메뉴 건너뛰기




Volumn 38, Issue 9, 2010, Pages 2891-2903

NUDT16 and ITPA play a dual protective role in maintaining chromosome stability and cell growth by eliminating dIDP/IDP and dITP/ITP from nucleotide pools in mammals

Author keywords

[No Author keywords available]

Indexed keywords

2' DEOXYINOSINE DIPHOSPHATE; 2' DEOXYINOSINE TRIPHOSPHATE; INOSINE DERIVATIVE; INOSINE DIPHOSPHATE; INOSINE TRIPHOSPHATASE; INOSINE TRIPHOSPHATE; NUCLEOTIDE; NUDIX HYDROLASE; NUDIX TYPE MOTIF 16; PHOSPHATASE; UNCLASSIFIED DRUG; 2'-DEOXYINOSINE TRIPHOSPHATE; ACID ANHYDRIDE HYDROLASE; DEOXYINOSINE DIPHOSPHATE; DRUG DERIVATIVE; INORGANIC PYROPHOSPHATASE; INOSINE DIPHOSPHATASE; NUDT16 PROTEIN, MOUSE; PURINE NUCLEOTIDE;

EID: 77953276559     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkp1250     Document Type: Article
Times cited : (57)

References (34)
  • 1
    • 2442617250 scopus 로고    scopus 로고
    • The defense mechanisms in mammalian cells against oxidative damage in nucleic acids and their involvement in the suppression of mutagenesis and cell death
    • Nakabeppu, Y., Tsuchimoto, D., Furuichi, M. and Sakumi, K. (2004) The defense mechanisms in mammalian cells against oxidative damage in nucleic acids and their involvement in the suppression of mutagenesis and cell death. Free Radic. Res., 38, 423-429.
    • (2004) Free Radic. Res. , vol.38 , pp. 423-429
    • Nakabeppu, Y.1    Tsuchimoto, D.2    Furuichi, M.3    Sakumi, K.4
  • 3
    • 0035796057 scopus 로고    scopus 로고
    • Molecular genetics and structural biology of human MutT homolog
    • Nakabeppu, Y. (2001) Molecular genetics and structural biology of human MutT homolog, MTH1. Mutat. Res., 477, 59-70.
    • (2001) MTH1. Mutat. Res. , vol.477 , pp. 59-70
    • Nakabeppu, Y.1
  • 4
    • 33745257002 scopus 로고    scopus 로고
    • MTH1, an oxidized purine nucleoside triphosphatase, prevents the cytotoxicity and neurotoxicity of oxidized purine nucleotides
    • Nakabeppu, Y., Kajitani, K., Sakamoto, K., Yamaguchi, H. and Tsuchimoto, D. (2006) MTH1, an oxidized purine nucleoside triphosphatase, prevents the cytotoxicity and neurotoxicity of oxidized purine nucleotides. DNA Rep., 5, 761-772.
    • (2006) DNA Rep. , vol.5 , pp. 761-772
    • Nakabeppu, Y.1    Kajitani, K.2    Sakamoto, K.3    Yamaguchi, H.4    Tsuchimoto, D.5
  • 5
    • 18244379589 scopus 로고    scopus 로고
    • Characterization of the structure and expression of mouse Itpa gene and its related sequences in the mouse genome
    • Behmanesh, M., Sakumi, K., Tsuchimoto, D., Torisu, K., Ohnishi-Honda, Y., Rancourt, D.E. and Nakabeppu, Y. (2005) Characterization of the structure and expression of mouse Itpa gene and its related sequences in the mouse genome. DNA Res., 12, 39-51.
    • (2005) DNA Res. , vol.12 , pp. 39-51
    • Behmanesh, M.1    Sakumi, K.2    Tsuchimoto, D.3    Torisu, K.4    Ohnishi-Honda, Y.5    Rancourt, D.E.6    Nakabeppu, Y.7
  • 7
    • 61349171254 scopus 로고    scopus 로고
    • Mouse RS21-C6 is a mammalian 2'-deoxycytidine 5'-triphosphate pyrophosphohydrolase that prefers 5-iodocytosine
    • Nonaka, M., Tsuchimoto, D., Sakumi, K. and Nakabeppu, Y. (2009) Mouse RS21-C6 is a mammalian 2'-deoxycytidine 5'-triphosphate pyrophosphohydrolase that prefers 5-iodocytosine. FEBS J., 276, 1654-1666.
    • (2009) FEBS J. , vol.276 , pp. 1654-1666
    • Nonaka, M.1    Tsuchimoto, D.2    Sakumi, K.3    Nakabeppu, Y.4
  • 9
    • 0016764619 scopus 로고
