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Volumn 4, Issue 3, 2014, Pages 678-703

New perspectives on oxidized genome damage and repair inhibition by pro-oxidant metals in neurological diseases

Author keywords

Alzheimer s disease; DNA base excision repair; Heavy metals; Metal homeostasis; Metal toxicity; Neurodegeneration; Parkinson s disease; Redox transition metals

Indexed keywords

AMYLOID PROTEIN; BER PROTEIN; CADMIUM; COPPER; FERRIC ION; LEAD; MANGANESE; MERCURY; METAL; REACTIVE OXYGEN METABOLITE; TRANSITION ELEMENT; UNCLASSIFIED DRUG;

EID: 84919786949     PISSN: None     EISSN: 2218273X     Source Type: Journal    
DOI: 10.3390/biom4030678     Document Type: Review
Times cited : (29)

References (192)
  • 1
    • 10844247373 scopus 로고    scopus 로고
    • Serum trace element levels and the complexity of inter-element relations in patients with parkinson’s disease
    • Hegde, M.L.; Shanmugavelu, P.; Vengamma, B.; Rao, T.S.; Menon, R.B.; Rao, R.V.; Rao, K.S. Serum trace element levels and the complexity of inter-element relations in patients with parkinson’s disease. J. Trace Elem. Med. Biol. 2004, 18, 163-171.
    • (2004) J. Trace Elem. Med. Biol. , vol.18 , pp. 163-171
    • Hegde, M.L.1    Shanmugavelu, P.2    Vengamma, B.3    Rao, T.S.4    Menon, R.B.5    Rao, R.V.6    Rao, K.S.7
  • 2
    • 84887048150 scopus 로고    scopus 로고
    • Role of metal ions in the self-assembly of the Alzheimer’s amyloid-beta peptide
    • Faller, P.; Hureau, C.; Berthoumieu, O. Role of metal ions in the self-assembly of the Alzheimer’s amyloid-beta peptide. Inorg. Chem. 2013, 52, 12193-12206.
    • (2013) Inorg. Chem. , vol.52 , pp. 12193-12206
    • Faller, P.1    Hureau, C.2    Berthoumieu, O.3
  • 3
    • 68249100265 scopus 로고    scopus 로고
    • Rising zinc: A significant cause of ischemic neuronal death in the CA1 region of rat hippocampus
    • Stork, C.J.; Li, Y.V. Rising zinc: A significant cause of ischemic neuronal death in the CA1 region of rat hippocampus. J. Cereb. Blood Flow Metab. 2009, 29, 1399-1408.
    • (2009) J. Cereb. Blood Flow Metab. , vol.29 , pp. 1399-1408
    • Stork, C.J.1    Li, Y.V.2
  • 4
    • 45449091529 scopus 로고    scopus 로고
    • Emerging links between premature ageing and defective DNA repair
    • Hanawalt, P.C. Emerging links between premature ageing and defective DNA repair. Mech. Ageing Dev. 2008, 129, 503-505.
    • (2008) Mech. Ageing Dev. , vol.129 , pp. 503-505
    • Hanawalt, P.C.1
  • 6
    • 0029915960 scopus 로고    scopus 로고
    • Effect of arsenic and cadmium on the persistence of mutagen-induced DNA lesions in human cells
    • Hartmann, A.; Speit, G. Effect of arsenic and cadmium on the persistence of mutagen-induced DNA lesions in human cells. Environ. Mol. Mutagen. 1996, 27, 98-104.
    • (1996) Environ. Mol. Mutagen. , vol.27 , pp. 98-104
    • Hartmann, A.1    Speit, G.2
  • 8
    • 84872445678 scopus 로고    scopus 로고
    • Cadmium induces neuronal cell death through reactive oxygen species activated by GADD153
    • Kim, S.; Cheon, H.S.; Kim, S.Y.; Juhnn, Y.S.; Kim, Y.Y. Cadmium induces neuronal cell death through reactive oxygen species activated by GADD153. BMC Cell Biol. 2013, doi: 10.1186/1471-2121-14-4.
    • (2013) BMC Cell Biol.
    • Kim, S.1    Cheon, H.S.2    Kim, S.Y.3    Juhnn, Y.S.4    Kim, Y.Y.5
  • 9
    • 77956545422 scopus 로고    scopus 로고
    • Specific inhibition of NEIL-initiated repair of oxidized base damage in human genome by copper and iron: Potential etiological linkage to neurodegenerative diseases
    • Hegde, M.L.; Hegde, P.M.; Holthauzen, L.M.; Hazra, T.K.; Rao, K.S.; Mitra, S. Specific inhibition of NEIL-initiated repair of oxidized base damage in human genome by copper and iron: Potential etiological linkage to neurodegenerative diseases. J. Biol. Chem. 2010, 285, 28812-28825.
    • (2010) J. Biol. Chem. , vol.285 , pp. 28812-28825
    • Hegde, M.L.1    Hegde, P.M.2    Holthauzen, L.M.3    Hazra, T.K.4    Rao, K.S.5    Mitra, S.6
  • 10
    • 0142226864 scopus 로고    scopus 로고
    • The role of metals in neurodegenerative processes: Aluminum, manganese, and zinc
    • Zatta, P.; Lucchini, R.; van Rensburg, S.J.; Taylor, A. The role of metals in neurodegenerative processes: Aluminum, manganese, and zinc. Brain Res. Bull. 2003, 62, 15-28.
    • (2003) Brain Res. Bull. , vol.62 , pp. 15-28
    • Zatta, P.1    Lucchini, R.2    van Rensburg, S.J.3    Taylor, A.4
  • 11
    • 69949175485 scopus 로고    scopus 로고
    • Elevated metals compromise repair of oxidative DNA damage via the base excision repair pathway: Implications of pathologic iron overload in the brain on integrity of neuronal DNA
    • Li, H.; Swiercz, R.; Englander, E.W. Elevated metals compromise repair of oxidative DNA damage via the base excision repair pathway: Implications of pathologic iron overload in the brain on integrity of neuronal DNA. J. Neurochem. 2009, 110, 1774-1783.
    • (2009) J. Neurochem. , vol.110 , pp. 1774-1783
    • Li, H.1    Swiercz, R.2    Englander, E.W.3
  • 12
    • 0028927261 scopus 로고
    • Reactions of oxyl radicals with DNA
    • Breen, A.P.; Murphy, J.A. Reactions of oxyl radicals with DNA. Free Radic. Biol. Med. 1995, 18, 1033-1077.
    • (1995) Free Radic. Biol. Med. , vol.18 , pp. 1033-1077
    • Breen, A.P.1    Murphy, J.A.2
  • 14
    • 0022272160 scopus 로고
    • Free-radical chemistry of cigarette smoke and its toxicological implications
    • Church, D.F.; Pryor, W.A. Free-radical chemistry of cigarette smoke and its toxicological implications. Environ. Health Perspect. 1985, 64, 111-126.
    • (1985) Environ. Health Perspect. , vol.64 , pp. 111-126
    • Church, D.F.1    Pryor, W.A.2
  • 16
    • 0030824455 scopus 로고    scopus 로고
    • Alpha particles initiate biological production of superoxide anions and hydrogen peroxide in human cells
    • Narayanan, P.K.; Goodwin, E.H.; Lehnert, B.E. Alpha particles initiate biological production of superoxide anions and hydrogen peroxide in human cells. Cancer Res. 1997, 57, 3963-3971.
    • (1997) Cancer Res. , vol.57 , pp. 3963-3971
    • Narayanan, P.K.1    Goodwin, E.H.2    Lehnert, B.E.3
  • 18
    • 62349103878 scopus 로고    scopus 로고
    • DNA repair in mammalian cells: DNA double-strand break repair: How to fix a broken relationship
    • Pardo, B.; Gomez-Gonzalez, B.; Aguilera, A. DNA repair in mammalian cells: DNA double-strand break repair: How to fix a broken relationship. Cell. Mol. Life Sci. 2009, 66, 1039-1056.
    • (2009) Cell. Mol. Life Sci. , vol.66 , pp. 1039-1056
    • Pardo, B.1    Gomez-Gonzalez, B.2    Aguilera, A.3
  • 19
    • 0031035450 scopus 로고    scopus 로고
    • The origin of the hydroxyl radical oxygen in the fenton reaction
    • Lloyd, R.V.; Hanna, P.M.; Mason, R.P. The origin of the hydroxyl radical oxygen in the fenton reaction. Free Radic. Biol. Med. 1997, 22, 885-888.
    • (1997) Free Radic. Biol. Med. , vol.22 , pp. 885-888
    • Lloyd, R.V.1    Hanna, P.M.2    Mason, R.P.3
  • 20
    • 0036381371 scopus 로고    scopus 로고
    • Iron and carcinogenesis: From fenton reaction to target genes
    • Toyokuni, S. Iron and carcinogenesis: From fenton reaction to target genes. Redox Rep. 2002, 7, 189-197.
    • (2002) Redox Rep. , vol.7 , pp. 189-197
    • Toyokuni, S.1
  • 23
    • 38049112778 scopus 로고    scopus 로고
    • Early steps in the DNA base excision/single-strand interruption repair pathway in mammalian cells
    • Hegde, M.L.; Hazra, T.K.; Mitra, S. Early steps in the DNA base excision/single-strand interruption repair pathway in mammalian cells. Cell Res. 2008, 18, 27-47.
    • (2008) Cell Res. , vol.18 , pp. 27-47
    • Hegde, M.L.1    Hazra, T.K.2    Mitra, S.3
  • 24
    • 0030898724 scopus 로고    scopus 로고
    • An assessment of oxidative damage to proteins, lipids, and DNA in brain from patients with Alzheimer’s disease
    • Lyras, L.; Cairns, N.J.; Jenner, A.; Jenner, P.; Halliwell, B. An assessment of oxidative damage to proteins, lipids, and DNA in brain from patients with Alzheimer’s disease. J. Neurochem. 1997, 68, 2061-2069.
