pp. 351-375
    • Liu, L.F.1
  • 184
    • 0024010012 scopus 로고
    • Topoisomerases: Novel therapeutic targets in cancer chemotherapy
    • Hsiang YH, Wu HY, Liu LF (1988) Topoisomerases: novel therapeutic targets in cancer chemotherapy. Biochem Pharmacol 37:1801-1812
    • (1988) Biochem Pharmacol , vol.37 , pp. 1801-1812
    • Hsiang, Y.H.1    Wu, H.Y.2    Liu, L.F.3
  • 185
    • 0027276902 scopus 로고
    • DNA topoisomerase I and II in cancer chemotherapy: Update and perspectives
    • Pommier Y (1993) DNA topoisomerase I and II in cancer chemotherapy: update and perspectives. Cancer Chemother Pharmacol 32:103-108
    • (1993) Cancer Chemother Pharmacol , vol.32 , pp. 103-108
    • Pommier, Y.1
  • 186
    • 0029144134 scopus 로고
    • Topoisomerase poisons: Harnessing the dark side of enzyme mechanism
    • Froelich-Ammon SJ, Osheroff N (1995) Topoisomerase poisons: harnessing the dark side of enzyme mechanism. J Biol Chem 270:21429-21432
    • (1995) J Biol Chem , vol.270 , pp. 21429-21432
    • Froelich-Ammon, S.J.1    Osheroff, N.2
  • 187
    • 0000536643 scopus 로고
    • DNA topoisomerase-targeting antitumor drugs can be studied in yeast
    • Nitiss J, Wang JC (1988) DNA topoisomerase-targeting antitumor drugs can be studied in yeast. Proc Natl Acad Sci USA 85:7501-7505
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 7501-7505
    • Nitiss, J.1    Wang, J.C.2
  • 188
    • 0023924786 scopus 로고
    • Identification of mammalian DNA topoisomerase I as an intracellular target of the anticancerdrug camptothecin
    • Hsiang YH, Liu LF (1988) Identification of mammalian DNA topoisomerase I as an intracellular target of the anticancerdrug camptothecin. Cancer Res 48:1722-1726
    • (1988) Cancer Res , vol.48 , pp. 1722-1726
    • Hsiang, Y.H.1    Liu, L.F.2
  • 189
    • 0028122503 scopus 로고
    • Yeast Saccharomyces cerevisiae as a model system to study the cytotoxic activity of the antitumor drug camptothecin
    • Bjornsti MA, Knab AM, Benedetti P (1994) Yeast Saccharomyces cerevisiae as a model system to study the cytotoxic activity of the antitumor drug camptothecin. Cancer Chemother Pharmacol 34:1-5
    • (1994) Cancer Chemother Pharmacol , vol.34 , pp. 1-5
    • Bjornsti, M.A.1    Knab, A.M.2    Benedetti, P.3
  • 190
    • 0024305936 scopus 로고
    • Expression of human DNA topoisomerase I in yeast cells lacking yeast DNA topoisomerase I: Restoration of sensitivity of the cells to the antitumor drug camptothecin
    • Bjornsti MA, Benedetti P, Viglianti GA, Wang JC (1989) Expression of human DNA topoisomerase I in yeast cells lacking yeast DNA topoisomerase I: restoration of sensitivity of the cells to the antitumor drug camptothecin. Cancer Res 49:6318-6323
    • (1989) Cancer Res , vol.49 , pp. 6318-6323
    • Bjornsti, M.A.1    Benedetti, P.2    Viglianti, G.A.3    Wang, J.C.4
  • 192
    • 0024229066 scopus 로고
    • Evidence that DNA topoisomerase I is necessary for the cytotoxic effects of camptothecin
    • Eng WK, Faucette L, Johnson RK, Sternglanz R (1988) Evidence that DNA topoisomerase I is necessary for the cytotoxic effects of camptothecin. Mol Pharmacol 34:755-760
    • (1988) Mol Pharmacol , vol.34 , pp. 755-760
    • Eng, W.K.1    Faucette, L.2    Johnson, R.K.3    Sternglanz, R.4
  • 193
    • 0024324205 scopus 로고
    • On the mechanism of topoisomerase I inhibition by camptothecin: Evidence for binding to an enzyme-DNA complex
    • Hertzberg RP, Caranfa MJ, Hecht SM (1989) On the mechanism of topoisomerase I inhibition by camptothecin: evidence for binding to an enzyme-DNA complex. Biochemistry 28:4629-4638
    • (1989) Biochemistry , vol.28 , pp. 4629-4638