    • Adenine nucleotide metabolism in relation to purine enzymes in liver, erythrocytes and cultured fibroblasts
    • Shenoy, T.S. and Clifford, A.J. (1975) Adenine nucleotide metabolism in relation to purine enzymes in liver, erythrocytes and cultured fibroblasts. Biochim. Biophys. Acta, 411, 133-143.
    • (1975) Biochim. Biophys. Acta , vol.411 , pp. 133-143
    • Shenoy, T.S.1    Clifford, A.J.2
  • 10
    • 0018786517 scopus 로고
    • Deoxyguanosine kinase Distinct molecular forms in mitochondria and cytosol
    • Gower, W.R. Jr, Carr, M.C. and Ives, D.H. (1979) Deoxyguanosine kinase. Distinct molecular forms in mitochondria and cytosol. J. Biol. Chem., 254, 2180-2183.
    • (1979) J. Biol. Chem. , vol.254 , pp. 2180-2183
    • Gower W.R., Jr.1    Carr, M.C.2    Ives, D.H.3
  • 11
    • 15844366977 scopus 로고    scopus 로고
    • Kinetics of muscle contraction and actomyosin NTP hydrolysis from rabbit using a series of metal-nucleotide substrates
    • Burton, K., White, H. and Sleep, J. (2005) Kinetics of muscle contraction and actomyosin NTP hydrolysis from rabbit using a series of metal-nucleotide substrates. J. Physiol., 563, 689-711.
    • (2005) J. Physiol. , vol.563 , pp. 689-711
    • Burton, K.1    White, H.2    Sleep, J.3
  • 12
    • 0038575033 scopus 로고    scopus 로고
    • RdgB acts to avoid chromosome fragmentation in Escherichia coli
    • Bradshaw, J.S. and Kuzminov, A. (2003) RdgB acts to avoid chromosome fragmentation in Escherichia coli. Mol. Microbiol., 48, 1711-1725.
    • (2003) Mol. Microbiol. , vol.48 , pp. 1711-1725
    • Bradshaw, J.S.1    Kuzminov, A.2
  • 14
    • 0037415380 scopus 로고    scopus 로고
    • Accumulation of 8-oxoguanine in the cellular DNA and the alteration of the OGG1 expression during ischemia-reperfusion injury in the rat kidney
    • Tsuruya, K., Furuichi, M., Tominaga, Y., Shinozaki, M., Tokumoto, M., Yoshimitsu, T., Fukuda, K., Kanai, H., Hirakata, H., Iida, M. et al. (2003) Accumulation of 8-oxoguanine in the cellular DNA and the alteration of the OGG1 expression during ischemia-reperfusion injury in the rat kidney. DNA Rep., 2, 211-229.
    • (2003) DNA Rep. , vol.2 , pp. 211-229
    • Tsuruya, K.1    Furuichi, M.2    Tominaga, Y.3    Shinozaki, M.4    Tokumoto, M.5    Yoshimitsu, T.6    Fukuda, K.7    Kanai, H.8    Hirakata, H.9    Iida, M.10
  • 15
    • 50349091399 scopus 로고    scopus 로고
    • Quantification of DNA damage products resulting from deamination, oxidation and reaction with products of lipid peroxidation by liquid chromatography isotope dilution tandem mass spectrometry
    • Taghizadeh, K., McFaline, J.L., Pang, B., Sullivan, M., Dong, M., Plummer, E. and Dedon, P.C. (2008) Quantification of DNA damage products resulting from deamination, oxidation and reaction with products of lipid peroxidation by liquid chromatography isotope dilution tandem mass spectrometry. Nat. Protoc., 3, 1287-1298.
    • (2008) Nat. Protoc. , vol.3 , pp. 1287-1298
    • Taghizadeh, K.1    McFaline, J.L.2    Pang, B.3    Sullivan, M.4    Dong, M.5    Plummer, E.6    Dedon, P.C.7
  • 16
    • 38549153790 scopus 로고    scopus 로고
    • Two distinct pathways of cell death triggered by oxidative damage to nuclear and mitochondrial DNAs
    • Oka, S., Ohno, M., Tsuchimoto, D., Sakumi, K., Furuichi, M. and Nakabeppu, Y. (2008) Two distinct pathways of cell death triggered by oxidative damage to nuclear and mitochondrial DNAs. EMBO J., 27, 421-432.
