메뉴 건너뛰기




Volumn 34, Issue 6, 2012, Pages 1317-1340

The role of DNA exonucleases in protecting genome stability and their impact on ageing

Author keywords

Ageing; Aging; DNA repair; DNA replication; EXDL2; EXOG; Exonuclease; FAN1; FEN1; Mitochondria; Proofreading; WRN

Indexed keywords

DNA; DNA (APURINIC OR APYRIMIDINIC SITE) LYASE; DNA DIRECTED DNA POLYMERASE GAMMA; DNA EXONUCLEASE; DNA POLYMERASE; DOUBLE STRANDED DNA; ENDONUCLEASE G; EXCISION REPAIR CROSS COMPLEMENTING PROTEIN 5; EXONUCLEASE; FANCONI ANEMIA PROTEIN; FLAP ENDONUCLEASE; MRE11 PROTEIN; PROTEIN P53; PROTEIN RAD9; THREE PRIME REPAIR EXONUCLEASE 1; THREE PRIME REPAIR EXONUCLEASE 2; UNCLASSIFIED DRUG; WERNER SYNDROME PROTEIN; APEX1 PROTEIN, HUMAN; APEX2 PROTEIN, HUMAN; DNA DIRECTED DNA POLYMERASE; DNA2 PROTEIN, HUMAN; EXODEOXYRIBONUCLEASE; FEN1 PROTEIN, HUMAN; HELICASE; PHOSPHOPROTEIN; POLG PROTEIN, HUMAN; RECQ HELICASE; TREX2 PROTEIN, HUMAN; WRN PROTEIN, HUMAN;

EID: 84876459277     PISSN: 01619152     EISSN: 15744647     Source Type: Journal    
DOI: 10.1007/s11357-011-9306-5     Document Type: Article
Times cited : (31)

References (215)
  • 1
    • 77953590923 scopus 로고    scopus 로고
    • Delineation of WRN helicase function with EXO1 in the replicational stress response
    • 1:CAS:528:DC%2BC3cXnvVOqsr8%3D 10.1016/j.dnarep.2010.03.014
    • Aggarwal M, Sommers JA, Morris C, Brosh RM Jr (2010) Delineation of WRN helicase function with EXO1 in the replicational stress response. DNA Repair (Amst) 9:765-776
    • (2010) DNA Repair (Amst) , vol.9 , pp. 765-776
    • Aggarwal, M.1    Sommers, J.A.2    Morris, C.3    Brosh, Jr.R.M.4
  • 2
    • 0029861118 scopus 로고    scopus 로고
    • Fanconi's anemia and malignancies
    • 8892734 1:STN:280:DyaK2s%2FkslyqsQ%3D%3D 10.1002/(SICI)1096-8652(199610) 53:2<99: AID-AJH7>3.0.CO;2-Z
    • Alter BP (1996) Fanconi's anemia and malignancies. Am J Hematol 53:99-110
    • (1996) Am J Hematol , vol.53 , pp. 99-110
    • Alter, B.P.1
  • 5
    • 0028837378 scopus 로고
    • Fanconi anemia
    • 7712649 1:STN:280:DyaK2M3ivVagsQ%3D%3D
    • Auerbach AD (1995) Fanconi anemia. Dermatol Clin 13:41-49
    • (1995) Dermatol Clin , vol.13 , pp. 41-49
    • Auerbach, A.D.1
  • 6
    • 34447551681 scopus 로고    scopus 로고
    • Roles of ATM and NBS1 in chromatin structure modulation and DNA double-strand break repair
    • 17486112 1:CAS:528:DC%2BD2sXmtVSmtbo%3D 10.1038/ncb1599
    • Berkovich E, Monnat RJ Jr, Kastan MB (2007) Roles of ATM and NBS1 in chromatin structure modulation and DNA double-strand break repair. Nat Cell Biol 9:683-690
    • (2007) Nat Cell Biol , vol.9 , pp. 683-690
    • Berkovich, E.1    Monnat, Jr.R.J.2    Kastan, M.B.3
  • 7
    • 0034677809 scopus 로고    scopus 로고
    • Human DNA damage checkpoint protein hRAD9 is a 3′ to 5′ exonuclease
    • 10713044 1:CAS:528:DC%2BD3cXitVymurw%3D 10.1074/jbc.275.11.7451
    • Bessho T, Sancar A (2000) Human DNA damage checkpoint protein hRAD9 is a 3′ to 5′ exonuclease. J Biol Chem 275:7451-7454
    • (2000) J Biol Chem , vol.275 , pp. 7451-7454
    • Bessho, T.1    Sancar, A.2
  • 8
    • 67349249697 scopus 로고    scopus 로고
    • DmWRNexo is a 3′-5′ exonuclease: Phenotypic and biochemical characterization of mutants of the Drosophila orthologue of human WRN exonuclease
    • 18956248 1:CAS:528:DC%2BD1MXlsVSjtrc%3D 10.1007/s10522-008-9181-3
    • Boubriak I, Mason PA, Clancy DJ, Dockray J, Saunders RD, Cox LS (2009) DmWRNexo is a 3′-5′ exonuclease: phenotypic and biochemical characterization of mutants of the Drosophila orthologue of human WRN exonuclease. Biogerontology 10:267-277
    • (2009) Biogerontology , vol.10 , pp. 267-277
    • Boubriak, I.1    Mason, P.A.2    Clancy, D.J.3    Dockray, J.4    Saunders, R.D.5    Cox, L.S.6
  • 11
    • 0037044311 scopus 로고    scopus 로고
    • Biochemical characterization of the WRN-FEN-1 functional interaction
    • 12356323 1:CAS:528:DC%2BD38XmvFWlsbw%3D 10.1021/bi026031j
    • Brosh RM Jr, Driscoll HC, Dianov GL, Sommers JA (2002a) Biochemical characterization of the WRN-FEN-1 functional interaction. Biochemistry 41:12204-12216
    • (2002) Biochemistry , vol.41 , pp. 12204-12216
    • Brosh, Jr.R.M.1    Driscoll, H.C.2    Dianov, G.L.3    Sommers, J.A.4
  • 12
    • 0037189485 scopus 로고    scopus 로고
    • Biochemical characterization of the DNA substrate specificity of Werner syndrome helicase
    • 11956187 1:CAS:528:DC%2BD38XltF2ns7k%3D 10.1074/jbc.M111446200
    • Brosh RM Jr, Waheed J, Sommers JA (2002b) Biochemical characterization of the DNA substrate specificity of Werner syndrome helicase. J Biol Chem 277:23236-23245
    • (2002) J Biol Chem , vol.277 , pp. 23236-23245
    • Brosh, Jr.R.M.1    Waheed, J.2    Sommers, J.A.3
  • 13
    • 0036772981 scopus 로고    scopus 로고
    • A nuclear 3′-5′ exonuclease proofreads for the exonuclease-deficient DNA polymerase alpha
    • 1:CAS:528:DC%2BD38XotFensrc%3D 10.1016/S1568-7864(02)00115-5
    • Brown KR, Weatherdon KL, Galligan CL, Skalski V (2002) A nuclear 3′-5′ exonuclease proofreads for the exonuclease-deficient DNA polymerase alpha. DNA Repair (Amst) 1:795-810
    • (2002) DNA Repair (Amst) , vol.1 , pp. 795-810
    • Brown, K.R.1    Weatherdon, K.L.2    Galligan, C.L.3    Skalski, V.4
  • 14
    • 59249107930 scopus 로고    scopus 로고
    • Interplay of Mre11 nuclease with Dna2 plus Sgs1 in Rad51-dependent recombinational repair
    • 19165339 10.1371/journal.pone.0004267 1:CAS:528:DC%2BD1MXhsF2ns74%3D
    • Budd ME, Campbell JL (2009) Interplay of Mre11 nuclease with Dna2 plus Sgs1 in Rad51-dependent recombinational repair. PLoS One 4:e4267
    • (2009) PLoS One , vol.4 , pp. 4267
    • Budd, M.E.1    Campbell, J.L.2
  • 15
    • 77953517313 scopus 로고    scopus 로고
    • Coordination of nucleases and helicases during DNA replication and double-strand break repair
    • L.S. Cox (eds) Royal Society of Chemistry Cambridge 10.1039/ 9781847559852-00112
    • Budd ME, Cox LS, Campbell JL (2009) Coordination of nucleases and helicases during DNA replication and double-strand break repair. In: Cox LS (ed) Molecular themes in DNA replication. Royal Society of Chemistry, Cambridge, pp 112-155
    • (2009) Molecular Themes in DNA Replication , pp. 112-155
    • Budd, M.E.1    Cox, L.S.2    Campbell, J.L.3
  • 16
    • 52949109260 scopus 로고    scopus 로고
    • Mre11 nuclease activity has essential roles in DNA repair and genomic stability distinct from ATM activation
    • 18854157 1:CAS:528:DC%2BD1cXht1Gkt7nJ 10.1016/j.cell.2008.08.015
    • Buis J, Wu Y, Deng Y, Leddon J, Westfield G, Eckersdorff M, Sekiguchi JM, Chang S, Ferguson DO (2008) Mre11 nuclease activity has essential roles in DNA repair and genomic stability distinct from ATM activation. Cell 135:85-96
    • (2008) Cell , vol.135 , pp. 85-96
    • Buis, J.1    Wu, Y.2    Deng, Y.3    Leddon, J.4    Westfield, G.5    Eckersdorff, M.6    Sekiguchi, J.M.7    Chang, S.8    Ferguson, D.O.9
  • 17
    • 33744502385 scopus 로고    scopus 로고
    • Human Ape2 protein has a 3′-5′ exonuclease activity that acts preferentially on mismatched base pairs
    • 16687656 1:CAS:528:DC%2BD28XmsVeisb8%3D 10.1093/nar/gkl259
    • Burkovics P, Szukacsov V, Unk I, Haracska L (2006) Human Ape2 protein has a 3′-5′ exonuclease activity that acts preferentially on mismatched base pairs. Nucleic Acids Res 34:2508-2515
    • (2006) Nucleic Acids Res , vol.34 , pp. 2508-2515
    • Burkovics, P.1    Szukacsov, V.2    Unk, I.3    Haracska, L.4
  • 18
    • 0034714240 scopus 로고    scopus 로고
    • Retention of the human Rad9 checkpoint complex in extraction-resistant nuclear complexes after DNA damage
    • 10852904 1:CAS:528:DC%2BD3cXmt1Okt78%3D 10.1074/jbc.M001244200
    • Burtelow MA, Kaufmann SH, Karnitz LM (2000) Retention of the human Rad9 checkpoint complex in extraction-resistant nuclear complexes after DNA damage. J Biol Chem 275:26343-26348
    • (2000) J Biol Chem , vol.275 , pp. 26343-26348
    • Burtelow, M.A.1    Kaufmann, S.H.2    Karnitz, L.M.3
  • 20
    • 0037027880 scopus 로고    scopus 로고
    • DNA structure dependent checkpoints as regulators of DNA repair
    • 1:CAS:528:DC%2BD38Xps12itL0%3D 10.1016/S1568-7864(02)00165-9
    • Carr AM (2002) DNA structure dependent checkpoints as regulators of DNA repair. DNA Repair (Amst) 1:983-994
    • (2002) DNA Repair (Amst) , vol.1 , pp. 983-994
    • Carr, A.M.1
  • 21
    • 0034625339 scopus 로고    scopus 로고
    • Fidelity of eucaryotic DNA polymerase delta holoenzyme from Schizosaccharomyces pombe
    • 10748208 1:CAS:528:DC%2BD3cXktFakt7c%3D 10.1074/jbc.M910278199
    • Chen X, Zuo S, Kelman Z, O'Donnell M, Hurwitz J, Goodman MF (2000) Fidelity of eucaryotic DNA polymerase delta holoenzyme from Schizosaccharomyces pombe. J Biol Chem 275:17677-17682
    • (2000) J Biol Chem , vol.275 , pp. 17677-17682
    • Chen, X.1    Zuo, S.2    Kelman, Z.3    O'Donnell, M.4    Hurwitz, J.5    Goodman, M.F.6
  • 22
    • 0035844130 scopus 로고    scopus 로고
    • ATM-dependent phosphorylation of human Rad9 is required for ionizing radiation-induced checkpoint activation
    • 11278446 1:CAS:528:DC%2BD3MXjvFars7k%3D 10.1074/jbc.M008871200
    • Chen MJ, Lin YT, Lieberman HB, Chen G, Lee EY (2001a) ATM-dependent phosphorylation of human Rad9 is required for ionizing radiation-induced checkpoint activation. J Biol Chem 276:16580-16586
    • (2001) J Biol Chem , vol.276 , pp. 16580-16586
    • Chen, M.J.1    Lin, Y.T.2    Lieberman, H.B.3    Chen, G.4    Lee, E.Y.5
  • 24
    • 34250303902 scopus 로고    scopus 로고
    • Biochemical and cellular characteristics of the 3′→5′ exonuclease TREX2
    • 17426129 1:CAS:528:DC%2BD2sXmt1Wqsb8%3D 10.1093/nar/gkm151
    • Chen MJ, Ma SM, Dumitrache LC, Hasty P (2007) Biochemical and cellular characteristics of the 3′→5′ exonuclease TREX2. Nucleic Acids Res 35:2682-2694
    • (2007) Nucleic Acids Res , vol.35 , pp. 2682-2694
    • Chen, M.J.1    Ma, S.M.2    Dumitrache, L.C.3    Hasty, P.4
  • 25
    • 0037034035 scopus 로고    scopus 로고
    • An exonucleolytic activity of human apurinic/apyrimidinic endonuclease on 3′ mispaired DNA
    • 11832948 1:CAS:528:DC%2BD38XhsVCjtr4%3D 10.1038/415655a
    • Chou KM, Cheng YC (2002) An exonucleolytic activity of human apurinic/apyrimidinic endonuclease on 3′ mispaired DNA. Nature 415:655-659
    • (2002) Nature , vol.415 , pp. 655-659
    • Chou, K.M.1    Cheng, Y.C.2
  • 26
    • 0038043250 scopus 로고    scopus 로고
    • The exonuclease activity of human apurinic/apyrimidinic endonuclease (APE1). Biochemical properties and inhibition by the natural dinucleotide Gp4G
    • 12624104 1:CAS:528:DC%2BD3sXjs1KhsL8%3D 10.1074/jbc.M212143200
    • Chou KM, Cheng YC (2003) The exonuclease activity of human apurinic/apyrimidinic endonuclease (APE1). Biochemical properties and inhibition by the natural dinucleotide Gp4G. J Biol Chem 278:18289-18296
    • (2003) J Biol Chem , vol.278 , pp. 18289-18296
    • Chou, K.M.1    Cheng, Y.C.2
  • 28
    • 33745501366 scopus 로고    scopus 로고
    • The exonuclease TREX1 is in the SET complex and acts in concert with NM23-H1 to degrade DNA during granzyme A-mediated cell death
    • 16818237 1:CAS:528:DC%2BD28XnsVyjs7s%3D 10.1016/j.molcel.2006.06.005
    • Chowdhury D, Beresford PJ, Zhu P, Zhang D, Sung JS, Demple B, Perrino FW, Lieberman J (2006) The exonuclease TREX1 is in the SET complex and acts in concert with NM23-H1 to degrade DNA during granzyme A-mediated cell death. Mol Cell 23:133-142
    • (2006) Mol Cell , vol.23 , pp. 133-142
    • Chowdhury, D.1    Beresford, P.J.2    Zhu, P.3    Zhang, D.4    Sung, J.S.5    Demple, B.6    Perrino, F.W.7    Lieberman, J.8
  • 29
    • 78049369870 scopus 로고    scopus 로고
    • Three prime exonuclease i (TREX1) is Fos/AP-1 regulated by genotoxic stress and protects against ultraviolet light and benzo(a)pyrene-induced DNA damage
    • 20511593 1:CAS:528:DC%2BC3cXhtlKltLzF 10.1093/nar/gkq455
    • Christmann M, Tomicic MT, Aasland D, Berdelle N, Kaina B (2010) Three prime exonuclease I (TREX1) is Fos/AP-1 regulated by genotoxic stress and protects against ultraviolet light and benzo(a)pyrene-induced DNA damage. Nucleic Acids Res 38:6418-6432
    • (2010) Nucleic Acids Res , vol.38 , pp. 6418-6432
