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Volumn 2010, Issue , 2010, Pages

Overview of DNA repair in Trypanosoma cruzi, Trypanosoma brucei, and Leishmania major

Author keywords

[No Author keywords available]

Indexed keywords

DNA; NUCLEOTIDE;

EID: 84860294717     PISSN: 20900201     EISSN: 2090021X     Source Type: Journal    
DOI: 10.4061/2010/840768     Document Type: Review
Times cited : (76)

References (121)
  • 1
    • 77953504479 scopus 로고    scopus 로고
    • Trypanosomatid parasites causing neglected diseases
    • 10.2174/092986710790979953
    • Nussbaum K., Honek J., Cadmus C. M., Efferth T., efferth@uni-mainz.de Trypanosomatid parasites causing neglected diseases. Current Medicinal Chemistry 2010 17 15 1594 1617 10.2174/092986710790979953
    • (2010) Current Medicinal Chemistry , vol.17 , Issue.15 , pp. 1594-1617
    • Nussbaum, K.1    Honek, J.2    Cadmus, C.M.3    Efferth, T.4
  • 2
    • 68949206715 scopus 로고    scopus 로고
    • Structural organization of Trypanosoma cruzi
    • 2-s2.0-68949206715
    • de Souza W., Structural organization of Trypanosoma cruzi. Memorias do Instituto Oswaldo Cruz 2009 104 1 89 100 2-s2.0-68949206715
    • (2009) Memorias Do Instituto Oswaldo Cruz , vol.104 , Issue.1 , pp. 89-100
    • De Souza, W.1
  • 3
    • 0036020251 scopus 로고    scopus 로고
    • Natural and induced dyskinetoplastic trypanosomatids: How to live without mitochondrial DNA
    • DOI 10.1016/S0020-7519(02)00020-6, PII S0020751902000206
    • Schnaufer A., Domingo G. J., Stuart K., Natural and induced dyskinetoplastic trypanosomatids: how to live without mitochondrial DNA. International Journal for Parasitology 2002 32 9 1071 1084 2-s2.0-0036020251 10.1016/S0020-7519(02)00020-6 (Pubitemid 34761901)
    • (2002) International Journal for Parasitology , vol.32 , Issue.9 , pp. 1071-1084
    • Schnaufer, A.1    Domingo, G.J.2    Stuart, K.3
  • 4
    • 0019075144 scopus 로고
    • Effect of inhibitors of electron transport and oxidative phosphorylation on Trypanosoma cruzi respiration and growth
    • 2-s2.0-0019075144
    • Stoppani A. O. M., Docampo R., de Boiso J. F., Frasch A. C. C., Effect of inhibitors of electron transport and oxidative phosphorylation on Trypanosoma cruzi respiration and growth. Molecular and Biochemical Parasitology 1980 2 1 3 21 2-s2.0-0019075144
    • (1980) Molecular and Biochemical Parasitology , vol.2 , Issue.1 , pp. 3-21
    • Stoppani, A.O.M.1    Docampo, R.2    De Boiso, J.F.3    Frasch, A.C.C.4
  • 5
    • 77954354604 scopus 로고    scopus 로고
    • Characterization of a Leishmania stage-specific mitochondrial membrane protein that enhances the activity of cytochrome c oxidase and its role in virulence
    • 10.1111/j.1365-2958.2010.07214.x
    • Dey R., Meneses C., Salotra P., Kamhawi S., Nakhasi H. L., Duncan R., robert.duncan@fda.hhs.gov Characterization of a Leishmania stage-specific mitochondrial membrane protein that enhances the activity of cytochrome c oxidase and its role in virulence. Molecular Microbiology 2010 77 2 399 414 10.1111/j.1365-2958.2010.07214.x
    • (2010) Molecular Microbiology , vol.77 , Issue.2 , pp. 399-414
    • Dey, R.1    Meneses, C.2    Salotra, P.3    Kamhawi, S.4    Nakhasi, H.L.5    Duncan, R.6
  • 10
    • 0035902108 scopus 로고    scopus 로고
    • Genome maintenance mechanisms for preventing cancer
    • DOI 10.1038/35077232
    • Hoeijmakers J. H. J., Genome maintenance mechanisms for preventing cancer. Nature 2001 411 6835 366 374 2-s2.0-0035902108 10.1038/35077232 (Pubitemid 32467046)
    • (2001) Nature , vol.411 , Issue.6835 , pp. 366-374
    • Hoeijmakers, J.H.J.1
  • 11
    • 77649165394 scopus 로고    scopus 로고
    • Maintaining genome stability at the replication fork
    • 10.1038/nrm2852
    • Branzei D., dana.branzei@ifom-ieo-campus.it Foiani M., marco.foiani@ifom-ieo-campus.it Maintaining genome stability at the replication fork. Nature Reviews Molecular Cell Biology 2010 11 3 208 219 10.1038/nrm2852
    • (2010) Nature Reviews Molecular Cell Biology , vol.11 , Issue.3 , pp. 208-219
    • Branzei, D.1
  • 12
    • 77449086623 scopus 로고    scopus 로고
    • DNA resection in eukaryotes: Deciding how to fix the break
    • 10.1038/nsmb.1710
    • Huertas P., DNA resection in eukaryotes: deciding how to fix the break. Nature Structural & Molecular Biology 2010 17 1 11 16 10.1038/nsmb.1710
    • (2010) Nature Structural & Molecular Biology , vol.17 , Issue.1 , pp. 11-16
    • Huertas, P.1
  • 13
    • 35348916597 scopus 로고    scopus 로고
    • Bacterial DNA repair genes and their eukaryotic homologues: 2. Role of bacterial mutator gene homologues in human disease. Overview of nucleotide pool sanitization and mismatch repair systems
    • Arczewska K. D., Kumierek J. T., Bacterial DNA repair genes and their eukaryotic homologues: 2. Role of bacterial mutator gene homologues in human disease. Overview of nucleotide pool sanitization and mismatch repair systems. Acta Biochimica Polonica 2007 54 3 435 457 2-s2.0-35348916597 (Pubitemid 47584023)
    • (2007) Acta Biochimica Polonica , vol.54 , Issue.3 , pp. 435-457
    • Arczewska, K.D.1    Kusmierek, J.T.2
  • 16
    • 0035312710 scopus 로고    scopus 로고
    • Characterization of uracil-DNA glycosylase activity from Trypanosoma cruzi and its stimulation by AP endonuclease
    • Fárez-Vidal M. E., Gallego C., Ruiz-Pérez L. M., González-Pacanowska D., Characterization of uracil-DNA glycosylase activity from Trypanosoma cruzi and its stimulation by AP endonuclease. Nucleic Acids Research 2001 29 7 1549 1555 2-s2.0-0035312710 (Pubitemid 32288503)
    • (2001) Nucleic Acids Research , vol.29 , Issue.7 , pp. 1549-1555
    • Farez-Vidal, M.E.1    Gallego, C.2    Ruiz-Perez, L.M.3    Gonzalez-Pacanowska, D.4
  • 17
    • 4444268722 scopus 로고    scopus 로고
    • Trypanosoma cruzi contains a single detectable uracil-DNA glycosylase and repairs uracil exclusively via short patch base excision repair
    • DOI 10.1016/j.jmb.2004.07.043, PII S0022283604008721
    • Pea-Diaz J., Akbari M., Sundheim O., Esther Farez-Vidal M., Andersen S., Sneve R., Gonzalez-Pacanowska D., Krokan H. E., Slupphaug G., Trypanosoma cruzi contains a single detectable uracil-DNA glycosylase and repairs uracil exclusively via short patch base excision repair. Journal of Molecular Biology 2004 342 3 787 799 2-s2.0-4444268722 10.1016/j.jmb.2004.07.043 (Pubitemid 39165650)
    • (2004) Journal of Molecular Biology , vol.342 , Issue.3 , pp. 787-799
    • Pena-Diaz, J.1    Akbari, M.2    Sundheim, O.3    Esther Farez-Vidal, M.4    Andersen, S.5    Sneve, R.6    Gonzalez-Pacanowska, D.7    Krokan, H.E.8    Slupphaug, G.9
  • 18
    • 0344915163 scopus 로고    scopus 로고
    • Apurinic/apyrimidinic endonuclease genes from the trypanosomatidae Leishmania major and Trypanosoma cruzi confer resistance to oxidizing agents in DNA repair-deficient Escherichia coli
    • DOI 10.1093/nar/27.3.771
