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Volumn 5, Issue 9, 2010, Pages

Characterisation of the SUMO-like domains of schizosaccharomyces pombe Rad60

Author keywords

[No Author keywords available]

Indexed keywords

RAD60 PROTEIN; SCHIZOSACCHAROMYCES POMBE PROTEIN; SUMO PROTEIN; UBIQUITIN; UNCLASSIFIED DRUG; HUS5 PROTEIN, S POMBE; NONHISTONE PROTEIN; RAD60 PROTEIN, S POMBE; UBIQUITIN CONJUGATING ENZYME;

EID: 77958608328     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0013009     Document Type: Article
Times cited : (4)

References (55)
  • 2
    • 33846636841 scopus 로고    scopus 로고
    • The role of SUMO in chromosome segregation
    • Watts FZ (2007) The role of SUMO in chromosome segregation. Chromosoma 116: 15-20.
    • (2007) Chromosoma , vol.116 , pp. 15-20
    • Watts, F.Z.1
  • 3
    • 0037068455 scopus 로고    scopus 로고
    • RAD6- dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO
    • Hoege C, Pfander B, Moldovan GL, Pyrowolakis G, Jentsch S (2002) RAD6- dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO. Nature 419: 135-141.
    • (2002) Nature , vol.419 , pp. 135-141
    • Hoege, C.1    Pfander, B.2    Moldovan, G.L.3    Pyrowolakis, G.4    Jentsch, S.5
  • 4
    • 0141831006 scopus 로고    scopus 로고
    • Control of spontaneous and damage-induced mutagenesis by SUMO and ubiquitin conjugation
    • Stelter P, Ulrich HD (2003) Control of spontaneous and damage-induced mutagenesis by SUMO and ubiquitin conjugation. Nature 425: 188-191.
    • (2003) Nature , vol.425 , pp. 188-191
    • Stelter, P.1    Ulrich, H.D.2
  • 5
    • 33750499289 scopus 로고    scopus 로고
    • Control of Rad52 recombination activity by double-strand break-induced SUMO modification
    • Sacher M, Pfander B, Hoege C, Jentsch S (2006) Control of Rad52 recombination activity by double-strand break-induced SUMO modification. Nat Cell Biol 8: 1284-1290.
    • (2006) Nat Cell Biol , vol.8 , pp. 1284-1290
    • Sacher, M.1    Pfander, B.2    Hoege, C.3    Jentsch, S.4
  • 6
    • 24344445216 scopus 로고    scopus 로고
    • Something about SUMO inhibits transcription
    • Gill G (2005) Something about SUMO inhibits transcription. Curr Opin Genet Dev 15: 536-541.
    • (2005) Curr Opin Genet Dev , vol.15 , pp. 536-541
    • Gill, G.1
  • 7
    • 22944474665 scopus 로고    scopus 로고
    • SUMOmodified PCNA recruits Srs2 to prevent recombination during S phase
    • Pfander B, Moldovan GL, Sacher M, Hoege C, Jentsch S (2005) SUMOmodified PCNA recruits Srs2 to prevent recombination during S phase. Nature 436: 428-433.
    • (2005) Nature , vol.436 , pp. 428-433
    • Pfander, B.1    Moldovan, G.L.2    Sacher, M.3    Hoege, C.4    Jentsch, S.5
  • 8
    • 21244449061 scopus 로고    scopus 로고
    • Crosstalk between SUMO and ubiquitin on PCNA is mediated by recruitment of the helicase Srs2p
    • Papouli E, Chen S, Davies AA, Huttner D, Krejci L, et al. (2005) Crosstalk between SUMO and ubiquitin on PCNA is mediated by recruitment of the helicase Srs2p. Mol Cell 19: 123-133.