    • Christmann, M.1    Tomicic, M.T.2    Aasland, D.3    Berdelle, N.4    Kaina, B.5
  • 30
    • 0043092025 scopus 로고    scopus 로고
    • Identification and characterization of the human mus81-eme1 endonuclease
    • 12721304 1:CAS:528:DC%2BD3sXltVSlt7o%3D 10.1074/jbc.M302882200
    • Ciccia A, Constantinou A, West SC (2003) Identification and characterization of the human mus81-eme1 endonuclease. J Biol Chem 278:25172-25178
    • (2003) J Biol Chem , vol.278 , pp. 25172-25178
    • Ciccia, A.1    Constantinou, A.2    West, S.C.3
  • 32
    • 4344649442 scopus 로고    scopus 로고
    • The Werner syndrome protein at the crossroads of DNA repair and apoptosis
    • 15336909 1:CAS:528:DC%2BD2cXntV2msr8%3D 10.1016/j.mad.2004.06.004
    • Comai L, Li B (2004) The Werner syndrome protein at the crossroads of DNA repair and apoptosis. Mech Ageing Dev 125:521-528
    • (2004) Mech Ageing Dev , vol.125 , pp. 521-528
    • Comai, L.1    Li, B.2
  • 33
    • 77956875652 scopus 로고    scopus 로고
    • Defective DSB repair correlates with abnormal nuclear morphology and is improved with FTI treatment in Hutchinson-Gilford progeria syndrome fibroblasts
    • 20599958 1:CAS:528:DC%2BC3cXht1Wmtb%2FF 10.1016/j.yexcr.2010.05.015
    • Constantinescu D, Csoka AB, Navara CS, Schatten GP (2010) Defective DSB repair correlates with abnormal nuclear morphology and is improved with FTI treatment in Hutchinson-Gilford progeria syndrome fibroblasts. Exp Cell Res 316:2747-2759
    • (2010) Exp Cell Res , vol.316 , pp. 2747-2759
    • Constantinescu, D.1    Csoka, A.B.2    Navara, C.S.3    Schatten, G.P.4
  • 34
  • 35
    • 55949088844 scopus 로고    scopus 로고
    • DNA2 resolves expanding flap in mitochondrial base excision repair
    • 19026774 1:CAS:528:DC%2BD1cXhsVKgt7bK 10.1016/j.molcel.2008.11.007
    • Copeland WC, Longley MJ (2008) DNA2 resolves expanding flap in mitochondrial base excision repair. Mol Cell 32:457-458
    • (2008) Mol Cell , vol.32 , pp. 457-458
    • Copeland, W.C.1    Longley, M.J.2
  • 36
    • 0030866223 scopus 로고    scopus 로고
    • Multiple pathways control cell growth and transformation: Overlapping and independent activities of p53 and p21Cip1/WAF1/Sdi1
    • 9390024 1:CAS:528:DyaK2sXnvV2jtrk%3D 10.1002/(SICI)1096-9896(199710)183: 2<134: AID-PATH960>3.0.CO;2-D
    • Cox LS (1997) Multiple pathways control cell growth and transformation: overlapping and independent activities of p53 and p21Cip1/WAF1/Sdi1. J Pathol 183:134-140
    • (1997) J Pathol , vol.183 , pp. 134-140
    • Cox, L.S.1
  • 37
    • 70350069069 scopus 로고    scopus 로고
    • Live fast, die young: New lessons in mammalian longevity
    • 19725776 1:CAS:528:DC%2BD1MXht1Ojt73F 10.1089/rej.2009.0894
    • Cox LS (2009) Live fast, die young: new lessons in mammalian longevity. Rejuvenation Res 12:283-288
    • (2009) Rejuvenation Res , vol.12 , pp. 283-288
    • Cox, L.S.1
  • 38
    • 84885041361 scopus 로고    scopus 로고
    • Ring structures and six-fold symmetry in DNA replication
    • L.S. Cox (eds) Royal Society of Chemistry Cambridge 10.1039/ 9781847559852-00047
    • Cox LS, Kearsey S (2009) Ring structures and six-fold symmetry in DNA replication. In: Cox LS (ed) Molecular themes in DNA replication. Royal Society of Chemistry, Cambridge, pp 47-85
    • (2009) Molecular Themes in DNA Replication , pp. 47-85
    • Cox, L.S.1    Kearsey, S.2
  • 39
    • 0029315510 scopus 로고
    • Tumour suppressors, kinases and clamps: How p53 regulates the cell cycle in response to DNA damage
    • 7575491 1:CAS:528:DyaK2MXntVarsr0%3D 10.1002/bies.950170606
    • Cox LS, Lane DP (1995) Tumour suppressors, kinases and clamps: how p53 regulates the cell cycle in response to DNA damage. Bioessays 17:501-508
    • (1995) Bioessays , vol.17 , pp. 501-508
    • Cox, L.S.1    Lane, D.P.2
  • 40
    • 73949127970 scopus 로고    scopus 로고
    • Increasing longevity through caloric restriction or rapamycin feeding in mammals: Common mechanisms for common outcomes?
    • 19678809 1:CAS:528:DC%2BD1MXht1Kkur7L 10.1111/j.1474-9726.2009.00509.x
    • Cox LS, Mattison JA (2009) Increasing longevity through caloric restriction or rapamycin feeding in mammals: common mechanisms for common outcomes? Aging Cell 8:607-613
    • (2009) Aging Cell , vol.8 , pp. 607-613
    • Cox, L.S.1    Mattison, J.A.2
  • 41
    • 36549068253 scopus 로고    scopus 로고
    • Modeling Werner Syndrome in Drosophila melanogaster: Hyper-recombination in flies lacking WRN-like exonuclease
    • 18056975 1:CAS:528:DC%2BD1cXpvVGgsg%3D%3D 10.1196/annals.1404.009
    • Cox LS, Clancy DJ, Boubriak I, Saunders RD (2007) Modeling Werner Syndrome in Drosophila melanogaster: hyper-recombination in flies lacking WRN-like exonuclease. Ann N Y Acad Sci 1119:274-288
    • (2007) Ann N y Acad Sci , vol.1119 , pp. 274-288
    • Cox, L.S.1    Clancy, D.J.2    Boubriak, I.3    Saunders, R.D.4
  • 42
    • 10344256183 scopus 로고    scopus 로고
    • Defective telomere lagging strand synthesis in cells lacking WRN helicase activity
    • 15591207 1:CAS:528:DC%2BD2cXhtVCqtbjM 10.1126/science.1103619
    • Crabbe L, Verdun RE, Haggblom CI, Karlseder J (2004) Defective telomere lagging strand synthesis in cells lacking WRN helicase activity. Science 306:1951-1953
    • (2004) Science , vol.306 , pp. 1951-1953
    • Crabbe, L.1    Verdun, R.E.2    Haggblom, C.I.3    Karlseder, J.4
  • 44
    • 77952703023 scopus 로고    scopus 로고
    • Identification of germ plasm-associated transcripts by microarray analysis of Xenopus vegetal cortex RNA
    • 20503379 1:CAS:528:DC%2BC3cXosFegtr0%3D 10.1002/dvdy.22304
    • Cuykendall TN, Houston DW (2010) Identification of germ plasm-associated transcripts by microarray analysis of Xenopus vegetal cortex RNA. Dev Dyn 239:1838-1848
    • (2010) Dev Dyn , vol.239 , pp. 1838-1848
    • Cuykendall, T.N.1    Houston, D.W.2
  • 45
    • 40249097634 scopus 로고    scopus 로고
    • EXOG, a novel paralog of endonuclease G in higher eukaryotes
    • 18187503 1:CAS:528:DC%2BD1cXislKiur4%3D 10.1093/nar/gkm1169
    • Cymerman IA, Chung I, Beckmann BM, Bujnicki JM, Meiss G (2008) EXOG, a novel paralog of endonuclease G in higher eukaryotes. Nucleic Acids Res 36:1369-1379
    • (2008) Nucleic Acids Res , vol.36 , pp. 1369-1379
    • Cymerman, I.A.1    Chung, I.2    Beckmann, B.M.3    Bujnicki, J.M.4    Meiss, G.5
  • 46
    • 0024278708 scopus 로고
    • Purification and properties of the major nuclease from mitochondria of Saccharomyces cerevisiae
    • 3286639 1:CAS:528:DyaL1cXktlCgs78%3D
    • Dake E, Hofmann TJ, McIntire S, Hudson A, Zassenhaus HP (1988) Purification and properties of the major nuclease from mitochondria of Saccharomyces cerevisiae. J Biol Chem 263:7691-7702
    • (1988) J Biol Chem , vol.263 , pp. 7691-7702
    • Dake, E.1    Hofmann, T.J.2    McIntire, S.3    Hudson, A.4    Zassenhaus, H.P.5
  • 47
    • 0036276388 scopus 로고    scopus 로고
    • The Mre11 complex: At the crossroads of DNA repair and checkpoint signalling
    • 11988766 10.1038/nrm805 1:CAS:528:DC%2BD38XjsFOgsLY%3D
    • D'Amours D, Jackson SP (2002) The Mre11 complex: at the crossroads of DNA repair and checkpoint signalling. Nat Rev Mol Cell Biol 3:317-327
    • (2002) Nat Rev Mol Cell Biol , vol.3 , pp. 317-327
    • D'Amours, D.1    Jackson, S.P.2
  • 48
    • 0035869155 scopus 로고    scopus 로고
    • DNA-binding and strand-annealing activities of human Mre11: Implications for its roles in DNA double-strand break repair pathways
    • 11238998 10.1093/nar/29.6.1317
    • de Jager M, Dronkert ML, Modesti M, Beerens CE, Kanaar R, van Gent DC (2001) DNA-binding and strand-annealing activities of human Mre11: implications for its roles in DNA double-strand break repair pathways. Nucleic Acids Res 29:1317-1325
    • (2001) Nucleic Acids Res , vol.29 , pp. 1317-1325
    • De Jager, M.1    Dronkert, M.L.2    Modesti, M.3    Beerens, C.E.4    Kanaar, R.5    Van Gent, D.C.6
  • 49
    • 79953143262 scopus 로고    scopus 로고
    • Polymerase epsilon is required to maintain replicative senescence
    • 21321081 1:CAS:528:DC%2BC3MXotFSjsb8%3D 10.1128/MCB.00144-10
    • Deshpande AM, Ivanova IG, Raykov V, Xue Y, Maringele L (2011) Polymerase epsilon is required to maintain replicative senescence. Mol Cell Biol 31:1637-1645
    • (2011) Mol Cell Biol , vol.31 , pp. 1637-1645
    • Deshpande, A.M.1    Ivanova, I.G.2    Raykov, V.3    Xue, Y.4    Maringele, L.5
  • 50
    • 0037031837 scopus 로고    scopus 로고
    • Mus81-Eme1 and Rqh1 involvement in processing stalled and collapsed replication forks
    • 12084712 1:CAS:528:DC%2BD38Xnt1Smtrc%3D 10.1074/jbc.M202120200
    • Doe CL, Ahn JS, Dixon J, Whitby MC (2002) Mus81-Eme1 and Rqh1 involvement in processing stalled and collapsed replication forks. J Biol Chem 277:32753-32759
    • (2002) J Biol Chem , vol.277 , pp. 32753-32759
    • Doe, C.L.1    Ahn, J.S.2    Dixon, J.3    Whitby, M.C.4
  • 51
    • 0029929070 scopus 로고    scopus 로고
    • The helix-hairpin-helix DNA-binding motif: A structural basis for non-sequence-specific recognition of DNA
    • 8692686 1:CAS:528:DyaK28XksVyjsbw%3D 10.1093/nar/24.13.2488
    • Doherty AJ, Serpell LC, Ponting CP (1996) The helix-hairpin-helix DNA-binding motif: a structural basis for non-sequence-specific recognition of DNA. Nucleic Acids Res 24:2488-2497
    • (1996) Nucleic Acids Res , vol.24 , pp. 2488-2497
    • Doherty, A.J.1    Serpell, L.C.2    Ponting, C.P.3
  • 52
    • 67649111979 scopus 로고    scopus 로고
    • Crystal structure of the rad9-rad1-hus1 DNA damage checkpoint complex - Implications for clamp loading and regulation
    • 19446481 1:CAS:528:DC%2BD1MXpsFCms70%3D 10.1016/j.molcel.2009.04.027
    • Dore AS, Kilkenny ML, Rzechorzek NJ, Pearl LH (2009) Crystal structure of the rad9-rad1-hus1 DNA damage checkpoint complex - implications for clamp loading and regulation. Mol Cell 34:735-745
    • (2009) Mol Cell , vol.34 , pp. 735-745
    • Dore, A.S.1    Kilkenny, M.L.2    Rzechorzek, N.J.3    Pearl, L.H.4
  • 55
    • 34548627532 scopus 로고    scopus 로고
    • DNA replication and transcription in mammalian mitochondria
    • 17408359 1:CAS:528:DC%2BD2sXhtVehtbzK 10.1146/annurev.biochem.76.060305. 152028
    • Falkenberg M, Larsson NG, Gustafsson CM (2007) DNA replication and transcription in mammalian mitochondria. Annu Rev Biochem 76:679-699
    • (2007) Annu Rev Biochem , vol.76 , pp. 679-699
    • Falkenberg, M.1    Larsson, N.G.2    Gustafsson, C.M.3
  • 57
    • 0030898435 scopus 로고    scopus 로고
    • Exonuclease i of Saccharomyces cerevisiae functions in mitotic recombination in vivo and in vitro
    • 9111347 1:CAS:528:DyaK2sXislGgt7s%3D
    • Fiorentini P, Huang KN, Tishkoff DX, Kolodner RD, Symington LS (1997) Exonuclease I of Saccharomyces cerevisiae functions in mitotic recombination in vivo and in vitro. Mol Cell Biol 17:2764-2773
    • (1997) Mol Cell Biol , vol.17 , pp. 2764-2773
    • Fiorentini, P.1    Huang, K.N.2    Tishkoff, D.X.3    Kolodner, R.D.4    Symington, L.S.5
  • 58
    • 79959913882 scopus 로고    scopus 로고
    • Characterization of the endonuclease and ATP-dependent flap endo/exonuclease of Dna2
    • 21572043 1:CAS:528:DC%2BC3MXot1Gls70%3D 10.1074/jbc.M111.243071
    • Fortini BK, Pokharel S, Polaczek P, Balakrishnan L, Bambara RA, Campbell JL (2011) Characterization of the endonuclease and ATP-dependent flap endo/exonuclease of Dna2. J Biol Chem 286:23763-23770
    • (2011) J Biol Chem , vol.286 , pp. 23763-23770
    • Fortini, B.K.1    Pokharel, S.2    Polaczek, P.3    Balakrishnan, L.4    Bambara, R.A.5    Campbell, J.L.6
  • 60
    • 0035369086 scopus 로고    scopus 로고
    • Structure of the replicating complex of a pol alpha family DNA polymerase
    • 11389835 1:CAS:528:DC%2BD3MXktlSqtrY%3D 10.1016/S0092-8674(01)00367-1
    • Franklin MC, Wang J, Steitz TA (2001) Structure of the replicating complex of a pol alpha family DNA polymerase. Cell 105:657-667
    • (2001) Cell , vol.105 , pp. 657-667
    • Franklin, M.C.1    Wang, J.2    Steitz, T.A.3
  • 61
    • 34247220441 scopus 로고    scopus 로고
    • New insights into the combined Cockayne/xeroderma pigmentosum complex: Human XPG protein can function in transcription factor stability