    • Pérez J., Gallego C., Bernier-Villamor V., Camacho A., González-Pacanowska D., Ruiz-Pérez L. M., Apurinic/apyrimidinic endonuclease genes from the trypanosomatidae Leishmania major and Trypanosoma cruzi confer resistance to oxidizing agents in DNA repair-deficient Escherichia coli. Nucleic Acids Research 1999 27 3 771 777 2-s2.0-0344915163 10.1093/nar/27.3.771 (Pubitemid 29209364)
    • (1999) Nucleic Acids Research , vol.27 , Issue.3 , pp. 771-777
    • Perez, J.1    Gallego, C.2    Bernier-Villamor, V.3    Camacho, A.4    Gonzalez-Pacanowska, D.5    Ruiz-Perez, L.M.6
  • 19
    • 17844405598 scopus 로고    scopus 로고
    • Overexpression of AP endonuclease protects Leishmania major cells against methotrexate induced DNA fragmentation and hydrogen peroxide
    • DOI 10.1016/j.molbiopara.2005.03.002
    • Gallego C., Estévez A. M., Fárez E., Ruiz-Pérez L. M., González-Pacanowska D., Overexpression of AP endonuclease protects Leishmania major cells against methotrexate induced DNA fragmentation and hydrogen peroxide. Molecular and Biochemical Parasitology 2005 141 2 191 197 2-s2.0-17844405598 10.1016/j.molbiopara.2005.03.002 (Pubitemid 40591563)
    • (2005) Molecular and Biochemical Parasitology , vol.141 , Issue.2 , pp. 191-197
    • Gallego, C.1    Estevez, A.M.2    Farez, E.3    Ruiz-Perez, L.M.4    Gonzalez-Pacanowska, D.5
  • 22
    • 1542677269 scopus 로고    scopus 로고
    • Trypanosoma brucei has two distinct mitochondrial DNA polymerase beta enzymes
    • 2-s2.0-1542677269
    • Saxowsky T. T., Choudhary G., Klingbeil M. M., Englund P. T., Trypanosoma brucei has two distinct mitochondrial DNA polymerase beta enzymes. The Journal of biological chemistry 2003 278 49 49095 49101 2-s2.0-1542677269
    • (2003) The Journal of Biological Chemistry , vol.278 , Issue.49 , pp. 49095-49101
    • Saxowsky, T.T.1    Choudhary, G.2    Klingbeil, M.M.3    Englund, P.T.4
  • 24
    • 67649870625 scopus 로고    scopus 로고
    • Transcriptionally active TFIIH of the early-diverged eukaryote Trypanosoma brucei harbors two novel core subunits but not a cyclin-activating kinase complex
    • 2-s2.0-67649870625 10.1093/nar/gkp236
    • Lee J. H., Jung H. S., Günzl A., Transcriptionally active TFIIH of the early-diverged eukaryote Trypanosoma brucei harbors two novel core subunits but not a cyclin-activating kinase complex. Nucleic Acids Research 2009 37 11 3811 3820 2-s2.0-67649870625 10.1093/nar/gkp236
    • (2009) Nucleic Acids Research , vol.37 , Issue.11 , pp. 3811-3820
    • Lee, J.H.1    Jung, H.S.2    Günzl, A.3
  • 25
    • 0037854703 scopus 로고    scopus 로고
    • Single-nucleotide polymorphisms of the Trypanosoma cruzi MSH2 gene support the existence of three phylogenetic lineages presenting differences in mismatch-repair efficiency
    • Augusto-Pinto L., Teixeira S. M. R., Pena S. D. J., Machado C. R., Single-nucleotide polymorphisms of the Trypanosoma cruzi MSH2 gene support the existence of three phylogenetic lineages presenting differences in mismatch-repair efficiency. Genetics 2003 164 1 117 126 2-s2.0-0037854703 (Pubitemid 36617698)
    • (2003) Genetics , vol.164 , Issue.1 , pp. 117-126
    • Augusto-Pinto, L.1    Teixeira, S.M.R.2    Pena, S.D.J.3    Machado, C.R.4
  • 26
    • 39649096265 scopus 로고    scopus 로고
    • Mismatch repair in Trypanosoma brucei: Heterologous expression of MSH2 from Trypanosoma cruzi provides new insights into the response to oxidative damage
    • 2-s2.0-39649096265 10.1016/j.gene.2007.12.021
    • Machado-Silva A., Teixeira S. M. R., Franco G. R., Macedo A. M., Pena S. D. J., McCulloch R., Machado C. R., Mismatch repair in Trypanosoma brucei: heterologous expression of MSH2 from Trypanosoma cruzi provides new insights into the response to oxidative damage. Gene 2008 411 1-2 19 26 2-s2.0-39649096265 10.1016/j.gene.2007.12.021
    • (2008) Gene , vol.411 , Issue.1-2 , pp. 19-26
    • Machado-Silva, A.1    Teixeira, S.M.R.2    Franco, G.R.3    Macedo, A.M.4    Pena, S.D.J.5    McCulloch, R.6    Machado, C.R.7
  • 27
    • 0346334419 scopus 로고    scopus 로고
    • Characterization of components of the mismatch repair machinery in Trypanosoma brucei
    • DOI 10.1046/j.1365-2958.2003.03804.x
    • Bell J. S., Harvey T. I., Sims A.-M., McCulloch R., Characterization of components of the mismatch repair machinery in Trypanosoma brucei. Molecular Microbiology 2004 51 1 159 173 2-s2.0-0346334419 10.1046/j.1365-2958.2003.03804. x (Pubitemid 38031079)
    • (2004) Molecular Microbiology , vol.51 , Issue.1 , pp. 159-173
    • Bell, J.S.1    Harvey, T.I.2    Sims, A.-M.3    McCulloch, R.4
  • 28
    • 0242581017 scopus 로고    scopus 로고
    • Mismatch Repair Regulates Homologous Recombination, but Has Little Influence on Antigenic Variation, in Trypanosoma brucei
    • DOI 10.1074/jbc.M308123200
    • Bell J. S., McCulloch R., Mismatch repair regulates homologous recombination, but has little influence on antigenic variation, in Trypanosoma brucei. Journal of Biological Chemistry 2003 278 46 45182 45188 2-s2.0-0242581017 10.1074/jbc.M308123200 (Pubitemid 37432651)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.46 , pp. 45182-45188
    • Bell, J.S.1    McCulloch, R.2
  • 29
    • 0036034858 scopus 로고    scopus 로고
    • Two pathways of homologous recombination in Trypanosoma brucei
    • DOI 10.1046/j.1365-2958.2002.03122.x
    • Conway C., Proudfoot C., Burton P., Barry J. D., McCulloch R., Two pathways of homologous recombination in Trypanosoma brucei. Molecular Microbiology 2002 45 6 1687 1700 2-s2.0-0036034858 10.1046/j.1365-2958.2002. 03122.x (Pubitemid 35231983)
    • (2002) Molecular Microbiology , vol.45 , Issue.6 , pp. 1687-1700
    • Conway, C.1    Proudfoot, C.2    Burton, P.3    Barry, J.D.4    McCulloch, R.5
  • 30
    • 13544275919 scopus 로고    scopus 로고
    • Telomere length regulation and transcriptional silencing in KU80-deficient Trypanosoma brucei
    • DOI 10.1093/nar/gkh991
    • Janzen C. J., Lander F., Dreesen O., Cross G. A. M., Telomere length regulation and transcriptional silencing in KU80-deficient Trypanosoma brucei. Nucleic Acids Research 2004 32 22 6575 6584 2-s2.0-13544275919 10.1093/nar/gkh991 (Pubitemid 40220369)
    • (2004) Nucleic Acids Research , vol.32 , Issue.22 , pp. 6575-6584
    • Janzen, C.J.1    Lander, F.2    Dreesen, O.3    Cross, G.A.M.4
  • 31
    • 0036861063 scopus 로고    scopus 로고
    • Trypanosoma brucei MRE11 is non-essential but influences growth, homologous recombination and DNA double-strand break repair
    • PII S0166685102001652
    • Tan K. S. W., Leal S. T. G., Cross G. A. M., Trypanosoma brucei MRE11 is non-essential but influences growth, homologous recombination and DNA double-strand break repair. Molecular and Biochemical Parasitology 2002 125 1-2 11 21 2-s2.0-0036861063 (Pubitemid 35449242)
    • (2002) Molecular and Biochemical Parasitology , vol.125 , Issue.1-2 , pp. 11-21
    • Tan, K.S.W.1    Leal, S.T.G.2    Cross, G.A.M.3
  • 32
    • 0037135587 scopus 로고    scopus 로고
    • Inactivation of Mre11 does not affect VSG gene duplication mediated by homologous recombination in Trypanosoma brucei
    • DOI 10.1074/jbc.M203205200
