메뉴 건너뛰기




Volumn 19, Issue , 2014, Pages 95-107

The cutting edges in DNA repair, licensing, and fidelity: DNA and RNA repair nucleases sculpt DNA to measure twice, cut once

Author keywords

APE1; Base excision repair; Crystallography; DNA; DNA repair; DNase; Double strand break repair; EndoIV; Endonucleases; EndoV; Enzyme DNA complex; Exo1; Exonuclease; FEN1; Genome maintenance; Magnesium; Manganese; Metals; Mismatch repair; Mre11; Nfi; Nfo; Nucleases; Nucleotide incision repair; RNA; RNase; Structure specific nuclease; TDP2; Telomere; UVDE; Vsr; Zinc

Indexed keywords

APURINIC ENDONUCLEASE 1; DEOXYRIBONUCLEASE; DEOXYRIBONUCLEASE I; ENDONUCLEASE; ENDONUCLEASE V; EXONUCLEASE; EXONUCLEASE 1; FLAP ENDONUCLEASE; PHOSPHODIESTERASE; POLYDEOXYRIBONUCLEOTIDE SYNTHASE; RIBONUCLEASE; UNCLASSIFIED DRUG; VERY SHORT PATCH REPAIR ENDONUCLEASE; APEX1 PROTEIN, HUMAN; DEOXYRIBONUCLEASE (PYRIMIDINE DIMER); DEOXYRIBONUCLEASE IV; DNA (APURINIC OR APYRIMIDINIC SITE) LYASE; DNA BINDING PROTEIN; FEN1 PROTEIN, HUMAN; MULTIENZYME COMPLEX; NUCLEAR PROTEIN; TDP2 PROTEIN, HUMAN; TRANSCRIPTION FACTOR; UV ENDONUCLEASE; VSR ENDONUCLEASE;

EID: 84902119190     PISSN: 15687864     EISSN: 15687856     Source Type: Journal    
DOI: 10.1016/j.dnarep.2014.03.022     Document Type: Article
Times cited : (78)

References (139)
  • 1
    • 0016402401 scopus 로고
    • The double helix: a personal view
    • Crick F. The double helix: a personal view. Nature 1974, 248:766-769.
    • (1974) Nature , vol.248 , pp. 766-769
    • Crick, F.1
  • 2
    • 0014462494 scopus 로고
    • DNA modification and restriction
    • Arber W., Linn S. DNA modification and restriction. Annu. Rev. Biochem. 1969, 38:467-500.
    • (1969) Annu. Rev. Biochem. , vol.38 , pp. 467-500
    • Arber, W.1    Linn, S.2
  • 3
    • 0014277562 scopus 로고
    • Host specificity of DNA produced by Escherichia coli, X. In vitro restriction of phage fd replicative form
    • Linn S., Arber W. Host specificity of DNA produced by Escherichia coli, X. In vitro restriction of phage fd replicative form. Proc. Nat. Acad. Sci. U.S.A. 1968, 59:1300-1306.
    • (1968) Proc. Nat. Acad. Sci. U.S.A. , vol.59 , pp. 1300-1306
    • Linn, S.1    Arber, W.2
  • 4
    • 84891061856 scopus 로고    scopus 로고
    • The awakening of DNA repair at Yale
    • Hanawalt P.C. The awakening of DNA repair at Yale. Yale J. Biol. Med. 2013, 86:517-523.
    • (2013) Yale J. Biol. Med. , vol.86 , pp. 517-523
    • Hanawalt, P.C.1
  • 5
    • 0028335180 scopus 로고
    • Functional domains within FEN-1 and RAD2 define a family of structure-specific endonucleases: implications for nucleotide excision repair
    • Harrington J.J., Lieber M.R. Functional domains within FEN-1 and RAD2 define a family of structure-specific endonucleases: implications for nucleotide excision repair. Genes Dev. 1994, 8:1344-1355.
    • (1994) Genes Dev. , vol.8 , pp. 1344-1355
    • Harrington, J.J.1    Lieber, M.R.2
  • 6
    • 0028917289 scopus 로고
    • DNA structural elements required for FEN-1 binding
    • Harrington J.J., Lieber M.R. DNA structural elements required for FEN-1 binding. J. Biol. Chem. 1995, 270:4503-4508.
    • (1995) J. Biol. Chem. , vol.270 , pp. 4503-4508
    • Harrington, J.J.1    Lieber, M.R.2
  • 7
    • 24044460415 scopus 로고    scopus 로고
    • DNA base damage recognition and removal: new twists and grooves
    • Huffman J.L., Sundheim O., Tainer J.A. DNA base damage recognition and removal: new twists and grooves. Mutat. Res. 2005, 577:55-76.
    • (2005) Mutat. Res. , vol.577 , pp. 55-76
    • Huffman, J.L.1    Sundheim, O.2    Tainer, J.A.3
  • 8
    • 0027376095 scopus 로고
    • Resolution of Holliday junctions by RuvC resolvase: cleavage specificity and DNA distortion
    • Bennett R.J., Dunderdale H.J., West S.C. Resolution of Holliday junctions by RuvC resolvase: cleavage specificity and DNA distortion. Cell 1993, 74:1021-1031.
    • (1993) Cell , vol.74 , pp. 1021-1031
    • Bennett, R.J.1    Dunderdale, H.J.2    West, S.C.3
  • 13
    • 44149094083 scopus 로고    scopus 로고
    • XPD helicase structures and activities: insights into the cancer and aging phenotypes from XPD mutations
    • Fan L., Fuss J.O., Cheng Q.J., Arvai A.S., Hammel M., Roberts V.A., Cooper P.K., Tainer J.A. XPD helicase structures and activities: insights into the cancer and aging phenotypes from XPD mutations. Cell 2008, 133:789-800.
    • (2008) Cell , vol.133 , pp. 789-800
    • Fan, L.1    Fuss, J.O.2    Cheng, Q.J.3    Arvai, A.S.4    Hammel, M.5    Roberts, V.A.6    Cooper, P.K.7    Tainer, J.A.8
  • 15
    • 84856699863 scopus 로고    scopus 로고
    • Unpairing and gating: sequence-independent substrate recognition by FEN superfamily nucleases
    • Grasby J.A., Finger L.D., Tsutakawa S.E., Atack J.M., Tainer J.A. Unpairing and gating: sequence-independent substrate recognition by FEN superfamily nucleases. Trends Biochem. Sci. 2012, 37:74-84.