    • 17466619 1:CAS:528:DC%2BD2sXltFCqtbs%3D 10.1016/j.molcel.2007.04.002
    • Friedberg EC, Wood RD (2007) New insights into the combined Cockayne/xeroderma pigmentosum complex: human XPG protein can function in transcription factor stability. Mol Cell 26:162-164
    • (2007) Mol Cell , vol.26 , pp. 162-164
    • Friedberg, E.C.1    Wood, R.D.2
  • 63
    • 0032476658 scopus 로고    scopus 로고
    • Distinct roles of two separable in vitro activities of yeast Mre11 in mitotic and meiotic recombination
    • 9799249 1:CAS:528:DyaK1cXnsVKhtb8%3D 10.1093/emboj/17.21.6412
    • Furuse M, Nagase Y, Tsubouchi H, Murakami-Murofushi K, Shibata T, Ohta K (1998) Distinct roles of two separable in vitro activities of yeast Mre11 in mitotic and meiotic recombination. EMBO J 17:6412-6425
    • (1998) EMBO J , vol.17 , pp. 6412-6425
    • Furuse, M.1    Nagase, Y.2    Tsubouchi, H.3    Murakami-Murofushi, K.4    Shibata, T.5    Ohta, K.6
  • 65
    • 0037066720 scopus 로고    scopus 로고
    • Human exonuclease i is required for 5′ and 3′ mismatch repair
    • 11809771 1:CAS:528:DC%2BD38XivFSjtLs%3D 10.1074/jbc.M111854200
    • Genschel J, Bazemore LR, Modrich P (2002) Human exonuclease I is required for 5′ and 3′ mismatch repair. J Biol Chem 277:13302-13311
    • (2002) J Biol Chem , vol.277 , pp. 13302-13311
    • Genschel, J.1    Bazemore, L.R.2    Modrich, P.3
  • 66
    • 0034958108 scopus 로고    scopus 로고
    • Defective DNA polymerase-delta proofreading causes cancer susceptibility in mice
    • 11385474 1:CAS:528:DC%2BD3MXktlGkt7w%3D 10.1038/88963
    • Goldsby RE, Lawrence NA, Hays LE, Olmsted EA, Chen X, Singh M, Preston BD (2001) Defective DNA polymerase-delta proofreading causes cancer susceptibility in mice. Nat Med 7:638-639
    • (2001) Nat Med , vol.7 , pp. 638-639
    • Goldsby, R.E.1    Lawrence, N.A.2    Hays, L.E.3    Olmsted, E.A.4    Chen, X.5    Singh, M.6    Preston, B.D.7
  • 67
    • 65949083750 scopus 로고    scopus 로고
    • Cytoplasmic functions of the tumour suppressor p53
    • 19407794 1:CAS:528:DC%2BD1MXlt1Srt7Y%3D 10.1038/nature07986
    • Green DR, Kroemer G (2009) Cytoplasmic functions of the tumour suppressor p53. Nature 458:1127-1130
    • (2009) Nature , vol.458 , pp. 1127-1130
    • Green, D.R.1    Kroemer, G.2
  • 68
    • 0028075835 scopus 로고
    • A conserved 5′ to 3′ exonuclease activity in the yeast and human nucleotide excision repair proteins RAD2 and XPG
    • 7989298 1:CAS:528:DyaK2cXmvFGks70%3D
    • Habraken Y, Sung P, Prakash L, Prakash S (1994a) A conserved 5′ to 3′ exonuclease activity in the yeast and human nucleotide excision repair proteins RAD2 and XPG. J Biol Chem 269:31342-31345
    • (1994) J Biol Chem , vol.269 , pp. 31342-31345
    • Habraken, Y.1    Sung, P.2    Prakash, L.3    Prakash, S.4
  • 69
    • 0028076863 scopus 로고
    • Human xeroderma pigmentosum group G gene encodes a DNA endonuclease
    • 8078765 1:CAS:528:DyaK2cXmt1ensb4%3D 10.1093/nar/22.16.3312
    • Habraken Y, Sung P, Prakash L, Prakash S (1994b) Human xeroderma pigmentosum group G gene encodes a DNA endonuclease. Nucleic Acids Res 22:3312-3316
    • (1994) Nucleic Acids Res , vol.22 , pp. 3312-3316
    • Habraken, Y.1    Sung, P.2    Prakash, L.3    Prakash, S.4
  • 70
    • 0034531986 scopus 로고    scopus 로고
    • Second human protein with homology to the Escherichia coli abasic endonuclease exonuclease III
    • 11152564 1:CAS:528:DC%2BD3MXpsFGh 10.1002/1098-2280(2000)36:4<312: AID-EM7>3.0.CO;2-K
    • Hadi MZ, Wilson DM III (2000) Second human protein with homology to the Escherichia coli abasic endonuclease exonuclease III. Environ Mol Mutagen 36:312-324
    • (2000) Environ Mol Mutagen , vol.36 , pp. 312-324
    • Hadi, M.Z.1    Wilson III, D.M.2
  • 71
    • 0015319592 scopus 로고
    • The biologic clock: The mitochondria?
    • 5016631 1:STN:280:DyaE387lsVCmug%3D%3D
    • Harman D (1972) The biologic clock: the mitochondria? J Am Geriatr Soc 20:145-147
    • (1972) J Am Geriatr Soc , vol.20 , pp. 145-147
    • Harman, D.1
  • 72
    • 32644449296 scopus 로고    scopus 로고
    • The Werner syndrome protein operates in base excision repair and cooperates with DNA polymerase beta
    • 16449207 1:CAS:528:DC%2BD28XhtlOmsrw%3D 10.1093/nar/gkj475
    • Harrigan JA, Wilson DM 3rd, Prasad R, Opresko PL, Beck G, May A, Wilson SH, Bohr VA (2006) The Werner syndrome protein operates in base excision repair and cooperates with DNA polymerase beta. Nucleic Acids Res 34:745-754
    • (2006) Nucleic Acids Res , vol.34 , pp. 745-754
    • Harrigan, J.A.1    Wilson III, D.M.2    Prasad, R.3    Opresko, P.L.4    Beck, G.5    May, A.6    Wilson, S.H.7    Bohr, V.A.8
  • 73
    • 0028281443 scopus 로고
    • The characterization of a mammalian DNA structure-specific endonuclease
    • 8131753 1:CAS:528:DyaK2cXkt12ltr8%3D
    • Harrington JJ, Lieber MR (1994) The characterization of a mammalian DNA structure-specific endonuclease. EMBO J 13:1235-1246
    • (1994) EMBO J , vol.13 , pp. 1235-1246
    • Harrington, J.J.1    Lieber, M.R.2
  • 76
    • 0028917961 scopus 로고
    • Sequence of human FEN-1, a structure-specific endonuclease, and chromosomal localization of the gene (FEN1) in mouse and human
    • 7774922 1:CAS:528:DyaK2MXjsFOitL4%3D 10.1016/0888-7543(95)80129-A
    • Hiraoka LR, Harrington JJ, Gerhard DS, Lieber MR, Hsieh CL (1995) Sequence of human FEN-1, a structure-specific endonuclease, and chromosomal localization of the gene (FEN1) in mouse and human. Genomics 25:220-225
    • (1995) Genomics , vol.25 , pp. 220-225
    • Hiraoka, L.R.1    Harrington, J.J.2    Gerhard, D.S.3    Lieber, M.R.4    Hsieh, C.L.5
  • 77
    • 0029919634 scopus 로고    scopus 로고
    • Somatic point mutations in the p53 gene of human tumors and cell lines: Updated compilation
    • 8594564 1:CAS:528:DyaK28XnsV2qtw%3D%3D 10.1093/nar/24.1.141
    • Hollstein M, Shomer B, Greenblatt M, Soussi T, Hovig E, Montesano R, Harris CC (1996) Somatic point mutations in the p53 gene of human tumors and cell lines: updated compilation. Nucleic Acids Res 24:141-146
    • (1996) Nucleic Acids Res , vol.24 , pp. 141-146
    • Hollstein, M.1    Shomer, B.2    Greenblatt, M.3    Soussi, T.4    Hovig, E.5    Montesano, R.6    Harris, C.C.7
  • 78
    • 0036261565 scopus 로고    scopus 로고
    • Mutations in DNA replication genes reduce yeast life span
    • 12024027 10.1128/MCB.22.12.4136-4146.2002 1:CAS:528:DC%2BD38XktlSmurY%3D
    • Hoopes LL, Budd M, Choe W, Weitao T, Campbell JL (2002) Mutations in DNA replication genes reduce yeast life span. Mol Cell Biol 22:4136-4146
    • (2002) Mol Cell Biol , vol.22 , pp. 4136-4146
    • Hoopes, L.L.1    Budd, M.2    Choe, W.3    Weitao, T.4    Campbell, J.L.5
  • 79
    • 3543028030 scopus 로고    scopus 로고
    • Deletion of mouse rad9 causes abnormal cellular responses to DNA damage, genomic instability, and embryonic lethality
    • 15282322 1:CAS:528:DC%2BD2cXmtlOjtLw%3D 10.1128/MCB.24.16.7235-7248.2004
    • Hopkins KM, Auerbach W, Wang XY, Hande MP, Hang H, Wolgemuth DJ, Joyner AL, Lieberman HB (2004) Deletion of mouse rad9 causes abnormal cellular responses to DNA damage, genomic instability, and embryonic lethality. Mol Cell Biol 24:7235-7248
    • (2004) Mol Cell Biol , vol.24 , pp. 7235-7248
    • Hopkins, K.M.1    Auerbach, W.2    Wang, X.Y.3    Hande, M.P.4    Hang, H.5    Wolgemuth, D.J.6    Joyner, A.L.7    Lieberman, H.B.8
  • 80
    • 0032538537 scopus 로고    scopus 로고
    • Newly discovered archaebacterial flap endonucleases show a structure-specific mechanism for DNA substrate binding and catalysis resembling human flap endonuclease-1
    • 9765234 1:CAS:528:DyaK1cXntVSht70%3D 10.1074/jbc.273.42.27154
    • Hosfield DJ, Frank G, Weng Y, Tainer JA, Shen B (1998a) Newly discovered archaebacterial flap endonucleases show a structure-specific mechanism for DNA substrate binding and catalysis resembling human flap endonuclease-1. J Biol Chem 273:27154-27161
    • (1998) J Biol Chem , vol.273 , pp. 27154-27161
    • Hosfield, D.J.1    Frank, G.2    Weng, Y.3    Tainer, J.A.4    Shen, B.5
  • 81
    • 0032475933 scopus 로고    scopus 로고
    • Structure of the DNA repair and replication endonuclease and exonuclease FEN-1: Coupling DNA and PCNA binding to FEN-1 activity
    • 9778254 1:CAS:528:DyaK1cXmslWls7w%3D 10.1016/S0092-8674(00)81789-4
    • Hosfield DJ, Mol CD, Shen B, Tainer JA (1998b) Structure of the DNA repair and replication endonuclease and exonuclease FEN-1: coupling DNA and PCNA binding to FEN-1 activity. Cell 95:135-146
    • (1998) Cell , vol.95 , pp. 135-146
    • Hosfield, D.J.1    Mol, C.D.2    Shen, B.3    Tainer, J.A.4
  • 82
    • 0037786682 scopus 로고    scopus 로고
    • A human DNA editing enzyme homologous to the Escherichia coli DnaQ/MutD protein
    • 10393201 1:CAS:528:DyaK1MXksFKltLs%3D 10.1093/emboj/18.13.3868
    • Hoss M, Robins P, Naven TJ, Pappin DJ, Sgouros J, Lindahl T (1999) A human DNA editing enzyme homologous to the Escherichia coli DnaQ/MutD protein. EMBO J 18:3868-3875
    • (1999) EMBO J , vol.18 , pp. 3868-3875
    • Hoss, M.1    Robins, P.2    Naven, T.J.3    Pappin, D.J.4    Sgouros, J.5    Lindahl, T.6
  • 83
    • 45449103427 scopus 로고    scopus 로고
    • DNA mismatch repair: Molecular mechanism, cancer, and ageing
    • 18406444 1:CAS:528:DC%2BD1cXns1Shur4%3D 10.1016/j.mad.2008.02.012
    • Hsieh P, Yamane K (2008) DNA mismatch repair: molecular mechanism, cancer, and ageing. Mech Ageing Dev 129:391-407
    • (2008) Mech Ageing Dev , vol.129 , pp. 391-407
    • Hsieh, P.1    Yamane, K.2
  • 84
    • 0026698636 scopus 로고
    • Extension of base mispairs by Taq DNA polymerase: Implications for single nucleotide discrimination in PCR
    • 1408758 1:CAS:528:DyaK3sXltlWqtQ%3D%3D 10.1093/nar/20.17.4567
    • Huang MM, Arnheim N, Goodman MF (1992) Extension of base mispairs by Taq DNA polymerase: implications for single nucleotide discrimination in PCR. Nucleic Acids Res 20:4567-4573
    • (1992) Nucleic Acids Res , vol.20 , pp. 4567-4573
    • Huang, M.M.1    Arnheim, N.2    Goodman, M.F.3
  • 85
    • 0031686571 scopus 로고    scopus 로고
    • The premature ageing syndrome protein, WRN, is a 3′ → 5′ exonuclease
    • 9771700 1:CAS:528:DyaK1cXms1amsLs%3D 10.1038/2410
    • Huang S, Li B, Gray MD, Oshima J, Mian IS, Campisi J (1998) The premature ageing syndrome protein, WRN, is a 3′ → 5′ exonuclease. Nat Genet 20:114-116
    • (1998) Nat Genet , vol.20 , pp. 114-116
    • Huang, S.1    Li, B.2    Gray, M.D.3    Oshima, J.4    Mian, I.S.5    Campisi, J.6
  • 86
    • 0034660246 scopus 로고    scopus 로고
    • Characterization of the human and mouse WRN 3′ → 5′ exonuclease
    • 10871373 1:CAS:528:DC%2BD3cXkslait70%3D 10.1093/nar/28.12.2396
    • Huang S, Beresten S, Li B, Oshima J, Ellis NA, Campisi J (2000) Characterization of the human and mouse WRN 3′ → 5′ exonuclease. Nucleic Acids Res 28:2396-2405
    • (2000) Nucleic Acids Res , vol.28 , pp. 2396-2405
    • Huang, S.1    Beresten, S.2    Li, B.3    Oshima, J.4    Ellis, N.A.5    Campisi, J.6
  • 87
    • 33745171416 scopus 로고    scopus 로고
    • Endonuclease G: A role for the enzyme in recombination and cellular proliferation
    • 16754849 1:CAS:528:DC%2BD28XmsVWjsrg%3D 10.1073/pnas.0603445103
    • Huang KJ, Ku CC, Lehman IR (2006) Endonuclease G: a role for the enzyme in recombination and cellular proliferation. Proc Natl Acad Sci U S A 103:8995-9000
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 8995-9000
    • Huang, K.J.1    Ku, C.C.2    Lehman, I.R.3
  • 88
    • 0035997349 scopus 로고    scopus 로고
    • Eukaryotic DNA polymerases
    • 12045093 1:CAS:528:DC%2BD38Xos1Clsbk%3D 10.1146/annurev.biochem.71. 090501.150041
    • Hubscher U, Maga G, Spadari S (2002) Eukaryotic DNA polymerases. Annu Rev Biochem 71:133-163
    • (2002) Annu Rev Biochem , vol.71 , pp. 133-163
    • Hubscher, U.1    Maga, G.2    Spadari, S.3
  • 89
    • 56749119855 scopus 로고    scopus 로고
    • Identification of Holliday junction resolvases from humans and yeast
    • 19020614 1:CAS:528:DC%2BD1cXhsVSjsLvE 10.1038/nature07470
    • Ip SC, Rass U, Blanco MG, Flynn HR, Skehel JM, West SC (2008) Identification of Holliday junction resolvases from humans and yeast. Nature 456:357-361.