    • (1997) J. Neurochem. , vol.68 , pp. 2061-2069
    • Lyras, L.1    Cairns, N.J.2    Jenner, A.3    Jenner, P.4    Halliwell, B.5
  • 25
    • 0032823769 scopus 로고    scopus 로고
    • Antioxidant defence mechanisms: From the beginning to the end (of the beginning)
    • Halliwell, B. Antioxidant defence mechanisms: From the beginning to the end (of the beginning). Free Radic. Res. 1999, 31, 261-272.
    • (1999) Free Radic. Res. , vol.31 , pp. 261-272
    • Halliwell, B.1
  • 26
    • 0027944954 scopus 로고
    • DNA single-strand breaks and cytotoxicity induced by chromate(VI), cadmium(II), and mercury(II) in hydrogen peroxide-resistant cell lines
    • Tsuzuki, K.; Sugiyama, M.; Haramaki, N. DNA single-strand breaks and cytotoxicity induced by chromate(VI), cadmium(II), and mercury(II) in hydrogen peroxide-resistant cell lines. Environ. Health Perspect. 1994, 102, 341-342.
    • (1994) Environ. Health Perspect. , vol.102 , pp. 341-342
    • Tsuzuki, K.1    Sugiyama, M.2    Haramaki, N.3
  • 27
    • 2442448514 scopus 로고    scopus 로고
    • Magnetic-field-induced DNA strand breaks in brain cells of the rat
    • Lai, H.; Singh, N.P. Magnetic-field-induced DNA strand breaks in brain cells of the rat. Environ. Health Perspect. 2004, 112, 687-694.
    • (2004) Environ. Health Perspect. , vol.112 , pp. 687-694
    • Lai, H.1    Singh, N.P.2
  • 28
    • 0029803172 scopus 로고    scopus 로고
    • Detection of 8-oxo-2'-deoxyguanosine, a marker of oxidative DNA damage, in culture medium from human mesothelial cells exposed to crocidolite asbestos
    • Chen, Q.; Marsh, J.; Ames, B.; Mossman, B. Detection of 8-oxo-2'-deoxyguanosine, a marker of oxidative DNA damage, in culture medium from human mesothelial cells exposed to crocidolite asbestos. Carcinogenesis 1996, 17, 2525-2527.
    • (1996) Carcinogenesis , vol.17 , pp. 2525-2527
    • Chen, Q.1    Marsh, J.2    Ames, B.3    Mossman, B.4
  • 29
    • 77954563673 scopus 로고    scopus 로고
    • 8-oxo-7,8-dihydroguanine: Links to gene expression, aging, and defense against oxidative stress
    • Radak, Z.; Boldogh, I. 8-oxo-7,8-dihydroguanine: Links to gene expression, aging, and defense against oxidative stress. Free Radic. Biol. Med. 2010, 49, 587-596.
    • (2010) Free Radic. Biol. Med. , vol.49 , pp. 587-596
    • Radak, Z.1    Boldogh, I.2
  • 30
    • 85013603520 scopus 로고    scopus 로고
    • Elevated copper in the amyloid plaques and iron in the cortex are observed in mouse models of Alzheimer’s disease that exhibit neurodegeneration
    • Bourassa, M.W.; Leskovjan, A.C.; Tappero, R.V.; Farquhar, E.R.; Colton, C.A.; van Nostrand, W.E.; Miller, L.M. Elevated copper in the amyloid plaques and iron in the cortex are observed in mouse models of Alzheimer’s disease that exhibit neurodegeneration. Biomed. Spectrosc. Imaging 2013, 2, 129-139.
    • (2013) Biomed. Spectrosc. Imaging , vol.2 , pp. 129-139
    • Bourassa, M.W.1    Leskovjan, A.C.2    Tappero, R.V.3    Farquhar, E.R.4    Colton, C.A.5    van Nostrand, W.E.6    Miller, L.M.7
  • 31
    • 84874587315 scopus 로고    scopus 로고
    • The missing link in the amyloid cascade of Alzheimer’s disease-Metal ions
    • Tiiman, A.; Palumaa, P.; Tougu, V. The missing link in the amyloid cascade of Alzheimer’s disease-Metal ions. Neurochem. Int. 2013, 62, 367-378.
    • (2013) Neurochem. Int. , vol.62 , pp. 367-378
    • Tiiman, A.1    Palumaa, P.2    Tougu, V.3
  • 33
    • 0028122150 scopus 로고
    • Aluminum neurotoxicity: An experimental approach to the induction of neurofilamentous inclusions
    • Strong, M.J. Aluminum neurotoxicity: An experimental approach to the induction of neurofilamentous inclusions. J. Neurol. Sci. 1994, 124, 20-26.
    • (1994) J. Neurol. Sci. , vol.124 , pp. 20-26
    • Strong, M.J.1
  • 36
    • 0029953341 scopus 로고    scopus 로고
    • Astrocytes, brain aging, and neurodegeneration
    • Schipper, H.M. Astrocytes, brain aging, and neurodegeneration. Neurobiol. Aging 1996, 17, 467-480.
    • (1996) Neurobiol. Aging , vol.17 , pp. 467-480
    • Schipper, H.M.1
  • 39
    • 72949108889 scopus 로고    scopus 로고
    • From manganism to manganese-induced parkinsonism: A conceptual model based on the evolution of exposure
    • Lucchini, R.G.; Martin, C.J.; Doney, B.C. From manganism to manganese-induced parkinsonism: A conceptual model based on the evolution of exposure. Neuromol. Med. 2009, 11, 311-321.
    • (2009) Neuromol. Med. , vol.11 , pp. 311-321
    • Lucchini, R.G.1    Martin, C.J.2    Doney, B.C.3
  • 42
    • 0032522507 scopus 로고    scopus 로고
    • Immune regulation within the central nervous system
    • Xiao, B.G.; Link, H. Immune regulation within the central nervous system. J. Neurol. Sci. 1998, 157, 1-12.
    • (1998) J. Neurol. Sci. , vol.157 , pp. 1-12
    • Xiao, B.G.1    Link, H.2
  • 43
    • 0026704075 scopus 로고
    • Alterations in levels of iron, ferritin, and other trace metals in neurodegenerative diseases affecting the basal ganglia. The royal kings and queens Parkinson’s disease research group
    • Dexter, D.T.; Jenner, P.; Schapira, A.H.; Marsden, C.D. Alterations in levels of iron, ferritin, and other trace metals in neurodegenerative diseases affecting the basal ganglia. The royal kings and queens Parkinson’s disease research group. Ann. Neurol. 1992, 32, S94-S100.
    • (1992) Ann. Neurol. , vol.32 , pp. S94-S100
    • Dexter, D.T.1    Jenner, P.2    Schapira, A.H.3    Marsden, C.D.4
  • 44
  • 46
    • 34447520021 scopus 로고    scopus 로고
    • Ferritin accumulation in dystrophic microglia is an early event in the development of Huntington’s disease
    • Simmons, D.A.; Casale, M.; Alcon, B.; Pham, N.; Narayan, N.; Lynch, G. Ferritin accumulation in dystrophic microglia is an early event in the development of Huntington’s disease. Glia 2007, 55, 1074-1084.
    • (2007) Glia , vol.55 , pp. 1074-1084
    • Simmons, D.A.1    Casale, M.2    Alcon, B.3    Pham, N.4    Narayan, N.5    Lynch, G.6
  • 48
    • 0036801448 scopus 로고    scopus 로고
    • Molecular mechanism of copper transport in wilson disease
    • Fatemi, N.; Sarkar, B. Molecular mechanism of copper transport in wilson disease. Environ. Health Perspect. 2002, 110, 695-698.
    • (2002) Environ. Health Perspect. , vol.110 , pp. 695-698
    • Fatemi, N.1    Sarkar, B.2
  • 50
    • 0034700982 scopus 로고    scopus 로고
    • Copper-induced conformational changes in the N-terminal domain of the Wilson disease copper-transporting ATPase
    • DiDonato, M.; Hsu, H.F.; Narindrasorasak, S.; Que, L., Jr.; Sarkar, B. Copper-induced conformational changes in the N-terminal domain of the Wilson disease copper-transporting ATPase. Biochemistry 2000, 39, 1890-1896.
    • (2000) Biochemistry , vol.39 , pp. 1890-1896
    • DiDonato, M.1    Hsu, H.F.2    Narindrasorasak, S.3    Que, L.4    Sarkar, B.5
  • 51
    • 84888024893 scopus 로고    scopus 로고
    • Metal storage disorders: Wilson disease and hemochromatosis
    • Kanwar, P.; Kowdley, K.V. Metal storage disorders: Wilson disease and hemochromatosis. Med. Clin. North Am. 2014, 98, 87-102.
    • (2014) Med. Clin. North Am. , vol.98 , pp. 87-102
    • Kanwar, P.1    Kowdley, K.V.2
  • 52
    • 58849116869 scopus 로고    scopus 로고
    • Dysregulation of iron homeostasis in the CNS contributes to disease progression in a mouse model of amyotrophic lateral sclerosis
    • Jeong, S.Y.; Rathore, K.I.; Schulz, K.; Ponka, P.; Arosio, P.; David, S. Dysregulation of iron homeostasis in the CNS contributes to disease progression in a mouse model of amyotrophic lateral sclerosis. J. Neurosci. 2009, 29, 610-619.
    • (2009) J. Neurosci. , vol.29 , pp. 610-619
    • Jeong, S.Y.1    Rathore, K.I.2    Schulz, K.3    Ponka, P.4    Arosio, P.5    David, S.6
  • 53
    • 0029017315 scopus 로고
    • Aluminum, calcium, and iron in the spinal cord of patients with sporadic amyotrophic lateral sclerosis using laser microprobe mass spectroscopy: A preliminary study
    • Kasarskis, E.J.; Tandon, L.; Lovell, M.A.; Ehmann, W.D. Aluminum, calcium, and iron in the spinal cord of patients with sporadic amyotrophic lateral sclerosis using laser microprobe mass spectroscopy: A preliminary study. J. Neurol. Sci. 1995, 130, 203-208.