    • (2008) EMBO J. , vol.27 , pp. 421-432
    • Oka, S.1    Ohno, M.2    Tsuchimoto, D.3    Sakumi, K.4    Furuichi, M.5    Nakabeppu, Y.6
  • 17
    • 0035369734 scopus 로고    scopus 로고
    • Human APE2 protein is mostly localized in the nuclei and to some extent in the mitochondria, while nuclear APE2 is partly associated with proliferating cell nuclear antigen
    • Tsuchimoto, D., Sakai, Y., Sakumi, K., Nishioka, K., Sasaki, M., Fujiwara, T. and Nakabeppu, Y. (2001) Human APE2 protein is mostly localized in the nuclei and to some extent in the mitochondria, while nuclear APE2 is partly associated with proliferating cell nuclear antigen. Nucleic Acids Res., 29, 2349-2360.
    • (2001) Nucleic Acids Res. , vol.29 , pp. 2349-2360
    • Tsuchimoto, D.1    Sakai, Y.2    Sakumi, K.3    Nishioka, K.4    Sasaki, M.5    Fujiwara, T.6    Nakabeppu, Y.7
  • 18
    • 0036801346 scopus 로고    scopus 로고
    • Repair of deaminated bases in DNA
    • Kow, Y.W. (2002) Repair of deaminated bases in DNA. Free Radic. Biol. Med., 33, 886-893.
    • (2002) Free Radic. Biol. Med. , vol.33 , pp. 886-893
    • Kow, Y.W.1
  • 20
    • 0018072314 scopus 로고
    • Enzymatic excision of free hypoxanthine from polydeoxynucleotides and DNA containing deoxyinosine monophosphate residues
    • Karran, P. and Lindahl, T. (1978) Enzymatic excision of free hypoxanthine from polydeoxynucleotides and DNA containing deoxyinosine monophosphate residues. J. Biol. Chem., 253, 5877-5879.
    • (1978) J. Biol. Chem. , vol.253 , pp. 5877-5879
    • Karran, P.1    Lindahl, T.2
  • 21
    • 0020490817 scopus 로고
    • Metabolism of dITP in HeLa cell extracts, incorporation into DNA by isolated nuclei and release of hypoxanthine from DNA by a hypoxanthine-DNA glycosylase activity
    • Myrnes, B., Guddal, P.H. and Krokan, H. (1982) Metabolism of dITP in HeLa cell extracts, incorporation into DNA by isolated nuclei and release of hypoxanthine from DNA by a hypoxanthine-DNA glycosylase activity. Nucleic Acids Res., 10, 3693-3701.
    • (1982) Nucleic Acids Res. , vol.10 , pp. 3693-3701
    • Myrnes, B.1    Guddal, P.H.2    Krokan, H.3
  • 22
    • 0028239225 scopus 로고
    • Excision of hypoxanthine from DNA containing dIMP residues by the Escherichia coli, yeast, rat, and human alkylpurine DNA glycosylases
    • Saparbaev, M. and Laval, J. (1994) Excision of hypoxanthine from DNA containing dIMP residues by the Escherichia coli, yeast, rat, and human alkylpurine DNA glycosylases. Proc. Natl Acad. Sci. USA, 91, 5873-5877.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 5873-5877
    • Saparbaev, M.1    Laval, J.2
  • 23
    • 0242380643 scopus 로고    scopus 로고
    • Incision at hypoxanthine residues in DNA by a mammalian homologue of the Escherichia coli antimutator enzyme endonuclease V
    • Moe, A., Ringvoll, J., Nordstrand, L.M., Eide, L., Bjørås, M., Seeberg, E., Rognes, T. and Klungland, A. (2003) Incision at hypoxanthine residues in DNA by a mammalian homologue of the Escherichia coli antimutator enzyme endonuclease V. Nucleic Acids Res., 31, 3893-3900.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 3893-3900
    • Moe, A.1    Ringvoll, J.2    Nordstrand, L.M.3    Eide, L.4    Bjørås, M.5    Seeberg, E.6    Rognes, T.7    Klungland, A.8
  • 24
    • 24944469578 scopus 로고    scopus 로고
    • The efficiency of hypoxanthine excision by alkyladenine DNA glycosylase is altered by changes in nearest neighbor bases