    • (2012) Trends Biochem. Sci. , vol.37 , pp. 74-84
    • Grasby, J.A.1    Finger, L.D.2    Tsutakawa, S.E.3    Atack, J.M.4    Tainer, J.A.5
  • 17
    • 84860722082 scopus 로고    scopus 로고
    • Double strand binding-single strand incision mechanism for human flap endonuclease: implications for the superfamily
    • Tsutakawa S.E., Tainer J.A. Double strand binding-single strand incision mechanism for human flap endonuclease: implications for the superfamily. Mech. Ageing Dev. 2012, 133:195-202.
    • (2012) Mech. Ageing Dev. , vol.133 , pp. 195-202
    • Tsutakawa, S.E.1    Tainer, J.A.2
  • 18
    • 84889004332 scopus 로고    scopus 로고
    • DNA sequences that interfere with transcription: implications for genome function and stability
    • Belotserkovskii B.P., Mirkin S.M., Hanawalt P.C. DNA sequences that interfere with transcription: implications for genome function and stability. Chem. Rev. 2013, 113:8620-8637.
    • (2013) Chem. Rev. , vol.113 , pp. 8620-8637
    • Belotserkovskii, B.P.1    Mirkin, S.M.2    Hanawalt, P.C.3
  • 19
    • 77955095659 scopus 로고    scopus 로고
    • Human AP endonuclease 1 (APE1): from mechanistic insights to druggable target in cancer
    • Abbotts R., Madhusudan S. Human AP endonuclease 1 (APE1): from mechanistic insights to druggable target in cancer. Cancer Treat. Rev. 2010, 36:425-435.
    • (2010) Cancer Treat. Rev. , vol.36 , pp. 425-435
    • Abbotts, R.1    Madhusudan, S.2
  • 20
    • 33847613569 scopus 로고    scopus 로고
    • Oxidative DNA damage repair in mammalian cells: a new perspective
    • Hazra T.K., Das A., Das S., Choudhury S., Kow Y.W., Roy R. Oxidative DNA damage repair in mammalian cells: a new perspective. DNA Repair 2007, 6:470-480.
    • (2007) DNA Repair , vol.6 , pp. 470-480
    • Hazra, T.K.1    Das, A.2    Das, S.3    Choudhury, S.4    Kow, Y.W.5    Roy, R.6
  • 21
    • 38049112778 scopus 로고    scopus 로고
    • Early steps in the DNA base excision/single-strand interruption repair pathway in mammalian cells
    • Hegde M.L., Hazra T.K., Mitra S. Early steps in the DNA base excision/single-strand interruption repair pathway in mammalian cells. Cell Res. 2008, 18:27-47.
    • (2008) Cell Res. , vol.18 , pp. 27-47
    • Hegde, M.L.1    Hazra, T.K.2    Mitra, S.3
  • 23
    • 84892927300 scopus 로고    scopus 로고
    • Human apurinic/apyrimidinic endonuclease 1
    • Li M., Wilson D.M. Human apurinic/apyrimidinic endonuclease 1. Antioxid. Redox Signaling 2013, 20:678-707.
    • (2013) Antioxid. Redox Signaling , vol.20 , pp. 678-707
    • Li, M.1    Wilson, D.M.2
  • 24
    • 33847673237 scopus 로고    scopus 로고
    • The intricate structural chemistry of base excision repair machinery: implications for DNA damage recognition, removal, and repair
    • Hitomi K., Iwai S., Tainer J.A. The intricate structural chemistry of base excision repair machinery: implications for DNA damage recognition, removal, and repair. DNA Repair 2007, 6:410-428.
    • (2007) DNA Repair , vol.6 , pp. 410-428
    • Hitomi, K.1    Iwai, S.2    Tainer, J.A.3
  • 25
    • 0015504248 scopus 로고
    • Rate of depurination of native deoxyribonucleic acid
    • Lindahl T., Nyberg B. Rate of depurination of native deoxyribonucleic acid. Biochemistry 1972, 11:3610-3618.
    • (1972) Biochemistry , vol.11 , pp. 3610-3618
    • Lindahl, T.1    Nyberg, B.2
  • 26
    • 0029829265 scopus 로고    scopus 로고
    • The redox/DNA repair protein, Ref-1, is essential for early embryonic development in mice
    • Xanthoudakis S., Smeyne R.J., Wallace J.D., Curran T. The redox/DNA repair protein, Ref-1, is essential for early embryonic development in mice. Proc. Nat. Acad. Sci. U.S.A. 1996, 93:8919-8923.
    • (1996) Proc. Nat. Acad. Sci. U.S.A. , vol.93 , pp. 8919-8923
    • Xanthoudakis, S.1    Smeyne, R.J.2    Wallace, J.D.3    Curran, T.4
  • 30
    • 0030916372 scopus 로고    scopus 로고
    • Evidence of reduced DNA repair in amyotrophic lateral sclerosis brain tissue
    • Kisby G.E., Milne J., Sweatt C. Evidence of reduced DNA repair in amyotrophic lateral sclerosis brain tissue. Neuroreport 1997, 8:1337-1340.
    • (1997) Neuroreport , vol.8 , pp. 1337-1340
    • Kisby, G.E.1    Milne, J.2    Sweatt, C.3
  • 31
    • 0035130776 scopus 로고    scopus 로고
    • Common polymorphisms and somatic mutations in human base excision repair genes in ovarian and endometrial cancers
    • Pieretti M., Khattar N.H., Smith S.A. Common polymorphisms and somatic mutations in human base excision repair genes in ovarian and endometrial cancers. Mutat. Res. 2001, 432:53-59.