    • (1995) J. Neurol. Sci. , vol.130 , pp. 203-208
    • Kasarskis, E.J.1    Tandon, L.2    Lovell, M.A.3    Ehmann, W.D.4
  • 55
    • 0014311623 scopus 로고
    • Topographic determination of zinc in human brain by atomic absorption spectrophotometry
    • Hu, K.H.; Friede, R.L. Topographic determination of zinc in human brain by atomic absorption spectrophotometry. J. Neurochem. 1968, 15, 677-685.
    • (1968) J. Neurochem. , vol.15 , pp. 677-685
    • Hu, K.H.1    Friede, R.L.2
  • 57
    • 8844270071 scopus 로고    scopus 로고
    • Co(II) and Cd(II) substitute for Zn(II) in the zinc finger derived from the DNA repair protein XPA, demonstrating a variety of potential mechanisms of toxicity
    • Kopera, E.; Schwerdtle, T.; Hartwig, A.; Bal, W. Co(II) and Cd(II) substitute for Zn(II) in the zinc finger derived from the DNA repair protein XPA, demonstrating a variety of potential mechanisms of toxicity. Chem. Res. Toxicol. 2004, 17, 1452-1458.
    • (2004) Chem. Res. Toxicol. , vol.17 , pp. 1452-1458
    • Kopera, E.1    Schwerdtle, T.2    Hartwig, A.3    Bal, W.4
  • 58
    • 80054950096 scopus 로고    scopus 로고
    • Biophysical analysis of the interaction of toxic metal ions and oxidants with the zinc finger domain of XPA
    • Hartwig, A.; Schwerdtle, T.; Bal, W. Biophysical analysis of the interaction of toxic metal ions and oxidants with the zinc finger domain of XPA. Methods Mol. Biol. 2010, 649, 399-410.
    • (2010) Methods Mol. Biol. , vol.649 , pp. 399-410
    • Hartwig, A.1    Schwerdtle, T.2    Bal, W.3
  • 59
    • 0037330220 scopus 로고    scopus 로고
    • Mechanism of NICKEl assault on the zinc finger of DNA repair protein XPA
    • Bal, W.; Schwerdtle, T.; Hartwig, A. Mechanism of NICKEl assault on the zinc finger of DNA repair protein XPA. Chem. Res. Toxicol. 2003, 16, 242-248.
    • (2003) Chem. Res. Toxicol. , vol.16 , pp. 242-248
    • Bal, W.1    Schwerdtle, T.2    Hartwig, A.3
  • 60
    • 84883266816 scopus 로고    scopus 로고
    • Cadmium induced cell apoptosis, DNA damage, decreased DNA repair capacity, and genomic instability during malignant transformation of human bronchial epithelial cells
    • Zhou, Z.; Wang, C.; Liu, H.; Huang, Q.; Wang, M.; Lei, Y. Cadmium induced cell apoptosis, DNA damage, decreased DNA repair capacity, and genomic instability during malignant transformation of human bronchial epithelial cells. Int. J. Med. Sci. 2013, 10, 1485-1496.
    • (2013) Int. J. Med. Sci. , vol.10 , pp. 1485-1496
    • Zhou, Z.1    Wang, C.2    Liu, H.3    Huang, Q.4    Wang, M.5    Lei, Y.6
  • 61
    • 0024455825 scopus 로고
    • Primary cancer of the lung in women
    • Smith, E.B. Primary cancer of the lung in women. J. Natl. Med. Assoc. 1989, 81, 945-948.
    • (1989) J. Natl. Med. Assoc. , vol.81 , pp. 945-948
    • Smith, E.B.1
  • 62
    • 33845970892 scopus 로고    scopus 로고
    • Linkage study of cancer risk among lead-exposed workers in new jersey
    • Lam, T.V.; Agovino, P.; Niu, X.; Roche, L. Linkage study of cancer risk among lead-exposed workers in new jersey. Sci. Total Environ. 2007, 372, 455-462.
    • (2007) Sci. Total Environ. , vol.372 , pp. 455-462
    • Lam, T.V.1    Agovino, P.2    Niu, X.3    Roche, L.4
  • 63
    • 77951440874 scopus 로고    scopus 로고
    • Lung cancer risk associated with occupational exposure to NICKEl, chromium VI, and cadmium in two population-based case-control studies in montreal
    • Beveridge, R.; Pintos, J.; Parent, M.E.; Asselin, J.; Siemiatycki, J. Lung cancer risk associated with occupational exposure to NICKEl, chromium VI, and cadmium in two population-based case-control studies in montreal. Am. J. Ind. Med. 2010, 53, 476-485.
    • (2010) Am. J. Ind. Med. , vol.53 , pp. 476-485
    • Beveridge, R.1    Pintos, J.2    Parent, M.E.3    Asselin, J.4    Siemiatycki, J.5
  • 64
    • 84880047017 scopus 로고    scopus 로고
    • Toxicogenomic approaches for understanding molecular mechanisms of heavy metal mutagenicity and carcinogenicity
    • Koedrith, P.; Kim, H.; Weon, J.I.; Seo, Y.R. Toxicogenomic approaches for understanding molecular mechanisms of heavy metal mutagenicity and carcinogenicity. Int. J. Hyg. Environ. Health 2013, 216, 587-598.
    • (2013) Int. J. Hyg. Environ. Health , vol.216 , pp. 587-598
    • Koedrith, P.1    Kim, H.2    Weon, J.I.3    Seo, Y.R.4
  • 65
    • 84866531506 scopus 로고    scopus 로고
    • The role of cadmium and NICKEl in estrogen receptor signaling and breast cancer: Metalloestrogens or not?
    • Aquino, N.B.; Sevigny, M.B.; Sabangan, J.; Louie, M.C. The role of cadmium and NICKEl in estrogen receptor signaling and breast cancer: Metalloestrogens or not? J. Environ. Sci. Health C 2012, 30, 189-224.
    • (2012) J. Environ. Sci. Health C , vol.30 , pp. 189-224
    • Aquino, N.B.1    Sevigny, M.B.2    Sabangan, J.3    Louie, M.C.4
  • 66
    • 0032836651 scopus 로고    scopus 로고
    • Initiation of base excision repair: Glycosylase mechanisms and structures
    • McCullough, A.K.; Dodson, M.L.; Lloyd, R.S. Initiation of base excision repair: Glycosylase mechanisms and structures. Annu. Rev. Biochem. 1999, 68, 255-285.
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 255-285
    • McCullough, A.K.1    Dodson, M.L.2    Lloyd, R.S.3
  • 67
    • 0037125133 scopus 로고    scopus 로고
    • A novel human DNA glycosylase that removes oxidative DNA damage and is homologous to Escherichia coli endonuclease VIII
    • Bandaru, V.; Sunkara, S.; Wallace, S.S.; Bond, J.P. A novel human DNA glycosylase that removes oxidative DNA damage and is homologous to Escherichia coli endonuclease VIII. DNA Repair 2002, 1, 517-529.
    • (2002) DNA Repair , vol.1 , pp. 517-529
    • Bandaru, V.1    Sunkara, S.2    Wallace, S.S.3    Bond, J.P.4
  • 68
    • 0037133684 scopus 로고    scopus 로고
    • Identification and characterization of a human DNA glycosylase for repair of modified bases in oxidatively damaged DNA
    • Hazra, T.K.; Izumi, T.; Boldogh, I.; Imhoff, B.; Kow, Y.W.; Jaruga, P.; Dizdaroglu, M.; Mitra, S. Identification and characterization of a human DNA glycosylase for repair of modified bases in oxidatively damaged DNA. Proc. Natl. Acad. Sci. USA 2002, 99, 3523-3528.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 3523-3528
    • Hazra, T.K.1    Izumi, T.2    Boldogh, I.3    Imhoff, B.4    Kow, Y.W.5    Jaruga, P.6    Dizdaroglu, M.7    Mitra, S.8
  • 69
    • 50649116450 scopus 로고    scopus 로고
    • Eukaryotic DNA ligases: Structural and functional insights
    • Ellenberger, T.; Tomkinson, A.E. Eukaryotic DNA ligases: Structural and functional insights. Annu. Rev. Biochem. 2008, 77, 313-338.
    • (2008) Annu. Rev. Biochem. , vol.77 , pp. 313-338
    • Ellenberger, T.1    Tomkinson, A.E.2
  • 70
    • 84863008841 scopus 로고    scopus 로고
    • The Fpg/Nei family of DNA glycosylases: Substrates, structures, and search for damage
    • Prakash, A.; Doublie, S.; Wallace, S.S. The Fpg/Nei family of DNA glycosylases: Substrates, structures, and search for damage. Prog. Mol. Biol. Transl. Sci. 2012, 110, 71-91.
    • (2012) Prog. Mol. Biol. Transl. Sci. , vol.110 , pp. 71-91
    • Prakash, A.1    Doublie, S.2    Wallace, S.S.3
  • 71
    • 0037162995 scopus 로고    scopus 로고
    • Identification and characterization of a novel human DNA glycosylase for repair of cytosine-derived lesions
    • Hazra, T.K.; Kow, Y.W.; Hatahet, Z.; Imhoff, B.; Boldogh, I.; Mokkapati, S.K.; Mitra, S.; Izumi, T. Identification and characterization of a novel human DNA glycosylase for repair of cytosine-derived lesions. J. Biol. Chem. 2002, 277, 30417-30420.
    • (2002) J. Biol. Chem. , vol.277 , pp. 30417-30420
    • Hazra, T.K.1    Kow, Y.W.2    Hatahet, Z.3    Imhoff, B.4    Boldogh, I.5    Mokkapati, S.K.6    Mitra, S.7    Izumi, T.8
  • 74
    • 84902073074 scopus 로고    scopus 로고
    • Base excision repair: A critical player in many games
    • Wallace, S.S. Base excision repair: A critical player in many games. DNA Repair 2014, 19, 14-26.