    • (2008) Nature , vol.456 , pp. 357-361
    • Ip, S.C.1    Rass, U.2    Blanco, M.G.3    Flynn, H.R.4    Skehel, J.M.5    West, S.C.6
  • 91
    • 78349259719 scopus 로고    scopus 로고
    • An mre11 mutation that promotes telomere recombination and an efficient bypass of senescence
    • 20421597 1:CAS:528:DC%2BC3cXhsFOnu7rN 10.1534/genetics.110.117598
    • Joseph IS, Kumari A, Bhattacharyya MK, Gao H, Li B, Lustig AJ (2010) An mre11 mutation that promotes telomere recombination and an efficient bypass of senescence. Genetics 185:761-770
    • (2010) Genetics , vol.185 , pp. 761-770
    • Joseph, I.S.1    Kumari, A.2    Bhattacharyya, M.K.3    Gao, H.4    Li, B.5    Lustig, A.J.6
  • 92
    • 70149110390 scopus 로고    scopus 로고
    • Evidence for a role of FEN1 in maintaining mitochondrial DNA integrity
    • 1:CAS:528:DC%2BD1MXhtFGqtrfL 10.1016/j.dnarep.2009.07.008
    • Kalifa L, Beutner G, Phadnis N, Sheu SS, Sia EA (2009) Evidence for a role of FEN1 in maintaining mitochondrial DNA integrity. DNA Repair (Amst) 8:1242-1249
    • (2009) DNA Repair (Amst) , vol.8 , pp. 1242-1249
    • Kalifa, L.1    Beutner, G.2    Phadnis, N.3    Sheu, S.S.4    Sia, E.A.5
  • 93
    • 1642545486 scopus 로고    scopus 로고
    • The protein components and mechanism of eukaryotic Okazaki fragment maturation
    • 14693726 1:CAS:528:DC%2BD2cXhsFWitL8%3D 10.1080/10409230390259382
    • Kao HI, Bambara RA (2003) The protein components and mechanism of eukaryotic Okazaki fragment maturation. Crit Rev Biochem Mol Biol 38:433-452
    • (2003) Crit Rev Biochem Mol Biol , vol.38 , pp. 433-452
    • Kao, H.I.1    Bambara, R.A.2
  • 94
    • 2442601582 scopus 로고    scopus 로고
    • On the roles of Saccharomyces cerevisiae Dna2p and Flap endonuclease 1 in Okazaki fragment processing
    • 14747468 1:CAS:528:DC%2BD2cXivVKhu7s%3D 10.1074/jbc.M313216200
    • Kao HI, Veeraraghavan J, Polaczek P, Campbell JL, Bambara RA (2004) On the roles of Saccharomyces cerevisiae Dna2p and Flap endonuclease 1 in Okazaki fragment processing. J Biol Chem 279:15014-15024
    • (2004) J Biol Chem , vol.279 , pp. 15014-15024
    • Kao, H.I.1    Veeraraghavan, J.2    Polaczek, P.3    Campbell, J.L.4    Bambara, R.A.5
  • 95
    • 33144469989 scopus 로고    scopus 로고
    • Exogenous expression of exonuclease domain-deleted WRN interferes with the repair of radiation-induced DNA damages
    • 1:CAS:528:DC%2BD28XhvVCqsbc%3D 10.1269/jrr.46.407
    • Kashino G, Kodama S, Suzuki K, Matsumoto T, Watanabe M (2005) Exogenous expression of exonuclease domain-deleted WRN interferes with the repair of radiation-induced DNA damages. J Radiat Res (Tokyo) 46:407-414
    • (2005) J Radiat Res (Tokyo) , vol.46 , pp. 407-414
    • Kashino, G.1    Kodama, S.2    Suzuki, K.3    Matsumoto, T.4    Watanabe, M.5
  • 96
    • 45549084168 scopus 로고    scopus 로고
    • P53 target gene AEN is a nuclear exonuclease required for p53-dependent apoptosis
    • 18264133 1:CAS:528:DC%2BD1cXntlCqu7o%3D 10.1038/onc.2008.32
    • Kawase T, Ichikawa H, Ohta T, Nozaki N, Tashiro F, Ohki R, Taya Y (2008) p53 target gene AEN is a nuclear exonuclease required for p53-dependent apoptosis. Oncogene 27:3797-3810
    • (2008) Oncogene , vol.27 , pp. 3797-3810
    • Kawase, T.1    Ichikawa, H.2    Ohta, T.3    Nozaki, N.4    Tashiro, F.5    Ohki, R.6    Taya, Y.7
  • 97
    • 0033624527 scopus 로고    scopus 로고
    • A DNA polymerase epsilon mutant that specifically causes +1 frameshift mutations within homonucleotide runs in yeast
    • 10924461 1:CAS:528:DC%2BD3cXmtFGqurs%3D
    • Kirchner JM, Tran H, Resnick MA (2000) A DNA polymerase epsilon mutant that specifically causes +1 frameshift mutations within homonucleotide runs in yeast. Genetics 155:1623-1632
    • (2000) Genetics , vol.155 , pp. 1623-1632
    • Kirchner, J.M.1    Tran, H.2    Resnick, M.A.3
  • 98
    • 72949123930 scopus 로고    scopus 로고
    • The Fanconi anemia pathway promotes replication-dependent DNA interstrand cross-link repair
    • 19965384 1:CAS:528:DC%2BD1MXhsFGmsL7L 10.1126/science.1182372
    • Knipscheer P, Raschle M, Smogorzewska A, Enoiu M, Ho TV, Scharer OD, Elledge SJ, Walter JC (2009) The Fanconi anemia pathway promotes replication-dependent DNA interstrand cross-link repair. Science 326:1698-1701
    • (2009) Science , vol.326 , pp. 1698-1701
    • Knipscheer, P.1    Raschle, M.2    Smogorzewska, A.3    Enoiu, M.4    Ho, T.V.5    Scharer, O.D.6    Elledge, S.J.7    Walter, J.C.8
  • 100
    • 79960323487 scopus 로고    scopus 로고
    • Increase in mitochondrial DNA mutations impairs retinal function and renders the retina vulnerable to injury
    • 21332926 1:CAS:528:DC%2BC3MXpvFCjsrk%3D 10.1111/j.1474-9726.2011.00690.x
    • Kong YX, Van Bergen N, Trounce IA, Bui BV, Chrysostomou V, Waugh H, Vingrys A, Crowston JG (2011) Increase in mitochondrial DNA mutations impairs retinal function and renders the retina vulnerable to injury. Aging Cell 10:572-583
    • (2011) Aging Cell , vol.10 , pp. 572-583
    • Kong, Y.X.1    Van Bergen, N.2    Trounce, I.A.3    Bui, B.V.4    Chrysostomou, V.5    Waugh, H.6    Vingrys, A.7    Crowston, J.G.8
  • 101
    • 79953160620 scopus 로고    scopus 로고
    • The high fidelity and unique error signature of human DNA polymerase epsilon
    • 21036870 10.1093/nar/gkq1034 1:CAS:528:DC%2BC3MXjsFyjtrc%3D
    • Korona DA, Lecompte KG, Pursell ZF (2010) The high fidelity and unique error signature of human DNA polymerase epsilon. Nucleic Acids Res 39:1763-1773
    • (2010) Nucleic Acids Res , vol.39 , pp. 1763-1773
    • Korona, D.A.1    Lecompte, K.G.2    Pursell, Z.F.3
  • 103
    • 67651177611 scopus 로고    scopus 로고
    • Do mtDNA deletions drive premature aging in mtDNA mutator mice?