    • Vallur, A.C., Maher, R.L. and Bloom, L.B. (2005) The efficiency of hypoxanthine excision by alkyladenine DNA glycosylase is altered by changes in nearest neighbor bases. DNA Rep., 4, 1088-1098.
    • (2005) DNA Rep. , vol.4 , pp. 1088-1098
    • Vallur, A.C.1    Maher, R.L.2    Bloom, L.B.3
  • 25
    • 62349103878 scopus 로고    scopus 로고
    • DNA double-strand break repair: how to fix a broken relationship
    • Pardo, B., Gómez-González, B. and Aguilera, A. (2009) DNA double-strand break repair: how to fix a broken relationship. Cell. Mol. Life Sci., 66, 1039-1056.
    • (2009) Cell. Mol. Life Sci. , vol.66 , pp. 1039-1056
    • Pardo, B.1    Gómez-González, B.2    Aguilera, A.3
  • 26
    • 0025275082 scopus 로고
    • Clastogenic inosine nucleotide as components of the chromosome breakage factor in scleroderma patients
    • Auclair, C., Gouyette, A., Levy, A. and Emerit, I. (1990) Clastogenic inosine nucleotide as components of the chromosome breakage factor in scleroderma patients. Arch. Biochem. Biophys., 278, 238-244.
    • (1990) Arch. Biochem. Biophys. , vol.278 , pp. 238-244
    • Auclair, C.1    Gouyette, A.2    Levy, A.3    Emerit, I.4
  • 27
    • 0035832370 scopus 로고    scopus 로고
    • As to the clastogenic-, sister-chromatid exchange inducing-and cytotoxic activity of inosine triphosphate in cultures of human peripheral lymphocytes
    • Vormittag, W. and Brannath, W. (2001) As to the clastogenic-, sister-chromatid exchange inducing-and cytotoxic activity of inosine triphosphate in cultures of human peripheral lymphocytes. Mutat. Res., 476, 71-81.
    • (2001) Mutat. Res. , vol.476 , pp. 71-81
    • Vormittag, W.1    Brannath, W.2
  • 28
    • 33746662847 scopus 로고    scopus 로고
    • Cohesin and DNA damage repair
    • Watrin, E. and Peters, J.M. (2006) Cohesin and DNA damage repair. Exp. Cell Res., 312, 2687-2693.
    • (2006) Exp. Cell Res. , vol.312 , pp. 2687-2693
    • Watrin, E.1    Peters, J.M.2
  • 29
    • 70449712619 scopus 로고    scopus 로고
    • A matter of choice: the establishment of sister chromatid cohesion
    • Uhlmann, F. (2009) A matter of choice: the establishment of sister chromatid cohesion. EMBO Rep., 10, 1095-1102.
    • (2009) EMBO Rep. , vol.10 , pp. 1095-1102
    • Uhlmann, F.1
  • 30
    • 0016719512 scopus 로고
    • ITP pyrophosphohydrolase and IDP phosphohydrolase in rat tissue
    • Vanderheiden, B.S. (1975) ITP pyrophosphohydrolase and IDP phosphohydrolase in rat tissue. J. Cell. Physiol., 86, 167-175.
    • (1975) J. Cell. Physiol. , vol.86 , pp. 167-175
    • Vanderheiden, B.S.1
  • 31
    • 0018772356 scopus 로고
    • Inosine di- and triphosphate synthesis in erythrocytes and cell extracts
    • Vanderheiden, B.S. (1979) Inosine di- and triphosphate synthesis in erythrocytes and cell extracts. J. Cell. Physiol., 99, 287-301.
    • (1979) J. Cell. Physiol. , vol.99 , pp. 287-301
    • Vanderheiden, B.S.1
  • 34
    • 34548339631 scopus 로고    scopus 로고
    • Pyrazolo[3,4-d]pyrimidine ribonucleosides related to 2-aminoadenosine and isoguanosine: synthesis, deamination and tautomerism
    • Seela, F. and Xu, K. (2007) Pyrazolo[3,4-d]pyrimidine ribonucleosides related to 2-aminoadenosine and isoguanosine: synthesis, deamination and tautomerism. Org. Biomol. Chem., 5, 3034-3045.
    • (2007) Org. Biomol. Chem. , vol.5 , pp. 3034-3045
    • Seela, F.1    Xu, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.