메뉴 건너뛰기




Volumn 113, Issue 12, 2004, Pages 1711-1721

Increased postischemic brain injury in mice deficient in uracil-DNA glycosylase

Author keywords

[No Author keywords available]

Indexed keywords

CYTOSINE; GLUCOSE; MITOCHONDRIAL DNA; NITRIC OXIDE; OXYGEN; RNA; URACIL; URACIL DNA GLYCOSYLTRANSFERASE; DNA GLYCOSYLTRANSFERASE; NITRIC OXIDE DONOR; NITROPRUSSIDE SODIUM; URACIL DNA GLYCOSIDASE;

EID: 3042766227     PISSN: 00219738     EISSN: None     Source Type: Journal    
DOI: 10.1172/JCI200420926     Document Type: Article
Times cited : (111)

References (37)
  • 1
    • 18044399360 scopus 로고    scopus 로고
    • Properties and functions of human uracil-DNA glycosylase form the Ung gene
    • Krokan, H.E., et al. 2001. Properties and functions of human uracil-DNA glycosylase form the Ung gene. Prog. Nucleic Acids Res. 68:366-386.
    • (2001) Prog. Nucleic Acids Res. , vol.68 , pp. 366-386
    • Krokan, H.E.1
  • 2
    • 0345379628 scopus 로고    scopus 로고
    • Phenotypic change caused by transcriptional bypass of uracil in nondividing cells
    • Viswanathan, A., You, H.J., and Doetsch, P.W. 1999. Phenotypic change caused by transcriptional bypass of uracil in nondividing cells. Science. 284:159-162.
    • (1999) Science , vol.284 , pp. 159-162
    • Viswanathan, A.1    You, H.J.2    Doetsch, P.W.3
  • 5
    • 0020461949 scopus 로고
    • Specific mutator effects of ung (uracil-DNA glycosylase) mutations in Escherichia coli
    • Duncan, B.K., and Weiss, B. 1982. Specific mutator effects of ung (uracil-DNA glycosylase) mutations in Escherichia coli. J. Bacteriol. 151:750-775.
    • (1982) J. Bacteriol. , vol.151 , pp. 750-775
    • Duncan, B.K.1    Weiss, B.2
  • 6
    • 0025790276 scopus 로고
    • The spectrum of spontaneous mutations in a Saccharomyces cerevisiae uracil-DNA glycosylase mutant limits the function of this enzyme to cytosine deamination repair
    • Impellizzeri, H.E., Anderson, B., and Burgers, P.M. 1991. The spectrum of spontaneous mutations in a Saccharomyces cerevisiae uracil-DNA glycosylase mutant limits the function of this enzyme to cytosine deamination repair. J. Bacteriol. 173:6807-6810.
    • (1991) J. Bacteriol. , vol.173 , pp. 6807-6810
    • Impellizzeri, H.E.1    Anderson, B.2    Burgers, P.M.3
  • 7
    • 0033636312 scopus 로고    scopus 로고
    • Uracil-DNA glycosylase (UNG)-deficient mice reveal a primary role of the enzyme during DNA replication
    • Nilsen, H., et al. 2000. Uracil-DNA glycosylase (UNG)-deficient mice reveal a primary role of the enzyme during DNA replication. Molecular Cell. 5:1059-1065.
    • (2000) Molecular Cell , vol.5 , pp. 1059-1065
    • Nilsen, H.1
  • 8
    • 0035421186 scopus 로고    scopus 로고
    • Excision of deaminated cytosine from the vertebrate genome: Role of the SMUG1 uracil-DNA glycosylase
    • Nilsen, H., et al. 2001. Excision of deaminated cytosine from the vertebrate genome: role of the SMUG1 uracil-DNA glycosylase. EMBO J. 20:4278-4286.
    • (2001) EMBO J. , vol.20 , pp. 4278-4286
    • Nilsen, H.1
  • 9
    • 0035945231 scopus 로고    scopus 로고
    • Uracil-DNA glycosylase-deficient yeast exhibit a mitochondrial mutator phenotype
    • Chatterjee, A., and Singh, K.K. 2001. Uracil-DNA glycosylase-deficient yeast exhibit a mitochondrial mutator phenotype. Nucleic Acids Res. 29:4935-4940.
    • (2001) Nucleic Acids Res. , vol.29 , pp. 4935-4940
    • Chatterjee, A.1    Singh, K.K.2
  • 10
    • 0035478431 scopus 로고    scopus 로고