    • Hertzberg, R.P.1    Caranfa, M.J.2    Hecht, S.M.3
  • 194
    • 0028711272 scopus 로고
    • The DNA binding, cleavage, and religation reactions of eukaryotic topoisomerases I and II
    • Andersen AH, Svejstrup JQ, Westergaard O (1994) The DNA binding, cleavage, and religation reactions of eukaryotic topoisomerases I and II. Adv Pharmacol 29:83-101
    • (1994) Adv Pharmacol , vol.29 , pp. 83-101
    • Andersen, A.H.1    Svejstrup, J.Q.2    Westergaard, O.3
  • 196
    • 0024469050 scopus 로고
    • The basis for camptothecin enhancement of DNA breakage by eucaryotic topoisomerase I
    • Porter SE, Champoux JJ (1989) The basis for camptothecin enhancement of DNA breakage by eucaryotic topoisomerase I. Nucleic Acids Res 17:8521-8532
    • (1989) Nucleic Acids Res , vol.17 , pp. 8521-8532
    • Porter, S.E.1    Champoux, J.J.2
  • 197
    • 0028999826 scopus 로고
    • Differential stabilization of eukaryotic DNA topoisomerase I cleavable complexes by camptothecin derivatives
    • Tanizawa A, Kohn KW, Kohlhagen G, Leteurtre F, Pommier Y (1995) Differential stabilization of eukaryotic DNA topoisomerase I cleavable complexes by camptothecin derivatives. Biochemistry 34:7200-7206
    • (1995) Biochemistry , vol.34 , pp. 7200-7206
    • Tanizawa, A.1    Kohn, K.W.2    Kohlhagen, G.3    Leteurtre, F.4    Pommier, Y.5
  • 198
    • 0022340594 scopus 로고
    • Camptothecin induces protein-linked DNA breaks via mammalian DNA topoisomerase I
    • Hsiang YH, Hertzberg R, Hecht S, Liu LF (1985) Camptothecin induces protein-linked DNA breaks via mammalian DNA topoisomerase I. J Biol Chem 260:14873-14878
    • (1985) J Biol Chem , vol.260 , pp. 14873-14878
    • Hsiang, Y.H.1    Hertzberg, R.2    Hecht, S.3    Liu, L.F.4
  • 199
    • 0026497126 scopus 로고
    • Topoisomerase-targeting antitumor drugs: Mechanisms of cytotoxicity and resistance
    • Liu LF, D'Arpa P (1992) Topoisomerase-targeting antitumor drugs: mechanisms of cytotoxicity and resistance. Important Adv Oncol 79-89
    • (1992) Important Adv Oncol , pp. 79-89
    • Liu, L.F.1    D'Arpa, P.2
  • 200
    • 0029738086 scopus 로고    scopus 로고
    • Induction of neuronal apoptosis by camptothecin, an inhibitor of DNA topoisomerase-I: Evidence for cell cycle-independent toxicity
    • Morris EJ, Geller HM (1996) Induction of neuronal apoptosis by camptothecin, an inhibitor of DNA topoisomerase-I: evidence for cell cycle-independent toxicity. J Cell Biol 134: 757-770
    • (1996) J Cell Biol , vol.134 , pp. 757-770
    • Morris, E.J.1    Geller, H.M.2
  • 201
    • 0030097371 scopus 로고    scopus 로고
    • Apoptosis of human leukemic cells induced by topoisomerase I and II inhibitors
    • Paris
    • Solary E, Dubrez L, Eymin B, Bertrand R, Pommier Y (1996) Apoptosis of human leukemic cells induced by topoisomerase I and II inhibitors. Bull Cancer (Paris) 83:205-212
    • (1996) Bull Cancer , vol.83 , pp. 205-212
    • Solary, E.1    Dubrez, L.2    Eymin, B.3    Bertrand, R.4    Pommier, Y.5
  • 202
    • 0026625512 scopus 로고
    • The involvement of active DNA synthesis in camptothecin-induced G2 arrest: Altered regulation of p34cdc2/cyclin B
    • Tsao YP, D'Arpa P, Liu LF (1992) The involvement of active DNA synthesis in camptothecin-induced G2 arrest: altered regulation of p34cdc2/cyclin B. Cancer Res 52:1823-1829
    • (1992) Cancer Res , vol.52 , pp. 1823-1829
    • Tsao, Y.P.1    D'Arpa, P.2    Liu, L.F.3
  • 203
    • 0025133118 scopus 로고
    • Involvement of nucleic acid synthesis in cell killing mechanisms of topoisomerase poisons