    • (2005) Mol Cell , vol.19 , pp. 123-133
    • Papouli, E.1    Chen, S.2    Davies, A.A.3    Huttner, D.4    Krejci, L.5
  • 9
    • 0037086643 scopus 로고    scopus 로고
    • Modification of the human thymine-DNA glycosylase by ubiquitin-like proteins facilitates enzymatic turnover
    • Hardeland U, Steinacher R, Jiricny J, Schar P (2002) Modification of the human thymine-DNA glycosylase by ubiquitin-like proteins facilitates enzymatic turnover. Embo J 21: 1456-1464.
    • (2002) Embo J , vol.21 , pp. 1456-1464
    • Hardeland, U.1    Steinacher, R.2    Jiricny, J.3    Schar, P.4
  • 10
    • 15944406765 scopus 로고    scopus 로고
    • SUMO: A history of modification
    • Hay RT (2005) SUMO: a history of modification. Mol Cell 18: 1-12.
    • (2005) Mol Cell , vol.18 , pp. 1-12
    • Hay, R.T.1
  • 12
    • 36348964395 scopus 로고    scopus 로고
    • The yeast Hex3.Slx8 heterodimer is a ubiquitin ligase stimulated by substrate sumoylation
    • Xie Y, Kerscher O, Kroetz MB, McConchie HF, Sung P, et al. (2007) The yeast Hex3.Slx8 heterodimer is a ubiquitin ligase stimulated by substrate sumoylation. J Biol Chem 282: 34176-34184.
    • (2007) J Biol Chem , vol.282 , pp. 34176-34184
    • Xie, Y.1    Kerscher, O.2    Kroetz, M.B.3    McConchie, H.F.4    Sung, P.5
  • 13
    • 43049093756 scopus 로고    scopus 로고
    • RNF4 is a poly-SUMO-specific E3 ubiquitin ligase required for arsenic-induced PML degradation
    • Tatham MH, Geoffroy MC, Shen L, Plechanovova A, Hattersley N, et al. (2008) RNF4 is a poly-SUMO-specific E3 ubiquitin ligase required for arsenic-induced PML degradation. Nat Cell Biol 10: 538-546.
    • (2008) Nat Cell Biol , vol.10 , pp. 538-546
    • Tatham, M.H.1    Geoffroy, M.C.2    Shen, L.3    Plechanovova, A.4    Hattersley, N.5
  • 14
    • 0030826334 scopus 로고    scopus 로고
    • Ubc9p is the conjugating enzyme for the ubiquitinlike protein Smt3p
    • Johnson ES, Blobel G (1997) Ubc9p is the conjugating enzyme for the ubiquitinlike protein Smt3p. J Biol Chem 272: 26799-26802.
    • (1997) J Biol Chem , vol.272 , pp. 26799-26802
    • Johnson, E.S.1    Blobel, G.2
  • 15
    • 0028898059 scopus 로고
    • The Schizosaccharomyces pombe hus5 gene encodes a ubiquitin conjugating enzyme required for normal mitosis
    • al-Khodairy F, Enoch T, Hagan IM, Carr AM (1995) The Schizosaccharomyces pombe hus5 gene encodes a ubiquitin conjugating enzyme required for normal mitosis. J Cell Sci 108: 475-486.
    • (1995) J Cell Sci , vol.108 , pp. 475-486
    • Al-Khodairy, F.1    Enoch, T.2    Hagan, I.M.3    Carr, A.M.4
  • 16
    • 11144324990 scopus 로고    scopus 로고
    • Nse2, a component of the Smc5-6 complex, is a SUMO ligase required for the response to DNA damage
    • Andrews EA, Palecek J, Sergeant J, Taylor E, Lehmann AR, et al. (2005) Nse2, a component of the Smc5-6 complex, is a SUMO ligase required for the response to DNA damage. Mol Cell Biol 25: 185-196.
    • (2005) Mol Cell Biol , vol.25 , pp. 185-196
    • Andrews, E.A.1    Palecek, J.2    Sergeant, J.3    Taylor, E.4    Lehmann, A.R.5
  • 17
    • 6344254386 scopus 로고    scopus 로고
    • Role of the fission yeast SUMO E3 ligase Pli1p in centromere and telomere maintenance
    • Xhemalce B, Seeler JS, Thon G, Dejean A, Arcangioli B (2004) Role of the fission yeast SUMO E3 ligase Pli1p in centromere and telomere maintenance. Embo J 23: 3844-3853.