    • (2001) Mutat. Res. , vol.432 , pp. 53-59
    • Pieretti, M.1    Khattar, N.H.2    Smith, S.A.3
  • 32
    • 78149466586 scopus 로고    scopus 로고
    • Small molecule inhibitors of DNA repair nuclease activities of APE1
    • Wilson D.M., Simeonov A. Small molecule inhibitors of DNA repair nuclease activities of APE1. Cell. Mol. Life Sci.: CMLS 2010, 67:3621-3631.
    • (2010) Cell. Mol. Life Sci.: CMLS , vol.67 , pp. 3621-3631
    • Wilson, D.M.1    Simeonov, A.2
  • 33
    • 34548276529 scopus 로고    scopus 로고
    • The DNA base excision repair protein Ape1/Ref-1 as a therapeutic and chemopreventive target
    • Fishel M.L., Kelley M.R. The DNA base excision repair protein Ape1/Ref-1 as a therapeutic and chemopreventive target. Mol. Aspects Med. 2007, 28:375-395.
    • (2007) Mol. Aspects Med. , vol.28 , pp. 375-395
    • Fishel, M.L.1    Kelley, M.R.2
  • 34
    • 78149471195 scopus 로고    scopus 로고
    • Understanding different functions of mammalian AP endonuclease (APE1) as a promising tool for cancer treatment
    • Tell G., Fantini D., Quadrifoglio F. Understanding different functions of mammalian AP endonuclease (APE1) as a promising tool for cancer treatment. Cell. Mol. Life Sci.: CMLS 2010, 67:3589-3608.
    • (2010) Cell. Mol. Life Sci.: CMLS , vol.67 , pp. 3589-3608
    • Tell, G.1    Fantini, D.2    Quadrifoglio, F.3
  • 36
    • 0042470700 scopus 로고    scopus 로고
    • Nuclease-deficient FEN-1 blocks Rad51/BRCA1-mediated repair and causes trinucleotide repeat instability
    • Spiro C., McMurray C.T. Nuclease-deficient FEN-1 blocks Rad51/BRCA1-mediated repair and causes trinucleotide repeat instability. Mol. Cell Biol. 2003, 23:6063-6074.
    • (2003) Mol. Cell Biol. , vol.23 , pp. 6063-6074
    • Spiro, C.1    McMurray, C.T.2
  • 37
    • 0032488872 scopus 로고    scopus 로고
    • Expansion and length-dependent fragility of CTG repeats in yeast
    • Freudenreich C.H., Kantrow S.M., Zakian V.A. Expansion and length-dependent fragility of CTG repeats in yeast. Science 1998, 279:853-856.
    • (1998) Science , vol.279 , pp. 853-856
    • Freudenreich, C.H.1    Kantrow, S.M.2    Zakian, V.A.3
  • 41
    • 84855378612 scopus 로고    scopus 로고
    • Functional FEN1 genetic variants contribute to risk of hepatocellular carcinoma, esophageal cancer, gastric cancer and colorectal cancer
    • Liu L., Zhou C., Zhou L., Peng L., Li D., Zhang X., Zhou M., Kuang P., Yuan Q., Song X., Yang M. Functional FEN1 genetic variants contribute to risk of hepatocellular carcinoma, esophageal cancer, gastric cancer and colorectal cancer. Carcinogenesis 2012, 33:119-123.
    • (2012) Carcinogenesis , vol.33 , pp. 119-123
    • Liu, L.1    Zhou, C.2    Zhou, L.3    Peng, L.4    Li, D.5    Zhang, X.6    Zhou, M.7    Kuang, P.8    Yuan, Q.9    Song, X.10    Yang, M.11
  • 46
    • 0034678917 scopus 로고    scopus 로고
    • Gene expression of flap endonuclease-1 during cell proliferation and differentiation
    • Kim I.S., Lee M.Y., Lee I.H., Shin S.L., Lee S.Y. Gene expression of flap endonuclease-1 during cell proliferation and differentiation. Biochim. Biophys. Acta 2000, 1496:333-340.
    • (2000) Biochim. Biophys. Acta , vol.1496 , pp. 333-340
    • Kim, I.S.1    Lee, M.Y.2    Lee, I.H.3    Shin, S.L.4    Lee, S.Y.5
  • 47
    • 0031788197 scopus 로고    scopus 로고
    • Fen1 expression: a novel marker for cell proliferation
    • Warbrick E., Coates P.J., Hall P.A. Fen1 expression: a novel marker for cell proliferation. J. Pathol. 1998, 186:319-324.
    • (1998) J. Pathol. , vol.186 , pp. 319-324
    • Warbrick, E.1    Coates, P.J.2    Hall, P.A.3
  • 48
    • 69249161787 scopus 로고    scopus 로고
    • FEN1 is overexpressed in testis, lung and brain tumors
    • Nikolova T., Christmann M., Kaina B. FEN1 is overexpressed in testis, lung and brain tumors. Anticancer Res. 2009, 29:2453-2459.
    • (2009) Anticancer Res. , vol.29 , pp. 2453-2459
    • Nikolova, T.1    Christmann, M.2    Kaina, B.3
  • 49
    • 0242551649 scopus 로고    scopus 로고
    • Increased expression and no mutation of the Flap endonuclease (FEN1) gene in human lung cancer
    • Sato M., Girard L., Sekine I., Sunaga N., Ramirez R.D., Kamibayashi C., Minna J.D. Increased expression and no mutation of the Flap endonuclease (FEN1) gene in human lung cancer. Oncogene 2003, 22:7243-7246.
    • (2003) Oncogene , vol.22 , pp. 7243-7246
    • Sato, M.1    Girard, L.2    Sekine, I.3    Sunaga, N.4    Ramirez, R.D.5    Kamibayashi, C.6    Minna, J.D.7
  • 53
    • 84872547120 scopus 로고    scopus 로고
    • Drugging topoisomerases: lessons and challenges
    • Pommier Y. Drugging topoisomerases: lessons and challenges. ACS Chem. Biol. 2013, 8:82-95.
    • (2013) ACS Chem. Biol. , vol.8 , pp. 82-95
    • Pommier, Y.1
  • 55
    • 33645212804 scopus 로고    scopus 로고
    • The time required for water attack at the phosphorus atom of simple phosphodiesters and of DNA
    • Schroeder G.K., Lad C., Wyman P., Williams N.H., Wolfenden R. The time required for water attack at the phosphorus atom of simple phosphodiesters and of DNA. Proc. Nat. Acad. Sci. U.S.A. 2006, 103:4052-4055.