    • D'Arpa P, Beardmore C, Liu LF (1990) Involvement of nucleic acid synthesis in cell killing mechanisms of topoisomerase poisons. Cancer Res 50:6919-6924
    • (1990) Cancer Res , vol.50 , pp. 6919-6924
    • D'Arpa, P.1    Beardmore, C.2    Liu, L.F.3
  • 204
    • 0024388737 scopus 로고
    • Differential requirement of DNA replication for the cytotoxicity of DNA topoisomerase I and II inhibitors in Chinese hamster DC3F cells
    • Holm C, Covey JM, Kerrigan D, Pommier Y (1989) Differential requirement of DNA replication for the cytotoxicity of DNA topoisomerase I and II inhibitors in Chinese hamster DC3F cells. Cancer Res 49:6365-6368
    • (1989) Cancer Res , vol.49 , pp. 6365-6368
    • Holm, C.1    Covey, J.M.2    Kerrigan, D.3    Pommier, Y.4
  • 205
    • 0028957974 scopus 로고
    • Mutation at the catalytic site of topoisomerase I in CEM/C2, a human leukemia cell line resistant to camptothecin
    • Fujimori A, Harker WG, Kohlhagen G, Hoki Y, Pommier Y (1995) Mutation at the catalytic site of topoisomerase I in CEM/C2, a human leukemia cell line resistant to camptothecin. Cancer Res 55:1339-1346
    • (1995) Cancer Res , vol.55 , pp. 1339-1346
    • Fujimori, A.1    Harker, W.G.2    Kohlhagen, G.3    Hoki, Y.4    Pommier, Y.5
  • 206
    • 0027368901 scopus 로고
    • Cloning of Chinese hamster DNA topoisomerase I cDNA and identification of a single point mutation responsible for camptothecin resistance
    • Tanizawa A, Beitrand R, Kohlhagen G, Tabuchi A, Jenkins J, Pommier Y (1993) Cloning of Chinese hamster DNA topoisomerase I cDNA and identification of a single point mutation responsible for camptothecin resistance. J Biol Chem 268:25463-25468
    • (1993) J Biol Chem , vol.268 , pp. 25463-25468
    • Tanizawa, A.1    Beitrand, R.2    Kohlhagen, G.3    Tabuchi, A.4    Jenkins, J.5    Pommier, Y.6
  • 207
    • 0027381388 scopus 로고
    • Mechanisms of camptothecin resistance in yeast DNA topoisomerase I mutants
    • Knab AM, Fertala J, Bjornsti MA (1993) Mechanisms of camptothecin resistance in yeast DNA topoisomerase I mutants. J Biol Chem 268:22322-22330
    • (1993) J Biol Chem , vol.268 , pp. 22322-22330
    • Knab, A.M.1    Fertala, J.2    Bjornsti, M.A.3
  • 209
    • 0028030721 scopus 로고
    • Identification of a mutant human topoisomerase I with intact catalytic activity and resistance to 9-nitrocamptothecin
    • Rubin E, Pantazis P, Bharti A, Toppmeyer D, Giovanella B, Kufe D (1994) Identification of a mutant human topoisomerase I with intact catalytic activity and resistance to 9-nitrocamptothecin. J Biol Chem 269:2433-2439
    • (1994) J Biol Chem , vol.269 , pp. 2433-2439
    • Rubin, E.1    Pantazis, P.2    Bharti, A.3    Toppmeyer, D.4    Giovanella, B.5    Kufe, D.6
  • 210
    • 0027881702 scopus 로고
    • Camptothecin resistance from a single mutation changing glycine 363 of human DNA topoisomerase I to cysteine
    • Benedetti P, Fiorani P, Capuani L, Wang JC (1993) Camptothecin resistance from a single mutation changing glycine 363 of human DNA topoisomerase I to cysteine. Cancer Res 53:4343-4348
    • (1993) Cancer Res , vol.53 , pp. 4343-4348
    • Benedetti, P.1    Fiorani, P.2    Capuani, L.3    Wang, J.C.4
  • 212
  • 216
    • 0027324850 scopus 로고
    • Therapeutic efficacy of the topoisomerase 1 inhibitor 7-ethyl-10-(4-[1-piperidino]-1-piperidino)-carbonyloxy-camptothecin against human tumor xenografts: Lack of cross-resistance in vivo in tumors with acquired resistance to the topoisomerase 1 inhibitor 9-dimethylaminomethyl-10-hydroxycamptothecin
