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Volumn 30, Issue , 2015, Pages 28-37

TDP1 promotes assembly of non-homologous end joining protein complexes on DNA

Author keywords

DNA dependent protein kinase (DNA PK); Ku70 80; Non homologous end joining (NHEJ); TDP1; XLF

Indexed keywords

PHOSPHODIESTERASE I; POLYDEOXYRIBONUCLEOTIDE SYNTHASE; TYROSYL DNA PHOSPHODIESTERASE 1; UNCLASSIFIED DRUG; CELL NUCLEUS ANTIGEN; DNA; DNA BINDING PROTEIN; DNA DEPENDENT PROTEIN KINASE; DNA LIGASE; KU ANTIGEN; NHEJ1 PROTEIN, HUMAN; PHOSPHODIESTERASE; TDP1 PROTEIN, HUMAN;

EID: 84925960154     PISSN: 15687864     EISSN: 15687856     Source Type: Journal    
DOI: 10.1016/j.dnarep.2015.03.003     Document Type: Article
Times cited : (34)

References (81)
  • 1
    • 27544445683 scopus 로고    scopus 로고
    • The DNA damage response during DNA replication
    • Branzei D., Foiani M. The DNA damage response during DNA replication. Curr. Opin. Cell Biol. 2005, 17:568-575.
    • (2005) Curr. Opin. Cell Biol. , vol.17 , pp. 568-575
    • Branzei, D.1    Foiani, M.2
  • 2
    • 77953229115 scopus 로고    scopus 로고
    • The mechanism of double-strand DNA break repair by the nonhomologous DNA end-joining pathway
    • Lieber M.R. The mechanism of double-strand DNA break repair by the nonhomologous DNA end-joining pathway. Annu. Rev. Biochem. 2010, 79:181-211.
    • (2010) Annu. Rev. Biochem. , vol.79 , pp. 181-211
    • Lieber, M.R.1
  • 6
    • 45749124305 scopus 로고    scopus 로고
    • Live cell imaging of XLF and XRCC4 reveals a novel view of protein assembly in the non-homologous end-joining pathway
    • Yano K., Chen D.J. Live cell imaging of XLF and XRCC4 reveals a novel view of protein assembly in the non-homologous end-joining pathway. Cell Cycle 2008, 7:1321-1325.
    • (2008) Cell Cycle , vol.7 , pp. 1321-1325
    • Yano, K.1    Chen, D.J.2
  • 7
    • 79952573454 scopus 로고    scopus 로고
    • Functional significance of the interaction with Ku in DNA double-strand break recognition of XLF
    • Yano K., Morotomi-Yano K., Lee K.J., Chen D.J. Functional significance of the interaction with Ku in DNA double-strand break recognition of XLF. FEBS Lett. 2011, 585:841-846.
    • (2011) FEBS Lett. , vol.585 , pp. 841-846
    • Yano, K.1    Morotomi-Yano, K.2    Lee, K.J.3    Chen, D.J.4
  • 8
    • 34247602569 scopus 로고    scopus 로고
    • Interaction of the Ku heterodimer with the DNA ligase IV/Xrcc4 complex and its regulation by DNA-PK
    • Costantini S., Woodbine L., Andreoli L., Jeggo P.A., Vindigni A. Interaction of the Ku heterodimer with the DNA ligase IV/Xrcc4 complex and its regulation by DNA-PK. DNA Repair (Amst.) 2007, 6:712-722.
    • (2007) DNA Repair (Amst.) , vol.6 , pp. 712-722
    • Costantini, S.1    Woodbine, L.2    Andreoli, L.3    Jeggo, P.A.4    Vindigni, A.5
  • 9
    • 0031939411 scopus 로고    scopus 로고
    • The XRCC4 gene product is a target for and interacts with the DNA-dependent protein kinase
    • Leber R., Wise T.W., Mizuta R., Meek K. The XRCC4 gene product is a target for and interacts with the DNA-dependent protein kinase. J. Biol. Chem. 1998, 273:1794-1801.
    • (1998) J. Biol. Chem. , vol.273 , pp. 1794-1801
    • Leber, R.1    Wise, T.W.2    Mizuta, R.3    Meek, K.4
  • 10
    • 0037187199 scopus 로고    scopus 로고
    • Defining interactions between DNA-PK and ligase IV/XRCC4
    • Hsu H.L., Yannone S.M., Chen D.J. Defining interactions between DNA-PK and ligase IV/XRCC4. DNA Repair (Amst.) 2002, 1:225-235.