    • (2006) Proc. Nat. Acad. Sci. U.S.A. , vol.103 , pp. 4052-4055
    • Schroeder, G.K.1    Lad, C.2    Wyman, P.3    Williams, N.H.4    Wolfenden, R.5
  • 58
    • 0034734377 scopus 로고    scopus 로고
    • Abasic site recognition by two apurinic/apyrimidinic endonuclease families in DNA base excision repair: the 3' ends justify the means
    • Mol C.D., Hosfield D.J., Tainer J.A. Abasic site recognition by two apurinic/apyrimidinic endonuclease families in DNA base excision repair: the 3' ends justify the means. Mutat. Res. 2000, 460:211-229.
    • (2000) Mutat. Res. , vol.460 , pp. 211-229
    • Mol, C.D.1    Hosfield, D.J.2    Tainer, J.A.3
  • 59
    • 79951678159 scopus 로고    scopus 로고
    • Nucleases: diversity of structure, function and mechanism
    • Yang W. Nucleases: diversity of structure, function and mechanism. Q. Rev. Biophys. 2011, 44:1-93.
    • (2011) Q. Rev. Biophys. , vol.44 , pp. 1-93
    • Yang, W.1
  • 60
    • 43049110531 scopus 로고    scopus 로고
    • Roles of metal ions in nucleases
    • Dupureur C.M. Roles of metal ions in nucleases. Curr. Opin. Chem. Biol. 2008, 12:250-255.
    • (2008) Curr. Opin. Chem. Biol. , vol.12 , pp. 250-255
    • Dupureur, C.M.1
  • 61
    • 0034437606 scopus 로고    scopus 로고
    • New recognition mode for a TG mismatch: the atomic structure of a very short patch repair endonuclease-DNA complex
    • Tsutakawa S.E., Morikawa K. New recognition mode for a TG mismatch: the atomic structure of a very short patch repair endonuclease-DNA complex. Cold Spring Harb. Symp. Quant. Biol. 2000, 65:233-239.
    • (2000) Cold Spring Harb. Symp. Quant. Biol. , vol.65 , pp. 233-239
    • Tsutakawa, S.E.1    Morikawa, K.2
  • 63
    • 0033529716 scopus 로고    scopus 로고
    • Structure of the DNA repair enzyme endonuclease IV and its DNA complex: double-nucleotide flipping at abasic sites and three-metal-ion catalysis
    • Hosfield D.J., Guan Y., Haas B.J., Cunningham R.P., Tainer J.A. Structure of the DNA repair enzyme endonuclease IV and its DNA complex: double-nucleotide flipping at abasic sites and three-metal-ion catalysis. Cell 1999, 98:397-408.
    • (1999) Cell , vol.98 , pp. 397-408
    • Hosfield, D.J.1    Guan, Y.2    Haas, B.J.3    Cunningham, R.P.4    Tainer, J.A.5
  • 64
    • 33846799362 scopus 로고    scopus 로고
    • Unraveling the three-metal-ion catalytic mechanism of the DNA repair enzyme endonuclease IV
    • Ivanov I., Tainer J.A., McCammon J.A. Unraveling the three-metal-ion catalytic mechanism of the DNA repair enzyme endonuclease IV. Proc. Nat. Acad. Sci. U.S.A. 2007, 104:1465-1470.
    • (2007) Proc. Nat. Acad. Sci. U.S.A. , vol.104 , pp. 1465-1470
    • Ivanov, I.1    Tainer, J.A.2    McCammon, J.A.3
  • 65
    • 0037034035 scopus 로고    scopus 로고
    • An exonucleolytic activity of human apurinic/apyrimidinic endonuclease on 3' mispaired DNA
    • Chou K.M., Cheng Y.C. An exonucleolytic activity of human apurinic/apyrimidinic endonuclease on 3' mispaired DNA. Nature 2002, 415:655-659.
    • (2002) Nature , vol.415 , pp. 655-659
    • Chou, K.M.1    Cheng, Y.C.2
  • 66
    • 0345305364 scopus 로고    scopus 로고
    • Characterisation of new substrate specificities of Escherichia coli and Saccharomyces cerevisiae AP endonucleases
    • Ishchenko A.A., Sanz G., Privezentzev C.V., Maksimenko A.V., Saparbaev M. Characterisation of new substrate specificities of Escherichia coli and Saccharomyces cerevisiae AP endonucleases. Nucleic Acids Res. 2003, 31:6344-6353.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 6344-6353
    • Ishchenko, A.A.1    Sanz, G.2    Privezentzev, C.V.3    Maksimenko, A.V.4    Saparbaev, M.5
  • 67
    • 22544450152 scopus 로고    scopus 로고
    • The 3'->5' exonuclease of Apn1 provides an alternative pathway to repair 7,8-dihydro-8-oxodeoxyguanosine in Saccharomyces cerevisiae
    • Ishchenko A.A., Yang X., Ramotar D., Saparbaev M. The 3'->5' exonuclease of Apn1 provides an alternative pathway to repair 7,8-dihydro-8-oxodeoxyguanosine in Saccharomyces cerevisiae. Mol. Cell Biol. 2005, 25:6380-6390.
    • (2005) Mol. Cell Biol. , vol.25 , pp. 6380-6390
    • Ishchenko, A.A.1    Yang, X.2    Ramotar, D.3    Saparbaev, M.4
  • 68
    • 0037049975 scopus 로고    scopus 로고
    • Alternative nucleotide incision repair pathway for oxidative DNA damage
    • Ischenko A.A., Saparbaev M.K. Alternative nucleotide incision repair pathway for oxidative DNA damage. Nature 2002, 415:183-187.
    • (2002) Nature , vol.415 , pp. 183-187
    • Ischenko, A.A.1    Saparbaev, M.K.2
  • 69
    • 0037474210 scopus 로고    scopus 로고
    • Characterization of an endonuclease IV 3'-5' exonuclease activity
    • Kerins S.M., Collins R., McCarthy T.V. Characterization of an endonuclease IV 3'-5' exonuclease activity. J. Biol. Chem. 2003, 278:3048-3054.