    • (2004) Embo J , vol.23 , pp. 3844-3853
    • Xhemalce, B.1    Seeler, J.S.2    Thon, G.3    Dejean, A.4    Arcangioli, B.5
  • 18
    • 0033615965 scopus 로고    scopus 로고
    • Cell cycle-regulated attachment of the ubiquitinrelated protein SUMO to the yeast septins
    • Johnson ES, Blobel G (1999) Cell cycle-regulated attachment of the ubiquitinrelated protein SUMO to the yeast septins. J Cell Biol 147: 981-994.
    • (1999) J Cell Biol , vol.147 , pp. 981-994
    • Johnson, E.S.1    Blobel, G.2
  • 19
    • 0035028618 scopus 로고    scopus 로고
    • Common properties of nuclear body protein sp100 and tif1alpha chromatin factor: Role of sumo modification
    • Seeler JS, Marchio A, Losson R, Desterro JM, Hay RT, et al. (2001) Common properties of nuclear body protein sp100 and tif1alpha chromatin factor: role of sumo modification. Mol Cell Biol 21: 3314-3324.
    • (2001) Mol Cell Biol , vol.21 , pp. 3314-3324
    • Seeler, J.S.1    Marchio, A.2    Losson, R.3    Desterro, J.M.4    Hay, R.T.5
  • 20
    • 0034680441 scopus 로고    scopus 로고
    • Covalent modification of p73alpha by SUMO-1. Two-hybrid screening with p73 identifies novel SUMO-1-interacting proteins and a SUMO-1 interaction motif
    • Minty A, Dumont X, Kaghad M, Caput D (2000) Covalent modification of p73alpha by SUMO-1. Two-hybrid screening with p73 identifies novel SUMO-1-interacting proteins and a SUMO-1 interaction motif. J Biol Chem 275: 36316-36323.
    • (2000) J Biol Chem , vol.275 , pp. 36316-36323
    • Minty, A.1    Dumont, X.2    Kaghad, M.3    Caput, D.4
  • 22
    • 25444484394 scopus 로고    scopus 로고
    • Proteins with two SUMO-like domains in chromatin-associated complexes: The RENi (Rad60- Esc2-NIP45) family
    • Novatchkova M, Bachmair A, Eisenhaber B, Eisenhaber F (2005) Proteins with two SUMO-like domains in chromatin-associated complexes: the RENi (Rad60- Esc2-NIP45) family. BMC Bioinformatics 6: 22.
    • (2005) BMC Bioinformatics , vol.6 , pp. 22
    • Novatchkova, M.1    Bachmair, A.2    Eisenhaber, B.3    Eisenhaber, F.4
  • 23
    • 0036812206 scopus 로고    scopus 로고
    • Restoration of silencing in Saccharomyces cerevisiae by tethering of a novel Sir2-interacting protein, Esc8
    • Cuperus G, Shore D (2002) Restoration of silencing in Saccharomyces cerevisiae by tethering of a novel Sir2-interacting protein, Esc8. Genetics 162: 633-645.
    • (2002) Genetics , vol.162 , pp. 633-645
    • Cuperus, G.1    Shore, D.2
  • 24
    • 56049110002 scopus 로고    scopus 로고
    • A SUMO-like domain protein, Esc2, is required for genome integrity and sister chromatid cohesion in Saccharomyces cerevisiae
    • Ohya T, Arai H, Kubota Y, Shinagawa H, Hishida T (2008) A SUMO-like domain protein, Esc2, is required for genome integrity and sister chromatid cohesion in Saccharomyces cerevisiae. Genetics 180: 41-50.