    • Ischemic injury and faulty gene transcripts in the brain
    • Liu, P.K., Grossmann, R.G., Hsu, C.Y., and Robertson, C. 2001. Ischemic injury and faulty gene transcripts in the brain. Trends Neurosci. 24:581-588.
    • (2001) Trends Neurosci. , vol.24 , pp. 581-588
    • Liu, P.K.1    Grossmann, R.G.2    Hsu, C.Y.3    Robertson, C.4
  • 11
    • 0028799654 scopus 로고
    • Calcium: Still center-stage in hypoxic-ishemic neuronal death
    • Choi, D.W. 1995. Calcium: still center-stage in hypoxic-ishemic neuronal death. Trends Neurosci. 18:58-60.
    • (1995) Trends Neurosci. , vol.18 , pp. 58-60
    • Choi, D.W.1
  • 12
    • 0026321495 scopus 로고
    • DNA deaminating ability and genotoxicity of nitric oxide and its progenitors
    • Wink, D.A., et al. 1991. DNA deaminating ability and genotoxicity of nitric oxide and its progenitors. Science. 254:1001-1003.
    • (1991) Science , vol.254 , pp. 1001-1003
    • Wink, D.A.1
  • 13
    • 0033755358 scopus 로고    scopus 로고
    • Differences in vulnerability to permanent focal cerebral ischemia among 3 common mouse strains
    • Majid, A., et al. 2000. Differences in vulnerability to permanent focal cerebral ischemia among 3 common mouse strains. Stroke. 31:2707-2714.
    • (2000) Stroke , vol.31 , pp. 2707-2714
    • Majid, A.1
  • 14
    • 0032507585 scopus 로고    scopus 로고
    • Differences in cerebrovascular anatomy of C57Black/6 and SV129 mice
    • Maeda, K., Hata, R., and Hossmann, K.-A. 1998. Differences in cerebrovascular anatomy of C57Black/6 and SV129 mice. NeuroReport. 9:1261-1265.
    • (1998) NeuroReport , vol.9 , pp. 1261-1265
    • Maeda, K.1    Hata, R.2    Hossmann, K.-A.3
  • 15
    • 0033168183 scopus 로고    scopus 로고
    • Postreplicative base excision repair in replication foci
    • Otterlei, M., et al. 1999. Postreplicative base excision repair in replication foci. EMBO J. 18:3834-3844.
    • (1999) EMBO J. , vol.18 , pp. 3834-3844
    • Otterlei, M.1
  • 16
    • 15844419144 scopus 로고    scopus 로고
    • Cloning and expression of human G/T mismatch-specific thymine-DNA glycosylase
    • Neddermann, P., et al. 1996. Cloning and expression of human G/T mismatch-specific thymine-DNA glycosylase. J. Biol. Chem. 271:12767-12774.
    • (1996) J. Biol. Chem. , vol.271 , pp. 12767-12774
    • Neddermann, P.1
  • 17
    • 0033575886 scopus 로고    scopus 로고
    • The thymine glycosylases MBD4 can bind to the product of deamination at methylated CpG sites
    • Hendrich, B., Hardeland, U., Ng, H.-H., Jiricny, J., and Bird, A. 1999. The thymine glycosylases MBD4 can bind to the product of deamination at methylated CpG sites. Nature. 401:301-304.
    • (1999) Nature , vol.401 , pp. 301-304
    • Hendrich, B.1    Hardeland, U.2    Ng, H.-H.3    Jiricny, J.4    Bird, A.5
  • 18
    • 0032575752 scopus 로고    scopus 로고
    • Mitochondria and apoptosis
    • Green, D.R., and Reed, C.J. 1998. Mitochondria and apoptosis. Science. 281:1309-1312.
    • (1998) Science , vol.281 , pp. 1309-1312
    • Green, D.R.1    Reed, C.J.2
  • 19
    • 0032404536 scopus 로고    scopus 로고
    • The central executioners of apoptosis: Caspases or mitochondria?
    • Green, D.R., and Kroemer, G. 1998. The central executioners of apoptosis: caspases or mitochondria? Trends Cell. Biol. 8:267-271.
    • (1998) Trends Cell. Biol. , vol.8 , pp. 267-271
    • Green, D.R.1    Kroemer, G.2
  • 20
    • 0037216491 scopus 로고    scopus 로고
    • Upregulation of mitochondrial base-excision repair capability within rat brain after brief ischemia