    • (2003) J. Biol. Chem. , vol.278 , pp. 3048-3054
    • Kerins, S.M.1    Collins, R.2    McCarthy, T.V.3
  • 72
    • 43049167396 scopus 로고    scopus 로고
    • Characterization of abasic endonuclease activity of human Ape1 on alternative substrates, as well as effects of ATP and sequence context on AP site incision
    • Berquist B.R., McNeill D.R., Wilson D.M. Characterization of abasic endonuclease activity of human Ape1 on alternative substrates, as well as effects of ATP and sequence context on AP site incision. J. Mol. Biol. 2008, 379:17-27.
    • (2008) J. Mol. Biol. , vol.379 , pp. 17-27
    • Berquist, B.R.1    McNeill, D.R.2    Wilson, D.M.3
  • 73
    • 0028923440 scopus 로고
    • Structure and function of the multifunctional DNA-repair enzyme exonuclease III
    • Mol C.D., Kuo C.F., Thayer M.M., Cunningham R.P., Tainer J.A. Structure and function of the multifunctional DNA-repair enzyme exonuclease III. Nature 1995, 374:381-386.
    • (1995) Nature , vol.374 , pp. 381-386
    • Mol, C.D.1    Kuo, C.F.2    Thayer, M.M.3    Cunningham, R.P.4    Tainer, J.A.5
  • 74
    • 0032167424 scopus 로고    scopus 로고
    • Base excision repair initiation revealed by crystal structures and binding kinetics of human uracil-DNA glycosylase with DNA
    • Parikh S.S., Mol C.D., Slupphaug G., Bharati S., Krokan H.E., Tainer J.A. Base excision repair initiation revealed by crystal structures and binding kinetics of human uracil-DNA glycosylase with DNA. EMBO J. 1998, 17:5214-5226.
    • (1998) EMBO J. , vol.17 , pp. 5214-5226
    • Parikh, S.S.1    Mol, C.D.2    Slupphaug, G.3    Bharati, S.4    Krokan, H.E.5    Tainer, J.A.6
  • 75
    • 0034719372 scopus 로고    scopus 로고
    • DNA-bound structures and mutants reveal abasic DNA binding by APE1 and DNA repair coordination
    • Mol C.D., Izumi T., Mitra S., Tainer J.A. DNA-bound structures and mutants reveal abasic DNA binding by APE1 and DNA repair coordination. Nature 2000, 403:451-456.
    • (2000) Nature , vol.403 , pp. 451-456
    • Mol, C.D.1    Izumi, T.2    Mitra, S.3    Tainer, J.A.4
  • 76
  • 79
    • 0033605817 scopus 로고    scopus 로고
    • Protein mimicry of DNA from crystal structures of the uracil-DNA glycosylase inhibitor protein and its complex with Escherichia coli uracil-DNA glycosylase
    • Putnam C.D., Shroyer M.J., Lundquist A.J., Mol C.D., Arvai A.S., Mosbaugh D.W., Tainer J.A. Protein mimicry of DNA from crystal structures of the uracil-DNA glycosylase inhibitor protein and its complex with Escherichia coli uracil-DNA glycosylase. J. Mol. Biol. 1999, 287:331-346.
    • (1999) J. Mol. Biol. , vol.287 , pp. 331-346
    • Putnam, C.D.1    Shroyer, M.J.2    Lundquist, A.J.3    Mol, C.D.4    Arvai, A.S.5    Mosbaugh, D.W.6    Tainer, J.A.7
  • 80
    • 27844526220 scopus 로고    scopus 로고
    • Protein mimicry of DNA and pathway regulation
    • Putnam C.D., Tainer J.A. Protein mimicry of DNA and pathway regulation. DNA Repair 2005, 4:1410-1420.
    • (2005) DNA Repair , vol.4 , pp. 1410-1420
    • Putnam, C.D.1    Tainer, J.A.2
  • 82
    • 0028137259 scopus 로고
    • A new ATP-independent DNA endonuclease from Schizosaccharomyces pombe that recognizes cyclobutane pyrimidine dimers and 6-4 photoproducts
    • Bowman K.K., Sidik K., Smith C.A., Taylor J.S., Doetsch P.W., Freyer G.A. A new ATP-independent DNA endonuclease from Schizosaccharomyces pombe that recognizes cyclobutane pyrimidine dimers and 6-4 photoproducts. Nucleic Acids Res. 1994, 22:3026-3032.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 3026-3032
    • Bowman, K.K.1    Sidik, K.2    Smith, C.A.3    Taylor, J.S.4    Doetsch, P.W.5    Freyer, G.A.6
  • 83
    • 0033151820 scopus 로고    scopus 로고
    • Substrate specificity of ultraviolet DNA endonuclease (UVDE/Uve1p) from Schizosaccharomyces pombe
    • Avery A.M., Kaur B., Taylor J.S., Mello J.A., Essigmann J.M., Doetsch P.W. Substrate specificity of ultraviolet DNA endonuclease (UVDE/Uve1p) from Schizosaccharomyces pombe. Nucleic Acids Res. 1999, 27:2256-2264.
    • (1999) Nucleic Acids Res. , vol.27 , pp. 2256-2264
    • Avery, A.M.1    Kaur, B.2    Taylor, J.S.3    Mello, J.A.4    Essigmann, J.M.5    Doetsch, P.W.6
  • 85
  • 87
    • 0033544707 scopus 로고    scopus 로고
    • Recognition of a TG mismatch: the crystal structure of very short patch repair endonuclease in complex with a DNA duplex
    • Tsutakawa S.E., Jingami H., Morikawa K. Recognition of a TG mismatch: the crystal structure of very short patch repair endonuclease in complex with a DNA duplex. Cell 1999, 99:615-623.