    • (2002) DNA Repair (Amst.) , vol.1 , pp. 225-235
    • Hsu, H.L.1    Yannone, S.M.2    Chen, D.J.3
  • 11
    • 0033569666 scopus 로고    scopus 로고
    • Yeast gene for a Tyr-DNA phosphodiesterase that repairs topoisomerase I complexes
    • Pouliot J.J., Yao K.C., Robertson C.A., Nash H.A. Yeast gene for a Tyr-DNA phosphodiesterase that repairs topoisomerase I complexes. Science 1999, 286:552-555.
    • (1999) Science , vol.286 , pp. 552-555
    • Pouliot, J.J.1    Yao, K.C.2    Robertson, C.A.3    Nash, H.A.4
  • 13
    • 0035834150 scopus 로고    scopus 로고
    • The tyrosyl-DNA phosphodiesterase Tdp1 is a member of the phospholipase D superfamily
    • Interthal H., Pouliot J.J., Champoux J.J. The tyrosyl-DNA phosphodiesterase Tdp1 is a member of the phospholipase D superfamily. Proc. Natl. Acad. Sci. U. S. A. 2001, 98:12009-12014.
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 12009-12014
    • Interthal, H.1    Pouliot, J.J.2    Champoux, J.J.3
  • 14
    • 33745154128 scopus 로고    scopus 로고
    • Tyrosyl-DNA phosphodiesterase (Tdp1) participates in the repair of Top2-mediated DNA damage
    • Nitiss K.C., Malik M., He X., White S.W., Nitiss J.L. Tyrosyl-DNA phosphodiesterase (Tdp1) participates in the repair of Top2-mediated DNA damage. Proc. Natl. Acad. Sci. U. S. A. 2006, 103:8953-8958.
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 8953-8958
    • Nitiss, K.C.1    Malik, M.2    He, X.3    White, S.W.4    Nitiss, J.L.5
  • 15
    • 84898947618 scopus 로고    scopus 로고
    • TDP1 deficiency sensitizes human cells to base damage via distinct topoisomerase I and PARP mechanisms with potential applications for cancer therapy
    • Alagoz M., Wells O.S., El-Khamisy S.F. TDP1 deficiency sensitizes human cells to base damage via distinct topoisomerase I and PARP mechanisms with potential applications for cancer therapy. Nucleic Acids Res. 2014, 42:3089-3103.
    • (2014) Nucleic Acids Res. , vol.42 , pp. 3089-3103
    • Alagoz, M.1    Wells, O.S.2    El-Khamisy, S.F.3
  • 16
    • 84859761985 scopus 로고    scopus 로고
    • Tyrosyl-DNA phosphodiesterase 1 (TDP1) repairs DNA damage induced by topoisomerases I and II and base alkylation in vertebrate cells
    • Murai J., Huang S.Y., Das B.B., Dexheimer T.S., Takeda S., Pommier Y. Tyrosyl-DNA phosphodiesterase 1 (TDP1) repairs DNA damage induced by topoisomerases I and II and base alkylation in vertebrate cells. J. Biol. Chem. 2012, 287:12848-12857.
    • (2012) J. Biol. Chem. , vol.287 , pp. 12848-12857
    • Murai, J.1    Huang, S.Y.2    Das, B.B.3    Dexheimer, T.S.4    Takeda, S.5    Pommier, Y.6
  • 17
    • 0037178839 scopus 로고    scopus 로고
    • Conversion of phosphoglycolate to phosphate termini on 3' overhangs of DNA double strand breaks by the human tyrosyl-DNA phosphodiesterase hTdp1
    • Inamdar K.V., Pouliot J.J., Zhou T., Lees-Miller S.P., Rasouli-Nia A., Povirk L.F. Conversion of phosphoglycolate to phosphate termini on 3' overhangs of DNA double strand breaks by the human tyrosyl-DNA phosphodiesterase hTdp1. J. Biol. Chem. 2002, 277:27162-27168.
    • (2002) J. Biol. Chem. , vol.277 , pp. 27162-27168
    • Inamdar, K.V.1    Pouliot, J.J.2    Zhou, T.3    Lees-Miller, S.P.4    Rasouli-Nia, A.5    Povirk, L.F.6
  • 19
    • 27744521320 scopus 로고    scopus 로고
    • Human Tdp1 cleaves a broad spectrum of substrates, including phosphoamide linkages
    • Interthal H., Chen H.J., Champoux J.J. Human Tdp1 cleaves a broad spectrum of substrates, including phosphoamide linkages. J. Biol. Chem. 2005, 280:36518-36528.