    • (2008) Genetics , vol.180 , pp. 41-50
    • Ohya, T.1    Arai, H.2    Kubota, Y.3    Shinagawa, H.4    Hishida, T.5
  • 25
    • 65249118311 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae Esc2 and Smc5-6 proteins promote sister chromatid junction-mediated intra-S repair
    • Sollier J, Driscoll R, Castellucci F, Foiani M, Jackson SP, et al. (2009) The Saccharomyces cerevisiae Esc2 and Smc5-6 proteins promote sister chromatid junction-mediated intra-S repair. Mol Biol Cell 20: 1671-1682.
    • (2009) Mol Biol Cell , vol.20 , pp. 1671-1682
    • Sollier, J.1    Driscoll, R.2    Castellucci, F.3    Foiani, M.4    Jackson, S.P.5
  • 26
    • 65249090885 scopus 로고    scopus 로고
    • Esc2 and Sgs1 act in functionally distinct branches of the homologous recombination repair pathway in Saccharomyces cerevisiae
    • Mankouri HW, Ngo HP, Hickson ID (2009) Esc2 and Sgs1 act in functionally distinct branches of the homologous recombination repair pathway in Saccharomyces cerevisiae. Mol Biol Cell 20: 1683-1694.
    • (2009) Mol Biol Cell , vol.20 , pp. 1683-1694
    • Mankouri, H.W.1    Ngo, H.P.2    Hickson, I.D.3
  • 27
    • 0030474682 scopus 로고    scopus 로고
    • NF-ATDriven interleukin-4 transcription potentiated by NIP45
    • Hodge MR, Chun HJ, Rengarajan J, Alt A, Lieberson R, et al. (1996) NF-ATDriven interleukin-4 transcription potentiated by NIP45. Science 274: 1903-1905.
    • (1996) Science , vol.274 , pp. 1903-1905
    • Hodge, M.R.1    Chun, H.J.2    Rengarajan, J.3    Alt, A.4    Lieberson, R.5
  • 28
    • 0036238641 scopus 로고    scopus 로고
    • The Schizosaccharomyces pombe rad60 gene is essential for repairing double-strand DNA breaks spontaneously occurring during replication and induced by DNA-damaging agents
    • Morishita T, Tsutsui Y, Iwasaki H, Shinagawa H (2002) The Schizosaccharomyces pombe rad60 gene is essential for repairing double-strand DNA breaks spontaneously occurring during replication and induced by DNA-damaging agents. Mol Cell Biol 22: 3537-3548.
    • (2002) Mol Cell Biol , vol.22 , pp. 3537-3548
    • Morishita, T.1    Tsutsui, Y.2    Iwasaki, H.3    Shinagawa, H.4
  • 29
    • 0042131895 scopus 로고    scopus 로고
    • Replication checkpoint kinase Cds1 regulates recombinational repair protein Rad60
    • Boddy MN, Shanahan P, McDonald WH, Lopez-Girona A, Noguchi E, et al. (2003) Replication checkpoint kinase Cds1 regulates recombinational repair protein Rad60. Mol Cell Biol 23: 5939-5946.
    • (2003) Mol Cell Biol , vol.23 , pp. 5939-5946
    • Boddy, M.N.1    Shanahan, P.2    McDonald, W.H.3    Lopez-Girona, A.4    Noguchi, E.5
  • 30
    • 33645210879 scopus 로고    scopus 로고
    • Rhp51- dependent recombination intermediates that do not generate checkpoint signal are accumulated in Schizosaccharomyces pombe rad60 and smc5/6 mutants after release from replication arrest
    • Miyabe I, Morishita T, Hishida T, Yonei S, Shinagawa H (2006) Rhp51- dependent recombination intermediates that do not generate checkpoint signal are accumulated in Schizosaccharomyces pombe rad60 and smc5/6 mutants after release from replication arrest. Mol Cell Biol 26: 343-353.