    • 19416127 1:CAS:528:DC%2BD1MXhtVSjtbbE 10.1111/j.1474-9726.2009.00484.x
    • Kraytsberg Y, Simon DK, Turnbull DM, Khrapko K (2009) Do mtDNA deletions drive premature aging in mtDNA mutator mice? Aging Cell 8:502-506
    • (2009) Aging Cell , vol.8 , pp. 502-506
    • Kraytsberg, Y.1    Simon, D.K.2    Turnbull, D.M.3    Khrapko, K.4
  • 105
    • 77957740230 scopus 로고    scopus 로고
    • Evolving views of DNA replication (in)fidelity
    • 19903750 1:CAS:528:DC%2BC38Xht1KksL%2FM 10.1101/sqb.2009.74.027
    • Kunkel TA (2009) Evolving views of DNA replication (in)fidelity. Cold Spring Harb Symp Quant Biol 74:91-101
    • (2009) Cold Spring Harb Symp Quant Biol , vol.74 , pp. 91-101
    • Kunkel, T.A.1
  • 106
    • 0033621354 scopus 로고    scopus 로고
    • The Werner syndrome gene product co-purifies with the DNA replication complex and interacts with PCNA and topoisomerase i
    • 10608841 1:CAS:528:DC%2BD3cXkt1Gguw%3D%3D 10.1074/jbc.274.53.37795
    • Lebel M, Spillare EA, Harris CC, Leder P (1999) The Werner syndrome gene product co-purifies with the DNA replication complex and interacts with PCNA and topoisomerase I. J Biol Chem 274:37795-37799
    • (1999) J Biol Chem , vol.274 , pp. 37795-37799
    • Lebel, M.1    Spillare, E.A.2    Harris, C.C.3    Leder, P.4
  • 107
    • 36949026694 scopus 로고    scopus 로고
    • Activation and regulation of ATM kinase activity in response to DNA double-strand breaks
    • 18066086 1:CAS:528:DC%2BD2sXhsVSmtbfE 10.1038/sj.onc.1210872
    • Lee JH, Paull TT (2007) Activation and regulation of ATM kinase activity in response to DNA double-strand breaks. Oncogene 26:7741-7748
    • (2007) Oncogene , vol.26 , pp. 7741-7748
    • Lee, J.H.1    Paull, T.T.2
  • 108
    • 0033621353 scopus 로고    scopus 로고
    • The RAD2 domain of human exonuclease 1 exhibits 5′ to 3′ exonuclease and flap structure-specific endonuclease activities
    • 10608837 1:CAS:528:DC%2BD3cXkt1Ggtw%3D%3D 10.1074/jbc.274.53.37763
    • Lee BI, Wilson DM III (1999) The RAD2 domain of human exonuclease 1 exhibits 5′ to 3′ exonuclease and flap structure-specific endonuclease activities. J Biol Chem 274:37763-37769
    • (1999) J Biol Chem , vol.274 , pp. 37763-37769
    • Lee, B.I.1    Wilson III, D.M.2
  • 109
    • 79954621884 scopus 로고    scopus 로고
    • Caenorhabditis elegans DNA-2 helicase/endonuclease plays a vital role in maintaining genome stability, morphogenesis, and life span
    • 21414295 1:CAS:528:DC%2BC3MXkvFaitLo%3D 10.1016/j.bbrc.2011.03.045
    • Lee MH, Hollis SE, Yoo BH, Nykamp K (2011) Caenorhabditis elegans DNA-2 helicase/endonuclease plays a vital role in maintaining genome stability, morphogenesis, and life span. Biochem Biophys Res Commun 407:495-500
    • (2011) Biochem Biophys Res Commun , vol.407 , pp. 495-500
    • Lee, M.H.1    Hollis, S.E.2    Yoo, B.H.3    Nykamp, K.4
  • 110
    • 0036714151 scopus 로고    scopus 로고
    • Displacement of DNA-PKcs from DNA ends by the Werner syndrome protein
    • 12202749 1:CAS:528:DC%2BD38Xms1Klt7o%3D 10.1093/nar/gkf488
    • Li B, Comai L (2002) Displacement of DNA-PKcs from DNA ends by the Werner syndrome protein. Nucleic Acids Res 30:3653-3661
    • (2002) Nucleic Acids Res , vol.30 , pp. 3653-3661
    • Li, B.1    Comai, L.2
  • 111
    • 0035811496 scopus 로고    scopus 로고
    • Endonuclease G is an apoptotic DNase when released from mitochondria
    • 11452314 1:CAS:528:DC%2BD3MXlt1Cqsr0%3D 10.1038/35083620
    • Li LY, Luo X, Wang X (2001) Endonuclease G is an apoptotic DNase when released from mitochondria. Nature 412:95-99
    • (2001) Nature , vol.412 , pp. 95-99
    • Li, L.Y.1    Luo, X.2    Wang, X.3
  • 112
    • 1842791545 scopus 로고    scopus 로고
    • Identification and biochemical characterization of a Werner's syndrome protein complex with Ku70/80 and poly(ADP-ribose) polymerase-1
    • 14734561 1:CAS:528:DC%2BD2cXis1elsrc%3D 10.1074/jbc.M311606200
    • Li B, Navarro S, Kasahara N, Comai L (2004) Identification and biochemical characterization of a Werner's syndrome protein complex with Ku70/80 and poly(ADP-ribose) polymerase-1. J Biol Chem 279:13659-13667
    • (2004) J Biol Chem , vol.279 , pp. 13659-13667
    • Li, B.1    Navarro, S.2    Kasahara, N.3    Comai, L.4
  • 113
    • 29244487517 scopus 로고    scopus 로고
    • A conserved and species-specific functional interaction between the Werner syndrome-like exonuclease atWEX and the Ku heterodimer in Arabidopsis
    • 16396834 1:CAS:528:DC%2BD2MXhtlagtbbF 10.1093/nar/gki984
    • Li B, Conway N, Navarro S, Comai L (2005) A conserved and species-specific functional interaction between the Werner syndrome-like exonuclease atWEX and the Ku heterodimer in Arabidopsis. Nucleic Acids Res 33:6861-6867
    • (2005) Nucleic Acids Res , vol.33 , pp. 6861-6867
    • Li, B.1    Conway, N.2    Navarro, S.3    Comai, L.4
  • 114
    • 67749084678 scopus 로고    scopus 로고
    • Biochemical properties of mammalian TREX1 and its association with DNA replication and inherited inflammatory disease
    • 19442247 1:CAS:528:DC%2BD1MXmtFSgurs%3D 10.1042/BST0370535
    • Lindahl T, Barnes DE, Yang YG, Robins P (2009) Biochemical properties of mammalian TREX1 and its association with DNA replication and inherited inflammatory disease. Biochem Soc Trans 37:535-538
    • (2009) Biochem Soc Trans , vol.37 , pp. 535-538
    • Lindahl, T.1    Barnes, D.E.2    Yang, Y.G.3    Robins, P.4
  • 115
    • 4344675706 scopus 로고    scopus 로고
    • The human Rad9 checkpoint protein stimulates the carbamoyl phosphate synthetase activity of the multifunctional protein CAD
    • 15326225 1:CAS:528:DC%2BD2cXnsVyhsr0%3D 10.1093/nar/gkh789
    • Lindsey-Boltz LA, Wauson EM, Graves LM, Sancar A (2004) The human Rad9 checkpoint protein stimulates the carbamoyl phosphate synthetase activity of the multifunctional protein CAD. Nucleic Acids Res 32:4524-4530
    • (2004) Nucleic Acids Res , vol.32 , pp. 4524-4530
    • Lindsey-Boltz, L.A.1    Wauson, E.M.2    Graves, L.M.3    Sancar, A.4
  • 116
    • 4544281398 scopus 로고    scopus 로고
    • Choreography of the DNA damage response: Spatiotemporal relationships among checkpoint and repair proteins
    • 15369670 1:CAS:528:DC%2BD2cXnvFehtb8%3D 10.1016/j.cell.2004.08.015
    • Lisby M, Barlow JH, Burgess RC, Rothstein R (2004) Choreography of the DNA damage response: spatiotemporal relationships among checkpoint and repair proteins. Cell 118:699-713
    • (2004) Cell , vol.118 , pp. 699-713
    • Lisby, M.1    Barlow, J.H.2    Burgess, R.C.3    Rothstein, R.4
  • 117
    • 1942422156 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae flap endonuclease 1 uses flap equilibration to maintain triplet repeat stability
    • 15082797 1:CAS:528:DC%2BD2cXjsVyrsbk%3D 10.1128/MCB.24.9.4049-4064.2004
    • Liu Y, Zhang H, Veeraraghavan J, Bambara RA, Freudenreich CH (2004) Saccharomyces cerevisiae flap endonuclease 1 uses flap equilibration to maintain triplet repeat stability. Mol Cell Biol 24:4049-4064
    • (2004) Mol Cell Biol , vol.24 , pp. 4049-4064
    • Liu, Y.1    Zhang, H.2    Veeraraghavan, J.3    Bambara, R.A.4    Freudenreich, C.H.5
  • 119
    • 77955290719 scopus 로고    scopus 로고
    • FAN1 acts with FANCI-FANCD2 to promote DNA interstrand cross-link repair
    • 20671156 1:CAS:528:DC%2BC3cXps1ehtbo%3D 10.1126/science.1192656
    • Liu T, Ghosal G, Yuan J, Chen J, Huang J (2010) FAN1 acts with FANCI-FANCD2 to promote DNA interstrand cross-link repair. Science 329:693-696
    • (2010) Science , vol.329 , pp. 693-696
    • Liu, T.1    Ghosal, G.2    Yuan, J.3    Chen, J.4    Huang, J.5
  • 120
    • 0035914329 scopus 로고    scopus 로고
    • The fidelity of human DNA polymerase gamma with and without exonucleolytic proofreading and the p55 accessory subunit
    • 11504725 1:CAS:528:DC%2BD3MXnvVentr4%3D 10.1074/jbc.M105230200
    • Longley MJ, Nguyen D, Kunkel TA, Copeland WC (2001) The fidelity of human DNA polymerase gamma with and without exonucleolytic proofreading and the p55 accessory subunit. J Biol Chem 276:38555-38562
    • (2001) J Biol Chem , vol.276 , pp. 38555-38562
    • Longley, M.J.1    Nguyen, D.2    Kunkel, T.A.3    Copeland, W.C.4
  • 121
    • 33645765164 scopus 로고    scopus 로고
    • Length-dependent degradation of single-stranded 3′ ends by the Werner syndrome protein (WRN): Implications for spatial orientation and coordinated 3′ to 5′ movement of its ATPase/helicase and exonuclease domains
    • 16503984 10.1186/1471-2199-7-6 1:CAS:528:DC%2BD28XksVWjsLY%3D
    • Machwe A, Xiao L, Orren DK (2006) Length-dependent degradation of single-stranded 3′ ends by the Werner syndrome protein (WRN): implications for spatial orientation and coordinated 3′ to 5′ movement of its ATPase/helicase and exonuclease domains. BMC Mol Biol 7:6
    • (2006) BMC Mol Biol , vol.7 , pp. 6
    • Machwe, A.1    Xiao, L.2    Orren, D.K.3
  • 123
    • 0035899864 scopus 로고    scopus 로고
    • DNA replication: Partners in the Okazaki two-step
    • 11676941 1:CAS:528:DC%2BD3MXnvFGjsL0%3D 10.1016/S0960-9822(01)00500-0
    • MacNeill SA (2001) DNA replication: partners in the Okazaki two-step. Curr Biol 11:R842-R844
    • (2001) Curr Biol , vol.11
    • Macneill, S.A.1
  • 124
    • 0033538461 scopus 로고    scopus 로고
    • Identification and expression of the TREX1 and TREX2 cDNA sequences encoding mammalian 3′→5′ exonucleases
    • 10391904 1:CAS:528:DyaK1MXksFKmt7s%3D 10.1074/jbc.274.28.19655
    • Mazur DJ, Perrino FW (1999) Identification and expression of the TREX1 and TREX2 cDNA sequences encoding mammalian 3′→5′ exonucleases. J Biol Chem 274:19655-19660
    • (1999) J Biol Chem , vol.274 , pp. 19655-19660
    • Mazur, D.J.1    Perrino, F.W.2
  • 125
    • 0035907239 scopus 로고    scopus 로고
    • Excision of 3′ termini by the Trex1 and TREX2 3′→ 5′ exonucleases. Characterization of the recombinant proteins
    • 11279105 1:CAS:528:DC%2BD3MXjvFGisb0%3D 10.1074/jbc.M100623200
    • Mazur DJ, Perrino FW (2001a) Excision of 3′ termini by the Trex1 and TREX2 3′→5′ exonucleases. Characterization of the recombinant proteins. J Biol Chem 276:17022-17029
    • (2001) J Biol Chem , vol.276 , pp. 17022-17029
    • Mazur, D.J.1    Perrino, F.W.2
  • 126
    • 0035805548 scopus 로고    scopus 로고
    • Structure and expression of the TREX1 and TREX2 3′→5′ exonuclease genes
    • 11278605 1:CAS:528:DC%2BD3MXjs1Okur8%3D 10.1074/jbc.M010051200
    • Mazur DJ, Perrino FW (2001b) Structure and expression of the TREX1 and TREX2 3′→5′ exonuclease genes. J Biol Chem 276:14718-14727
    • (2001) J Biol Chem , vol.276 , pp. 14718-14727
    • Mazur, D.J.1    Perrino, F.W.2
  • 127
    • 33645512251 scopus 로고    scopus 로고
    • Trt-1 is the Caenorhabditis elegans catalytic subunit of telomerase
    • 16477310 10.1371/journal.pgen.0020018 1:CAS:528:DC%2BD28XhvFKmurY%3D
    • Meier B, Clejan I, Liu Y, Lowden M, Gartner A, Hodgkin J, Ahmed S (2006) trt-1 is the Caenorhabditis elegans catalytic subunit of telomerase. PLoS Genet 2:e18
    • (2006) PLoS Genet , vol.2 , pp. 18
    • Meier, B.1    Clejan, I.2    Liu, Y.3    Lowden, M.4    Gartner, A.5    Hodgkin, J.6    Ahmed, S.7
  • 128
    • 0019160038 scopus 로고
    • Mitochondrial role in cell aging
    • 7009178 1:CAS:528:DyaL3MXlvFyrsw%3D%3D 10.1016/0531-5565(80)90010-8
    • Miquel J, Economos AC, Fleming J, Johnson JE Jr (1980) Mitochondrial role in cell aging. Exp Gerontol 15:575-591
    • (1980) Exp Gerontol , vol.15 , pp. 575-591
    • Miquel, J.1    Economos, A.C.2    Fleming, J.3    Johnson, Jr.J.E.4
  • 129
    • 0034749425 scopus 로고    scopus 로고
    • DNA damage-dependent nuclear dynamics of the Mre11 complex
    • 11113202 1:CAS:528:DC%2BD3MXptVSj 10.1128/MCB.21.1.281-288.2001
    • Mirzoeva OK, Petrini JH (2001) DNA damage-dependent nuclear dynamics of the Mre11 complex. Mol Cell Biol 21:281-288
    • (2001) Mol Cell Biol , vol.21 , pp. 281-288
    • Mirzoeva, O.K.1    Petrini, J.H.2
  • 130
    • 0032931844 scopus 로고    scopus 로고
    • The nuclease activity of Mre11 is required for meiosis but not for mating type switching, end joining, or telomere maintenance
    • 9858579 1:CAS:528:DyaK1MXhvFOrtg%3D%3D