    • (2005) J. Biol. Chem. , vol.280 , pp. 36518-36528
    • Interthal, H.1    Chen, H.J.2    Champoux, J.J.3
  • 20
    • 84886828375 scopus 로고    scopus 로고
    • TDP1 repairs nuclear and mitochondrial DNA damage induced by chain-terminating anticancer and antiviral nucleoside analogs
    • Huang S.Y., Murai J., Dalla Rosa I., Dexheimer T.S., Naumova A., Gmeiner W.H., Pommier Y. TDP1 repairs nuclear and mitochondrial DNA damage induced by chain-terminating anticancer and antiviral nucleoside analogs. Nucleic Acids Res. 2013, 41:7793-7803.
    • (2013) Nucleic Acids Res. , vol.41 , pp. 7793-7803
    • Huang, S.Y.1    Murai, J.2    Dalla Rosa, I.3    Dexheimer, T.S.4    Naumova, A.5    Gmeiner, W.H.6    Pommier, Y.7
  • 23
    • 77952300162 scopus 로고    scopus 로고
    • The DNA binding and 3'-end preferential activity of human tyrosyl-DNA phosphodiesterase
    • Dexheimer T.S., Stephen A.G., Fivash M.J., Fisher R.J., Pommier Y. The DNA binding and 3'-end preferential activity of human tyrosyl-DNA phosphodiesterase. Nucleic Acids Res. 2010, 38:2444-2452.
    • (2010) Nucleic Acids Res. , vol.38 , pp. 2444-2452
    • Dexheimer, T.S.1    Stephen, A.G.2    Fivash, M.J.3    Fisher, R.J.4    Pommier, Y.5
  • 24
    • 21844437071 scopus 로고    scopus 로고
    • SCAN1 mutant Tdp1 accumulates the enzyme - DNA intermediate and causes camptothecin hypersensitivity
    • Interthal H., Chen H.J., Kehl-Fie T.E., Zotzmann J., Leppard J.B., Champoux J.J. SCAN1 mutant Tdp1 accumulates the enzyme - DNA intermediate and causes camptothecin hypersensitivity. EMBO J. 2005, 24:2224-2233.
    • (2005) EMBO J. , vol.24 , pp. 2224-2233
    • Interthal, H.1    Chen, H.J.2    Kehl-Fie, T.E.3    Zotzmann, J.4    Leppard, J.B.5    Champoux, J.J.6
  • 26
    • 13744253911 scopus 로고    scopus 로고
    • Deficiency in 3'-phosphoglycolate processing in human cells with a hereditary mutation in tyrosyl-DNA phosphodiesterase (TDP1)
    • Zhou T., Lee J.W., Tatavarthi H., Lupski J.R., Valerie K., Povirk L.F. Deficiency in 3'-phosphoglycolate processing in human cells with a hereditary mutation in tyrosyl-DNA phosphodiesterase (TDP1). Nucleic Acids Res. 2005, 33:289-297.
    • (2005) Nucleic Acids Res. , vol.33 , pp. 289-297
    • Zhou, T.1    Lee, J.W.2    Tatavarthi, H.3    Lupski, J.R.4    Valerie, K.5    Povirk, L.F.6
  • 27
    • 84877824758 scopus 로고    scopus 로고
    • Processing of damaged DNA ends for double-strand break repair in mammalian cells
    • Povirk L.F. Processing of damaged DNA ends for double-strand break repair in mammalian cells. ISRN Mol. Biol. 2012, 2012:1-16.
    • (2012) ISRN Mol. Biol. , vol.2012 , pp. 1-16
    • Povirk, L.F.1
  • 29
    • 77749270650 scopus 로고    scopus 로고
    • Yeast Tdp1 regulates the fidelity of nonhomologous end joining
    • Bahmed K., Nitiss K.C., Nitiss J.L. Yeast Tdp1 regulates the fidelity of nonhomologous end joining. Proc. Natl. Acad. Sci. U. S. A. 2010, 107:4057-4062.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 4057-4062
    • Bahmed, K.1    Nitiss, K.C.2    Nitiss, J.L.3
  • 30
    • 80054698886 scopus 로고    scopus 로고
    • Effect of the inositol polyphosphate InsP(6) on DNA-PK-dependent phosphorylation
    • Hanakahi L. Effect of the inositol polyphosphate InsP(6) on DNA-PK-dependent phosphorylation. Mol. Cancer Res. 2011, 9:1366-1376.