    • (2006) Mol Cell Biol , vol.26 , pp. 343-353
    • Miyabe, I.1    Morishita, T.2    Hishida, T.3    Yonei, S.4    Shinagawa, H.5
  • 31
    • 33748809503 scopus 로고    scopus 로고
    • SUMO-binding motifs mediate the Rad60-dependent response to replicative stress and selfassociation
    • Raffa GD, Wohlschlegel J, Yates JR, 3rd, Boddy MN (2006) SUMO-binding motifs mediate the Rad60-dependent response to replicative stress and selfassociation. J Biol Chem 281: 27973-27981.
    • (2006) J Biol Chem , vol.281 , pp. 27973-27981
    • Raffa, G.D.1    Wohlschlegel, J.2    Yates III, J.R.3    Boddy, M.N.4
  • 32
    • 38549138271 scopus 로고    scopus 로고
    • Smc5/6: A link between DNA repair and unidirectional replication?
    • Murray JM, Carr AM (2008) Smc5/6: a link between DNA repair and unidirectional replication? Nat Rev Mol Cell Biol 9: 177-182.
    • (2008) Nat Rev Mol Cell Biol , vol.9 , pp. 177-182
    • Murray, J.M.1    Carr, A.M.2
  • 33
    • 11144326866 scopus 로고    scopus 로고
    • Composition and architecture of the Schizosaccharomyces pombe Rad18 (Smc5-6) complex
    • Sergeant J, Taylor E, Palecek J, Fousteri M, Andrews EA, et al. (2005) Composition and architecture of the Schizosaccharomyces pombe Rad18 (Smc5-6) complex. Mol Cell Biol 25: 172-184.
    • (2005) Mol Cell Biol , vol.25 , pp. 172-184
    • Sergeant, J.1    Taylor, E.2    Palecek, J.3    Fousteri, M.4    Andrews, E.A.5
  • 35
    • 57349094259 scopus 로고    scopus 로고
    • Nse1 RING-like domain supports functions of the Smc5-Smc6 holocomplex in genome stability
    • Pebernard S, Perry JJ, Tainer JA, Boddy MN (2008) Nse1 RING-like domain supports functions of the Smc5-Smc6 holocomplex in genome stability. Mol Biol Cell 19: 4099-4109.
    • (2008) Mol Biol Cell , vol.19 , pp. 4099-4109
    • Pebernard, S.1    Perry, J.J.2    Tainer, J.A.3    Boddy, M.N.4
  • 36
    • 23344442009 scopus 로고    scopus 로고
    • Human MMS21/NSE2 is a SUMO ligase required for DNA repair
    • Potts PR, Yu H (2005) Human MMS21/NSE2 is a SUMO ligase required for DNA repair. Mol Cell Biol 25: 7021-7032.
    • (2005) Mol Cell Biol , vol.25 , pp. 7021-7032
    • Potts, P.R.1    Yu, H.2
  • 37
    • 16344370926 scopus 로고    scopus 로고
    • A SUMO ligase is part of a nuclear multiprotein complex that affects DNA repair and chromosomal organization
    • Zhao X, Blobel G (2005) A SUMO ligase is part of a nuclear multiprotein complex that affects DNA repair and chromosomal organization. Proc Natl Acad Sci U S A 102: 4777-4782.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 4777-4782
    • Zhao, X.1    Blobel, G.2
  • 38
    • 33845985979 scopus 로고    scopus 로고
    • The Smc5-Smc6 DNA repair complex. bridging of the Smc5-Smc6 heads by the KLEISIN, Nse4, and non-Kleisin subunits
    • Palecek J, Vidot S, Feng M, Doherty AJ, Lehmann AR (2006) The Smc5-Smc6 DNA repair complex. bridging of the Smc5-Smc6 heads by the KLEISIN, Nse4, and non-Kleisin subunits. J Biol Chem 281: 36952-36959.