    • (1999) Cell , vol.99 , pp. 615-623
    • Tsutakawa, S.E.1    Jingami, H.2    Morikawa, K.3
  • 89
    • 0034641947 scopus 로고    scopus 로고
    • The crystal structure of DNA mismatch repair protein MutS binding to a G×T mismatch
    • Lamers M.H., Perrakis A., Enzlin J.H., Winterwerp H.H., de Wind N., Sixma T.K. The crystal structure of DNA mismatch repair protein MutS binding to a G×T mismatch. Nature 2000, 407:711-717.
    • (2000) Nature , vol.407 , pp. 711-717
    • Lamers, M.H.1    Perrakis, A.2    Enzlin, J.H.3    Winterwerp, H.H.4    de Wind, N.5    Sixma, T.K.6
  • 90
    • 2342559194 scopus 로고    scopus 로고
    • Functional interactions between the MutL and Vsr proteins of Escherichia coli are dependent on the N-terminus of Vsr
    • Monastiriakos S.K., Doiron K.M., Siponen M.I., Cupples C.G. Functional interactions between the MutL and Vsr proteins of Escherichia coli are dependent on the N-terminus of Vsr. DNA Repair 2004, 3:639-647.
    • (2004) DNA Repair , vol.3 , pp. 639-647
    • Monastiriakos, S.K.1    Doiron, K.M.2    Siponen, M.I.3    Cupples, C.G.4
  • 91
    • 70350064591 scopus 로고    scopus 로고
    • Changes in the conformation of the Vsr endonuclease amino-terminal domain accompany DNA cleavage
    • Polosina Y.Y., Cupples C.G. Changes in the conformation of the Vsr endonuclease amino-terminal domain accompany DNA cleavage. J. Biochem. 2009, 146:523-526.
    • (2009) J. Biochem. , vol.146 , pp. 523-526
    • Polosina, Y.Y.1    Cupples, C.G.2
  • 92
    • 0028032935 scopus 로고
    • Strand-specific cleavage of mismatch-containing DNA by deoxyinosine 3'-endonuclease from Escherichia coli
    • Yao M., Kow Y.W. Strand-specific cleavage of mismatch-containing DNA by deoxyinosine 3'-endonuclease from Escherichia coli. J. Biol. Chem. 1994, 269:31390-31396.
    • (1994) J. Biol. Chem. , vol.269 , pp. 31390-31396
    • Yao, M.1    Kow, Y.W.2
  • 93
    • 0028845857 scopus 로고
    • Interaction of deoxyinosine 3'-endonuclease from Escherichia coli with DNA containing deoxyinosine
    • Yao M., Kow Y.W. Interaction of deoxyinosine 3'-endonuclease from Escherichia coli with DNA containing deoxyinosine. J. Biol. Chem. 1995, 270:28609-28616.
    • (1995) J. Biol. Chem. , vol.270 , pp. 28609-28616
    • Yao, M.1    Kow, Y.W.2
  • 94
    • 10544239535 scopus 로고    scopus 로고
    • Cleavage of insertion/deletion mismatches, flap and pseudo-Y DNA structures by deoxyinosine 3'-endonuclease from Escherichia coli
    • Yao M., Kow Y.W. Cleavage of insertion/deletion mismatches, flap and pseudo-Y DNA structures by deoxyinosine 3'-endonuclease from Escherichia coli. J. Biol. Chem. 1996, 271:30672-30676.
    • (1996) J. Biol. Chem. , vol.271 , pp. 30672-30676
    • Yao, M.1    Kow, Y.W.2
  • 95
    • 1842338079 scopus 로고    scopus 로고
    • Further characterization of Escherichia coli endonuclease V. Mechanism of recognition for deoxyinosine, deoxyuridine, and base mismatches in DNA
    • Yao M., Kow Y.W. Further characterization of Escherichia coli endonuclease V. Mechanism of recognition for deoxyinosine, deoxyuridine, and base mismatches in DNA. J. Biol. Chem. 1997, 272:30774-30779.
    • (1997) J. Biol. Chem. , vol.272 , pp. 30774-30779
    • Yao, M.1    Kow, Y.W.2
  • 96
    • 0035979334 scopus 로고    scopus 로고
    • Multiple cleavage activities of endonuclease V from Thermotoga maritima: recognition and strand nicking mechanism
    • Huang J., Lu J., Barany F., Cao W. Multiple cleavage activities of endonuclease V from Thermotoga maritima: recognition and strand nicking mechanism. Biochemistry 2001, 40:8738-8748.
    • (2001) Biochemistry , vol.40 , pp. 8738-8748
    • Huang, J.1    Lu, J.2    Barany, F.3    Cao, W.4
  • 98
    • 3242875178 scopus 로고    scopus 로고
    • Cleavage of deoxyoxanosine-containing oligodeoxyribonucleotides by bacterial endonuclease V
    • Hitchcock T.M., Gao H., Cao W. Cleavage of deoxyoxanosine-containing oligodeoxyribonucleotides by bacterial endonuclease V. Nucleic Acids Res. 2004, 32:4071-4080.
    • (2004) Nucleic Acids Res. , vol.32 , pp. 4071-4080
    • Hitchcock, T.M.1    Gao, H.2    Cao, W.3
  • 102
    • 79953838905 scopus 로고    scopus 로고
    • Structures of human exonuclease 1 DNA complexes suggest a unified mechanism for nuclease family
    • Orans J., McSweeney E.A., Iyer R.R., Hast M.A., Hellinga H.W., Modrich P., Beese L.S. Structures of human exonuclease 1 DNA complexes suggest a unified mechanism for nuclease family. Cell 2011, 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
  • 105
    • 79960377998 scopus 로고    scopus 로고
    • XPB and XPD helicases in TFIIH orchestrate DNA duplex opening and damage verification to coordinate repair with transcription and cell cycle via CAK kinase
    • Fuss J.O., Tainer J.A. XPB and XPD helicases in TFIIH orchestrate DNA duplex opening and damage verification to coordinate repair with transcription and cell cycle via CAK kinase. DNA Repair 2011, 10:697-713.
    • (2011) DNA Repair , vol.10 , pp. 697-713
    • Fuss, J.O.1    Tainer, J.A.2
  • 107
  • 108
    • 0032567535 scopus 로고    scopus 로고
    • Identification of a potent DNase activity associated with RNase T of Escherichia coli
    • Viswanathan M., Dower K.W., Lovett S.T. Identification of a potent DNase activity associated with RNase T of Escherichia coli. J. Biol. Chem. 1998, 273:35126-35131.