    • (2011) Mol. Cancer Res. , vol.9 , pp. 1366-1376
    • Hanakahi, L.1
  • 31
    • 56349167080 scopus 로고    scopus 로고
    • E1B 55k-independent dissociation of the DNA ligase IV/XRCC4 complex by E4 34k during adenovirus infection
    • Jayaram S., Gilson T., Ehrlich E.S., Yu X.F., Ketner G., Hanakahi L. E1B 55k-independent dissociation of the DNA ligase IV/XRCC4 complex by E4 34k during adenovirus infection. Virology 2008, 382:163-170.
    • (2008) Virology , vol.382 , pp. 163-170
    • Jayaram, S.1    Gilson, T.2    Ehrlich, E.S.3    Yu, X.F.4    Ketner, G.5    Hanakahi, L.6
  • 32
    • 0022340978 scopus 로고
    • Isolation of monoclonal antibodies specific for human c-myc proto-oncogene product
    • Evan G.I., Lewis G.K., Ramsay G., Bishop J.M. Isolation of monoclonal antibodies specific for human c-myc proto-oncogene product. Mol. Cell. Biol. 1985, 5:3610-3616.
    • (1985) Mol. Cell. Biol. , vol.5 , pp. 3610-3616
    • Evan, G.I.1    Lewis, G.K.2    Ramsay, G.3    Bishop, J.M.4
  • 33
    • 0345061277 scopus 로고    scopus 로고
    • Association of XRCC1 and tyrosyl DNA phosphodiesterase (Tdp1) for the repair of topoisomerase I-mediated DNA lesions
    • Plo I., Liao Z.Y., Barcelo J.M., Kohlhagen G., Caldecott K.W., Weinfeld M., Pommier Y. Association of XRCC1 and tyrosyl DNA phosphodiesterase (Tdp1) for the repair of topoisomerase I-mediated DNA lesions. DNA Repair (Amst.) 2003, 2:1087-1100.
    • (2003) DNA Repair (Amst.) , vol.2 , pp. 1087-1100
    • Plo, I.1    Liao, Z.Y.2    Barcelo, J.M.3    Kohlhagen, G.4    Caldecott, K.W.5    Weinfeld, M.6    Pommier, Y.7
  • 34
    • 34547829271 scopus 로고    scopus 로고
    • Novel high-throughput electrochemiluminescent assay for identification of human tyrosyl-DNA phosphodiesterase (Tdp1) inhibitors and characterization of furamidine (NSC 305831) as an inhibitor of Tdp1
    • Antony S., Marchand C., Stephen A.G., Thibaut L., Agama K.K., Fisher R.J., Pommier Y. Novel high-throughput electrochemiluminescent assay for identification of human tyrosyl-DNA phosphodiesterase (Tdp1) inhibitors and characterization of furamidine (NSC 305831) as an inhibitor of Tdp1. Nucleic Acids Res. 2007, 35:4474-4484.
    • (2007) Nucleic Acids Res. , vol.35 , pp. 4474-4484
    • Antony, S.1    Marchand, C.2    Stephen, A.G.3    Thibaut, L.4    Agama, K.K.5    Fisher, R.J.6    Pommier, Y.7
  • 36
    • 0026651978 scopus 로고
    • Ethidium bromide provides a simple tool for identifying genuine DNA-independent protein associations
    • Lai J.S., Herr W. Ethidium bromide provides a simple tool for identifying genuine DNA-independent protein associations. Proc. Natl. Acad. Sci. U. S. A. 1992, 89:6958-6962.
    • (1992) Proc. Natl. Acad. Sci. U. S. A. , vol.89 , pp. 6958-6962
    • Lai, J.S.1    Herr, W.2
  • 37
    • 0028199891 scopus 로고
    • Inhibition of p53 DNA binding by human papillomavirus E6 proteins
    • Lechner M.S., Laimins L.A. Inhibition of p53 DNA binding by human papillomavirus E6 proteins. J. Virol. 1994, 68:4262-4273.