    • (2006) J Biol Chem , vol.281 , pp. 36952-36959
    • Palecek, J.1    Vidot, S.2    Feng, M.3    Doherty, A.J.4    Lehmann, A.R.5
  • 39
    • 67649809770 scopus 로고    scopus 로고
    • Architecture of the Smc5/6 Complex of Saccharomyces cerevisiae Reveals a Unique Interaction between the Nse5-6 Subcomplex and the Hinge Regions of Smc5 and Smc6
    • Duan X, Yang Y, Chen YH, Arenz J, Rangi GK, et al. (2009) Architecture of the Smc5/6 Complex of Saccharomyces cerevisiae Reveals a Unique Interaction between the Nse5-6 Subcomplex and the Hinge Regions of Smc5 and Smc6. J Biol Chem 284: 8507-8515.
    • (2009) J Biol Chem , vol.284 , pp. 8507-8515
    • Duan, X.1    Yang, Y.2    Chen, Y.H.3    Arenz, J.4    Rangi, G.K.5
  • 40
    • 0031818471 scopus 로고    scopus 로고
    • Heterologous modules for efficient and versatile PCR-based gene targeting in Schizosaccharomyces pombe
    • Bahler J, Wu JQ, Longtine MS, Shah NG, McKenzie A, 3rd, et al. (1998) Heterologous modules for efficient and versatile PCR-based gene targeting in Schizosaccharomyces pombe. Yeast 14: 943-951.
    • (1998) Yeast , vol.14 , pp. 943-951
    • Bahler, J.1    Wu, J.Q.2    Longtine, M.S.3    Shah, N.G.4    McKenzie III, A.5
  • 41
    • 37049028325 scopus 로고    scopus 로고
    • Gene tagging and gene replacement using recombinase-mediated cassette exchange in Schizosaccharomyces pombe
    • Watson AT, Garcia V, Bone N, Carr AM, Armstrong J (2008) Gene tagging and gene replacement using recombinase-mediated cassette exchange in Schizosaccharomyces pombe. Gene 407: 63-74.
    • (2008) Gene , vol.407 , pp. 63-74
    • Watson, A.T.1    Garcia, V.2    Bone, N.3    Carr, A.M.4    Armstrong, J.5
  • 42
    • 0027441494 scopus 로고
    • TATA box mutations in the Schizosaccharomyces pombe nmt1 promoter affect transcription efficiency but not the transcription start point or thiamine repressibility
    • Basi G, Schmid E, Maundrell K (1993) TATA box mutations in the Schizosaccharomyces pombe nmt1 promoter affect transcription efficiency but not the transcription start point or thiamine repressibility. Gene 123: 131-136.
    • (1993) Gene , vol.123 , pp. 131-136
    • Basi, G.1    Schmid, E.2    Maundrell, K.3
  • 43
    • 77951219176 scopus 로고    scopus 로고
    • Structural basis for regulation of poly-SUMO chain by a SUMO-like domain of Nip45
    • Sekiyama N, Arita K, Ikeda Y, Hashiguchi K, Ariyoshi M, et al. Structural basis for regulation of poly-SUMO chain by a SUMO-like domain of Nip45. Proteins 78: 1491-1502.
    • Proteins , vol.78 , pp. 1491-1502
    • Sekiyama, N.1    Arita, K.2    Ikeda, Y.3    Hashiguchi, K.4    Ariyoshi, M.5
  • 44
    • 0034599577 scopus 로고    scopus 로고
    • A novel SMC protein complex in Schizosaccharomyces pombe contains the Rad18 DNA repair protein
    • Fousteri MI, Lehmann AR (2000) A novel SMC protein complex in Schizosaccharomyces pombe contains the Rad18 DNA repair protein. Embo J 19: 1691-1702.
    • (2000) Embo J , vol.19 , pp. 1691-1702
    • Fousteri, M.I.1    Lehmann, A.R.2
  • 45
    • 6344291070 scopus 로고    scopus 로고
    • Rad62 protein functionally and physically associates with the smc5/smc6 protein complex and is required for chromosome integrity and recombination repair in fission yeast
    • Morikawa H, Morishita T, Kawane S, Iwasaki H, Carr AM, et al. (2004) Rad62 protein functionally and physically associates with the smc5/smc6 protein complex and is required for chromosome integrity and recombination repair in fission yeast. Mol Cell Biol 24: 9401-9413.