    • (2014) DNA Repair , vol.19 , pp. 14-26
    • Wallace, S.S.1
  • 76
    • 0034659935 scopus 로고    scopus 로고
    • The lyase activity of the DNA repair protein beta-polymerase protects from DNA-damage-induced cytotoxicity
    • Sobol, R.W.; Prasad, R.; Evenski, A.; Baker, A.; Yang, X.P.; Horton, J.K.; Wilson, S.H. The lyase activity of the DNA repair protein beta-polymerase protects from DNA-damage-induced cytotoxicity. Nature 2000, 405, 807-810.
    • (2000) Nature , vol.405 , pp. 807-810
    • Sobol, R.W.1    Prasad, R.2    Evenski, A.3    Baker, A.4    Yang, X.P.5    Horton, J.K.6    Wilson, S.H.7
  • 78
    • 55249083320 scopus 로고    scopus 로고
    • Physical and functional interaction between human oxidized base-specific DNA glycosylase NEIL1 and flap endonuclease 1
    • Hegde, M.L.; Theriot, C.A.; Das, A.; Hegde, P.M.; Guo, Z.; Gary, R.K.; Hazra, T.K.; Shen, B.; Mitra, S. Physical and functional interaction between human oxidized base-specific DNA glycosylase NEIL1 and flap endonuclease 1. J. Biol. Chem. 2008, 283, 27028-27037.
    • (2008) J. Biol. Chem. , vol.283 , pp. 27028-27037
    • Hegde, M.L.1    Theriot, C.A.2    Das, A.3    Hegde, P.M.4    Guo, Z.5    Gary, R.K.6    Hazra, T.K.7    Shen, B.8    Mitra, S.9
  • 79
    • 3943086339 scopus 로고    scopus 로고
    • Flap endonuclease 1: A central component of DNA metabolism
    • Liu, Y.; Kao, H.I.; Bambara, R.A. Flap endonuclease 1: A central component of DNA metabolism. Annu. Rev. Biochem. 2004, 73, 589-615.
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 589-615
    • Liu, Y.1    Kao, H.I.2    Bambara, R.A.3
  • 83
    • 41249094475 scopus 로고    scopus 로고
    • Interaction of the human DNA glycosylase NEIL1 with proliferating cell nuclear antigen. The potential for replication-associated repair of oxidized bases in mammalian genomes
    • Dou, H.; Theriot, C.A.; Das, A.; Hegde, M.L.; Matsumoto, Y.; Boldogh, I.; Hazra, T.K.; Bhakat, K.K.; Mitra, S. Interaction of the human DNA glycosylase NEIL1 with proliferating cell nuclear antigen. The potential for replication-associated repair of oxidized bases in mammalian genomes. J. Biol. Chem. 2008, 283, 3130-3140.
    • (2008) J. Biol. Chem. , vol.283 , pp. 3130-3140
    • Dou, H.1    Theriot, C.A.2    Das, A.3    Hegde, M.L.4    Matsumoto, Y.5    Boldogh, I.6    Hazra, T.K.7    Bhakat, K.K.8    Mitra, S.9
  • 84
    • 0029958378 scopus 로고    scopus 로고
    • A eukaryotic enzyme that can disjoin dead-end covalent complexes between DNA and type I topoisomerases
    • Yang, S.W.; Burgin, A.B., Jr.; Huizenga, B.N.; Robertson, C.A.; Yao, K.C.; Nash, H.A. A eukaryotic enzyme that can disjoin dead-end covalent complexes between DNA and type I topoisomerases. Proc. Natl. Acad. Sci. USA 1996, 93, 11534-11539.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 11534-11539
    • Yang, S.W.1    Burgin, A.B.2    Huizenga, B.N.3    Robertson, C.A.4    Yao, K.C.5    Nash, H.A.6
  • 85
    • 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
  • 88
    • 34248215322 scopus 로고    scopus 로고
    • Actions of aprataxin in multiple DNA repair pathways
    • Rass, U.; Ahel, I.; West, S.C. Actions of aprataxin in multiple DNA repair pathways. J. Biol. Chem. 2007, 282, 9469-9474.
    • (2007) J. Biol. Chem. , vol.282 , pp. 9469-9474
    • Rass, U.1    Ahel, I.2    West, S.C.3
  • 91
    • 48249095920 scopus 로고    scopus 로고
    • Single-strand break repair and genetic disease
    • Caldecott, K.W. Single-strand break repair and genetic disease. Nat. Rev. Genet. 2008, 9, 619-631.
    • (2008) Nat. Rev. Genet. , vol.9 , pp. 619-631
    • Caldecott, K.W.1
  • 93
    • 34548535219 scopus 로고    scopus 로고
    • TDP1 facilitates repair of ionizing radiation-induced DNA single-strand breaks
    • El-Khamisy, S.F.; Hartsuiker, E.; Caldecott, K.W. TDP1 facilitates repair of ionizing radiation-induced DNA single-strand breaks. DNA Repair 2007, 6, 1485-1495.
    • (2007) DNA Repair , vol.6 , pp. 1485-1495
    • El-Khamisy, S.F.1    Hartsuiker, E.2    Caldecott, K.W.3
  • 94
    • 0035890069 scopus 로고    scopus 로고
    • XRCC1 coordinates the initial and late stages of DNA abasic site repair through protein-protein interactions
    • Vidal, A.E.; Boiteux, S.; Hickson, I.D.; Radicella, J.P. XRCC1 coordinates the initial and late stages of DNA abasic site repair through protein-protein interactions. EMBO J. 2001, 20, 6530-6539.
    • (2001) EMBO J. , vol.20 , pp. 6530-6539
    • Vidal, A.E.1    Boiteux, S.2    Hickson, I.D.3    Radicella, J.P.4
  • 95
    • 57349170258 scopus 로고    scopus 로고
    • Regulatory role of human AP-endonuclease (APE1/Ref-1) in YB-1-mediated activation of the multidrug resistance gene MDR1
    • Chattopadhyay, R.; Das, S.; Maiti, A.K.; Boldogh, I.; Xie, J.; Hazra, T.K.; Kohno, K.; Mitra, S.; Bhakat, K.K. Regulatory role of human AP-endonuclease (APE1/Ref-1) in YB-1-mediated activation of the multidrug resistance gene MDR1. Mol. Cell. Biol. 2008, 28, 7066-7080.
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 7066-7080
    • Chattopadhyay, R.1    Das, S.2    Maiti, A.K.3    Boldogh, I.4    Xie, J.5    Hazra, T.K.6    Kohno, K.7    Mitra, S.8    Bhakat, K.K.9
  • 96
    • 0035877851 scopus 로고    scopus 로고
    • Stimulation of human endonuclease III by Y box-binding protein 1 (DNA-binding protein ß). Interaction between a base excision repair enzyme and a transcription factor
    • Marenstein, D.R.; Ocampo, M.T.; Chan, M.K.; Altamirano, A.; Basu, A.K.; Boorstein, R.J.; Cunningham, R.P.; Teebor, G.W. Stimulation of human endonuclease III by Y box-binding protein 1 (DNA-binding protein ß). Interaction between a base excision repair enzyme and a transcription factor. J. Biol. Chem. 2001, 276, 21242-21249.
    • (2001) J. Biol. Chem. , vol.276 , pp. 21242-21249
    • Marenstein, D.R.1    Ocampo, M.T.2    Chan, M.K.3    Altamirano, A.4    Basu, A.K.5    Boorstein, R.J.6    Cunningham, R.P.7    Teebor, G.W.8
  • 97
    • 84867261398 scopus 로고    scopus 로고
    • Enhancement of NEIL1 protein-initiated oxidized DNA base excision repair by heterogeneous nuclear ribonucleoprotein U (hnRNP-U) via direct interaction
    • Hegde, M.L.; Banerjee, S.; Hegde, P.M.; Bellot, L.J.; Hazra, T.K.; Boldogh, I.; Mitra, S. Enhancement of NEIL1 protein-initiated oxidized DNA base excision repair by heterogeneous nuclear ribonucleoprotein U (hnRNP-U) via direct interaction. J. Biol. Chem. 2012, 287, 34202-34211.
    • (2012) J. Biol. Chem. , vol.287 , pp. 34202-34211
    • Hegde, M.L.1    Banerjee, S.2    Hegde, P.M.3    Bellot, L.J.4    Hazra, T.K.5    Boldogh, I.6    Mitra, S.7
  • 98
    • 3042674067 scopus 로고    scopus 로고
    • Acetylation of the human DNA glycosylase NEIL2 and inhibition of its activity
    • Bhakat, K.K.; Hazra, T.K.; Mitra, S. Acetylation of the human DNA glycosylase NEIL2 and inhibition of its activity. Nucleic Acids Res. 2004, 32, 3033-3039.
    • (2004) Nucleic Acids Res. , vol.32 , pp. 3033-3039
    • Bhakat, K.K.1    Hazra, T.K.2    Mitra, S.3
  • 99
    • 33644514315 scopus 로고    scopus 로고
    • Acetylation of human 8-oxoguanine-DNA glycosylase by p300 and its role in 8-oxoguanine repair in vivo
    • Bhakat, K.K.; Mokkapati, S.K.; Boldogh, I.; Hazra, T.K.; Mitra, S. Acetylation of human 8-oxoguanine-DNA glycosylase by p300 and its role in 8-oxoguanine repair in vivo. Mol. Cell. Biol. 2006, 26, 1654-1665.
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 1654-1665
    • Bhakat, K.K.1    Mokkapati, S.K.2    Boldogh, I.3    Hazra, T.K.4    Mitra, S.5
  • 100
    • 79251647522 scopus 로고    scopus 로고
    • Human AP endonuclease (APE1/Ref-1) and its acetylation regulate YB-1-p300 recruitment and RNA polymerase II loading in the drug-induced activation of multidrug resistance gene MDR1
    • Sengupta, S.; Mantha, A.K.; Mitra, S.; Bhakat, K.K. Human AP endonuclease (APE1/Ref-1) and its acetylation regulate YB-1-p300 recruitment and RNA polymerase II loading in the drug-induced activation of multidrug resistance gene MDR1. Oncogene 2010, 30, 482-493.