    • (1994) J. Virol. , vol.68 , pp. 4262-4273
    • Lechner, M.S.1    Laimins, L.A.2
  • 38
    • 31744440828 scopus 로고    scopus 로고
    • Protein-protein interaction assays: eliminating false positive interactions
    • Nguyen T.N., Goodrich J.A. Protein-protein interaction assays: eliminating false positive interactions. Nat. Methods 2006, 3:135-139.
    • (2006) Nat. Methods , vol.3 , pp. 135-139
    • Nguyen, T.N.1    Goodrich, J.A.2
  • 39
    • 79957706011 scopus 로고    scopus 로고
    • Effects of DNA and protein size on substrate cleavage by human tyrosyl-DNA phosphodiesterase 1
    • Interthal H., Champoux J.J. Effects of DNA and protein size on substrate cleavage by human tyrosyl-DNA phosphodiesterase 1. Biochem. J. 2011, 436:559-566.
    • (2011) Biochem. J. , vol.436 , pp. 559-566
    • Interthal, H.1    Champoux, J.J.2
  • 40
    • 0036493236 scopus 로고    scopus 로고
    • Processing of nucleopeptides mimicking the topoisomerase I-DNA covalent complex by tyrosyl-DNA phosphodiesterase
    • Debethune L., Kohlhagen G., Grandas A., Pommier Y. Processing of nucleopeptides mimicking the topoisomerase I-DNA covalent complex by tyrosyl-DNA phosphodiesterase. Nucleic Acids Res. 2002, 30:1198-1204.
    • (2002) Nucleic Acids Res. , vol.30 , pp. 1198-1204
    • Debethune, L.1    Kohlhagen, G.2    Grandas, A.3    Pommier, Y.4
  • 41
    • 34249685474 scopus 로고    scopus 로고
    • Length-dependent binding of human XLF to DNA and stimulation of XRCC4.DNA ligase IV activity
    • Lu H., Pannicke U., Schwarz K., Lieber M.R. Length-dependent binding of human XLF to DNA and stimulation of XRCC4.DNA ligase IV activity. J. Biol. Chem. 2007, 282:11155-11162.
    • (2007) J. Biol. Chem. , vol.282 , pp. 11155-11162
    • Lu, H.1    Pannicke, U.2    Schwarz, K.3    Lieber, M.R.4
  • 47
    • 0036178630 scopus 로고    scopus 로고
    • The crystal structure of human tyrosyl-DNA phosphodiesterase, Tdp1
    • Davies D.R., Interthal H., Champoux J.J., Hol W.G. The crystal structure of human tyrosyl-DNA phosphodiesterase, Tdp1. Structure 2002, 10:237-248.
    • (2002) Structure , vol.10 , pp. 237-248
    • Davies, D.R.1    Interthal, H.2    Champoux, J.J.3    Hol, W.G.4
  • 48
    • 84859186894 scopus 로고    scopus 로고
    • SUMO modification of the neuroprotective protein TDP1 facilitates chromosomal single-strand break repair
    • Hudson J.J., Chiang S.C., Wells O.S., Rookyard C., El-Khamisy S.F. SUMO modification of the neuroprotective protein TDP1 facilitates chromosomal single-strand break repair. Nat. Commun. 2012, 3:733.
    • (2012) Nat. Commun. , vol.3 , pp. 733
    • Hudson, J.J.1    Chiang, S.C.2    Wells, O.S.3    Rookyard, C.4    El-Khamisy, S.F.5
  • 49
    • 77951916582 scopus 로고    scopus 로고
    • TDP1 serine 81 promotes interaction with DNA ligase IIIalpha and facilitates cell survival following DNA damage
    • Chiang S.C., Carroll J., El-Khamisy S.F. TDP1 serine 81 promotes interaction with DNA ligase IIIalpha and facilitates cell survival following DNA damage. Cell Cycle 2010, 9:588-595.
    • (2010) Cell Cycle , vol.9 , pp. 588-595
    • Chiang, S.C.1    Carroll, J.2    El-Khamisy, S.F.3
  • 51
    • 28544448011 scopus 로고    scopus 로고
    • Autophosphorylation of DNA-dependent protein kinase regulates DNA end processing and may also alter double-strand break repair pathway choice
    • Cui X., Yu Y., Gupta S., Cho Y.M., Lees-Miller S.P., Meek K. Autophosphorylation of DNA-dependent protein kinase regulates DNA end processing and may also alter double-strand break repair pathway choice. Mol. Cell. Biol. 2005, 25:10842-10852.