    • (1998) J. Biol. Chem. , vol.273 , pp. 35126-35131
    • Viswanathan, M.1    Dower, K.W.2    Lovett, S.T.3
  • 109
    • 0037119408 scopus 로고    scopus 로고
    • The physiological role of RNase T can be explained by its unusual substrate specificity
    • Zuo Y., Deutscher M.P. The physiological role of RNase T can be explained by its unusual substrate specificity. J. Biol. Chem. 2002, 277:29654-29661.
    • (2002) J. Biol. Chem. , vol.277 , pp. 29654-29661
    • Zuo, Y.1    Deutscher, M.P.2
  • 110
    • 79955799175 scopus 로고    scopus 로고
    • Double-strand break repair-independent role for BRCA2 in blocking stalled replication fork degradation by MRE11
    • Schlacher K., Christ N., Siaud N., Egashira A., Wu H., Jasin M. Double-strand break repair-independent role for BRCA2 in blocking stalled replication fork degradation by MRE11. Cell 2011, 145:529-542.
    • (2011) Cell , vol.145 , pp. 529-542
    • Schlacher, K.1    Christ, N.2    Siaud, N.3    Egashira, A.4    Wu, H.5    Jasin, M.6
  • 112
    • 77956819782 scopus 로고    scopus 로고
    • ATM regulates Mre11-dependent DNA end-degradation and microhomology-mediated end joining
    • Rahal E.A., Henricksen L.A., Li Y., Williams R.S., Tainer J.A., Dixon K. ATM regulates Mre11-dependent DNA end-degradation and microhomology-mediated end joining. Cell Cycle 2010, 9:2866-2877.
    • (2010) Cell Cycle , vol.9 , pp. 2866-2877
    • Rahal, E.A.1    Henricksen, L.A.2    Li, Y.3    Williams, R.S.4    Tainer, J.A.5    Dixon, K.6
  • 118
    • 84871192231 scopus 로고    scopus 로고
    • Mre11 ATLD17/18 mutation retains Tel1/ATM activity but blocks DNA double-strand break repair
    • Limbo O., Moiani D., Kertokalio A., Wyman C., Tainer J.A., Russell P. Mre11 ATLD17/18 mutation retains Tel1/ATM activity but blocks DNA double-strand break repair. Nucleic Acids Res. 2012, 40:11435-11449.
    • (2012) Nucleic Acids Res. , vol.40 , pp. 11435-11449
    • Limbo, O.1    Moiani, D.2    Kertokalio, A.3    Wyman, C.4    Tainer, J.A.5    Russell, P.6
  • 119
    • 80855133532 scopus 로고    scopus 로고
    • Crystal structure of human Mre11: understanding tumorigenic mutations
    • Park Y.B., Chae J., Kim Y.C., Cho Y. Crystal structure of human Mre11: understanding tumorigenic mutations. Structure 2011, 19:1591-1602.
    • (2011) Structure , vol.19 , pp. 1591-1602
    • Park, Y.B.1    Chae, J.2    Kim, Y.C.3    Cho, Y.4
  • 120
    • 0032085295 scopus 로고    scopus 로고
    • The 3' to 5' exonuclease activity of Mre 11 facilitates repair of DNA double-strand breaks
    • Paull T.T., Gellert M. The 3' to 5' exonuclease activity of Mre 11 facilitates repair of DNA double-strand breaks. Mol. Cell 1998, 1:969-979.
    • (1998) Mol. Cell , vol.1 , pp. 969-979
    • Paull, T.T.1    Gellert, M.2
  • 121
    • 0035929667 scopus 로고    scopus 로고
    • DNA structure-specific nuclease activities in the Saccharomyces cerevisiae Rad50*Mre11 complex
    • Trujillo K.M., Sung P. DNA structure-specific nuclease activities in the Saccharomyces cerevisiae Rad50*Mre11 complex. J. Biol. Chem. 2001, 276:35458-35464.
    • (2001) J. Biol. Chem. , vol.276 , pp. 35458-35464
    • Trujillo, K.M.1    Sung, P.2
  • 122
    • 84856074733 scopus 로고    scopus 로고
    • ATP hydrolysis by RAD50 protein switches MRE11 enzyme from endonuclease to exonuclease
    • Majka J., Alford B., Ausio J., Finn R.M., McMurray C.T. ATP hydrolysis by RAD50 protein switches MRE11 enzyme from endonuclease to exonuclease. J. Biol. Chem. 2012, 287:2328-2341.
    • (2012) J. Biol. Chem. , vol.287 , pp. 2328-2341
    • Majka, J.1    Alford, B.2    Ausio, J.3    Finn, R.M.4    McMurray, C.T.5
  • 123
    • 79956301873 scopus 로고    scopus 로고
    • Crystal structure of the Mre11-Rad50-ATPgammaS complex: understanding the interplay between Mre11 and Rad50
    • Lim H.S., Kim J.S., Park Y.B., Gwon G.H., Cho Y. Crystal structure of the Mre11-Rad50-ATPgammaS complex: understanding the interplay between Mre11 and Rad50. Genes Dev. 2011, 25:1091-1104.
    • (2011) Genes Dev. , vol.25 , pp. 1091-1104
    • Lim, H.S.1    Kim, J.S.2    Park, Y.B.3    Gwon, G.H.4    Cho, Y.5
  • 125
    • 84855870632 scopus 로고    scopus 로고
    • ATP driven structural changes of the bacterial Mre11:Rad50 catalytic head complex
    • Mockel C., Lammens K., Schele A., Hopfner K.P. ATP driven structural changes of the bacterial Mre11:Rad50 catalytic head complex. Nucleic Acids Res. 2012, 40:914-927.