    • Chen, D., et al. 2003. Upregulation of mitochondrial base-excision repair capability within rat brain after brief ischemia. J. Cereb. Blood FlowMetab. 23:88-98.
    • (2003) J. Cereb. Blood FlowMetab. , vol.23 , pp. 88-98
    • Chen, D.1
  • 21
    • 0031952184 scopus 로고    scopus 로고
    • Efficient repair of basic sites in DNA by mitochondrial enzymes
    • Pinz, K.G., and Bogenhagen, D.F. 1998. Efficient repair of basic sites in DNA by mitochondrial enzymes. Mol. Cell. Biol. 18:1257-1265.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 1257-1265
    • Pinz, K.G.1    Bogenhagen, D.F.2
  • 22
    • 0343517173 scopus 로고    scopus 로고
    • Detection of DNA base-excision repair activity for oxidative lesions in adult brain mitochondria
    • Chen, D., Lan, J., Pei, W., and Chen, J. 2000. Detection of DNA base-excision repair activity for oxidative lesions in adult brain mitochondria. J. Neurosci. Res. 61:225-236.
    • (2000) J. Neurosci. Res. , vol.61 , pp. 225-236
    • Chen, D.1    Lan, J.2    Pei, W.3    Chen, J.4
  • 23
    • 0036316413 scopus 로고    scopus 로고
    • Age-dependent decline of DNA repair activity of oxidative lesions in rat brain mitochondria
    • Chen, D., et al. 2002. Age-dependent decline of DNA repair activity of oxidative lesions in rat brain mitochondria. J. Neurocbem. 81:1273-1284.
    • (2002) J. Neurochem. , vol.81 , pp. 1273-1284
    • Chen, D.1
  • 24
  • 25
    • 0031892704 scopus 로고    scopus 로고
    • Attenuation of delayed neuronal cell death after mild focal ischemia by inhibitors of the caspase family
    • Endres, M., et al. 1998. Attenuation of delayed neuronal cell death after mild focal ischemia by inhibitors of the caspase family. J. Cereb. Blood Flow Metab. 18:238-247.
    • (1998) J. Cereb. Blood Flow Metab. , vol.18 , pp. 238-247
    • Endres, M.1
  • 26
    • 0036167790 scopus 로고    scopus 로고
    • Gene expression profiling in perilesional and contralateral areas after ischemia in rat brain
    • Keyvani, K., Witte, O.W., and Paulus, W. 2002. Gene expression profiling in perilesional and contralateral areas after ischemia in rat brain. J. Cereb. Blood Flow Metab. 22:153-160.
    • (2002) J. Cereb. Blood Flow Metab. , vol.22 , pp. 153-160
    • Keyvani, K.1    Witte, O.W.2    Paulus, W.3
  • 27
    • 10744222117 scopus 로고    scopus 로고
    • Restriction-mediated differential display (RMDD) identifies pip92 as a pro-apoptotic gene product induced during focal cerebral ischemia
    • Schneider, A., et al. 2004. Restriction-mediated differential display (RMDD) identifies pip92 as a pro-apoptotic gene product induced during focal cerebral ischemia. J. Cereb. Blood Flow Metab. 24:224-236.
    • (2004) J. Cereb. Blood Flow Metab. , vol.24 , pp. 224-236
    • Schneider, A.1
  • 28
    • 0029954239 scopus 로고    scopus 로고
    • Generation of mice with a 200-kb amyloid precursor protein gene deletion by Cre recombinase-mediated site-specific recombination in embryonic stem cells
    • Li, Z.W., et al. 1996. Generation of mice with a 200-kb amyloid precursor protein gene deletion by Cre recombinase-mediated site-specific recombination in embryonic stem cells. Proc. Natl. Acad. Sci. U. S. A. 93:6158-6162.
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 6158-6162
    • Li, Z.W.1
  • 29
    • 0026509977 scopus 로고
    • FDC-P1 myeloid cells engineered to express fibroblast growth factor receptor 1 proliferate and differentiate in the presence of fibroblast growth factor and heparin