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 10842-10852
    • Cui, X.1    Yu, Y.2    Gupta, S.3    Cho, Y.M.4    Lees-Miller, S.P.5    Meek, K.6
  • 53
    • 0030009738 scopus 로고    scopus 로고
    • The DNA-dependent protein kinase is inactivated by autophosphorylation of the catalytic subunit
    • Chan D.W., Lees-Miller S.P. The DNA-dependent protein kinase is inactivated by autophosphorylation of the catalytic subunit. J. Biol. Chem. 1996, 271:8936-8941.
    • (1996) J. Biol. Chem. , vol.271 , pp. 8936-8941
    • Chan, D.W.1    Lees-Miller, S.P.2
  • 56
    • 78649446475 scopus 로고    scopus 로고
    • A structural model for regulation of NHEJ by DNA-PKcs autophosphorylation
    • Dobbs T.A., Tainer J.A., Lees-Miller S.P. A structural model for regulation of NHEJ by DNA-PKcs autophosphorylation. DNA Repair (Amst.) 2010, 9:1307-1314.
    • (2010) DNA Repair (Amst.) , vol.9 , pp. 1307-1314
    • Dobbs, T.A.1    Tainer, J.A.2    Lees-Miller, S.P.3
  • 60
    • 84896717088 scopus 로고    scopus 로고
    • Is non-homologous end-joining really an inherently error-prone process?
    • Betermier M., Bertrand P., Lopez B.S. Is non-homologous end-joining really an inherently error-prone process?. PLoS Genet. 2014, 10:e1004086.
    • (2014) PLoS Genet. , vol.10 , pp. e1004086
    • Betermier, M.1    Bertrand, P.2    Lopez, B.S.3
  • 61
    • 20444441966 scopus 로고    scopus 로고
    • Substrate specificity of tyrosyl-DNA phosphodiesterase I (Tdp1)
    • Raymond A.C., Staker B.L., Burgin A.B. Substrate specificity of tyrosyl-DNA phosphodiesterase I (Tdp1). J. Biol. Chem. 2005, 280:22029-22035.
    • (2005) J. Biol. Chem. , vol.280 , pp. 22029-22035
    • Raymond, A.C.1    Staker, B.L.2    Burgin, A.B.3
  • 62
    • 0034871092 scopus 로고    scopus 로고
    • Pathways for repair of topoisomerase I covalent complexes in Saccharomyces cerevisiae
    • Pouliot J.J., Robertson C.A., Nash H.A. Pathways for repair of topoisomerase I covalent complexes in Saccharomyces cerevisiae. Genes Cells 2001, 6:677-687.
    • (2001) Genes Cells , vol.6 , pp. 677-687
    • Pouliot, J.J.1    Robertson, C.A.2    Nash, H.A.3
  • 66
    • 79959267641 scopus 로고    scopus 로고
    • Unique and redundant functions of ATM and DNA-PKcs during V(D)J recombination
    • Gapud E.J., Sleckman B.P. Unique and redundant functions of ATM and DNA-PKcs during V(D)J recombination. Cell Cycle 2011, 10:1928-1935.
    • (2011) Cell Cycle , vol.10 , pp. 1928-1935
    • Gapud, E.J.1    Sleckman, B.P.2
  • 68
    • 63549131291 scopus 로고    scopus 로고
    • In vitro complementation of Tdp1 deficiency indicates a stabilized enzyme-DNA adduct from tyrosyl but not glycolate lesions as a consequence of the SCAN1 mutation
    • Hawkins A.J., Subler M.A., Akopiants K., Wiley J.L., Taylor S.M., Rice A.C., Windle J.J., Valerie K., Povirk L.F. In vitro complementation of Tdp1 deficiency indicates a stabilized enzyme-DNA adduct from tyrosyl but not glycolate lesions as a consequence of the SCAN1 mutation. DNA Repair 2009, 8:654-663.
    • (2009) DNA Repair , vol.8 , pp. 654-663
    • Hawkins, A.J.1    Subler, M.A.2    Akopiants, K.3    Wiley, J.L.4    Taylor, S.M.5    Rice, A.C.6    Windle, J.J.7    Valerie, K.8    Povirk, L.F.9
  • 69
    • 36248984333 scopus 로고    scopus 로고
    • TDP1 facilitates chromosomal single-strand break repair in neurons and is neuroprotective in vivo
    • Katyal S., el-Khamisy S.F., Russell H.R., Li Y., Ju L., Caldecott K.W., McKinnon P.J. TDP1 facilitates chromosomal single-strand break repair in neurons and is neuroprotective in vivo. EMBO J. 2007, 26:4720-4731.