    • Robinson N. P., McCulloch R., Conway C., Browitt A., Barry J. D., Inactivation of Mre11 does not affect VSG gene duplication mediated by homologous recombination in Trypanosoma brucei. Journal of Biological Chemistry 2002 277 29 26185 26193 2-s2.0-0037135587 10.1074/jbc.M203205200 (Pubitemid 34967105)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.29 , pp. 26185-26193
    • Robinson, N.P.1    McCulloch, R.2    Conway, C.3    Browitt, A.4    David Barry, J.5
  • 34
    • 0032723013 scopus 로고    scopus 로고
    • A role for RAD51 and homologous recombination in Trypanosoma brucei antigenic variation
    • 2-s2.0-0032723013 10.1101/gad.13.21.2875
    • McCulloch R., Barry J. D., A role for RAD51 and homologous recombination in Trypanosoma brucei antigenic variation. Genes and Development 1999 13 21 2875 2888 2-s2.0-0032723013 10.1101/gad.13.21.2875
    • (1999) Genes and Development , vol.13 , Issue.21 , pp. 2875-2888
    • McCulloch, R.1    Barry, J.D.2
  • 35
    • 0035400352 scopus 로고    scopus 로고
    • Identification and characterisation of a RAD51 gene from Leishmania major
    • DOI 10.1016/S0166-6851(01)00288-2, PII S0166685101002882
    • McKean P. G., Keen J. K., Smith D. F., Benson F. E., Identification and characterisation of a RAD51 gene from Leishmania major. Molecular and Biochemical Parasitology 2001 115 2 209 216 2-s2.0-0035400352 10.1016/S0166-6851(01)00288-2 (Pubitemid 32566230)
    • (2001) Molecular and Biochemical Parasitology , vol.115 , Issue.2 , pp. 209-216
    • McKean, P.G.1    Keen, J.K.2    Smith, D.F.3    Benson, F.E.4
  • 36
    • 30544454048 scopus 로고    scopus 로고
    • Trypanosoma brucei DMC1 does not act in DNA recombination, repair or antigenic variation in bloodstream stage cells
    • DOI 10.1016/j.molbiopara.2005.10.007, PII S0166685105003038
    • Proudfoot C., McCulloch R., Trypanosoma brucei DMC1 does not act in DNA recombination, repair or antigenic variation in bloodstream stage cells. Molecular and Biochemical Parasitology 2006 145 2 245 253 2-s2.0-30544454048 10.1016/j.molbiopara.2005.10.007 (Pubitemid 43083366)
    • (2006) Molecular and Biochemical Parasitology , vol.145 , Issue.2 , pp. 245-253
    • Proudfoot, C.1    McCulloch, R.2
  • 37
    • 43449106468 scopus 로고    scopus 로고
    • Trypanosoma brucei BRCA2 acts in antigenic variation and has undergone a recent expansion in BRC repeat number that is important during homologous recombination
    • DOI 10.1111/j.1365-2958.2008.06230.x
    • Hartley C. L., McCulloch R., Trypanosoma brucei BRCA2 acts in antigenic variation and has undergone a recent expansion in BRC repeat number that is important during homologous recombination. Molecular Microbiology 2008 68 5 1237 1251 2-s2.0-43449106468 10.1111/j.1365-2958.2008.06230.x (Pubitemid 351670200)
    • (2008) Molecular Microbiology , vol.68 , Issue.5 , pp. 1237-1251
    • Hartley, C.L.1    McCulloch, R.2
  • 38
    • 29244484238 scopus 로고    scopus 로고
    • Distinct roles for two RAD51-related genes in Trypanosoma brucei antigenic variation
    • DOI 10.1093/nar/gki996
    • Proudfoot C., McCulloch R., Distinct roles for two RAD51-related genes in Trypanosoma brucei antigenic variation. Nucleic Acids Research 2005 33 21 6906 6919 2-s2.0-29244484238 10.1093/nar/gki996 (Pubitemid 41830494)
    • (2005) Nucleic Acids Research , vol.33 , Issue.21 , pp. 6906-6919
    • Proudfoot, C.1    McCulloch, R.2
  • 40
    • 58149136352 scopus 로고    scopus 로고
    • DNA polymerase kappa from Trypanosoma cruzi localizes to the mitochondria, bypasses 8-oxoguanine lesions and performs DNA synthesis in a recombination intermediate
    • 2-s2.0-58149136352 10.1111/j.1365-2958.2008.06521.x
    • Rajão M. A., Passos-Silva D. G., DaRocha W. D., Franco G. R., Macedo A. M., Pena S. D. J., Teixeira S. M., Machado C. R., DNA polymerase kappa from Trypanosoma cruzi localizes to the mitochondria, bypasses 8-oxoguanine lesions and performs DNA synthesis in a recombination intermediate. Molecular Microbiology 2009 71 1 185 197 2-s2.0-58149136352 10.1111/j.1365-2958.2008. 06521.x
    • (2009) Molecular Microbiology , vol.71 , Issue.1 , pp. 185-197
    • Rajão, M.A.1    Passos-Silva, D.G.2    Darocha, W.D.3    Franco, G.R.4    Macedo, A.M.5    Pena, S.D.J.6    Teixeira, S.M.7    Machado, C.R.8
  • 41
    • 0034028030 scopus 로고    scopus 로고
    • 6-alkylguanine by alkyltransferases
    • DOI 10.1016/S1383-5742(00)00017-X, PII S138357420000017X
    • Pegg A. E., Repair of O6-alkylguanine by alkyltransferases. Mutation Research 2000 462 2-3 83 100 2-s2.0-0034028030 10.1016/S1383-5742(00)00017-X (Pubitemid 30190216)
    • (2000) Mutation Research - Reviews in Mutation Research , vol.462 , Issue.2-3 , pp. 83-100
    • Pegg, A.E.1
  • 42
    • 0035221419 scopus 로고    scopus 로고
    • The DNA-repair protein AlkB, EGL-9, and leprecan define new families of 2-oxoglutarate- and iron-dependent dioxygenases
    • 2-s2.0-0035221419
    • Aravind L., Koonin E. V., The DNA-repair protein AlkB, EGL-9, and leprecan define new families of 2-oxoglutarate- and iron-dependent dioxygenases. Genome Biology 2001 2 3 RESEARCH0007 2-s2.0-0035221419
    • (2001) Genome Biology , vol.2 , Issue.3
    • Aravind, L.1    Koonin, E.V.2
  • 43
    • 57749109103 scopus 로고    scopus 로고
    • Structure and function of photolyase and in vivo enzymology: 50th anniversary
    • 2-s2.0-57749109103 10.1074/jbc.R800052200
    • Sancar A., Structure and function of photolyase and in vivo enzymology: 50th anniversary. Journal of Biological Chemistry 2008 283 47 32153 32157 2-s2.0-57749109103 10.1074/jbc.R800052200
    • (2008) Journal of Biological Chemistry , vol.283 , Issue.47 , pp. 32153-32157
    • Sancar, A.1
  • 44
    • 62349120246 scopus 로고    scopus 로고
    • Base excision repair: The long and short of it
    • 2-s2.0-62349120246 10.1007/s00018-009-8736-z
    • Robertson A. B., Klungland A., Rognes T., Leiros I., Base excision repair: the long and short of it. Cellular and Molecular Life Sciences 2009 66 6 981 993 2-s2.0-62349120246 10.1007/s00018-009-8736-z
    • (2009) Cellular and Molecular Life Sciences , vol.66 , Issue.6 , pp. 981-993
    • Robertson, A.B.1    Klungland, A.2    Rognes, T.3    Leiros, I.4
  • 45
    • 0029842307 scopus 로고    scopus 로고
    • Reconstitution of DNA base excision-repair with purified human proteins: Interaction between DNA polymerase β and the XRCC1 protein
    • Kubota Y., Nash R. A., Klungland A., Schär P., Barnes D. E., Lindahl T., Reconstitution of DNA base excision-repair with purified human proteins: interaction between DNA polymerase β and the XRCC1 protein. EMBO Journal 1996 15 23 6662 6670 2-s2.0-0029842307 (Pubitemid 26413798)
    • (1996) EMBO Journal , vol.15 , Issue.23 , pp. 6662-6670
    • Kubota, Y.1    Nash, R.A.2    Klungland, A.3    Schar, P.4    Barnes, D.E.5    Lindahl, T.6
  • 47
    • 0032502675 scopus 로고    scopus 로고
    • Involvement of flap endonuclease 1 in base excision DNA repair
    • DOI 10.1074/jbc.273.15.8842
    • Kim K., Biade S., Matsumoto Y., Involvement of flap endonuclease 1 in base excision DNA repair. Journal of Biological Chemistry 1998 273 15 8842 8848 2-s2.0-0032502675 10.1074/jbc.273.15.8842 (Pubitemid 28176165)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.15 , pp. 8842-8848