    • (2004) Mol Cell Biol , vol.24 , pp. 9401-9413
    • Morikawa, H.1    Morishita, T.2    Kawane, S.3    Iwasaki, H.4    Carr, A.M.5
  • 48
    • 0026553768 scopus 로고
    • The folding of an enzyme. II. Substructure of barnase and the contribution of different interactions to protein stability
    • Serrano L, Kellis JT, Jr., Cann P, Matouschek A, Fersht AR (1992) The folding of an enzyme. II. Substructure of barnase and the contribution of different interactions to protein stability. J Mol Biol 224: 783-804.
    • (1992) J Mol Biol , vol.224 , pp. 783-804
    • Serrano, L.1    Kellis Jr., J.T.2    Cann, P.3    Matouschek, A.4    Fersht, A.R.5
  • 49
    • 0032574698 scopus 로고    scopus 로고
    • Context-dependent nature of destabilizing mutations on the stability of FKBP12
    • Main ER, Fulton KF, Jackson SE (1998) Context-dependent nature of destabilizing mutations on the stability of FKBP12. Biochemistry 37: 6145-6153.
    • (1998) Biochemistry , vol.37 , pp. 6145-6153
    • Main, E.R.1    Fulton, K.F.2    Jackson, S.E.3
  • 50
    • 0027384577 scopus 로고
    • Effect of cavity-creating mutations in the hydrophobic core of chymotrypsin inhibitor 2
    • Jackson SE, Moracci M, el Masry N, Johnson CM, Fersht AR (1993) Effect of cavity-creating mutations in the hydrophobic core of chymotrypsin inhibitor 2. Biochemistry 32: 11259-11269.
    • (1993) Biochemistry , vol.32 , pp. 11259-11269
    • Jackson, S.E.1    Moracci, M.2    el Masry, N.3    Johnson, C.M.4    Fersht, A.R.5
  • 52
    • 0025784689 scopus 로고
    • Cloning and characterisation of the rad9 DNA repair gene from Schizosaccharomyces pombe
    • Murray JM, Carr AM, Lehmann AR, Watts FZ (1991) Cloning and characterisation of the rad9 DNA repair gene from Schizosaccharomyces pombe. Nucleic Acids Res 19: 3525-3531.
    • (1991) Nucleic Acids Res , vol.19 , pp. 3525-3531
    • Murray, J.M.1    Carr, A.M.2    Lehmann, A.R.3    Watts, F.Z.4
  • 54
    • 0028850628 scopus 로고
    • The rad18 gene of Schizosaccharomyces pombe defines a new subgroup of the SMC superfamily involved in DNA repair
    • Lehmann AR, Walicka M, Griffiths DJ, Murray JM, Watts FZ, et al. (1995) The rad18 gene of Schizosaccharomyces pombe defines a new subgroup of the SMC superfamily involved in DNA repair. Mol Cell Biol 15: 7067-7080.
    • (1995) Mol Cell Biol , vol.15 , pp. 7067-7080
    • Lehmann, A.R.1    Walicka, M.2    Griffiths, D.J.3    Murray, J.M.4    Watts, F.Z.5
  • 55
    • 0030699088 scopus 로고    scopus 로고
    • Role of Schizosaccharomyces pombe RecQ homolog, recombination, and checkpoint genes in UV damage tolerance
    • Murray JM, Lindsay HD, Munday CA, Carr AM (1997) Role of Schizosaccharomyces pombe RecQ homolog, recombination, and checkpoint genes in UV damage tolerance. Mol Cell Biol 17: 6868-6875.
    • (1997) Mol Cell Biol , vol.17 , pp. 6868-6875
    • Murray, J.M.1    Lindsay, H.D.2    Munday, C.A.3    Carr, A.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.