    • Moreau S, Ferguson JR, Symington LS (1999) The nuclease activity of Mre11 is required for meiosis but not for mating type switching, end joining, or telomere maintenance. Mol Cell Biol 19:556-566
    • (1999) Mol Cell Biol , vol.19 , pp. 556-566
    • Moreau, S.1    Ferguson, J.R.2    Symington, L.S.3
  • 131
    • 0035692142 scopus 로고    scopus 로고
    • Overlapping functions of the Saccharomyces cerevisiae Mre11, Exo1 and Rad27 nucleases in DNA metabolism
    • 11779786 1:CAS:528:DC%2BD38XntFKksA%3D%3D
    • Moreau S, Morgan EA, Symington LS (2001) Overlapping functions of the Saccharomyces cerevisiae Mre11, Exo1 and Rad27 nucleases in DNA metabolism. Genetics 159:1423-1433
    • (2001) Genetics , vol.159 , pp. 1423-1433
    • Moreau, S.1    Morgan, E.A.2    Symington, L.S.3
  • 132
    • 3242672339 scopus 로고    scopus 로고
    • Gene-targeted mice lacking the Trex1 (DNase III) 3′→5′ DNA exonuclease develop inflammatory myocarditis
    • 15254239 1:CAS:528:DC%2BD2cXmtlKltbc%3D 10.1128/MCB.24.15.6719-6727.2004
    • Morita M, Stamp G, Robins P, Dulic A, Rosewell I, Hrivnak G, Daly G, Lindahl T, Barnes DE (2004) Gene-targeted mice lacking the Trex1 (DNase III) 3′→5′ DNA exonuclease develop inflammatory myocarditis. Mol Cell Biol 24:6719-6727
    • (2004) Mol Cell Biol , vol.24 , pp. 6719-6727
    • Morita, M.1    Stamp, G.2    Robins, P.3    Dulic, A.4    Rosewell, I.5    Hrivnak, G.6    Daly, G.7    Lindahl, T.8    Barnes, D.E.9
  • 134
    • 0030604728 scopus 로고    scopus 로고
    • P53 protein exhibits 3′-to-5′ exonuclease activity
    • 8674115 1:CAS:528:DyaK28XjvF2iu7k%3D 10.1016/S0092-8674(00)81309-4
    • Mummenbrauer T, Janus F, Muller B, Wiesmuller L, Deppert W, Grosse F (1996) p53 protein exhibits 3′-to-5′ exonuclease activity. Cell 85:1089-1099
    • (1996) Cell , vol.85 , pp. 1089-1099
    • Mummenbrauer, T.1    Janus, F.2    Muller, B.3    Wiesmuller, L.4    Deppert, W.5    Grosse, F.6
  • 135
    • 0024315865 scopus 로고
    • DNA repair
    • 2519777 1:CAS:528:DyaL1MXksFamsrs%3D 10.1021/tx00010a001
    • Myles GM, Sancar A (1989) DNA repair. Chem Res Toxicol 2:197-226
    • (1989) Chem Res Toxicol , vol.2 , pp. 197-226
    • Myles, G.M.1    Sancar, A.2
  • 137
    • 0035102952 scopus 로고    scopus 로고
    • Novel function of Rad27 (FEN-1) in restricting short-sequence recombination
    • 11259584 1:CAS:528:DC%2BD3MXitVCqurk%3D 10.1128/MCB.21.7.2349-2358.2001
    • Negritto MC, Qiu J, Ratay DO, Shen B, Bailis AM (2001) Novel function of Rad27 (FEN-1) in restricting short-sequence recombination. Mol Cell Biol 21:2349-2358
    • (2001) Mol Cell Biol , vol.21 , pp. 2349-2358
    • Negritto, M.C.1    Qiu, J.2    Ratay, D.O.3    Shen, B.4    Bailis, A.M.5
  • 138
    • 33646390723 scopus 로고    scopus 로고
    • Evidence for extrinsic exonucleolytic proofreading
    • 16687920 1:CAS:528:DC%2BD28XmvV2ksrk%3D 10.4161/cc.5.9.2736
    • Nick McElhinny SA, Pavlov YI, Kunkel TA (2006) Evidence for extrinsic exonucleolytic proofreading. Cell Cycle 5:958-962
    • (2006) Cell Cycle , vol.5 , pp. 958-962
    • Nick McElhinny, S.A.1    Pavlov, Y.I.2    Kunkel, T.A.3
  • 139
    • 84885038889 scopus 로고    scopus 로고
    • Mechanisms for high fidelity DNA replication
    • L.S. Cox (eds) Royal Society of Chemistry Cambridge 10.1039/ 9781847559852-00086
    • Nick McElhinny SA, Pursell ZF, Kunkel TA (2009) Mechanisms for high fidelity DNA replication. In: Cox LS (ed) Molecular themes in DNA replication. Royal Society of Chemistry, Cambridge, pp 86-111
    • (2009) Molecular Themes in DNA Replication , pp. 86-111
    • Nick McElhinny, S.A.1    Pursell, Z.F.2    Kunkel, T.A.3
  • 141
    • 79951688343 scopus 로고    scopus 로고
    • BLM-DNA2-RPA-MRN and EXO1-BLM-RPA-MRN constitute two DNA end resection machineries for human DNA break repair
    • 21325134 1:CAS:528:DC%2BC3MXjtVait7Y%3D 10.1101/gad.2003811
    • Nimonkar AV, Genschel J, Kinoshita E, Polaczek P, Campbell JL, Wyman C, Modrich P, Kowalczykowski SC (2011) BLM-DNA2-RPA-MRN and EXO1-BLM-RPA-MRN constitute two DNA end resection machineries for human DNA break repair. Genes Dev 25:350-362
    • (2011) Genes Dev , vol.25 , pp. 350-362
    • Nimonkar, A.V.1    Genschel, J.2    Kinoshita, E.3    Polaczek, P.4    Campbell, J.L.5    Wyman, C.6    Modrich, P.7    Kowalczykowski, S.C.8
  • 142
    • 0028342664 scopus 로고
    • Cloning of senescent cell-derived inhibitors of DNA synthesis using an expression screen
    • 8125163 1:CAS:528:DyaK2cXis1ans7g%3D 10.1006/excr.1994.1063
    • Noda A, Ning Y, Venable SF, Pereira-Smith OM, Smith JR (1994) Cloning of senescent cell-derived inhibitors of DNA synthesis using an expression screen. Exp Cell Res 211:90-98
    • (1994) Exp Cell Res , vol.211 , pp. 90-98
    • Noda, A.1    Ning, Y.2    Venable, S.F.3    Pereira-Smith, O.M.4    Smith, J.R.5
  • 143
    • 79955698235 scopus 로고    scopus 로고
    • Accumulating mitochondrial DNA mutations drive premature hematopoietic aging phenotypes distinct from physiological stem cell aging
    • 21549326 1:CAS:528:DC%2BC3MXlvVyntb8%3D 10.1016/j.stem.2011.03.009
    • Norddahl GL, Pronk CJ, Wahlestedt M, Sten G, Nygren JM, Ugale A, Sigvardsson M, Bryder D (2011) Accumulating mitochondrial DNA mutations drive premature hematopoietic aging phenotypes distinct from physiological stem cell aging. Cell Stem Cell 8:499-510
    • (2011) Cell Stem Cell , vol.8 , pp. 499-510
    • Norddahl, G.L.1    Pronk, C.J.2    Wahlestedt, M.3    Sten, G.4    Nygren, J.M.5    Ugale, A.6    Sigvardsson, M.7    Bryder, D.8
  • 144
    • 0028085556 scopus 로고
    • XPG endonuclease makes the 3′ incision in human DNA nucleotide excision repair
    • 8090225 10.1038/371432a0
    • O'Donovan A, Davies AA, Moggs JG, West SC, Wood RD (1994) XPG endonuclease makes the 3′ incision in human DNA nucleotide excision repair. Nature 371:432-435
    • (1994) Nature , vol.371 , pp. 432-435
    • O'Donovan, A.1    Davies, A.A.2    Moggs, J.G.3    West, S.C.4    Wood, R.D.5
  • 145
    • 18744377469 scopus 로고    scopus 로고
    • Mammalian mitochondrial endonuclease G. Digestion of R-loops and localization in intermembrane space
    • 12444964 1:CAS:528:DC%2BD38XpsVOqtrg%3D 10.1046/j.1432-1033.2002.03238.x
    • Ohsato T, Ishihara N, Muta T, Umeda S, Ikeda S, Mihara K, Hamasaki N, Kang D (2002) Mammalian mitochondrial endonuclease G. Digestion of R-loops and localization in intermembrane space. Eur J Biochem 269:5765-5770
    • (2002) Eur J Biochem , vol.269 , pp. 5765-5770
    • Ohsato, T.1    Ishihara, N.2    Muta, T.3    Umeda, S.4    Ikeda, S.5    Mihara, K.6    Hamasaki, N.7    Kang, D.8
  • 146
    • 0037175018 scopus 로고    scopus 로고
    • Telomere-binding protein TRF2 binds to and stimulates the Werner and Bloom syndrome helicases
    • 12181313 1:CAS:528:DC%2BD38XnvFyms7c%3D 10.1074/jbc.M205396200
    • Opresko PL, von Kobbe C, Laine JP, Harrigan J, Hickson ID, Bohr VA (2002) Telomere-binding protein TRF2 binds to and stimulates the Werner and Bloom syndrome helicases. J Biol Chem 277:41110-41119
    • (2002) J Biol Chem , vol.277 , pp. 41110-41119
    • Opresko, P.L.1    Von Kobbe, C.2    Laine, J.P.3    Harrigan, J.4    Hickson, I.D.5    Bohr, V.A.6
  • 147
    • 2942637828 scopus 로고    scopus 로고
    • The Werner syndrome helicase and exonuclease cooperate to resolve telomeric D loops in a manner regulated by TRF1 and TRF2
    • 15200954 1:CAS:528:DC%2BD2cXlslemtr0%3D 10.1016/j.molcel.2004.05.023
    • Opresko PL, Otterlei M, Graakjaer J, Bruheim P, Dawut L, Kolvraa S, May A, Seidman MM, Bohr VA (2004) The Werner syndrome helicase and exonuclease cooperate to resolve telomeric D loops in a manner regulated by TRF1 and TRF2. Mol Cell 14:763-774
    • (2004) Mol Cell , vol.14 , pp. 763-774
    • Opresko, P.L.1    Otterlei, M.2    Graakjaer, J.3    Bruheim, P.4    Dawut, L.5    Kolvraa, S.6    May, A.7    Seidman, M.M.8    Bohr, V.A.9
  • 148
    • 25444533047 scopus 로고    scopus 로고
    • POT1 stimulates RecQ helicases WRN and BLM to unwind telomeric DNA substrates
    • 16030011 1:CAS:528:DC%2BD2MXpvVyrtbc%3D 10.1074/jbc.M505211200
    • Opresko PL, Mason PA, Podell ER, Lei M, Hickson ID, Cech TR, Bohr VA (2005) POT1 stimulates RecQ helicases WRN and BLM to unwind telomeric DNA substrates. J Biol Chem 280:32069-32080
    • (2005) J Biol Chem , vol.280 , pp. 32069-32080
    • Opresko, P.L.1    Mason, P.A.2    Podell, E.R.3    Lei, M.4    Hickson, I.D.5    Cech, T.R.6    Bohr, V.A.7
  • 149
    • 79953838905 scopus 로고    scopus 로고
    • Structures of human exonuclease 1 DNA complexes suggest a unified mechanism for nuclease family
    • 21496642 1:CAS:528:DC%2BC3MXkvVGlsbs%3D 10.1016/j.cell.2011.03.005
    • Orans J, McSweeney EA, Iyer RR, Hast MA, Hellinga HW, Modrich P, Beese LS (2011) Structures of human exonuclease 1 DNA complexes suggest a unified mechanism for nuclease family. Cell 145:212-223
    • (2011) Cell , vol.145 , pp. 212-223
    • Orans, J.1    McSweeney, E.A.2    Iyer, R.R.3    Hast, M.A.4    Hellinga, H.W.5    Modrich, P.6    Beese, L.S.7
  • 150
    • 0032540926 scopus 로고    scopus 로고
    • A human homologue of the Schizosaccharomyces pombe rad1+ checkpoint gene encodes an exonuclease
    • 9660799 1:CAS:528:DyaK1cXkvVCgsrg%3D 10.1074/jbc.273.29.18332
    • Parker AE, Van de Weyer I, Laus MC, Oostveen I, Yon J, Verhasselt P, Luyten WH (1998) A human homologue of the Schizosaccharomyces pombe rad1+ checkpoint gene encodes an exonuclease. J Biol Chem 273:18332-18339
    • (1998) J Biol Chem , vol.273 , pp. 18332-18339
    • Parker, A.E.1    Van De Weyer, I.2    Laus, M.C.3    Oostveen, I.4    Yon, J.5    Verhasselt, P.6    Luyten, W.H.7
  • 152
    • 0032085295 scopus 로고    scopus 로고
    • The 3′ to 5′ exonuclease activity of Mre 11 facilitates repair of DNA double-strand breaks
    • 9651580 1:CAS:528:DyaK1cXktlKltLk%3D 10.1016/S1097-2765(00)80097-0
    • Paull TT, Gellert M (1998) The 3′ to 5′ exonuclease activity of Mre 11 facilitates repair of DNA double-strand breaks. Mol Cell 1:969-979
    • (1998) Mol Cell , vol.1 , pp. 969-979
    • Paull, T.T.1    Gellert, M.2
  • 153
    • 30944452765 scopus 로고    scopus 로고
    • Evidence that errors made by DNA polymerase alpha are corrected by DNA polymerase delta
    • 16431373 1:CAS:528:DC%2BD28Xosl2lsg%3D%3D 10.1016/j.cub.2005.12.002
    • Pavlov YI, Frahm C, Nick McElhinny SA, Niimi A, Suzuki M, Kunkel TA (2006) Evidence that errors made by DNA polymerase alpha are corrected by DNA polymerase delta. Curr Biol 16:202-207
    • (2006) Curr Biol , vol.16 , pp. 202-207
    • Pavlov, Y.I.1    Frahm, C.2    Nick McElhinny, S.A.3    Niimi, A.4    Suzuki, M.5    Kunkel, T.A.6
  • 154
    • 0025315748 scopus 로고
    • Hydrolysis of 3′-terminal mispairs in vitro by the 3′-5′ exonuclease of DNA polymerase delta permits subsequent extension by DNA polymerase alpha
    • 2166556 1:CAS:528:DyaK3cXitlWltL0%3D 10.1021/bi00474a002
    • Perrino FW, Loeb LA (1990) Hydrolysis of 3′-terminal mispairs in vitro by the 3′-5′ exonuclease of DNA polymerase delta permits subsequent extension by DNA polymerase alpha. Biochemistry 29:5226-5231
    • (1990) Biochemistry , vol.29 , pp. 5226-5231
    • Perrino, F.W.1    Loeb, L.A.2
  • 156
    • 0242582500 scopus 로고    scopus 로고
    • Biochemical characterization of an exonuclease from Arabidopsis thaliana reveals similarities to the DNA exonuclease of the human Werner syndrome protein
    • 12937173 1:CAS:528:DC%2BD3sXoslWmtrg%3D 10.1074/jbc.M303891200
    • Plchova H, Hartung F, Puchta H (2003) Biochemical characterization of an exonuclease from Arabidopsis thaliana reveals similarities to the DNA exonuclease of the human Werner syndrome protein. J Biol Chem 278:44128-44138
    • (2003) J Biol Chem , vol.278 , pp. 44128-44138
    • Plchova, H.1    Hartung, F.2    Puchta, H.3
  • 157
    • 0033580940 scopus 로고    scopus 로고
    • Human exonuclease 1 functionally complements its yeast homologues in DNA recombination, RNA primer removal, and mutation avoidance
    • 10364235 1:CAS:528:DyaK1MXktVylsLs%3D 10.1074/jbc.274.25.17893