    • (2010) Oncogene , vol.30 , pp. 482-493
    • Sengupta, S.1    Mantha, A.K.2    Mitra, S.3    Bhakat, K.K.4
  • 101
    • 0036184090 scopus 로고    scopus 로고
    • Association of CBP/p300 acetylase and thymine DNA glycosylase links DNA repair and transcription
    • Tini, M.; Benecke, A.; Um, S.J.; Torchia, J.; Evans, R.M.; Chambon, P. Association of CBP/p300 acetylase and thymine DNA glycosylase links DNA repair and transcription. Mol. Cell 2002, 9, 265-277.
    • (2002) Mol. Cell , vol.9 , pp. 265-277
    • Tini, M.1    Benecke, A.2    Um, S.J.3    Torchia, J.4    Evans, R.M.5    Chambon, P.6
  • 102
    • 0031439356 scopus 로고    scopus 로고
    • The DNA repair activity of human redox/repair protein APE/Ref-1 is inactivated by phosphorylation
    • Yacoub, A.; Kelley, M.R.; Deutsch, W.A. The DNA repair activity of human redox/repair protein APE/Ref-1 is inactivated by phosphorylation. Cancer Res. 1997, 57, 5457-5459.
    • (1997) Cancer Res. , vol.57 , pp. 5457-5459
    • Yacoub, A.1    Kelley, M.R.2    Deutsch, W.A.3
  • 103
    • 0033611583 scopus 로고    scopus 로고
    • Phosphorylation of the DNA repair protein APE/Ref-1 by CKII affects redox regulation of AP-1
    • Fritz, G.; Kaina, B. Phosphorylation of the DNA repair protein APE/Ref-1 by CKII affects redox regulation of AP-1. Oncogene 1999, 18, 1033-1040.
    • (1999) Oncogene , vol.18 , pp. 1033-1040
    • Fritz, G.1    Kaina, B.2
  • 108
    • 14044278774 scopus 로고    scopus 로고
    • Noncovalent SUMO-1 binding activity of thymine DNA glycosylase (TDG) is required for its SUMO-1 modification and colocalization with the promyelocytic leukemia protein
    • Takahashi, H.; Hatakeyama, S.; Saitoh, H.; Nakayama, K.I. Noncovalent SUMO-1 binding activity of thymine DNA glycosylase (TDG) is required for its SUMO-1 modification and colocalization with the promyelocytic leukemia protein. J. Biol. Chem. 2005, 280, 5611-5621.
    • (2005) J. Biol. Chem. , vol.280 , pp. 5611-5621
    • Takahashi, H.1    Hatakeyama, S.2    Saitoh, H.3    Nakayama, K.I.4
  • 109
    • 0037086643 scopus 로고    scopus 로고
    • Modification of the human thymine-DNA glycosylase by ubiquitin-like proteins facilitates enzymatic turnover
    • Hardeland, U.; Steinacher, R.; Jiricny, J.; Schar, P. Modification of the human thymine-DNA glycosylase by ubiquitin-like proteins facilitates enzymatic turnover. EMBO J. 2002, 21, 1456-1464.
    • (2002) EMBO J. , vol.21 , pp. 1456-1464
    • Hardeland, U.1    Steinacher, R.2    Jiricny, J.3    Schar, P.4
  • 110
    • 17144410054 scopus 로고    scopus 로고
    • Functionality of human thymine DNA glycosylase requires SUMO-regulated changes in protein conformation
    • Steinacher, R.; Schar, P. Functionality of human thymine DNA glycosylase requires SUMO-regulated changes in protein conformation. Curr. Biol. 2005, 15, 616-623.
    • (2005) Curr. Biol. , vol.15 , pp. 616-623
    • Steinacher, R.1    Schar, P.2
  • 111
    • 33846025995 scopus 로고    scopus 로고
    • Methylation of DNA polymerase beta by protein arginine methyltransferase 1 regulates its binding to proliferating cell nuclear antigen
    • El-Andaloussi, N.; Valovka, T.; Toueille, M.; Hassa, P.O.; Gehrig, P.; Covic, M.; Hubscher, U.; Hottiger, M.O. Methylation of DNA polymerase beta by protein arginine methyltransferase 1 regulates its binding to proliferating cell nuclear antigen. FASEB J. 2007, 21, 26-34.
    • (2007) FASEB J. , vol.21 , pp. 26-34
    • El-Andaloussi, N.1    Valovka, T.2    Toueille, M.3    Hassa, P.O.4    Gehrig, P.5    Covic, M.6    Hubscher, U.7    Hottiger, M.O.8
  • 112
    • 0037163025 scopus 로고    scopus 로고
    • Direct interaction between mammalian DNA polymerase beta and proliferating cell nuclear antigen
    • Kedar, P.S.; Kim, S.J.; Robertson, A.; Hou, E.; Prasad, R.; Horton, J.K.; Wilson, S.H. Direct interaction between mammalian DNA polymerase beta and proliferating cell nuclear antigen. J. Biol. Chem. 2002, 277, 31115-31123.
    • (2002) J. Biol. Chem. , vol.277 , pp. 31115-31123
    • Kedar, P.S.1    Kim, S.J.2    Robertson, A.3    Hou, E.4    Prasad, R.5    Horton, J.K.6    Wilson, S.H.7
  • 113
    • 55549139051 scopus 로고    scopus 로고
    • The expanding field of poly(ADP-ribosyl)ation reactions. Protein modifications: Beyond the usual suspects. review series
    • Hakme, A.; Wong, H.K.; Dantzer, F.; Schreiber, V. The expanding field of poly(ADP-ribosyl)ation reactions. Protein modifications: Beyond the usual suspects. review series. EMBO Rep. 2008, 9, 1094-1100.
    • (2008) EMBO Rep. , vol.9 , pp. 1094-1100
    • Hakme, A.1    Wong, H.K.2    Dantzer, F.3    Schreiber, V.4
  • 114
    • 0142009654 scopus 로고    scopus 로고
    • A requirement for PARP-1 for the assembly or stability of XRCC1 nuclear foci at sites of oxidative DNA damage
    • El-Khamisy, S.F.; Masutani, M.; Suzuki, H.; Caldecott, K.W. A requirement for PARP-1 for the assembly or stability of XRCC1 nuclear foci at sites of oxidative DNA damage. Nucleic Acids Res. 2003, 31, 5526-5533.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 5526-5533
    • El-Khamisy, S.F.1    Masutani, M.2    Suzuki, H.3    Caldecott, K.W.4
  • 116
    • 78650877882 scopus 로고    scopus 로고
    • The role of MutY homolog (Myh1) in controlling the histone deacetylase Hst4 in the fission yeast Schizosaccharomyces pombe
    • Chang, D.Y.; Shi, G.; Durand-Dubief, M.; Ekwall, K.; Lu, A.L. The role of MutY homolog (Myh1) in controlling the histone deacetylase Hst4 in the fission yeast Schizosaccharomyces pombe. J. Mol. Biol. 2011, 405, 653-665.
    • (2011) J. Mol. Biol. , vol.405 , pp. 653-665
    • Chang, D.Y.1    Shi, G.2    Durand-Dubief, M.3    Ekwall, K.4    Lu, A.L.5
  • 117
    • 84862978423 scopus 로고    scopus 로고
    • Oxidized base damage and single-strand break repair in mammalian genomes: Role of disordered regions and posttranslational modifications in early enzymes
    • Hegde, M.L.; Izumi, T.; Mitra, S. Oxidized base damage and single-strand break repair in mammalian genomes: Role of disordered regions and posttranslational modifications in early enzymes. Prog. Mol. Biol. Transl. Sci. 2012, 110, 123-153.
    • (2012) Prog. Mol. Biol. Transl. Sci. , vol.110 , pp. 123-153
    • Hegde, M.L.1    Izumi, T.2    Mitra, S.3
  • 118
    • 78149469033 scopus 로고    scopus 로고
    • Functions of disordered regions in mammalian early base excision repair proteins
    • Hegde, M.L.; Hazra, T.K.; Mitra, S. Functions of disordered regions in mammalian early base excision repair proteins. Cell. Mol. Life Sci. 2010, 67, 3573-3587.
    • (2010) Cell. Mol. Life Sci. , vol.67 , pp. 3573-3587
    • Hegde, M.L.1    Hazra, T.K.2    Mitra, S.3
  • 120
    • 0033026606 scopus 로고    scopus 로고
    • Nucleotide substitution rate of mammalian mitochondrial genomes
    • Pesole, G.; Gissi, C.; de Chirico, A.; Saccone, C. Nucleotide substitution rate of mammalian mitochondrial genomes. J. Mol. Evol. 1999, 48, 427-434.
    • (1999) J. Mol. Evol. , vol.48 , pp. 427-434
    • Pesole, G.1    Gissi, C.2    de Chirico, A.3    Saccone, C.4
  • 121
    • 0031032817 scopus 로고    scopus 로고
    • Mitochondrial DNA damage is more extensive and persists longer than nuclear DNA damage in human cells following oxidative stress
    • Yakes, F.M.; van Houten, B. Mitochondrial DNA damage is more extensive and persists longer than nuclear DNA damage in human cells following oxidative stress. Proc. Natl. Acad. Sci. USA 1997, 94, 514-519.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 514-519
    • Yakes, F.M.1    van Houten, B.2
  • 123
    • 55049124777 scopus 로고    scopus 로고
    • Long patch base excision repair in mammalian mitochondrial genomes
    • Szczesny, B.; Tann, A.W.; Longley, M.J.; Copeland, W.C.; Mitra, S. Long patch base excision repair in mammalian mitochondrial genomes. J. Biol. Chem. 2008, 283, 26349-26356.
    • (2008) J. Biol. Chem. , vol.283 , pp. 26349-26356
    • Szczesny, B.1    Tann, A.W.2    Longley, M.J.3    Copeland, W.C.4    Mitra, S.5
  • 124
    • 0015255237 scopus 로고
    • Studies on nitrosodimethylamine: Preferential methylation of mitochondrial DNA in rats and hamsters
    • Wunderlich, V.; Tetzlaff, I.; Graffi, A. Studies on nitrosodimethylamine: Preferential methylation of mitochondrial DNA in rats and hamsters. Chem. Biol. Interact. 1972, 4, 81-89.