    • Kim, K.1    Biade, S.2    Matsumoto, Y.3
  • 48
    • 0033198919 scopus 로고    scopus 로고
    • Poly(ADP-ribosyl)ation reactions in the regulation of nuclear functions
    • DOI 10.1042/0264-6021:3420249
    • D'Amours D., Desnoyers S., D'Silva I., Poirier G. G., Poly(ADP-ribosyl)ation reactions in the regulation of nuclear functions. Biochemical Journal 1999 342 2 249 268 2-s2.0-0033198919 10.1042/0264-6021: 3420249 (Pubitemid 29425344)
    • (1999) Biochemical Journal , vol.342 , Issue.2 , pp. 249-268
    • D'Amours, D.1    Desnoyers, S.2    D'Silva, I.3    Poirier, G.G.4
  • 49
    • 3042627356 scopus 로고    scopus 로고
    • XRCC1-DNA polymerase β interaction is required for efficient base excision repair
    • DOI 10.1093/nar/gkh567
    • Dianova I. I., Sleeth K. M., Allinson S. L., Parsons J. L., Breslin C., Caldecott K. W., Dianov G. L., XRCC1-DNA polymerase β interaction is required for efficient base excision repair. Nucleic Acids Research 2004 32 8 2550 2555 2-s2.0-3042627356 10.1093/nar/gkh567 (Pubitemid 38854807)
    • (2004) Nucleic Acids Research , vol.32 , Issue.8 , pp. 2550-2555
    • Dianova, I.I.1    Sleeth, K.M.2    Allinson, S.L.3    Parsons, J.L.4    Breslin, C.5    Caldecott, K.W.6    Dianov, G.L.7
  • 50
    • 58549094699 scopus 로고    scopus 로고
    • Distribution and roles of X-family DNA polymerases in eukaryotes
    • 2-s2.0-58549094699 10.1016/j.biochi.2008.07.005
    • Uchiyama Y., Takeuchi R., Kodera H., Sakaguchi K., Distribution and roles of X-family DNA polymerases in eukaryotes. Biochimie 2009 91 2 165 170 2-s2.0-58549094699 10.1016/j.biochi.2008.07.005
    • (2009) Biochimie , vol.91 , Issue.2 , pp. 165-170
    • Uchiyama, Y.1    Takeuchi, R.2    Kodera, H.3    Sakaguchi, K.4
  • 51
    • 72449144718 scopus 로고    scopus 로고
    • Single-nucleotide and long-patch base excision repair of DNA damage in plants
    • 10.1111/j.1365-313X.2009.03994.x
    • Córdoba-Caero D., Morales-Ruiz T., Roldán-Arjona T., Ariza R. R., ge1roarr@uco.es Single-nucleotide and long-patch base excision repair of DNA damage in plants. Plant Journal 2009 60 4 716 728 10.1111/j.1365-313X.2009. 03994.x
    • (2009) Plant Journal , vol.60 , Issue.4 , pp. 716-728
    • Córdoba-Caero, D.1    Morales-Ruiz, T.2    Roldán-Arjona, T.3    Ariza, R.R.4
  • 52
    • 0034192265 scopus 로고    scopus 로고
    • The human OGG1 gene: Structure, functions, and its implication in the process of carcinogenesis
    • DOI 10.1006/abbi.2000.1773
    • Boiteux S., Radicella J. P., The human OGG1 gene: structure, functions, and its implication in the process of carcinogenesis. Archives of Biochemistry and Biophysics 2000 377 1 1 8 2-s2.0-0034192265 10.1006/abbi.2000.1773 (Pubitemid 30257280)
    • (2000) Archives of Biochemistry and Biophysics , vol.377 , Issue.1 , pp. 1-8
    • Boiteux, S.1    Radicella, J.P.2
  • 53
    • 4544273926 scopus 로고    scopus 로고
    • Error-prone replication of oxidatively damaged DNA by a high-fidelity DNA polymerase
    • DOI 10.1038/nature02908
    • Hsu G. W., Ober M., Carell T., Beese L. S., Error-prone replication of oxidatively damaged DNA by a high-fidelity DNA polymerase. Nature 2004 431 7005 217 221 2-s2.0-4544273926 10.1038/nature02908 (Pubitemid 39243477)
    • (2004) Nature , vol.431 , Issue.7005 , pp. 217-221
    • Hsu, G.W.1    Ober, M.2    Carell, T.3    Beese, L.S.4
  • 54
    • 34147174320 scopus 로고    scopus 로고
    • Significance of error-avoiding mechanisms for oxidative DNA damage in carcinogenesis
    • DOI 10.1111/j.1349-7006.2007.00409.x
    • Tsuzuki T., Nakatsu Y., Nakabeppu Y., Significance of error-avoiding mechanisms for oxidative DNA damage in carcinogenesis. Cancer Science 2007 98 4 465 470 2-s2.0-34147174320 10.1111/j.1349-7006.2007.00409.x (Pubitemid 46562735)
    • (2007) Cancer Science , vol.98 , Issue.4 , pp. 465-470
    • Tsuzuki, T.1    Nakatsu, Y.2    Nakabeppu, Y.3
  • 55
    • 0025061165 scopus 로고
    • Timing of nuclear and kinetoplast DNA replication and early morphological events in the cell cycle of Trypanosoma brucei
    • Woodward R., Gull K., Timing of nuclear and kinetoplast DNA replication and early morphological events in the cell cycle of Trypanosoma brucei. Journal of Cell Science 1990 95 1 49 57 2-s2.0-0025061165 (Pubitemid 20044150)
    • (1990) Journal of Cell Science , vol.95 , Issue.1 , pp. 49-57
    • Woodward, R.1    Gull, K.2
  • 56
    • 0036342502 scopus 로고    scopus 로고
    • Multiple mitochondrial DNA polymerases in Trypanosoma brucei
    • DOI 10.1016/S1097-2765(02)00571-3
    • Klingbeil M. M., Motyka S. A., Englund P. T., Multiple mitochondrial DNA polymerases in Trypanosoma brucei. Molecular Cell 2002 10 1 175 186 2-s2.0-0036342502 10.1016/S1097-2765(02)00571-3 (Pubitemid 34876571)
    • (2002) Molecular Cell , vol.10 , Issue.1 , pp. 175-186
    • Klingbeil, M.M.1    Motyka, S.A.2    Englund, P.T.3
  • 57
    • 0017037597 scopus 로고
    • Nuclear location of mammalian DNA polymerase activities
    • Foster D. N., Gurney T. Jr., Nuclear location of mammalian DNA polymerase activities. Journal of Biological Chemistry 1976 251 24 7893 7898 2-s2.0-0017037597 (Pubitemid 8015803)
    • (1976) Journal of Biological Chemistry , vol.251 , Issue.24 , pp. 7893-7898
    • Foster, D.N.1    Gurney Jr., T.2
  • 58
    • 0035883821 scopus 로고    scopus 로고
    • Nuclear DNA polymerase beta from Leishmania infantum. Cloning, molecular analysis and developmental regulation
    • Taladriz S., Hanke T., Ramiro M. J., García-Díaz M., García De Lacoba M., Blanco L., Larraga V., Nuclear DNA polymerase beta from Leishmania infantum. Cloning, molecular analysis and developmental regulation. Nucleic Acids Research 2001 29 18 3822 3834 2-s2.0-0035883821 (Pubitemid 32916045)
    • (2001) Nucleic Acids Research , vol.29 , Issue.18 , pp. 3822-3834
    • Taladriz, S.1    Hanke, T.2    Ramiro, M.J.3    Garcia-Diaz, M.4    Garcia De Lacoba, M.5    Blanco, L.6    Larraga, V.7
  • 60
    • 0032963791 scopus 로고    scopus 로고
    • RNA polymerase II transcription suppresses nucleosomal modulation of UV- induced (6-4) photoproduct and cyclobutane pyrimidine dimer repair in yeast
    • Tijsterman M., De Pril R., Tasseron-De Jong J. G., Brouwer J., RNA polymerase II transcription suppresses nucleosomal modulation of UV- induced (6-4) photoproduct and cyclobutane pyrimidine dimer repair in yeast. Molecular and Cellular Biology 1999 19 1 934 940 2-s2.0-0032963791 (Pubitemid 29018495)
    • (1999) Molecular and Cellular Biology , vol.19 , Issue.1 , pp. 934-940
    • Tijsterman, M.1    De Pril, R.2    Tasseron-De Jong, J.G.3    Brouwer, J.4
  • 61
    • 62349131315 scopus 로고    scopus 로고
    • Nucleotide excision repair: Variations on versatility
    • 2-s2.0-62349131315 10.1007/s00018-009-8737-y
    • Nouspikel T., Nucleotide excision repair: variations on versatility. Cellular and Molecular Life Sciences 2009 66 6 994 1009 2-s2.0-62349131315 10.1007/s00018-009-8737-y
    • (2009) Cellular and Molecular Life Sciences , vol.66 , Issue.6 , pp. 994-1009