    • Qiu J, Qian Y, Chen V, Guan MX, Shen B (1999) Human exonuclease 1 functionally complements its yeast homologues in DNA recombination, RNA primer removal, and mutation avoidance. J Biol Chem 274:17893-17900
    • (1999) J Biol Chem , vol.274 , pp. 17893-17900
    • Qiu, J.1    Qian, Y.2    Chen, V.3    Guan, M.X.4    Shen, B.5
  • 159
    • 0345824623 scopus 로고    scopus 로고
    • Asymmetry of DNA replication fork progression in Werner's syndrome
    • 12882351 10.1046/j.1474-9728.2002.00002.x
    • Rodriguez-Lopez AM, Jackson DA, Iborra F, Cox LS (2002) Asymmetry of DNA replication fork progression in Werner's syndrome. Aging Cell 1:30-39
    • (2002) Aging Cell , vol.1 , pp. 30-39
    • Rodriguez-Lopez, A.M.1    Jackson, D.A.2    Iborra, F.3    Cox, L.S.4
  • 160
    • 0037291821 scopus 로고    scopus 로고
    • Characterisation of the interaction between WRN, the helicase/exonuclease defective in progeroid Werner's syndrome, and an essential replication factor, PCNA
    • 12633936 1:CAS:528:DC%2BD3sXhvFWqs7w%3D 10.1016/S0047-6374(02)00131-8
    • Rodriguez-Lopez AM, Jackson DA, Nehlin JO, Iborra F, Warren AV, Cox LS (2003) Characterisation of the interaction between WRN, the helicase/exonuclease defective in progeroid Werner's syndrome, and an essential replication factor, PCNA. Mech Ageing Dev 124:167-174
    • (2003) Mech Ageing Dev , vol.124 , pp. 167-174
    • Rodriguez-Lopez, A.M.1    Jackson, D.A.2    Nehlin, J.O.3    Iborra, F.4    Warren, A.V.5    Cox, L.S.6
  • 161
    • 33947401804 scopus 로고    scopus 로고
    • Correction of proliferation and drug sensitivity defects in the progeroid Werner's Syndrome by Holliday junction resolution
    • 17378750 1:CAS:528:DC%2BD2sXjtlWntrc%3D 10.1089/rej.2006.0503
    • Rodriguez-Lopez AM, Whitby MC, Borer CM, Bachler MA, Cox LS (2007) Correction of proliferation and drug sensitivity defects in the progeroid Werner's Syndrome by Holliday junction resolution. Rejuvenation Res 10:27-40
    • (2007) Rejuvenation Res , vol.10 , pp. 27-40
    • Rodriguez-Lopez, A.M.1    Whitby, M.C.2    Borer, C.M.3    Bachler, M.A.4    Cox, L.S.5
  • 163
    • 77950265945 scopus 로고    scopus 로고
    • Linking functional decline of telomeres, mitochondria and stem cells during ageing
    • 20336134 1:CAS:528:DC%2BC3cXjvVGlsbo%3D 10.1038/nature08982
    • Sahin E, Depinho RA (2010) Linking functional decline of telomeres, mitochondria and stem cells during ageing. Nature 464:520-528
    • (2010) Nature , vol.464 , pp. 520-528
    • Sahin, E.1    Depinho, R.A.2
  • 164
    • 0036787870 scopus 로고    scopus 로고
    • Homologous recombination resolution defect in Werner syndrome
    • 12242278 1:CAS:528:DC%2BD38XnsFKitro%3D 10.1128/MCB.22.20.6971-6978.2002
    • Saintigny Y, Makienko K, Swanson C, Emond MJ, Monnat RJ Jr (2002) Homologous recombination resolution defect in Werner syndrome. Mol Cell Biol 22:6971-6978
    • (2002) Mol Cell Biol , vol.22 , pp. 6971-6978
    • Saintigny, Y.1    Makienko, K.2    Swanson, C.3    Emond, M.J.4    Monnat, Jr.R.J.5
  • 166
    • 37549044311 scopus 로고    scopus 로고
    • Crystallization and preliminary crystallographic analysis of the catalytic domain of human flap endonuclease 1 in complex with a nicked DNA product: Use of a DPCS kit for efficient protein-DNA complex crystallization
    • 18097100 10.1107/S1744309107065372 1:CAS:528:DC%2BD2sXhsVKrt7vN
    • Sakurai S, Kitano K, Morioka H, Hakoshima T (2008) Crystallization and preliminary crystallographic analysis of the catalytic domain of human flap endonuclease 1 in complex with a nicked DNA product: use of a DPCS kit for efficient protein-DNA complex crystallization. Acta Crystallogr Sect F Struct Biol Cryst Commun 64:39-43
    • (2008) Acta Crystallogr Sect F Struct Biol Cryst Commun , vol.64 , pp. 39-43
    • Sakurai, S.1    Kitano, K.2    Morioka, H.3    Hakoshima, T.4
  • 167
    • 43449117492 scopus 로고    scopus 로고
    • Identification and characterization of a Drosophila ortholog of WRN exonuclease that is required to maintain genome integrity
    • 18346216 1:CAS:528:DC%2BD1cXntFWnt7g%3D 10.1111/j.1474-9726.2008.00388.x
    • Saunders RD, Boubriak I, Clancy DJ, Cox LS (2008) Identification and characterization of a Drosophila ortholog of WRN exonuclease that is required to maintain genome integrity. Aging Cell 7:418-425
    • (2008) Aging Cell , vol.7 , pp. 418-425
    • Saunders, R.D.1    Boubriak, I.2    Clancy, D.J.3    Cox, L.S.4
  • 169
    • 1842452746 scopus 로고    scopus 로고
    • Structural and functional characterization of mitochondrial EndoG, a sugar non-specific nuclease which plays an important role during apoptosis
    • 15066427 1:CAS:528:DC%2BD2cXivVeltro%3D 10.1016/j.jmb.2004.02.069
    • Schafer P, Scholz SR, Gimadutdinow O, Cymerman IA, Bujnicki JM, Ruiz-Carrillo A, Pingoud A, Meiss G (2004) Structural and functional characterization of mitochondrial EndoG, a sugar non-specific nuclease which plays an important role during apoptosis. J Mol Biol 338:217-228
    • (2004) J Mol Biol , vol.338 , pp. 217-228
    • Schafer, P.1    Scholz, S.R.2    Gimadutdinow, O.3    Cymerman, I.A.4    Bujnicki, J.M.5    Ruiz-Carrillo, A.6    Pingoud, A.7    Meiss, G.8
  • 170
    • 0033568292 scopus 로고    scopus 로고
    • Drosophila and human RecQ5 exist in different isoforms generated by alternative splicing
    • 10471747 1:CAS:528:DyaK1MXmsVyjt78%3D 10.1093/nar/27.18.3762
    • Sekelsky JJ, Brodsky MH, Rubin GM, Hawley RS (1999) Drosophila and human RecQ5 exist in different isoforms generated by alternative splicing. Nucleic Acids Res 27:3762-3769
    • (1999) Nucleic Acids Res , vol.27 , pp. 3762-3769
    • Sekelsky, J.J.1    Brodsky, M.H.2    Rubin, G.M.3    Hawley, R.S.4
  • 171
    • 0037593470 scopus 로고    scopus 로고
    • The exonucleolytic and endonucleolytic cleavage activities of human exonuclease 1 are stimulated by an interaction with the carboxyl-terminal region of the Werner syndrome protein
    • 12704184 1:CAS:528:DC%2BD3sXkslygsbo%3D 10.1074/jbc.M212798200
    • Sharma S, Sommers JA, Driscoll HC, Uzdilla L, Wilson TM, Brosh RM Jr (2003) The exonucleolytic and endonucleolytic cleavage activities of human exonuclease 1 are stimulated by an interaction with the carboxyl-terminal region of the Werner syndrome protein. J Biol Chem 278:23487-23496
    • (2003) J Biol Chem , vol.278 , pp. 23487-23496
    • Sharma, S.1    Sommers, J.A.2    Driscoll, H.C.3    Uzdilla, L.4    Wilson, T.M.5    Brosh, Jr.R.M.6
  • 172
    • 42049116919 scopus 로고    scopus 로고
    • The RecQ helicase WRN is required for normal replication fork progression after DNA damage or replication fork arrest
    • 18250621 1:CAS:528:DC%2BD1cXmvVWqt78%3D 10.4161/cc.7.6.5566
    • Sidorova JM, Li N, Folch A, Monnat RJ Jr (2008) The RecQ helicase WRN is required for normal replication fork progression after DNA damage or replication fork arrest. Cell Cycle 7:796-807
    • (2008) Cell Cycle , vol.7 , pp. 796-807
    • Sidorova, J.M.1    Li, N.2    Folch, A.3    Monnat, Jr.R.J.4
  • 173
    • 34447533257 scopus 로고    scopus 로고
    • Deficient mismatch repair improves organismal fitness and survival of mice with dysfunctional telomeres
    • 17785530 1:CAS:528:DC%2BD2sXhtVaks73J 10.1101/gad.430107
    • Siegl-Cachedenier I, Munoz P, Flores JM, Klatt P, Blasco MA (2007) Deficient mismatch repair improves organismal fitness and survival of mice with dysfunctional telomeres. Genes Dev 21:2234-2247
    • (2007) Genes Dev , vol.21 , pp. 2234-2247
    • Siegl-Cachedenier, I.1    Munoz, P.2    Flores, J.M.3    Klatt, P.4    Blasco, M.A.5
  • 174
    • 0034682754 scopus 로고    scopus 로고
    • A 3′-5′ exonuclease in human leukemia cells: Implications for resistance to 1-beta-D-arabinofuranosylcytosine and 9-beta-D-arabinofuranosyl- 2-fluoroadenine 5′-monophosphate
    • 10833512 1:CAS:528:DC%2BD3cXmtVehtLo%3D 10.1074/jbc.M001460200
    • Skalski V, Brown KR, Choi BY, Lin ZY, Chen S (2000) A 3′-5′ exonuclease in human leukemia cells: implications for resistance to 1-beta-D-arabinofuranosylcytosine and 9-beta-D-arabinofuranosyl-2-fluoroadenine 5′-monophosphate. J Biol Chem 275:25814-25819
    • (2000) J Biol Chem , vol.275 , pp. 25814-25819
    • Skalski, V.1    Brown, K.R.2    Choi, B.Y.3    Lin, Z.Y.4    Chen, S.5
  • 177
    • 3242891189 scopus 로고    scopus 로고
    • The Mre11 complex and the metabolism of chromosome breaks: The importance of communicating and holding things together
    • 1:CAS:528:DC%2BD2cXmtVeqsb0%3D 10.1016/j.dnarep.2004.03.014
    • Stracker TH, Theunissen JW, Morales M, Petrini JH (2004) The Mre11 complex and the metabolism of chromosome breaks: the importance of communicating and holding things together. DNA Repair (Amst) 3:845-854
    • (2004) DNA Repair (Amst) , vol.3 , pp. 845-854
    • Stracker, T.H.1    Theunissen, J.W.2    Morales, M.3    Petrini, J.H.4
  • 178
    • 1842685207 scopus 로고    scopus 로고
    • The Werner syndrome protein has separable recombination and survival functions
    • 1:CAS:528:DC%2BD2cXjtVOjsL8%3D 10.1016/j.dnarep.2004.01.002
    • Swanson C, Saintigny Y, Emond MJ, Monnat RJ Jr (2004) The Werner syndrome protein has separable recombination and survival functions. DNA Repair (Amst) 3:475-482
    • (2004) DNA Repair (Amst) , vol.3 , pp. 475-482
    • Swanson, C.1    Saintigny, Y.2    Emond, M.J.3    Monnat, Jr.R.J.4
  • 179
    • 0036785375 scopus 로고    scopus 로고
    • S-phase-specific interaction of the Fanconi anemia protein, FANCD2, with BRCA1 and RAD51
    • 12239151 1:CAS:528:DC%2BD38XnvVGisL0%3D 10.1182/blood-2002-01-0278
    • Taniguchi T, Garcia-Higuera I, Andreassen PR, Gregory RC, Grompe M, D'Andrea AD (2002) S-phase-specific interaction of the Fanconi anemia protein, FANCD2, with BRCA1 and RAD51. Blood 100:2414-2420
    • (2002) Blood , vol.100 , pp. 2414-2420
    • Taniguchi, T.1    Garcia-Higuera, I.2    Andreassen, P.R.3    Gregory, R.C.4    Grompe, M.5    D'Andrea, A.D.6
  • 180
    • 0029119097 scopus 로고
    • Novel DNA binding motifs in the DNA repair enzyme endonuclease III crystal structure
    • 7664751 1:CAS:528:DyaK2MXnvVekt7o%3D
    • Thayer MM, Ahern H, Xing D, Cunningham RP, Tainer JA (1995) Novel DNA binding motifs in the DNA repair enzyme endonuclease III crystal structure. EMBO J 14:4108-4120
    • (1995) EMBO J , vol.14 , pp. 4108-4120
    • Thayer, M.M.1    Ahern, H.2    Xing, D.3    Cunningham, R.P.4    Tainer, J.A.5
  • 181
    • 1242263318 scopus 로고    scopus 로고
    • Hereditary non-polyposis colorectal cancer and the role of hPMS2 and hEXO1 mutations
    • 14756672 1:STN:280:DC%2BD2c%2FpsVShsA%3D%3D 10.1111/j.1399-0004.2004. 00214.x
    • Thompson E, Meldrum CJ, Crooks R, McPhillips M, Thomas L, Spigelman AD, Scott RJ (2004) Hereditary non-polyposis colorectal cancer and the role of hPMS2 and hEXO1 mutations. Clin Genet 65:215-225
    • (2004) Clin Genet , vol.65 , pp. 215-225
    • Thompson, E.1    Meldrum, C.J.2    Crooks, R.3    McPhillips, M.4    Thomas, L.5    Spigelman, A.D.6    Scott, R.J.7
  • 182
    • 1542284083 scopus 로고    scopus 로고
    • Deficiency in the nuclease activity of xeroderma pigmentosum G in mice leads to hypersensitivity to UV irradiation
    • 14993263 1:CAS:528:DC%2BD2cXitVWqsbw%3D 10.1128/MCB.24.6.2237-2242.2004
    • Tian M, Jones DA, Smith M, Shinkura R, Alt FW (2004) Deficiency in the nuclease activity of xeroderma pigmentosum G in mice leads to hypersensitivity to UV irradiation. Mol Cell Biol 24:2237-2242
    • (2004) Mol Cell Biol , vol.24 , pp. 2237-2242
    • Tian, M.1    Jones, D.A.2    Smith, M.3    Shinkura, R.4    Alt, F.W.5
  • 183
    • 0030806219 scopus 로고    scopus 로고
    • Identification and characterization of Saccharomyces cerevisiae EXO1, a gene encoding an exonuclease that interacts with MSH2
    • 9207118 1:CAS:528:DyaK2sXksFyht7g%3D 10.1073/pnas.94.14.7487
    • Tishkoff DX, Boerger AL, Bertrand P, Filosi N, Gaida GM, Kane MF, Kolodner RD (1997) Identification and characterization of Saccharomyces cerevisiae EXO1, a gene encoding an exonuclease that interacts with MSH2. Proc Natl Acad Sci U S A 94:7487-7492
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 7487-7492