    • Li, M., and Bernard, O. 1992. FDC-P1 myeloid cells engineered to express fibroblast growth factor receptor 1 proliferate and differentiate in the presence of fibroblast growth factor and heparin. Proc. Natl. Acad. Sci. U. S. A. 89:3315-3319.
    • (1992) Proc. Natl. Acad. Sci. U. S. A. , vol.89 , pp. 3315-3319
    • Li, M.1    Bernard, O.2
  • 30
    • 0037076434 scopus 로고    scopus 로고
    • Mutations associated with base excision repair deficiency and methylation-induced genotoxic stress
    • Sobol, R. W., et al. 2002. Mutations associated with base excision repair deficiency and methylation-induced genotoxic stress. Proc. Natl. Acad. Sci. U. S. A. 99:6860-6865.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 6860-6865
    • Sobol, R.W.1
  • 31
    • 0029973192 scopus 로고    scopus 로고
    • Damage, repair and mutagenesis in nuclear genes after mouse forebrain ischemia-reperfusion
    • Liu, P.K., et al. 1996. Damage, repair and mutagenesis in nuclear genes after mouse forebrain ischemia-reperfusion. J. Neurosci. 16:6795-6806.
    • (1996) J. Neurosci. , vol.16 , pp. 6795-6806
    • Liu, P.K.1
  • 32
    • 0028868824 scopus 로고
    • Serum-free B27/neurobasal medium supports differentiated growth of neurons from the striatum, substantia nigra, septum, cerebral cortex, cerebellum, and dentate gyrus
    • Brewer, G.J. 1995. Serum-free B27/neurobasal medium supports differentiated growth of neurons from the striatum, substantia nigra, septum, cerebral cortex, cerebellum, and dentate gyrus. J. Neurosci. Res. 42:674-683.
    • (1995) J. Neurosci. Res. , vol.42 , pp. 674-683
    • Brewer, G.J.1
  • 33
    • 0033823057 scopus 로고    scopus 로고
    • Melatonin is protective in necrotic but not in caspase-dependent, free-radical-independent apoptotic neuronal cell death in primary neuronal cultures
    • Harms, C., et al. 2001. Melatonin is protective in necrotic but not in caspase-dependent, free-radical-independent apoptotic neuronal cell death in primary neuronal cultures. FASEB J. 14:1814-1824.
    • (2001) FASEB J. , vol.14 , pp. 1814-1824
    • Harms, C.1
  • 34
    • 4043063467 scopus 로고
    • Mitochondrial depolarization accompanies cytochrome c release during apoptosis in PC6 cells
    • Heiskanen, K.M., Bhat, M.B., Wang, H.W., and Ma, J. 1982. Mitochondrial depolarization accompanies cytochrome c release during apoptosis in PC6 cells. J. Biol. Chem. 274:2654-2659.
    • (1982) J. Biol. Chem. , vol.274 , pp. 2654-2659
    • Heiskanen, K.M.1    Bhat, M.B.2    Wang, H.W.3    Ma, J.4
  • 35
    • 0032555154 scopus 로고    scopus 로고
    • Stroke protection by 3-hydroxy methylglutaryl-CoA reductase inhibitors mediated by endothelial nitric oxide synthase
    • Endres, M., et al. 1998. Stroke protection by 3-hydroxy methylglutaryl-CoA reductase inhibitors mediated by endothelial nitric oxide synthase. Proc. Natl. Acad. Sci. U. S. A. 95:8880-8885.
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 8880-8885
    • Endres, M.1
  • 37
    • 12644251998 scopus 로고    scopus 로고
    • Base excision repair deficient mice lacking the Aag alkyladenine DNA glycosylase
    • Engelward, B.P., et al. 1997. Base excision repair deficient mice lacking the Aag alkyladenine DNA glycosylase. Proc. Natl. Acad. Sci. U. S. A. 94:13087-13092.
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 13087-13092
    • Engelward, B.P.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.