    • (1972) Chem. Biol. Interact. , vol.4 , pp. 81-89
    • Wunderlich, V.1    Tetzlaff, I.2    Graffi, A.3
  • 126
    • 70349749966 scopus 로고    scopus 로고
    • The role of environmental mercury, lead and pesticide exposure in development of amyotrophic lateral sclerosis
    • Johnson, F.O.; Atchison, W.D. The role of environmental mercury, lead and pesticide exposure in development of amyotrophic lateral sclerosis. Neurotoxicology 2009, 30, 761-765.
    • (2009) Neurotoxicology , vol.30 , pp. 761-765
    • Johnson, F.O.1    Atchison, W.D.2
  • 127
    • 23744463617 scopus 로고    scopus 로고
    • Tissue-specific accumulation of cadmium in subcellular compartments of eastern oysters Crassostrea virginica Gmelin (Bivalvia: Ostreidae)
    • Sokolova, I.M.; Ringwood, A.H.; Johnson, C. Tissue-specific accumulation of cadmium in subcellular compartments of eastern oysters Crassostrea virginica Gmelin (Bivalvia: Ostreidae). Aquat. Toxicol. 2005, 74, 218-228.
    • (2005) Aquat. Toxicol. , vol.74 , pp. 218-228
    • Sokolova, I.M.1    Ringwood, A.H.2    Johnson, C.3
  • 128
    • 0036904776 scopus 로고    scopus 로고
    • Base excision repair capacity in mitochondria and nuclei: Tissue-specific variations
    • Karahalil, B.; Hogue, B.A.; de Souza-Pinto, N.C.; Bohr, V.A. Base excision repair capacity in mitochondria and nuclei: Tissue-specific variations. FASEB J. 2002, 16, 1895-1902.
    • (2002) FASEB J. , vol.16 , pp. 1895-1902
    • Karahalil, B.1    Hogue, B.A.2    de Souza-Pinto, N.C.3    Bohr, V.A.4
  • 129
    • 77953036663 scopus 로고    scopus 로고
    • Age- and tissue-specific changes in mitochondrial and nuclear DNA base excision repair activity in mice: Susceptibility of skeletal muscles to oxidative injury
    • Szczesny, B.; Tann, A.W.; Mitra, S. Age- and tissue-specific changes in mitochondrial and nuclear DNA base excision repair activity in mice: Susceptibility of skeletal muscles to oxidative injury. Mech. Ageing Dev. 2010, 131, 330-337.
    • (2010) Mech. Ageing Dev. , vol.131 , pp. 330-337
    • Szczesny, B.1    Tann, A.W.2    Mitra, S.3
  • 130
    • 45449112761 scopus 로고    scopus 로고
    • Brain capacity for repair of oxidatively damaged DNA and preservation of neuronal function
    • Englander, E.W. Brain capacity for repair of oxidatively damaged DNA and preservation of neuronal function. Mech. Ageing Dev. 2008, 129, 475-482.
    • (2008) Mech. Ageing Dev. , vol.129 , pp. 475-482
    • Englander, E.W.1
  • 131
    • 2442572164 scopus 로고    scopus 로고
    • Apurinic/apyrimidinic endonuclease (APE/Ref-1) haploinsufficient mice display tissue-specific differences in DNA polymerase beta-dependent base excision repair
    • Raffoul, J.J.; Cabelof, D.C.; Nakamura, J.; Meira, L.B.; Friedberg, E.C.; Heydari, A.R. Apurinic/apyrimidinic endonuclease (APE/Ref-1) haploinsufficient mice display tissue-specific differences in DNA polymerase beta-dependent base excision repair. J. Biol. Chem. 2004, 279, 18425-18433.
    • (2004) J. Biol. Chem. , vol.279 , pp. 18425-18433
    • Raffoul, J.J.1    Cabelof, D.C.2    Nakamura, J.3    Meira, L.B.4    Friedberg, E.C.5    Heydari, A.R.6
  • 132
    • 84866284780 scopus 로고    scopus 로고
    • Endonuclease VIII-like 1 (NEIL1) promotes short-term spatial memory retention and protects from ischemic stroke-induced brain dysfunction and death in mice
    • Canugovi, C.; Yoon, J.S.; Feldman, N.H.; Croteau, D.L.; Mattson, M.P.; Bohr, V.A. Endonuclease VIII-like 1 (NEIL1) promotes short-term spatial memory retention and protects from ischemic stroke-induced brain dysfunction and death in mice. Proc. Natl. Acad. Sci. USA 2012, 109, 14948-14953.
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 14948-14953
    • Canugovi, C.1    Yoon, J.S.2    Feldman, N.H.3    Croteau, D.L.4    Mattson, M.P.5    Bohr, V.A.6
  • 133
    • 32944471308 scopus 로고    scopus 로고
    • Hematopoietic tissue-specific expression of mouse NEIL3 for endonuclease VIII-like protein
    • Torisu, K.; Tsuchimoto, D.; Ohnishi, Y.; Nakabeppu, Y. Hematopoietic tissue-specific expression of mouse NEIL3 for endonuclease VIII-like protein. J. Biochem. 2005, 138, 763-772.
    • (2005) J. Biochem. , vol.138 , pp. 763-772
    • Torisu, K.1    Tsuchimoto, D.2    Ohnishi, Y.3    Nakabeppu, Y.4
  • 136
    • 84874548507 scopus 로고    scopus 로고
    • Loss of NEIL3, the major DNA glycosylase activity for removal of hydantoins in single stranded DNA, reduces cellular proliferation and sensitizes cells to genotoxic stress
    • Rolseth, V.; Krokeide, S.Z.; Kunke, D.; Neurauter, C.G.; Suganthan, R.; Sejersted, Y.; Hildrestrand, G.A.; Bjoras, M.; Luna, L. Loss of NEIL3, the major DNA glycosylase activity for removal of hydantoins in single stranded DNA, reduces cellular proliferation and sensitizes cells to genotoxic stress. Biochim. Biophys. Acta 2013, 1833, 1157-1164.
    • (2013) Biochim. Biophys. Acta , vol.1833 , pp. 1157-1164
    • Rolseth, V.1    Krokeide, S.Z.2    Kunke, D.3    Neurauter, C.G.4    Suganthan, R.5    Sejersted, Y.6    Hildrestrand, G.A.7    Bjoras, M.8    Luna, L.9
  • 138
    • 80053128348 scopus 로고    scopus 로고
    • Study of DNA damage via the comet assay and base excision repair activities in rat brain neurons and astrocytes during aging
    • Swain, U.; Subba Rao, K. Study of DNA damage via the comet assay and base excision repair activities in rat brain neurons and astrocytes during aging. Mech. Ageing Dev. 2011, 132, 374-381.
    • (2011) Mech. Ageing Dev. , vol.132 , pp. 374-381
    • Swain, U.1    Subba Rao, K.2
  • 139
    • 33847667547 scopus 로고    scopus 로고
    • Mitochondrial dysfunction in Parkinson’s disease
    • Fukae, J.; Mizuno, Y.; Hattori, N. Mitochondrial dysfunction in Parkinson’s disease. Mitochondrion 2007, 7, 58-62.
    • (2007) Mitochondrion , vol.7 , pp. 58-62
    • Fukae, J.1    Mizuno, Y.2    Hattori, N.3
  • 141
    • 70349991252 scopus 로고    scopus 로고
    • Role of APE1 in differentiated neuroblastoma SH-SY5Y cells in response to oxidative stress: Use of APE1 small molecule inhibitors to delineate APE1 functions
    • Jiang, Y.; Guo, C.; Fishel, M.L.; Wang, Z.Y.; Vasko, M.R.; Kelley, M.R. Role of APE1 in differentiated neuroblastoma SH-SY5Y cells in response to oxidative stress: Use of APE1 small molecule inhibitors to delineate APE1 functions. DNA Repair 2009, 8, 1273-1282.
    • (2009) DNA Repair , vol.8 , pp. 1273-1282
    • Jiang, Y.1    Guo, C.2    Fishel, M.L.3    Wang, Z.Y.4    Vasko, M.R.5    Kelley, M.R.6
  • 142
    • 12344291209 scopus 로고    scopus 로고
    • The multifunctional DNA repair/redox enzyme APE1/Ref-1 promotes survival of neurons after oxidative stress
    • Vasko, M.R.; Guo, C.; Kelley, M.R. The multifunctional DNA repair/redox enzyme APE1/Ref-1 promotes survival of neurons after oxidative stress. DNA Repair 2005, 4, 367-379.
    • (2005) DNA Repair , vol.4 , pp. 367-379
    • Vasko, M.R.1    Guo, C.2    Kelley, M.R.3
  • 143
    • 51049100621 scopus 로고    scopus 로고
    • Implications of apurinic/apyrimidinic endonuclease in reactive oxygen signaling response after cisplatin treatment of dorsal root ganglion neurons
    • Jiang, Y.; Guo, C.; Vasko, M.R.; Kelley, M.R. Implications of apurinic/apyrimidinic endonuclease in reactive oxygen signaling response after cisplatin treatment of dorsal root ganglion neurons. Cancer Res. 2008, 68, 6425-6434.
    • (2008) Cancer Res. , vol.68 , pp. 6425-6434
    • Jiang, Y.1    Guo, C.2    Vasko, M.R.3    Kelley, M.R.4
  • 144
    • 68849105162 scopus 로고    scopus 로고
    • DNA 3'-phosphatase activity is critical for rapid global rates of single-strand break repair following oxidative stress
    • Breslin, C.; Caldecott, K.W. DNA 3'-phosphatase activity is critical for rapid global rates of single-strand break repair following oxidative stress. Mol. Cell. Biol. 2009, 29, 4653-4662.
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 4653-4662
    • Breslin, C.1    Caldecott, K.W.2
  • 145
    • 0032100860 scopus 로고    scopus 로고
    • Mammalian base excision repair and DNA polymerase beta
    • Wilson, S.H. Mammalian base excision repair and DNA polymerase beta. Mutat. Res. 1998, 407, 203-215.