    • Tishkoff, D.X.1    Boerger, A.L.2    Bertrand, P.3    Filosi, N.4    Gaida, G.M.5    Kane, M.F.6    Kolodner, R.D.7
  • 184
    • 0032533518 scopus 로고    scopus 로고
    • Identification of a human gene encoding a homologue of Saccharomyces cerevisiae EXO1, an exonuclease implicated in mismatch repair and recombination
    • 9823303 1:CAS:528:DyaK1cXnsFSmtr8%3D
    • Tishkoff DX, Amin NS, Viars CS, Arden KC, Kolodner RD (1998) Identification of a human gene encoding a homologue of Saccharomyces cerevisiae EXO1, an exonuclease implicated in mismatch repair and recombination. Cancer Res 58:5027-5031
    • (1998) Cancer Res , vol.58 , pp. 5027-5031
    • Tishkoff, D.X.1    Amin, N.S.2    Viars, C.S.3    Arden, K.C.4    Kolodner, R.D.5
  • 185
    • 4043133233 scopus 로고    scopus 로고
    • The human Rad9/Rad1/Hus1 damage sensor clamp interacts with DNA polymerase beta and increases its DNA substrate utilisation efficiency: Implications for DNA repair
    • 15314187 1:CAS:528:DC%2BD2cXltlyju70%3D 10.1093/nar/gkh652
    • Toueille M, El-Andaloussi N, Frouin I, Freire R, Funk D, Shevelev I, Friedrich-Heineken E, Villani G, Hottiger MO, Hubscher U (2004) The human Rad9/Rad1/Hus1 damage sensor clamp interacts with DNA polymerase beta and increases its DNA substrate utilisation efficiency: implications for DNA repair. Nucleic Acids Res 32:3316-3324
    • (2004) Nucleic Acids Res , vol.32 , pp. 3316-3324
    • Toueille, M.1    El-Andaloussi, N.2    Frouin, I.3    Freire, R.4    Funk, D.5    Shevelev, I.6    Friedrich-Heineken, E.7    Villani, G.8    Hottiger, M.O.9    Hubscher, U.10
  • 186
    • 0032588388 scopus 로고    scopus 로고
    • The 3′→5′ exonucleases of DNA polymerases delta and epsilon and the 5′→3′ exonuclease Exo1 have major roles in postreplication mutation avoidance in Saccharomyces cerevisiae
    • 10022887 1:CAS:528:DyaK1MXhsFeqtbk%3D
    • Tran HT, Gordenin DA, Resnick MA (1999) The 3′→5′ exonucleases of DNA polymerases delta and epsilon and the 5′→3′ exonuclease Exo1 have major roles in postreplication mutation avoidance in Saccharomyces cerevisiae. Mol Cell Biol 19:2000-2007
    • (1999) Mol Cell Biol , vol.19 , pp. 2000-2007
    • Tran, H.T.1    Gordenin, D.A.2    Resnick, M.A.3
  • 189
    • 0033915812 scopus 로고    scopus 로고
    • Exo1 roles for repair of DNA double-strand breaks and meiotic crossing over in Saccharomyces cerevisiae
    • 10888664 1:CAS:528:DC%2BD3cXkvFCitb4%3D
    • Tsubouchi H, Ogawa H (2000) Exo1 roles for repair of DNA double-strand breaks and meiotic crossing over in Saccharomyces cerevisiae. Mol Biol Cell 11:2221-2233
    • (2000) Mol Biol Cell , vol.11 , pp. 2221-2233
    • Tsubouchi, H.1    Ogawa, H.2
  • 191
    • 0024296644 scopus 로고
    • Sequence and expression of NUC1, the gene encoding the mitochondrial nuclease in Saccharomyces cerevisiae
    • 2836792 1:CAS:528:DyaL1cXmt1elsLs%3D 10.1093/nar/16.8.3297
    • Vincent RD, Hofmann TJ, Zassenhaus HP (1988) Sequence and expression of NUC1, the gene encoding the mitochondrial nuclease in Saccharomyces cerevisiae. Nucleic Acids Res 16:3297-3312
    • (1988) Nucleic Acids Res , vol.16 , pp. 3297-3312
    • Vincent, R.D.1    Hofmann, T.J.2    Zassenhaus, H.P.3
  • 192
    • 0033534613 scopus 로고    scopus 로고
    • Human homologs of Schizosaccharomyces pombe rad1, hus1, and rad9 form a DNA damage-responsive protein complex
    • 9872989 1:CAS:528:DyaK1MXmtFGgsg%3D%3D 10.1074/jbc.274.2.567
    • Volkmer E, Karnitz LM (1999) Human homologs of Schizosaccharomyces pombe rad1, hus1, and rad9 form a DNA damage-responsive protein complex. J Biol Chem 274:567-570
    • (1999) J Biol Chem , vol.274 , pp. 567-570
    • Volkmer, E.1    Karnitz, L.M.2
  • 193
    • 65349103899 scopus 로고    scopus 로고
    • Blinded by the light: The growing complexity of p53
    • 19410540 1:CAS:528:DC%2BD1MXlvFams74%3D 10.1016/j.cell.2009.04.037
    • Vousden KH, Prives C (2009) Blinded by the light: the growing complexity of p53. Cell 137:413-431
    • (2009) Cell , vol.137 , pp. 413-431
    • Vousden, K.H.1    Prives, C.2
  • 194
    • 0028363546 scopus 로고
    • Reconstitution of complete SV40 DNA replication with purified replication factors
    • 8144677 1:CAS:528:DyaK2cXjtFOrtL8%3D
    • Waga S, Bauer G, Stillman B (1994) Reconstitution of complete SV40 DNA replication with purified replication factors. J Biol Chem 269:10923-10934
    • (1994) J Biol Chem , vol.269 , pp. 10923-10934
    • Waga, S.1    Bauer, G.2    Stillman, B.3
  • 196
    • 0030913166 scopus 로고    scopus 로고
    • Homologous regions of Fen1 and p21Cip1 compete for binding to the same site on PCNA: A potential mechanism to co-ordinate DNA replication and repair
    • 9178907 1:CAS:528:DyaK2sXjs1Kqsrc%3D 10.1038/sj.onc.1201072
    • Warbrick E, Lane DP, Glover DM, Cox LS (1997) Homologous regions of Fen1 and p21Cip1 compete for binding to the same site on PCNA: a potential mechanism to co-ordinate DNA replication and repair. Oncogene 14:2313-2321
    • (1997) Oncogene , vol.14 , pp. 2313-2321
    • Warbrick, E.1    Lane, D.P.2    Glover, D.M.3    Cox, L.S.4
  • 197
    • 0345708269 scopus 로고    scopus 로고
    • Evidence that yeast SGS1, DNA2, SRS2, and FOB1 interact to maintain rDNA stability
    • 14643435 1:CAS:528:DC%2BD3sXpt1ertbs%3D 10.1016/j.mrfmmm.2003.08.015
    • Weitao T, Budd M, Campbell JL (2003a) Evidence that yeast SGS1, DNA2, SRS2, and FOB1 interact to maintain rDNA stability. Mutat Res 532:157-172
    • (2003) Mutat Res , vol.532 , pp. 157-172
    • Weitao, T.1    Budd, M.2    Campbell, J.L.3
  • 198
    • 0038604455 scopus 로고    scopus 로고
    • Dna2 helicase/nuclease causes replicative fork stalling and double-strand breaks in the ribosomal DNA of Saccharomyces cerevisiae
    • 12686542 10.1074/jbc.M301610200 1:CAS:528:DC%2BD3sXksF2isbg%3D
    • Weitao T, Budd M, Hoopes LL, Campbell JL (2003b) Dna2 helicase/nuclease causes replicative fork stalling and double-strand breaks in the ribosomal DNA of Saccharomyces cerevisiae. J Biol Chem 278:22513-22522
    • (2003) J Biol Chem , vol.278 , pp. 22513-22522
    • Weitao, T.1    Budd, M.2    Hoopes, L.L.3    Campbell, J.L.4
  • 199
    • 0032771002 scopus 로고    scopus 로고
    • Stability of the human fragile X (CGG)(n) triplet repeat array in Saccharomyces cerevisiae deficient in aspects of DNA metabolism
    • 10409756 1:CAS:528:DyaK1MXkvVKjtr4%3D
    • White PJ, Borts RH, Hirst MC (1999) Stability of the human fragile X (CGG)(n) triplet repeat array in Saccharomyces cerevisiae deficient in aspects of DNA metabolism. Mol Cell Biol 19:5675-5684
    • (1999) Mol Cell Biol , vol.19 , pp. 5675-5684
    • White, P.J.1    Borts, R.H.2    Hirst, M.C.3
  • 200
    • 33845417285 scopus 로고    scopus 로고
    • Tissue specific mutagenic and carcinogenic responses in NER defective mouse models
    • 16769089 1:CAS:528:DC%2BD28Xhtlaqs7bO 10.1016/j.mrfmmm.2005.12.018
    • Wijnhoven SW, Hoogervorst EM, de Waard H, van der Horst GT, van Steeg H (2007) Tissue specific mutagenic and carcinogenic responses in NER defective mouse models. Mutat Res 614:77-94
    • (2007) Mutat Res , vol.614 , pp. 77-94
    • Wijnhoven, S.W.1    Hoogervorst, E.M.2    De Waard, H.3    Van Der Horst, G.T.4    Van Steeg, H.5
  • 201
    • 24944494068 scopus 로고    scopus 로고
    • A nanomachine for making ends meet: MRN is a flexing scaffold for the repair of DNA double-strand breaks
    • 16168369 1:CAS:528:DC%2BD2MXhtVyhtb%2FI 10.1016/j.molcel.2005.07.006
    • Williams RS, Tainer JA (2005) A nanomachine for making ends meet: MRN is a flexing scaffold for the repair of DNA double-strand breaks. Mol Cell 19:724-726
    • (2005) Mol Cell , vol.19 , pp. 724-726
    • Williams, R.S.1    Tainer, J.A.2
  • 202
    • 0038690166 scopus 로고    scopus 로고
    • Properties of and substrate determinants for the exonuclease activity of human apurinic endonuclease Ape1
    • 12860125 1:CAS:528:DC%2BD3sXlt1aqu74%3D 10.1016/S0022-2836(03)00712-5
    • Wilson DM, III (2003) Properties of and substrate determinants for the exonuclease activity of human apurinic endonuclease Ape1. J Mol Biol 330:1027-1037
    • (2003) J Mol Biol , vol.330 , pp. 1027-1037
    • Wilson III, D.M.1
  • 204
    • 68949137117 scopus 로고    scopus 로고
    • Structure and functional implications of the human rad9-hus1-rad1 cell cycle checkpoint complex
    • 19535328 1:CAS:528:DC%2BD1MXovFWrs7Y%3D 10.1074/jbc.C109.022384
    • Xu M, Bai L, Gong Y, Xie W, Hang H, Jiang T (2009) Structure and functional implications of the human rad9-hus1-rad1 cell cycle checkpoint complex. J Biol Chem 284:20457-20461
    • (2009) J Biol Chem , vol.284 , pp. 20457-20461
    • Xu, M.1    Bai, L.2    Gong, Y.3    Xie, W.4    Hang, H.5    Jiang, T.6
  • 205
    • 79952282182 scopus 로고    scopus 로고
    • Chemical-induced cancer incidence and underlying mechanisms in Fen1 mutant mice
    • 20972458 1:CAS:528:DC%2BC3cXhtlagsr%2FN 10.1038/onc.2010.482
    • Xu H, Zheng L, Dai H, Zhou M, Hua Y, Shen B (2011) Chemical-induced cancer incidence and underlying mechanisms in Fen1 mutant mice. Oncogene 30:1072-1081
    • (2011) Oncogene , vol.30 , pp. 1072-1081
    • Xu, H.1    Zheng, L.2    Dai, H.3    Zhou, M.4    Hua, Y.5    Shen, B.6
  • 206
    • 0032555220 scopus 로고    scopus 로고
    • Bloom's and Werner's syndrome genes suppress hyperrecombination in yeast sgs1 mutant: Implication for genomic instability in human diseases
    • 9671747 1:CAS:528:DyaK1cXkvFalsLk%3D 10.1073/pnas.95.15.8733
    • Yamagata K, Kato J, Shimamoto A, Goto M, Furuichi Y, Ikeda H (1998) Bloom's and Werner's syndrome genes suppress hyperrecombination in yeast sgs1 mutant: implication for genomic instability in human diseases. Proc Natl Acad Sci U S A 95:8733-8738
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 8733-8738
    • Yamagata, K.1    Kato, J.2    Shimamoto, A.3    Goto, M.4    Furuichi, Y.5    Ikeda, H.6
  • 207
    • 36248988008 scopus 로고    scopus 로고
    • Trex1 exonuclease degrades ssDNA to prevent chronic checkpoint activation and autoimmune disease
    • 18045533 1:CAS:528:DC%2BD2sXhsVCntbbL 10.1016/j.cell.2007.10.017
    • Yang YG, Lindahl T, Barnes DE (2007) Trex1 exonuclease degrades ssDNA to prevent chronic checkpoint activation and autoimmune disease. Cell 131:873-886
    • (2007) Cell , vol.131 , pp. 873-886
    • Yang, Y.G.1    Lindahl, T.2    Barnes, D.E.3
  • 210
    • 0028012341 scopus 로고
    • Analysis of the role of the NUC1 endo/exonuclease in yeast mitochondrial DNA recombination
    • 8087883 1:CAS:528:DyaK2cXksFelt7g%3D 10.1007/BF00309540
    • Zassenhaus HP, Denniger G (1994) Analysis of the role of the NUC1 endo/exonuclease in yeast mitochondrial DNA recombination. Curr Genet 25:142-149
    • (1994) Curr Genet , vol.25 , pp. 142-149
    • Zassenhaus, H.P.1    Denniger, G.2
  • 211
  • 212
    • 21444436726 scopus 로고    scopus 로고
    • Novel function of the flap endonuclease 1 complex in processing stalled DNA replication forks
    • 15592449 1:CAS:528:DC%2BD2MXitVertw%3D%3D 10.1038/sj.embor.7400313
    • Zheng L, Zhou M, Chai Q, Parrish J, Xue D, Patrick SM, Turchi JJ, Yannone SM, Chen D, Shen B (2005) Novel function of the flap endonuclease 1 complex in processing stalled DNA replication forks. EMBO Rep 6:83-89
    • (2005) EMBO Rep , vol.6 , pp. 83-89
    • Zheng, L.1    Zhou, M.2    Chai, Q.3    Parrish, J.4    Xue, D.5    Patrick, S.M.6    Turchi, J.J.7    Yannone, S.M.8    Chen, D.9    Shen, B.10
  • 214
    • 55049112210 scopus 로고    scopus 로고
    • Human DNA2 is a mitochondrial nuclease/helicase for efficient processing of DNA replication and repair intermediates
    • 18995831 1:CAS:528:DC%2BD1cXhsVSms77F 10.1016/j.molcel.2008.09.024
    • Zheng L, Zhou M, Guo Z, Lu H, Qian L, Dai H, Qiu J, Yakubovskaya E, Bogenhagen DF, Demple B, Shen B (2008) Human DNA2 is a mitochondrial nuclease/helicase for efficient processing of DNA replication and repair intermediates. Mol Cell 32:325-336
    • (2008) Mol Cell , vol.32 , pp. 325-336
    • Zheng, L.1    Zhou, M.2    Guo, Z.3    Lu, H.4    Qian, L.5    Dai, H.6    Qiu, J.7    Yakubovskaya, E.8    Bogenhagen, D.F.9    Demple, B.10    Shen, B.11


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.