    • Nouspikel, T.1
  • 62
    • 0035374836 scopus 로고    scopus 로고
    • Centrosome protein centrin 2/caltractin 1 is part of the xeroderma pigmentosum group C complex that initiates global genome nucleotide excision repair
    • 2-s2.0-0035374836 10.1074/jbc.M100855200
    • Araki M., Masutani C., Takemura M., Uchida A., Sugasawa K., Kondoh J., Ohkuma Y., Hanaoka F., Centrosome protein centrin 2/caltractin 1 is part of the xeroderma pigmentosum group C complex that initiates global genome nucleotide excision repair. Journal of Biological Chemistry 2001 276 22 18665 18672 2-s2.0-0035374836 10.1074/jbc.M100855200
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.22 , pp. 18665-18672
    • Araki, M.1    Masutani, C.2    Takemura, M.3    Uchida, A.4    Sugasawa, K.5    Kondoh, J.6    Ohkuma, Y.7    Hanaoka, F.8
  • 63
    • 0037031210 scopus 로고    scopus 로고
    • Xeroderma pigmentosum complementation group E and UV-damaged DNA-binding protein
    • DOI 10.1016/S1568-7864(02)00052-6, PII S1568786402000526
    • Tang J., Chu G., Xeroderma pigmentosum complementation group E and UV-damaged DNA-binding protein. DNA Repair 2002 1 8 601 616 2-s2.0-0037031210 10.1016/S1568-7864(02)00052-6 (Pubitemid 34765611)
    • (2002) DNA Repair , vol.1 , Issue.8 , pp. 601-616
    • Tang, J.1    Chu, G.2
  • 64
    • 34247513888 scopus 로고    scopus 로고
    • Distinct Roles for the XPB/p52 and XPD/p44 Subcomplexes of TFIIH in Damaged DNA Opening during Nucleotide Excision Repair
    • DOI 10.1016/j.molcel.2007.03.009, PII S1097276507001542
    • Coin F., Oksenych V., Egly J.-M., Distinct roles for the XPB/p52 and XPD/p44 subcomplexes of TFIIH in damaged DNA opening during nucleotide excision repair. Molecular Cell 2007 26 2 245 256 2-s2.0-34247513888 10.1016/j.molcel. 2007.03.009 (Pubitemid 46656218)
    • (2007) Molecular Cell , vol.26 , Issue.2 , pp. 245-256
    • Coin, F.1    Oksenych, V.2    Egly, J.-M.3
  • 66
    • 0028085556 scopus 로고
    • XPG endonuclease makes the 3' incision in human DNA nucleotide excision repair
    • DOI 10.1038/371432a0
    • O'Donovan A., Davies A. A., Moggs J. G., West S. C., Wood R. D., XPG endonuclease makes the 3' incision in human DNA nucleotide excision repair. Nature 1994 371 6496 432 435 2-s2.0-0028085556 10.1038/371432a0 (Pubitemid 24302560)
    • (1994) Nature , vol.371 , Issue.6496 , pp. 432-435
    • O'Donovan, A.1    Davies, A.A.2    Moggs, J.G.3    West, S.C.4    Wood, R.D.5
  • 67
    • 0029870677 scopus 로고    scopus 로고
    • Reaction mechanism of human DNA repair excision nuclease
    • DOI 10.1074/jbc.271.14.8285
    • Mu D., Hsu D. S., Sancar A., Reaction mechanism of human DNA repair excision nuclease. Journal of Biological Chemistry 1996 271 14 8285 8294 2-s2.0-0029870677 10.1074/jbc.271.14.8285 (Pubitemid 26108661)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.14 , pp. 8285-8294
    • Mu, D.1    Hsu, D.S.2    Sancar, A.3
  • 68
    • 0026569926 scopus 로고
    • The function of DNA polymerases in DNA repair synthesis of ultraviolet-irradiated human fibroblasts
    • 2-s2.0-0026569926 10.1016/0167-4781(92)90480-N
    • Popanda O., Thielmann H. W., The function of DNA polymerases in DNA repair synthesis of ultraviolet-irradiated human fibroblasts. Biochimica et Biophysica Acta 1992 1129 2 155 160 2-s2.0-0026569926 10.1016/0167-4781(92) 90480-N
    • (1992) Biochimica et Biophysica Acta , vol.1129 , Issue.2 , pp. 155-160
    • Popanda, O.1    Thielmann, H.W.2
  • 69
    • 0026546407 scopus 로고
    • Proliferating cell nuclear antigen is required for DNA excision repair
    • 2-s2.0-0026546407 10.1016/0092-8674(92)90416-A
    • Shivji M. K. K., Kenny M. K., Wood R. D., Proliferating cell nuclear antigen is required for DNA excision repair. Cell 1992 69 2 367 374 2-s2.0-0026546407 10.1016/0092-8674(92)90416-A
    • (1992) Cell , vol.69 , Issue.2 , pp. 367-374
    • Shivji, M.K.K.1    Kenny, M.K.2    Wood, R.D.3
  • 70
    • 34447302016 scopus 로고    scopus 로고
    • Sealing of Chromosomal DNA Nicks during Nucleotide Excision Repair Requires XRCC1 and DNA Ligase IIIα in a Cell-Cycle-Specific Manner
    • DOI 10.1016/j.molcel.2007.06.014, PII S1097276507004042
    • Moser J., Kool H., Giakzidis I., Caldecott K., Mullenders L. H. F., Fousteri M. I., Sealing of chromosomal DNA nicks during nucleotide excision repair requires XRCC1 and DNA ligase III α in a cell-cycle-specific manner. Molecular Cell 2007 27 2 311 323 2-s2.0-34447302016 10.1016/j.molcel. 2007.06.014 (Pubitemid 47058307)
    • (2007) Molecular Cell , vol.27 , Issue.2 , pp. 311-323
    • Moser, J.1    Kool, H.2    Giakzidis, I.3    Caldecott, K.4    Mullenders, L.H.F.5    Fousteri, M.I.6
  • 71
    • 62349130094 scopus 로고    scopus 로고
    • DNA repair in mammalian cells: Transcription-coupled DNA repair: Directing your effort where it's most needed
    • 10.1007/s00018-009-8738-x
    • Tornaletti S., silviat@ufl.edu DNA repair in mammalian cells: transcription-coupled DNA repair: directing your effort where it's most needed. Cellular and Molecular Life Sciences 2009 66 6 1010 1020 10.1007/s00018-009- 8738-x
    • (2009) Cellular and Molecular Life Sciences , vol.66 , Issue.6 , pp. 1010-1020
    • Tornaletti, S.1
  • 72
    • 0942278966 scopus 로고    scopus 로고
    • The eukaryotic nucleotide excision repair pathway
    • DOI 10.1016/j.biochi.2003.10.017
    • Costa R. M. A., Chiganas V., Galhardo R. D. S., Carvalho H., Menck C. F. M., The eukaryotic nucleotide excision repair pathway. Biochimie 2003 85 11 1083 1099 2-s2.0-0942278966 10.1016/j.biochi.2003.10.017 (Pubitemid 38142363)
    • (2003) Biochimie , vol.85 , Issue.11 , pp. 1083-1099
    • Costa, R.M.A.1    Chigancas, V.2    Galhardo, R.D.S.3    Carvalho, H.4    Menck, C.F.M.5
  • 74
    • 33744795969 scopus 로고    scopus 로고
    • CSA-dependent degradation of CSB by the ubiquitin-proteasome pathway establishes a link between complementation factors of the Cockayne syndrome
    • DOI 10.1101/gad.378206
    • Groisman R., Kuraoka I., Chevallier O., Gaye N., Magnaldo T., Tanaka K., Kisselev A. F., Harel-Bellan A., Nakatani Y., CSA-dependent degradation of CSB by the ubiquitin-proteasome pathway establishes a link between complementation factors of the Cockayne syndrome. Genes and Development 2006 20 11 1429 1434 2-s2.0-33744795969 10.1101/gad.378206 (Pubitemid 43830649)
    • (2006) Genes and Development , vol.20 , Issue.11 , pp. 1429-1434
    • Groisman, R.1    Kuraoka, I.2    Chevallier, O.3    Gaye, N.4    Magnaldo, T.5    Tanaka, K.6    Kisselev, A.F.7    Harel-Bellan, A.8    Nakatani, Y.9
  • 75
    • 0242442569 scopus 로고    scopus 로고
    • Dna Mismatch Repair: Molecular Mechanisms and Biological Function
    • DOI 10.1146/annurev.micro.57.030502.090847
    • Schofield M. J., Hsieh P., Dna mismatch repair: molecular mechanisms and biological function. Annual Review of Microbiology 2003 57 579 608 2-s2.0-0242442569 10.1146/annurev.micro.57.030502.090847 (Pubitemid 37406637)
    • (2003) Annual Review of Microbiology , vol.57 , pp. 579-608
    • Schofield, M.J.1    Hsieh, P.2