    • (2007) EMBO J. , vol.26 , pp. 4720-4731
    • Katyal, S.1    el-Khamisy, S.F.2    Russell, H.R.3    Li, Y.4    Ju, L.5    Caldecott, K.W.6    McKinnon, P.J.7
  • 72
    • 84919400644 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerases in double-strand break repair: focus on PARP1, PARP2 and PARP3
    • Beck C., Robert I., Reina-San-Martin B., Schreiber V., Dantzer F. Poly(ADP-ribose) polymerases in double-strand break repair: focus on PARP1, PARP2 and PARP3. Exp. Cell Res. 2014, 329:18-25.
    • (2014) Exp. Cell Res. , vol.329 , pp. 18-25
    • Beck, C.1    Robert, I.2    Reina-San-Martin, B.3    Schreiber, V.4    Dantzer, F.5
  • 73
    • 84858159092 scopus 로고    scopus 로고
    • Terminally differentiated astrocytes lack DNA damage response signaling and are radioresistant but retain DNA repair proficiency
    • Schneider L., Fumagalli M., d'Adda di Fagagna F. Terminally differentiated astrocytes lack DNA damage response signaling and are radioresistant but retain DNA repair proficiency. Cell Death Differ. 2012, 19:582-591.
    • (2012) Cell Death Differ. , vol.19 , pp. 582-591
    • Schneider, L.1    Fumagalli, M.2    d'Adda di Fagagna, F.3
  • 74
    • 84896537743 scopus 로고    scopus 로고
    • 53BP1, BRCA1 and the choice between recombination and end joining at DNA double-strand breaks
    • Daley J.M., Sung P. 53BP1, BRCA1 and the choice between recombination and end joining at DNA double-strand breaks. Mol. Cell. Biol. 2014, 34.
    • (2014) Mol. Cell. Biol. , vol.34
    • Daley, J.M.1    Sung, P.2
  • 76
    • 79955663428 scopus 로고    scopus 로고
    • Tidying up loose ends: the role of polynucleotide kinase/phosphatase in DNA strand break repair
    • Weinfeld M., Mani R.S., Abdou I., Aceytuno R.D., Glover J.N. Tidying up loose ends: the role of polynucleotide kinase/phosphatase in DNA strand break repair. Trends Biochem. Sci. 2011, 36:262-271.
    • (2011) Trends Biochem. Sci. , vol.36 , pp. 262-271
    • Weinfeld, M.1    Mani, R.S.2    Abdou, I.3    Aceytuno, R.D.4    Glover, J.N.5
  • 78
    • 79957506234 scopus 로고    scopus 로고
    • Coordination of DNA-PK activation and nuclease processing of DNA termini in NHEJ
    • Pawelczak K.S., Bennett S.M., Turchi J.J. Coordination of DNA-PK activation and nuclease processing of DNA termini in NHEJ. Antioxid. Redox Signal. 2011, 14:2531-2543.
    • (2011) Antioxid. Redox Signal. , vol.14 , pp. 2531-2543
    • Pawelczak, K.S.1    Bennett, S.M.2    Turchi, J.J.3
  • 79
    • 80054683238 scopus 로고    scopus 로고
    • Polynucleotide kinase and aprataxin-like forkhead-associated protein (PALF) acts as both a single-stranded DNA endonuclease and a single-stranded DNA 3' exonuclease and can participate in DNA end joining in a biochemical system
    • Li S., Kanno S., Watanabe R., Ogiwara H., Kohno T., Watanabe G., Yasui A., Lieber M.R. Polynucleotide kinase and aprataxin-like forkhead-associated protein (PALF) acts as both a single-stranded DNA endonuclease and a single-stranded DNA 3' exonuclease and can participate in DNA end joining in a biochemical system. J. Biol. Chem. 2011, 286:36368-36377.
    • (2011) J. Biol. Chem. , vol.286 , pp. 36368-36377
    • Li, S.1    Kanno, S.2    Watanabe, R.3    Ogiwara, H.4    Kohno, T.5    Watanabe, G.6    Yasui, A.7    Lieber, M.R.8


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