    • (1998) Mutat. Res. , vol.407 , pp. 203-215
    • Wilson, S.H.1
  • 146
    • 34247148449 scopus 로고    scopus 로고
    • Base excision repair and the central nervous system
    • Wilson, D.M., 3rd; McNeill, D.R. Base excision repair and the central nervous system. Neuroscience 2007, 145, 1187-1200.
    • (2007) Neuroscience , vol.145 , pp. 1187-1200
    • Wilson, D.M.1    McNeill, D.R.2
  • 147
    • 67349099614 scopus 로고    scopus 로고
    • Extracts of proliferating and non-proliferating human cells display different base excision pathways and repair fidelity
    • Akbari, M.; Pena-Diaz, J.; Andersen, S.; Liabakk, N.B.; Otterlei, M.; Krokan, H.E. Extracts of proliferating and non-proliferating human cells display different base excision pathways and repair fidelity. DNA Repair 2009, 8, 834-843.
    • (2009) DNA Repair , vol.8 , pp. 834-843
    • Akbari, M.1    Pena-Diaz, J.2    Andersen, S.3    Liabakk, N.B.4    Otterlei, M.5    Krokan, H.E.6
  • 148
    • 53749101402 scopus 로고    scopus 로고
    • DNA polymerase beta-catalyzed-PCNA independent long patch base excision repair synthesis: A mechanism for repair of oxidatively damaged DNA ends in post-mitotic brain
    • Wei, W.; Englander, E.W. DNA polymerase beta-catalyzed-PCNA independent long patch base excision repair synthesis: A mechanism for repair of oxidatively damaged DNA ends in post-mitotic brain. J. Neurochem. 2008, 107, 734-744.
    • (2008) J. Neurochem. , vol.107 , pp. 734-744
    • Wei, W.1    Englander, E.W.2
  • 149
    • 79954453376 scopus 로고    scopus 로고
    • Alzheimer’s disease & metals: Therapeutic opportunities
    • Kenche, V.B.; Barnham, K.J. Alzheimer’s disease & metals: Therapeutic opportunities. Br. J. Pharmacol. 2011, 163, 211-219.
    • (2011) Br. J. Pharmacol. , vol.163 , pp. 211-219
    • Kenche, V.B.1    Barnham, K.J.2
  • 150
    • 84883168593 scopus 로고    scopus 로고
    • Increased iron levels and decreased tissue integrity in hippocampus of Alzheimer’s disease detected in vivo with magnetic resonance imaging
    • Raven, E.P.; Lu, P.H.; Tishler, T.A.; Heydari, P.; Bartzokis, G. Increased iron levels and decreased tissue integrity in hippocampus of Alzheimer’s disease detected in vivo with magnetic resonance imaging. J. Alzheimers Dis. 2013, 37, 127-136.
    • (2013) J. Alzheimers Dis. , vol.37 , pp. 127-136
    • Raven, E.P.1    Lu, P.H.2    Tishler, T.A.3    Heydari, P.4    Bartzokis, G.5
  • 151
    • 77950533625 scopus 로고    scopus 로고
    • Divalent metal transporter, iron, and Parkinson’s disease: A pathological relationship
    • Lee, H.P.; Zhu, X.; Liu, G.; Chen, S.G.; Perry, G.; Smith, M.A.; Lee, H.G. Divalent metal transporter, iron, and Parkinson’s disease: A pathological relationship. Cell Res. 2010, 20, 397-399.
    • (2010) Cell Res. , vol.20 , pp. 397-399
    • Lee, H.P.1    Zhu, X.2    Liu, G.3    Chen, S.G.4    Perry, G.5    Smith, M.A.6    Lee, H.G.7
  • 152
    • 85005896338 scopus 로고    scopus 로고
    • Heavy metals in locus ceruleus and motor neurons in motor neuron disease
    • Pamphlett, R.; Kum Jew, S. Heavy metals in locus ceruleus and motor neurons in motor neuron disease. Acta Neuropathol. Commun. 2013, doi: 10.1186/2051-5960-1-81.
    • (2013) Acta Neuropathol. Commun.
    • Pamphlett, R.1    Kum Jew, S.2
  • 153
    • 78149277684 scopus 로고    scopus 로고
    • Abnormal iron metabolism in fibroblasts from a patient with the neurodegenerative disease hereditary ferritinopathy
    • Barbeito, A.G.; Levade, T.; Delisle, M.B.; Ghetti, B.; Vidal, R. Abnormal iron metabolism in fibroblasts from a patient with the neurodegenerative disease hereditary ferritinopathy. Mol. Neurodegener. 2010, doi: 10.1186/1750-1326-5-50.
    • (2010) Mol. Neurodegener.
    • Barbeito, A.G.1    Levade, T.2    Delisle, M.B.3    Ghetti, B.4    Vidal, R.5
  • 154
    • 59149084006 scopus 로고    scopus 로고
    • Ceruloplasmin in neurodegenerative diseases
    • Texel, S.J.; Xu, X.; Harris, Z.L. Ceruloplasmin in neurodegenerative diseases. Biochem. Soc. Trans. 2008, 36, 1277-1281.
    • (2008) Biochem. Soc. Trans. , vol.36 , pp. 1277-1281
    • Texel, S.J.1    Xu, X.2    Harris, Z.L.3
  • 155
    • 12244269061 scopus 로고    scopus 로고
    • A brief history of brain iron research
    • Koeppen, A.H. A brief history of brain iron research. J. Neurol. Sci. 2003, 207, 95-97.
    • (2003) J. Neurol. Sci. , vol.207 , pp. 95-97
    • Koeppen, A.H.1
  • 156
    • 0033491572 scopus 로고    scopus 로고
    • Changes associated with delay of mammary cancer by retinoid analogues in transgenic mice bearing c-neu oncogene
    • Rao, G.N.; Ney, E.; Herbert, R.A. Changes associated with delay of mammary cancer by retinoid analogues in transgenic mice bearing c-neu oncogene. Breast Cancer Res. Treat. 1999, 58, 241-254.
    • (1999) Breast Cancer Res. Treat. , vol.58 , pp. 241-254
    • Rao, G.N.1    Ney, E.2    Herbert, R.A.3
  • 159
    • 0025736680 scopus 로고
    • Iron in brain function and dysfunction with emphasis on Parkinson’s disease
    • Youdim, M.B.; Ben-Shachar, D.; Riederer, P. Iron in brain function and dysfunction with emphasis on Parkinson’s disease. Eur. Neurol. 1991, 31, 34-40.
    • (1991) Eur. Neurol. , vol.31 , pp. 34-40
    • Youdim, M.B.1    Ben-Shachar, D.2    Riederer, P.3
  • 161
    • 84879554419 scopus 로고    scopus 로고
    • Aluminum in the central nervous system (CNS): Toxicity in humans and animals, vaccine adjuvants, and autoimmunity
    • Shaw, C.A.; Tomljenovic, L. Aluminum in the central nervous system (CNS): Toxicity in humans and animals, vaccine adjuvants, and autoimmunity. Immunol. Res. 2013, 56, 304-316.
    • (2013) Immunol. Res. , vol.56 , pp. 304-316
    • Shaw, C.A.1    Tomljenovic, L.2
  • 163
    • 0031350095 scopus 로고    scopus 로고
    • Biological models for the study of aluminum neurotoxicity
    • Zatta, P. Biological models for the study of aluminum neurotoxicity. Acta Med. Romana 1997, 35, 592-600.
    • (1997) Acta Med. Romana , vol.35 , pp. 592-600
    • Zatta, P.1
  • 164
    • 33744940785 scopus 로고    scopus 로고
    • Amyloid beta and neuromelanin-Toxic or protective molecules? The cellular context makes the difference
    • Rao, K.S.; Hegde, M.L.; Anitha, S.; Musicco, M.; Zucca, F.A.; Turro, N.J.; Zecca, L. Amyloid beta and neuromelanin-Toxic or protective molecules? The cellular context makes the difference. Prog. Neurobiol. 2006, 78, 364-373.
    • (2006) Prog. Neurobiol. , vol.78 , pp. 364-373
    • Rao, K.S.1    Hegde, M.L.2    Anitha, S.3    Musicco, M.4    Zucca, F.A.5    Turro, N.J.6    Zecca, L.7
  • 166
    • 0034992436 scopus 로고    scopus 로고
    • Postnatal inorganic lead exposure decreases the number of spontaneously active midbrain dopamine neurons in the rat
    • Tavakoli-Nezhad, M.; Barron, A.J.; Pitts, D.K. Postnatal inorganic lead exposure decreases the number of spontaneously active midbrain dopamine neurons in the rat. Neurotoxicology 2001, 22, 259-269.
    • (2001) Neurotoxicology , vol.22 , pp. 259-269
    • Tavakoli-Nezhad, M.1    Barron, A.J.2    Pitts, D.K.3
  • 168
    • 38149024924 scopus 로고    scopus 로고
    • Alzheimer’s disease (AD)-like pathology in aged monkeys after infantile exposure to environmental metal lead (PB): Evidence for a developmental origin and environmental link for AD
    • Wu, J.; Basha, M.R.; Brock, B.; Cox, D.P.; Cardozo-Pelaez, F.; McPherson, C.A.; Harry, J.; Rice, D.C.; Maloney, B.; Chen, D.; et al. Alzheimer’s disease (AD)-like pathology in aged monkeys after infantile exposure to environmental metal lead (PB): Evidence for a developmental origin and environmental link for AD. J. Neurosci. 2008, 28, 3-9.
    • (2008) J. Neurosci. , vol.28 , pp. 3-9
    • Wu, J.1    Basha, M.R.2    Brock, B.3    Cox, D.P.4    Cardozo-Pelaez, F.5    McPherson, C.A.6    Harry, J.7    Rice, D.C.8    Maloney, B.9    Chen, D.10
  • 169
    • 78751611201 scopus 로고    scopus 로고
    • Deleterious effects in mice of fish-associated methylmercury contained in a diet mimicking the western populations’ average fish consumption
    • Bourdineaud, J.P.; Fujimura, M.; Laclau, M.; Sawada, M.; Yasutake, A. Deleterious effects in mice of fish-associated methylmercury contained in a diet mimicking the western populations’ average fish consumption. Environ. Int. 2011, 37, 303-313.