  • 76
    • 0034653444 scopus 로고    scopus 로고
    • Mutator phenotype due to loss of heterozygosity in diploid yeast strains with mutations in MSH2 and MLH1
    • DOI 10.1016/S0378-4274(99)00276-3, PII S0378427499002763
    • Drotschmann K., Shcherbakova P. V., Kunkel T. A., Mutator phenotype due to loss of heterozygosity in diploid yeast strains with mutations in MSH2 and MLH1. Toxicology Letters 2000 112-113 239 244 2-s2.0-0034653444 10.1016/S0378-4274(99)00276-3 (Pubitemid 30138129)
    • (2000) Toxicology Letters , vol.112-113 , pp. 239-244
    • Drotschmann, K.1    Shcherbakova, P.V.2    Kunkel, T.A.3
  • 77
    • 0029860724 scopus 로고    scopus 로고
    • High mutation frequencies among Escherichia coli and Salmonella pathogens
    • DOI 10.1126/science.274.5290.1208
    • LeClerc J. E., Li B., Payne W. L., Cebula T. A., High mutation frequencies among Escherichia coli and Salmonella pathogens. Science 1996 274 5290 1208 1211 2-s2.0-0029860724 10.1126/science.274.5290.1208 (Pubitemid 26389290)
    • (1996) Science , vol.274 , Issue.5290 , pp. 1208-1211
    • LeClerc, J.E.1    Li, B.2    Payne, W.L.3    Cebula, T.A.4
  • 78
    • 0035118974 scopus 로고    scopus 로고
    • Second-order selection in bacterial evolution: Selection acting on mutation and recombination rates in the course of adaptation
    • DOI 10.1016/S0923-2508(00)01163-3
    • Tenaillon O., Taddei F., Radman M., Matic I., Second-order selection in bacterial evolution: selection acting on mutation and recombination rates in the course of adaptation. Research in Microbiology 2001 152 1 11 16 2-s2.0-0035118974 10.1016/S0923-2508(00)01163-3 (Pubitemid 32168113)
    • (2001) Research in Microbiology , vol.152 , Issue.1 , pp. 11-16
    • Tenaillon, O.1    Taddei, F.2    Radman, M.3    Matic, I.4
  • 79
    • 0032979190 scopus 로고    scopus 로고
    • Mutators, population size, adaptive landscape and the adaptation of asexual populations of bacteria
    • Tenaillon O., Toupance B., Nagard H. L., Taddei F., Godelle B., Mutators, population size, adaptive landscape and the adaptation of asexual populations of bacteria. Genetics 1999 152 2 485 493 2-s2.0-0032979190 (Pubitemid 29272703)
    • (1999) Genetics , vol.152 , Issue.2 , pp. 485-493
    • Tenaillon, O.1    Toupance, B.2    Nagard, H.L.3    Taddei, F.4    Godelle, B.5
  • 80
    • 1642444868 scopus 로고    scopus 로고
    • Trypanosoma cruzi: Genetic structure of populations and relevance of genetic variability to the pathogenesis of chagas disease
    • Macedo A. M., Machado C. R., Oliveira R. P., Pena S. D. J., Trypanosoma cruzi: genetic structure of populations and relevance of genetic variability to the pathogenesis of chagas disease. Memorias do Instituto Oswaldo Cruz 2004 99 1 1 12 2-s2.0-1642444868 (Pubitemid 38406258)
    • (2004) Memorias do Instituto Oswaldo Cruz , vol.99 , Issue.1 , pp. 1-12
    • Macedo, A.M.1    Machado, C.R.2    Oliveira, R.P.3    Pena, S.D.J.4
  • 82
    • 0038326937 scopus 로고    scopus 로고
    • Trypanosoma cruzi clonal diversity and the epidemiology of Chagas' disease
    • DOI 10.1016/S1286-4579(03)00050-9
    • Buscaglia C. A., Di Noia J. M., Trypanosoma cruzi clonal diversity and the epidemiology of Chagas' disease. Microbes and Infection 2003 5 5 419 427 2-s2.0-0038326937 10.1016/S1286-4579(03)00050-9 (Pubitemid 36549184)
    • (2003) Microbes and Infection , vol.5 , Issue.5 , pp. 419-427
    • Buscaglia, C.A.1    Di Noia, J.M.2
  • 84
    • 34548588250 scopus 로고    scopus 로고
    • Sequence diversity and differential expression of Tc52 immuno-regulatory protein in Trypanosoma cruzi: Potential implications in the biological variability of strains
    • DOI 10.1007/s00436-007-0651-3
    • Mathieu-Daudé F., Bosseno M.-F., Garzon E., Lelièvre J., Sereno D., Ouaissi A., Brenière S. F., Sequence diversity and differential expression of Tc52 immuno-regulatory protein in Trypanosoma cruzi: potential implications in the biological variability of strains. Parasitology Research 2007 101 5 1355 1363 2-s2.0-34548588250 10.1007/s00436-007-0651-3 (Pubitemid 47389448)
    • (2007) Parasitology Research , vol.101 , Issue.5 , pp. 1355-1363
    • Mathieu-Daude, F.1    Bosseno, M.-F.2    Garzon, E.3    Lelievre, J.4    Sereno, D.5    Ouaissi, A.6    Breniere, S.F.7
  • 86
    • 0035845015 scopus 로고    scopus 로고
    • Molecular cloning and characterization of the DNA mismatch repair gene class 2 from the Trypanosoma cruzi
    • DOI 10.1016/S0378-1119(01)00549-2, PII S0378111901005492
    • Augusto-Pinto L., Bartholomeu D. C., Teixeira S. M. R., Pena S. D. J., Machado C. R., Molecular cloning and characterization of the DNA mismatch repair gene class 2 from the Trypanosoma cruzi. Gene 2001 272 1-2 323 333 2-s2.0-0035845015 10.1016/S0378-1119(01)00549-2 (Pubitemid 32695425)
    • (2001) Gene , vol.272 , Issue.1-2 , pp. 323-333
    • Augusto-Pinto, L.1    Bartholomeu, D.C.2    Teixeira, S.M.R.3    Pena, S.D.J.4    Machado, C.R.5
  • 87
    • 34250630882 scopus 로고    scopus 로고
    • Reduced host cell reactivation of oxidative DNA damage in human cells deficient in the mismatch repair gene hMSH2
    • DOI 10.1093/mutage/gem008
    • Pitsikas P., Lee D., Rainbow A. J., Reduced host cell reactivation of oxidative DNA damage in human cells deficient in the mismatch repair gene hMSH2. Mutagenesis 2007 22 3 235 243 2-s2.0-34250630882 10.1093/mutage/gem008 (Pubitemid 47355714)
    • (2007) Mutagenesis , vol.22 , Issue.3 , pp. 235-243
    • Pitsikas, P.1    Lee, D.2    Rainbow, A.J.3
  • 88
    • 26244452150 scopus 로고    scopus 로고
    • The Helicobacter pylori MutS protein confers protection from oxidative DNA damage
    • DOI 10.1111/j.1365-2958.2005.04833.x
    • Wang G., Alamuri P., Humayun M. Z., Taylor D. E., Maier R. J., The Helicobacter pylori MutS protein confers protection from oxidative DNA damage. Molecular Microbiology 2005 58 1 166 176 2-s2.0-26244452150 10.1111/j.1365-2958. 2005.04833.x (Pubitemid 41415038)
    • (2005) Molecular Microbiology , vol.58 , Issue.1 , pp. 166-176
    • Wang, G.1    Alamuri, P.2    Zafri Humayun, M.3    Taylor, D.E.4    Maier, R.J.5
  • 89
    • 0033934776 scopus 로고    scopus 로고
    • Arabidopsis MutS homologs - AtMSH2, AtMSH3, AtMSH6, and a novel AtMSH7 - Form three distinct protein heterodimers with different specificities for mismatched DNA
    • DOI 10.1105/tpc.12.6.991
    • Culligan K. M., Hays J. B., Arabidopsis MutS homologs-AtMSH2, AtMSH3, AtMSH6, and a novel AtMSH7 - form three distinct protein heterodimers with different specificities for mismatched DNA. Plant Cell 2000 12 6 991 1002 2-s2.0-0033934776 10.1105/tpc.12.6.991 (Pubitemid 30458042)
    • (2000) Plant Cell , vol.12 , Issue.6 , pp. 991-1002
    • Culligan, K.M.1    Hays, J.B.2
  • 90
    • 38049155945 scopus 로고    scopus 로고
    • Regulation of DNA double-strand break repair pathway choice
    • 2-s2.0-38049155945 10.1038/cr.2007.111
    • Shrivastav M., De Haro L. P., Nickoloff J. A., Regulation of DNA double-strand break repair pathway choice. Cell Research 2008 18 1 134 147 2-s2.0-38049155945 10.1038/cr.2007.111