    • Houghton PJ, Cheshire PJ, Hallman JC, Bissery MC, Mathieu-Boue A, Houghton JA (1993) Therapeutic efficacy of the topoisomerase 1 inhibitor 7-ethyl-10-(4-[1-piperidino]-1-piperidino)-carbonyloxy-camptothecin against human tumor xenografts: lack of cross-resistance in vivo in tumors with acquired resistance to the topoisomerase 1 inhibitor 9-dimethylaminomethyl-10-hydroxycamptothecin. Cancer Res 53:2823-2829
    • (1993) Cancer Res , vol.53 , pp. 2823-2829
    • Houghton, P.J.1    Cheshire, P.J.2    Hallman, J.C.3    Bissery, M.C.4    Mathieu-Boue, A.5    Houghton, J.A.6
  • 217
    • 0025996996 scopus 로고
    • Intracellular roles of SN-38, a metabolite of the camplothecin derivative CPT-11, in the antitumor effect of CPT-11
    • Kawato Y, Aonuma M, Hirota Y, Kuga H, Sato K (1991) Intracellular roles of SN-38, a metabolite of the camplothecin derivative CPT-11, in the antitumor effect of CPT-11. Cancer Res 51:4187-4191
    • (1991) Cancer Res , vol.51 , pp. 4187-4191
    • Kawato, Y.1    Aonuma, M.2    Hirota, Y.3    Kuga, H.4    Sato, K.5
  • 218
    • 0025272187 scopus 로고
    • Metabolism and pharmacokinetics of the camptothecin analogue CPT- 11 in the mouse
    • Kaneda N, Nagata H, Furuta T, Yokokura T (1990) Metabolism and pharmacokinetics of the camptothecin analogue CPT- 11 in the mouse. Cancer Res 50:1715-1720
    • (1990) Cancer Res , vol.50 , pp. 1715-1720
    • Kaneda, N.1    Nagata, H.2    Furuta, T.3    Yokokura, T.4
  • 220
    • 0028844445 scopus 로고
    • Reduced albumin binding promotes the stability and activity of topotecan in human blood
    • Mi Z, Malak H, Burke TG (1995) Reduced albumin binding promotes the stability and activity of topotecan in human blood. Biochemistry 34:13722-13728
    • (1995) Biochemistry , vol.34 , pp. 13722-13728
    • Mi, Z.1    Malak, H.2    Burke, T.G.3
  • 221
    • 0029041130 scopus 로고
    • Analysis of topoisomerase I/DNA complexes in patients administered lopotecan
    • Subramanian D, Kraut E, Staubus A, Young DC, Muller MT (1995) Analysis of topoisomerase I/DNA complexes in patients administered lopotecan. Cancer Res 55:2097-2103
    • (1995) Cancer Res , vol.55 , pp. 2097-2103
    • Subramanian, D.1    Kraut, E.2    Staubus, A.3    Young, D.C.4    Muller, M.T.5
  • 222
    • 0027511840 scopus 로고
    • Plasma and cerebrospinal fluid pharmacokinetic study of topotecan in non human primates
    • Blaney SM, Cole DE, Balis FM, Godwin K, Poplack DG (1993) Plasma and cerebrospinal fluid pharmacokinetic study of topotecan in non human primates. Cancer Res 53:725-727
    • (1993) Cancer Res , vol.53 , pp. 725-727
    • Blaney, S.M.1    Cole, D.E.2    Balis, F.M.3    Godwin, K.4    Poplack, D.G.5
  • 223
    • 0026328062 scopus 로고
    • Synergistic cell killing by ionizing radiation and topoisomerase I inhibitor topotecan (SK&F 104864)
    • Muttern MR, Hofmann GA, McCabe FE, Johnson RK (1991) Synergistic cell killing by ionizing radiation and topoisomerase I inhibitor topotecan (SK&F 104864). Cancer Res 51:5813-5826
    • (1991) Cancer Res , vol.51 , pp. 5813-5826
    • Muttern, M.R.1    Hofmann, G.A.2    McCabe, F.E.3    Johnson, R.K.4
  • 225
    • 0027520356 scopus 로고
    • Poisons of DNA topoisomerases I and II
    • Paris
    • Charcosset JY, Soues S, Eaval F (1993) [Poisons of DNA topoisomerases I and II]. Bull Cancer (Paris) 80:923-954
    • (1993) Bull Cancer , vol.80 , pp. 923-954
    • Charcosset, J.Y.1    Soues, S.2    Eaval, F.3
  • 226
    • 0028564789 scopus 로고
    • Pleiotropic resistance associated with topoisomerases
    • Paris
    • Riou JF, Pommier Y (1994) [Pleiotropic resistance associated with topoisomerases]. Bull Cancer (Paris) 81:62s-68s
    • (1994) Bull Cancer , vol.81
    • Riou, J.F.1    Pommier, Y.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.