    • (2011) Environ. Int. , vol.37 , pp. 303-313
    • Bourdineaud, J.P.1    Fujimura, M.2    Laclau, M.3    Sawada, M.4    Yasutake, A.5
  • 170
    • 0029953552 scopus 로고    scopus 로고
    • Oxidative stress in neurotoxic effects of methylmercury poisoning
    • Yee, S.; Choi, B.H. Oxidative stress in neurotoxic effects of methylmercury poisoning. Neurotoxicology 1996, 17, 17-26.
    • (1996) Neurotoxicology , vol.17 , pp. 17-26
    • Yee, S.1    Choi, B.H.2
  • 171
    • 3042743587 scopus 로고    scopus 로고
    • First evidence for helical transitions in supercoiled DNA by amyloid beta peptide (1-42) and aluminum: A new insight in understanding Alzheimer’s disease
    • Hegde, M.L.; Anitha, S.; Latha, K.S.; Mustak, M.S.; Stein, R.; Ravid, R.; Rao, K.S. First evidence for helical transitions in supercoiled DNA by amyloid beta peptide (1-42) and aluminum: A new insight in understanding Alzheimer’s disease. J. Mol. Neurosci. 2004, 22, 19-31.
    • (2004) J. Mol. Neurosci. , vol.22 , pp. 19-31
    • Hegde, M.L.1    Anitha, S.2    Latha, K.S.3    Mustak, M.S.4    Stein, R.5    Ravid, R.6    Rao, K.S.7
  • 172
    • 33747682291 scopus 로고    scopus 로고
    • Trace elements in Alzheimer’s disease brain: A new hypothesis
    • Rao, K.S.J.; Rao, R.V.; Shanmugavelu, P.; Menon, R.B. Trace elements in Alzheimer’s disease brain: A new hypothesis. Alzheimers Rep. 1999, 2, 241-246.
    • (1999) Alzheimers Rep. , vol.2 , pp. 241-246
    • Rao, K.S.J.1    Rao, R.V.2    Shanmugavelu, P.3    Menon, R.B.4
  • 173
    • 15744361815 scopus 로고    scopus 로고
    • An algorithmic approach to understand trace elemental homeostasis in serum samples of parkinson disease
    • Pande, M.B.; Nagabhushan, P.; Hegde, M.L.; Rao, T.S.; Rao, K.S. An algorithmic approach to understand trace elemental homeostasis in serum samples of parkinson disease. Comput. Biol. Med. 2005, 35, 475-493.
    • (2005) Comput. Biol. Med. , vol.35 , pp. 475-493
    • Pande, M.B.1    Nagabhushan, P.2    Hegde, M.L.3    Rao, T.S.4    Rao, K.S.5
  • 174
    • 84899495020 scopus 로고    scopus 로고
    • Characterization of biometal profiles in neurological disorders
    • Pfaender, S.; Grabrucker, A.M. Characterization of biometal profiles in neurological disorders. Metallomics 2014, 6, 960-977.
    • (2014) Metallomics , vol.6 , pp. 960-977
    • Pfaender, S.1    Grabrucker, A.M.2
  • 175
    • 79955671212 scopus 로고    scopus 로고
    • Oxidative genome damage and its repair in neurodegenerative diseases: Function of transition metals as a double-edged sword
    • Hegde, M.L.; Hegde, P.M.; Rao, K.S.; Mitra, S. Oxidative genome damage and its repair in neurodegenerative diseases: Function of transition metals as a double-edged sword. J. Alzheimers Dis. 2011, 24, 183-198.
    • (2011) J. Alzheimers Dis. , vol.24 , pp. 183-198
    • Hegde, M.L.1    Hegde, P.M.2    Rao, K.S.3    Mitra, S.4
  • 176
    • 0021265803 scopus 로고
    • Analysis of metal-induced DNA lesions and DNA-repair replication in mammalian cells
    • Robison, S.H.; Cantoni, O.; Costa, M. Analysis of metal-induced DNA lesions and DNA-repair replication in mammalian cells. Mutat. Res. 1984, 131, 173-181.
    • (1984) Mutat. Res. , vol.131 , pp. 173-181
    • Robison, S.H.1    Cantoni, O.2    Costa, M.3
  • 178
    • 0033667376 scopus 로고    scopus 로고
    • Plasma protein thiol oxidation and carbonyl formation in chronic renal failure
    • Himmelfarb, J.; McMonagle, E.; McMenamin, E. Plasma protein thiol oxidation and carbonyl formation in chronic renal failure. Kidney Int. 2000, 58, 2571-2578.
    • (2000) Kidney Int. , vol.58 , pp. 2571-2578
    • Himmelfarb, J.1    McMonagle, E.2    McMenamin, E.3
  • 181
    • 34548614799 scopus 로고    scopus 로고
    • Defective DNA repair and neurodegenerative disease
    • Rass, U.; Ahel, I.; West, S.C. Defective DNA repair and neurodegenerative disease. Cell 2007, 130, 991-1004.
    • (2007) Cell , vol.130 , pp. 991-1004
    • Rass, U.1    Ahel, I.2    West, S.C.3
  • 182
  • 183
    • 84867379842 scopus 로고    scopus 로고
    • Nuclear and mitochondrial DNA repair in selected eukaryotic aging model systems
    • Gredilla, R.; Garm, C.; Stevnsner, T. Nuclear and mitochondrial DNA repair in selected eukaryotic aging model systems. Oxid. Med. Cell. Longev. 2012, doi: 10.1155/2012/282438.
    • (2012) Oxid. Med. Cell. Longev.
    • Gredilla, R.1    Garm, C.2    Stevnsner, T.3
  • 184
    • 0028099191 scopus 로고
    • Role of DNA repair inhibition in lead- and cadmium-induced genotoxicity: A review
    • Hartwig, A. Role of DNA repair inhibition in lead- and cadmium-induced genotoxicity: A review. Environ. Health Perspect. 1994, 102, 45-50.
    • (1994) Environ. Health Perspect. , vol.102 , pp. 45-50
    • Hartwig, A.1
  • 185
    • 20244382069 scopus 로고    scopus 로고
    • Occupational exposure to heavy metals: DNA damage induction and DNA repair inhibition prove co-exposures to cadmium, cobalt and lead as more dangerous than hitherto expected
    • Hengstler, J.G.; Bolm-Audorff, U.; Faldum, A.; Janssen, K.; Reifenrath, M.; Gotte, W.; Jung, D.; Mayer-Popken, O.; Fuchs, J.; Gebhard, S.; et al. Occupational exposure to heavy metals: DNA damage induction and DNA repair inhibition prove co-exposures to cadmium, cobalt and lead as more dangerous than hitherto expected. Carcinogenesis 2003, 24, 63-73.
    • (2003) Carcinogenesis , vol.24 , pp. 63-73
    • Hengstler, J.G.1    Bolm-Audorff, U.2    Faldum, A.3    Janssen, K.4    Reifenrath, M.5    Gotte, W.6    Jung, D.7    Mayer-Popken, O.8    Fuchs, J.9    Gebhard, S.10
  • 186
    • 33749568015 scopus 로고    scopus 로고
    • Magnesium, essential for base excision repair enzymes, inhibits substrate binding of N-methylpurine-DNA glycosylase
    • Adhikari, S.; Toretsky, J.A.; Yuan, L.; Roy, R. Magnesium, essential for base excision repair enzymes, inhibits substrate binding of N-methylpurine-DNA glycosylase. J. Biol. Chem. 2006, 281, 29525-29532.
    • (2006) J. Biol. Chem. , vol.281 , pp. 29525-29532
    • Adhikari, S.1    Toretsky, J.A.2    Yuan, L.3    Roy, R.4
  • 187
    • 33748788230 scopus 로고    scopus 로고
    • Metal inhibition of human n-methylpurine-DNA glycosylase activity in base excision repair
    • Wang, P.; Guliaev, A.B.; Hang, B. Metal inhibition of human n-methylpurine-DNA glycosylase activity in base excision repair. Toxicol. Lett. 2006, 166, 237-247.
    • (2006) Toxicol. Lett. , vol.166 , pp. 237-247
    • Wang, P.1    Guliaev, A.B.2    Hang, B.3
  • 188
    • 72949103910 scopus 로고    scopus 로고
    • Cadmium and copper inhibit both DNA repair activities of polynucleotide kinase
    • Whiteside, J.R.; Box, C.L.; McMillan, T.J.; Allinson, S.L. Cadmium and copper inhibit both DNA repair activities of polynucleotide kinase. DNA Repair 2010, 9, 83-89.
    • (2010) DNA Repair , vol.9 , pp. 83-89
    • Whiteside, J.R.1    Box, C.L.2    McMillan, T.J.3    Allinson, S.L.4
  • 190
    • 0141540494 scopus 로고    scopus 로고
    • Challenges and complexities of alpha-synuclein toxicity: New postulates in unfolding the mystery associated with Parkinson’s disease
    • Hegde, M.L.; Jagannatha Rao, K.S. Challenges and complexities of alpha-synuclein toxicity: New postulates in unfolding the mystery associated with Parkinson’s disease. Arch. Biochem. Biophys. 2003, 418, 169-178.
    • (2003) Arch. Biochem. Biophys. , vol.418 , pp. 169-178
    • Hegde, M.L.1    Jagannatha Rao, K.S.2
  • 191
    • 84897496599 scopus 로고    scopus 로고
    • Molecular characterization of neuroprotective activities of plant based products could revive their utilization and lead discovery of new drug candidates for brain diseases
    • Hegde, M.L. Molecular characterization of neuroprotective activities of plant based products could revive their utilization and lead discovery of new drug candidates for brain diseases. J. Pharm. Bioallied Sci. 2014, 6, 63-64.
    • (2014) J. Pharm. Bioallied Sci. , vol.6 , pp. 63-64
    • Hegde, M.L.1


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