    • (2008) Cell Research , vol.18 , Issue.1 , pp. 134-147
    • Shrivastav, M.1    De Haro, L.P.2    Nickoloff, J.A.3
  • 91
    • 0038730984 scopus 로고    scopus 로고
    • The paradoxical relationship between NHEJ and telomeric fusion
    • DOI 10.1016/S1097-2765(03)00200-4
    • Williams B., Lustig A. J., The paradoxical relationship between NHEJ and telomeric fusion. Molecular Cell 2003 11 5 1125 1126 2-s2.0-0038730984 10.1016/S1097-2765(03)00200-4 (Pubitemid 36645132)
    • (2003) Molecular Cell , vol.11 , Issue.5 , pp. 1125-1126
    • Williams, B.1    Lustig, A.J.2
  • 92
    • 35348871435 scopus 로고    scopus 로고
    • Ku heterodimer-independent end joining in Trypanosoma brucei cell extracts relies upon sequence microhomology
    • DOI 10.1128/EC.00212-07
    • Burton P., McBride D. J., Wilkes J. M., Barry J. D., McCulloch R., Ku heterodimer-independent end joining in Trypanosoma brucei cell extracts relies upon sequence microhomology. Eukaryotic Cell 2007 6 10 1773 1781 2-s2.0-35348871435 10.1128/EC.00212-07 (Pubitemid 47585567)
    • (2007) Eukaryotic Cell , vol.6 , Issue.10 , pp. 1773-1781
    • Burton, P.1    McBride, D.J.2    Wilkes, J.M.3    Barry, J.D.4    McCulloch, R.5
  • 93
    • 3242886313 scopus 로고    scopus 로고
    • Homologous recombination-mediated double-strand break repair
    • DOI 10.1016/j.dnarep.2004.03.037, PII S1568786404001090
    • Wyman C., Ristic D., Kanaar R., Homologous recombination-mediated double-strand break repair. DNA Repair 2004 3 8-9 827 833 2-s2.0-3242886313 10.1016/j.dnarep.2004.03.037 (Pubitemid 38997924)
    • (2004) DNA Repair , vol.3 , Issue.8-9 , pp. 827-833
    • Wyman, C.1    Ristic, D.2    Kanaar, R.3
  • 94
    • 10344263324 scopus 로고    scopus 로고
    • Recombination proteins in yeast
    • DOI 10.1146/annurev.genet.38.072902.091500
    • Krogh B. O., Symington L. S., Recombination proteins in yeast. Annual Review of Genetics 2004 38 233 271 2-s2.0-10344263324 10.1146/annurev.genet.38. 072902.091500 (Pubitemid 40013729)
    • (2004) Annual Review of Genetics , vol.38 , pp. 233-271
    • Krogh, B.O.1    Symington, L.S.2
  • 95
    • 2442494879 scopus 로고    scopus 로고
    • Molecular players of homologous recombination in protozoan parasites: Implications for generating antigenic variation
    • DOI 10.1016/j.meegid.2004.01.008, PII S1567134804000103
    • Bhattacharyya M. K., Norris D. E., Kumar N., Molecular players of homologous recombination in protozoan parasites: implications for generating antigenic variation. Infection, Genetics and Evolution 2004 4 2 91 98 2-s2.0-2442494879 10.1016/j.meegid.2004.01.008 (Pubitemid 38647292)
    • (2004) Infection, Genetics and Evolution , vol.4 , Issue.2 , pp. 91-98
    • Kanti Bhattacharyya, M.1    Norris, D.E.2    Kumar, N.3
  • 96
    • 67249163230 scopus 로고    scopus 로고
    • Genomic organization and expression profile of the mucin-associated surface protein (masp) family of the human pathogen Trypanosoma cruzi
    • 2-s2.0-67249163230 10.1093/nar/gkp172
    • Bartholomeu D. C., Cerqueira G. C., Leão A. C. A., daRocha W. D., Pais F. S., Macedo C., Djikeng A., Teixeira S. M. R., El-Sayed N. M., Genomic organization and expression profile of the mucin-associated surface protein (masp) family of the human pathogen Trypanosoma cruzi. Nucleic Acids Research 2009 37 10 3407 3417 2-s2.0-67249163230 10.1093/nar/gkp172
    • (2009) Nucleic Acids Research , vol.37 , Issue.10 , pp. 3407-3417
    • Bartholomeu, D.C.1    Cerqueira, G.C.2    Leão, A.C.A.3    Darocha, W.D.4    Pais, F.S.5    Macedo, C.6    Djikeng, A.7    Teixeira, S.M.R.8    El-Sayed, N.M.9
  • 97
    • 0033198238 scopus 로고    scopus 로고
    • Genetic manipulation of kinetoplastida
    • DOI 10.1016/S0169-4758(99)01498-2, PII S0169475899014982
    • Clayton C. E., Genetic manipulation of kinetoplastida. Parasitology Today 1999 15 9 372 378 2-s2.0-0033198238 10.1016/S0169-4758(99)01498-2 (Pubitemid 29392918)
    • (1999) Parasitology Today , vol.15 , Issue.9 , pp. 372-378
    • Clayton, C.E.1
  • 98
    • 0037226127 scopus 로고    scopus 로고
    • Protozomics: Trypanosomatid parasite genetics comes of age
    • DOI 10.1038/nrg980
    • Beverley S. M., Protozomics: trypanosomatid parasite genetics comes of age. Nature Reviews Genetics 2003 4 1 11 19 2-s2.0-0037226127 10.1038/nrg980 (Pubitemid 36043211)
    • (2003) Nature Reviews Genetics , vol.4 , Issue.1 , pp. 11-19
    • Beverley, S.M.1
  • 100
    • 34250863858 scopus 로고    scopus 로고
    • Trypnosoma brucei homologous recombination is dependent on substrate length and homology, though displays a differential dependence on mismatch repair as substrate length decreases
    • DOI 10.1093/nar/gkm249
    • Barnes R. L., McCulloch R., Trypanosoma brucei homologous recombination is dependent on substrate length and homology, though displays a differential dependence on mismatch repair as substrate length decreases. Nucleic Acids Research 2007 35 10 3478 3493 2-s2.0-34250863858 10.1093/nar/gkm249 (Pubitemid 47073608)
    • (2007) Nucleic Acids Research , vol.35 , Issue.10 , pp. 3478-3493
    • Barnes, R.L.1    McCulloch, R.2
  • 101
    • 0036746010 scopus 로고    scopus 로고
    • The clonal theory of parasitic protozoa: 12 years on
    • 2-s2.0-0036746010 10.1016/S1471-4922(02)02357-7
    • Tibayrenc M., Ayala F. J., The clonal theory of parasitic protozoa: 12 years on. Trends in Parasitology 2002 18 9 405 410 2-s2.0-0036746010 10.1016/S1471-4922(02)02357-7
    • (2002) Trends in Parasitology , vol.18 , Issue.9 , pp. 405-410
    • Tibayrenc, M.1    Ayala, F.J.2
  • 102
    • 0019207221 scopus 로고
    • Evidence for diploidy and mating in trypanosomes
    • DOI 10.1038/287536a0
    • Tait A., Evidence for diploidy and mating in trypanosomes. Nature 1980 287 5782 536 538 2-s2.0-0019207221 (Pubitemid 11232850)
    • (1980) Nature , vol.287 , Issue.5782 , pp. 536-538
    • Tait, A.1
  • 103
    • 0029988837 scopus 로고    scopus 로고
    • Polymorphisms in Trypanosoma cruzi: Evidence of genetic recombination
    • DOI 10.1016/0001-706X(95)00138-5
    • Bogliolo A. R., Lauria-Pires L., Gibson W. C., Polymorphisms in Trypanosoma cruzi: evidence of genetic recombination. Acta Tropica 1996 61 1 31 40 2-s2.0-0029988837 10.1016/0001-706X(95)00138-5 (Pubitemid 26142947)
    • (1996) Acta Tropica , vol.61 , Issue.1 , pp. 31-40
    • Bogliolo, A.R.1    Lauria-Pires, L.2    Gibson, W.C.3
  • 104
    • 0029868150 scopus 로고    scopus 로고
    • Genetic exchange as a possible source of genomic diversity in sylvatic populations of Trypanosoma cruzi
    • Carrasco H. J., Frame I. A., Valente S. A., Miles M. A., Genetic exchange as a possible source of genomic diversity in sylvatic populations of Trypanosoma cruzi. American Journal of Tropical Medicine and Hygiene 1996 54 4 418 424 2-s2.0-0029868150 (Pubitemid 26126653)
    • (1996) American Journal of Tropical Medicine and Hygiene , vol.54 , Issue.4 , pp. 418-424
    • Carrasco, H.J.1    Frame, I.A.2    Valente, S.A.3    Miles, M.A.4
  • 106
    • 0032991895 scopus 로고    scopus 로고
    • How do protozoan parasites survive inside macrophages?