    • (2012) Nucleic Acids Res. , vol.40 , pp. 914-927
    • Mockel, C.1    Lammens, K.2    Schele, A.3    Hopfner, K.P.4
  • 128
    • 0034093291 scopus 로고    scopus 로고
    • Passing the baton in base excision repair
    • Wilson S.H., Kunkel T.A. Passing the baton in base excision repair. Nat. Struct. Biol. 2000, 7:176-178.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 176-178
    • Wilson, S.H.1    Kunkel, T.A.2
  • 130
    • 0742321956 scopus 로고    scopus 로고
    • Structural basis for FEN-1 substrate specificity and PCNA-mediated activation in DNA replication and repair
    • Chapados B.R., Hosfield D.J., Han S., Qiu J., Yelent B., Shen B., Tainer J.A. Structural basis for FEN-1 substrate specificity and PCNA-mediated activation in DNA replication and repair. Cell 2004, 116:39-50.
    • (2004) Cell , vol.116 , pp. 39-50
    • Chapados, B.R.1    Hosfield, D.J.2    Han, S.3    Qiu, J.4    Yelent, B.5    Shen, B.6    Tainer, J.A.7
  • 131
    • 0035965238 scopus 로고    scopus 로고
    • Stimulation of eukaryotic flap endonuclease-1 activities by proliferating cell nuclear antigen (PCNA) is independent of its in vitro interaction via a consensus PCNA binding region
    • Frank G., Qiu J., Zheng L., Shen B. Stimulation of eukaryotic flap endonuclease-1 activities by proliferating cell nuclear antigen (PCNA) is independent of its in vitro interaction via a consensus PCNA binding region. J. Biol. Chem. 2001, 276:36295-36302.
    • (2001) J. Biol. Chem. , vol.276 , pp. 36295-36302
    • Frank, G.1    Qiu, J.2    Zheng, L.3    Shen, B.4
  • 132
    • 27144495464 scopus 로고    scopus 로고
    • The two DNA clamps Rad9/Rad1/Hus1 complex and proliferating cell nuclear antigen differentially regulate flap endonuclease 1 activity
    • Friedrich-Heineken E., Toueille M., Tannler B., Burki C., Ferrari E., Hottiger M.O., Hubscher U. The two DNA clamps Rad9/Rad1/Hus1 complex and proliferating cell nuclear antigen differentially regulate flap endonuclease 1 activity. J. Mol. Biol. 2005, 353:980-989.
    • (2005) J. Mol. Biol. , vol.353 , pp. 980-989
    • Friedrich-Heineken, E.1    Toueille, M.2    Tannler, B.3    Burki, C.4    Ferrari, E.5    Hottiger, M.O.6    Hubscher, U.7
  • 133
    • 0034679597 scopus 로고    scopus 로고
    • Two modes of FEN1 binding to PCNA regulated by DNA
    • Gomes X.V., Burgers P.M. Two modes of FEN1 binding to PCNA regulated by DNA. EMBO J. 2000, 19:3811-3821.
    • (2000) EMBO J. , vol.19 , pp. 3811-3821
    • Gomes, X.V.1    Burgers, P.M.2
  • 134
    • 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
    • Hosfield D.J., Mol C.D., Shen B., Tainer J.A. Structure of the DNA repair and replication endonuclease and exonuclease FEN-1: coupling DNA and PCNA binding to FEN-1 activity. Cell 1998, 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
  • 135
    • 0041885325 scopus 로고    scopus 로고
    • Proliferating cell nuclear antigen (PCNA): a dancer with many partners
    • Maga G., Hubscher U. Proliferating cell nuclear antigen (PCNA): a dancer with many partners. J. Cell Sci. 2003, 116:3051-3060.
    • (2003) J. Cell Sci. , vol.116 , pp. 3051-3060
    • Maga, G.1    Hubscher, U.2
  • 136
    • 34249066085 scopus 로고    scopus 로고
    • PCNA, the maestro of the replication fork
    • Moldovan G.L., Pfander B., Jentsch S. PCNA, the maestro of the replication fork. Cell 2007, 129:665-679.
    • (2007) Cell , vol.129 , pp. 665-679
    • Moldovan, G.L.1    Pfander, B.2    Jentsch, S.3
  • 137
    • 84861873482 scopus 로고    scopus 로고
    • Repair complexes of FEN1 endonuclease, DNA, and Rad9-Hus1-Rad1 are distinguished from their PCNA counterparts by functionally important stability
    • Querol-Audi J., Yan C., Xu X., Tsutakawa S.E., Tsai M.S., Tainer J.A., Cooper P.K., Nogales E., Ivanov I. Repair complexes of FEN1 endonuclease, DNA, and Rad9-Hus1-Rad1 are distinguished from their PCNA counterparts by functionally important stability. Proc. Nat. Acad. Sci. U.S.A. 2012, 109:8528-8533.
    • (2012) Proc. Nat. Acad. Sci. U.S.A. , vol.109 , pp. 8528-8533
    • Querol-Audi, J.1    Yan, C.2    Xu, X.3    Tsutakawa, S.E.4    Tsai, M.S.5    Tainer, J.A.6    Cooper, P.K.7    Nogales, E.8    Ivanov, I.9
  • 138
    • 34147209417 scopus 로고    scopus 로고
    • Disruption of the FEN-1/PCNA interaction results in DNA replication defects, pulmonary hypoplasia, pancytopenia, and newborn lethality in mice
    • Zheng L., Dai H., Qiu J., Huang Q., Shen B. Disruption of the FEN-1/PCNA interaction results in DNA replication defects, pulmonary hypoplasia, pancytopenia, and newborn lethality in mice. Mol. Cell Biol. 2007, 27:3176-3186.
    • (2007) Mol. Cell Biol. , vol.27 , pp. 3176-3186
    • Zheng, L.1    Dai, H.2    Qiu, J.3    Huang, Q.4    Shen, B.5
  • 139
    • 0030749867 scopus 로고    scopus 로고
    • Conditional gene targeted deletion by Cre recombinase demonstrates the requirement for the double-strand break repair Mre11 protein in murine embryonic stem cells
    • Xiao Y., Weaver D.T. Conditional gene targeted deletion by Cre recombinase demonstrates the requirement for the double-strand break repair Mre11 protein in murine embryonic stem cells. Nucleic Acids Res. 1997, 25:2985-2991.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 2985-2991
    • Xiao, Y.1    Weaver, D.T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.