    • DOI 10.1016/S0169-4758(98)01362-3, PII S0169475898013623
    • Bogdan C., Röllinghoff M., How do protozoan parasites survive inside macrophages? Parasitology Today 1999 15 1 22 28 2-s2.0-0032991895 10.1016/S0169-4758(98)01362-3 (Pubitemid 29246041)
    • (1999) Parasitology Today , vol.15 , Issue.1 , pp. 22-28
    • Bogdan, C.1    Rollinghoff, M.2
  • 107
    • 43349103776 scopus 로고    scopus 로고
    • Sequence homology and microhomology dominate chromosomal double-strand break repair in African trypanosomes
    • DOI 10.1093/nar/gkn104
    • Glover L., McCulloch R., Horn D., Sequence homology and microhomology dominate chromosomal double-strand break repair in African trypanosomes. Nucleic Acids Research 2008 36 8 2608 2618 2-s2.0-43349103776 10.1093/nar/gkn104 (Pubitemid 351659575)
    • (2008) Nucleic Acids Research , vol.36 , Issue.8 , pp. 2608-2618
    • Glover, L.1    McCulloch, R.2    Horn, D.3
  • 109
    • 0027652660 scopus 로고
    • Influence of heat shock, drugs, and radiation on karyotype of Leishmania major
    • 2-s2.0-0027652660
    • Seo M., Chun D. K., Hong S. T., Lee S. H., Influence of heat shock, drugs, and radiation on karyotype of Leishmania major. Korean Journal of Parasitology 1993 31 3 277 283 2-s2.0-0027652660
    • (1993) Korean Journal of Parasitology , vol.31 , Issue.3 , pp. 277-283
    • Seo, M.1    Chun, D.K.2    Hong, S.T.3    Lee, S.H.4
  • 111
    • 0031466027 scopus 로고    scopus 로고
    • RAD51 interacts with the evolutionarily conserved BRC motifs in the human breast cancer susceptibility gene brca2
    • DOI 10.1074/jbc.272.51.31941
    • Wong A. K. C., Pero R., Ormonde P. A., Tavtigian S. V., Bartel P. L., RAD51 interacts with the evolutionarily conserved BRC motifs in the human breast cancer susceptibility gene brca2. Journal of Biological Chemistry 1997 272 51 31941 31944 2-s2.0-0031466027 10.1074/jbc.272.51.31941 (Pubitemid 28011857)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.51 , pp. 31941-31944
    • Wong, A.K.C.1    Pero, R.2    Ormonde, P.A.3    Tavtigian, S.V.4    Bartel, P.L.5
  • 114
    • 0029968845 scopus 로고    scopus 로고
    • Targeting of exogenous DNA into Trypanosoma brucei requires a high degree of homology between donor and target DNA
    • DOI 10.1016/0166-6851(95)02560-X
    • Blundell P. A., Rudenko G., Borst P., Targeting of exogenous DNA into Trypanosoma brucei requires a high degree of homology between donor and target DNA. Molecular and Biochemical Parasitology 1996 76 1-2 215 229 2-s2.0-0029968845 10.1016/0166-6851(95)02560-X (Pubitemid 26122736)
    • (1996) Molecular and Biochemical Parasitology , vol.76 , Issue.1-2 , pp. 215-229
    • Blundell, P.A.1    Rudenko, G.2    Borst, P.3
  • 115
    • 34249941966 scopus 로고    scopus 로고
    • Translesion synthesis: Y-family polymerases and the polymerase switch
    • DOI 10.1016/j.dnarep.2007.02.003, PII S1568786407000535, Replication Fork Repair Processes
    • Lehmann A. R., Niimi A., Ogi T., Brown S., Sabbioneda S., Wing J. F., Kannouche P. L., Green C. M., Translesion synthesis: Y-family polymerases and the polymerase switch. DNA Repair 2007 6 7 891 899 2-s2.0-34249941966 10.1016/j.dnarep.2007.02.003 (Pubitemid 46880470)
    • (2007) DNA Repair , vol.6 , Issue.7 , pp. 891-899
    • Lehmann, A.R.1    Niimi, A.2    Ogi, T.3    Brown, S.4    Sabbioneda, S.5    Wing, J.F.6    Kannouche, P.L.7    Green, C.M.8
  • 116
    • 21244506437 scopus 로고    scopus 로고
    • Eukaryotic translesion synthesis DNA polymerases: Specificity of structure and function
    • DOI 10.1146/annurev.biochem.74.082803.133250
    • Prakash S., Johnson R. E., Prakash L., Eukaryotic translesion synthesis DNA polymerases: specificity of structure and function. Annual Review of
    • (2005) Annual Review of Biochemistry , vol.74 , pp. 317-353
    • Prakash, S.1    Johnson, R.E.2    Prakash, L.3
  • 117
    • 70350028726 scopus 로고    scopus 로고
    • Trypanosoma cruzi infection disturbs mitochondrial membrane potential and ROS production rate in cardiomyocytes
    • 2-s2.0-70350028726 10.1016/j.freeradbiomed.2009.08.008
    • Gupta S., Bhatia V., Wen J.-J., Wu Y., Huang M.-H., Garg N. J., Trypanosoma cruzi infection disturbs mitochondrial membrane potential and ROS production rate in cardiomyocytes. Free Radical Biology and Medicine 2009 47 10 1414 1421 2-s2.0-70350028726 10.1016/j.freeradbiomed.2009.08.008
    • (2009) Free Radical Biology and Medicine , vol.47 , Issue.10 , pp. 1414-1421
    • Gupta, S.1    Bhatia, V.2    Wen, J.-J.3    Wu, Y.4    Huang, M.-H.5    Garg, N.J.6
  • 118
    • 34548021449 scopus 로고    scopus 로고
    • Immune system recognition of Trypanosoma cruzi
    • DOI 10.1016/j.coi.2007.06.003, PII S0952791507001069
    • Tarleton R. L., Immune system recognition of Trypanosoma cruzi. Current Opinion in Immunology 2007 19 4 430 434 2-s2.0-34548021449 10.1016/j.coi.2007. 06.003 (Pubitemid 47284855)
    • (2007) Current Opinion in Immunology , vol.19 , Issue.4 , pp. 430-434
    • Tarleton, R.L.1
  • 120
    • 15044361524 scopus 로고    scopus 로고
    • Real time PCR strategy for the identification of major lineages of Trypanosoma cruzi directly in chronically infected human tissues
    • DOI 10.1016/j.ijpara.2004.10.023
    • Freitas J. M., Lages-Silva E., Crema E., Pena S. D. J., Macedo A. M., Real time PCR strategy for the identification of major lineages of Trypanosoma cruzi directly in chronically infected human tissues. International Journal for Parasitology 2005 35 4 411 417 2-s2.0-15044361524 10.1016/j.ijpara.2004.10.023 (Pubitemid 40381159)
    • (2005) International Journal for Parasitology , vol.35 , Issue.4 , pp. 411-417
    • Freitas, J.M.1    Lages-Silva, E.2    Crema, E.3    Pena, S.D.J.4    Macedo, A.M.5
  • 121
    • 0032892643 scopus 로고    scopus 로고
    • The complexity of the sylvatic cycle of Trypanosoma cruzi in Rio de Janeiro state (Brazil) revealed by the non-transcribed spacer of the mini-exon gene
    • DOI 10.1017/S0031182098003709
    • Fernandes O., Mangia R. H., Lisboa C. V., Pinho A. P., Morel C. M., Zingales B., Campbell D. A., Jansen A. M., The complexity of the sylvatic cycle of Trypanosoma cruzi in Rio de Janeiro state (Brazil) revealed by the non-transcribed spacer of the mini-exon gene. Parasitology 1999 118 2 161 166 2-s2.0-0032892643 10.1017/S0031182098003709 (Pubitemid 29051865)
    • (1999) Parasitology , vol.118 , Issue.2 , pp. 161-166
    • Fernandes, O.1    Mangia, R.H.2    Lisboa, C.V.3    Pinho, A.P.4    Morel, C.M.5    Zingales, B.6    Campbell, D.A.7    Jansen, A.M.8


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