메뉴 건너뛰기




Volumn 290, Issue 34, 2015, Pages 20734-20742

The AlkB family of Fe(II)/α-ketoglutarate-dependent dioxygenases: Repairing nucleic acid alkylation damage and beyond

Author keywords

[No Author keywords available]

Indexed keywords

ALKYLATION; DNA; ENZYMES; ESCHERICHIA COLI; MAMMALS; REPAIR; SUBSTRATES;

EID: 84939856406     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.R115.656462     Document Type: Short Survey
Times cited : (297)

References (97)
  • 1
    • 0017395439 scopus 로고
    • A new pathway for DNA repair in Escherichia coli
    • Samson, L., and Cairns, J. (1977) A new pathway for DNA repair in Escherichia coli. Nature 267, 281-283
    • (1977) Nature , vol.267 , pp. 281-283
    • Samson, L.1    Cairns, J.2
  • 2
    • 0035221419 scopus 로고    scopus 로고
    • The DNA-repair protein AlkB, EGL-9, and leprecan define new families of 2-oxoglutarate- and iron-dependent dioxygenases
    • RESEARCH0007
    • Aravind, L., and Koonin, E. V. (2001) The DNA-repair protein AlkB, EGL-9, and leprecan define new families of 2-oxoglutarate- and iron-dependent dioxygenases. Genome Biol. 2, RESEARCH0007
    • (2001) Genome Biol. , vol.2
    • Aravind, L.1    Koonin, E.V.2
  • 3
    • 0742305875 scopus 로고    scopus 로고
    • Repairing DNA-methylation damage
    • Sedgwick, B. (2004) Repairing DNA-methylation damage. Nat. Rev. Mol. Cell Biol. 5, 148-157
    • (2004) Nat. Rev. Mol. Cell Biol. , vol.5 , pp. 148-157
    • Sedgwick, B.1
  • 5
    • 84902182150 scopus 로고    scopus 로고
    • Mechanism and function of oxidative reversal of DNA and RNA methylation
    • Shen, L., Song, C.-X., He, C., and Zhang, Y. (2014) Mechanism and function of oxidative reversal of DNA and RNA methylation. Annu. Rev. Biochem. 83, 585-614
    • (2014) Annu. Rev. Biochem. , vol.83 , pp. 585-614
    • Shen, L.1    Song, C.-X.2    He, C.3    Zhang, Y.4
  • 6
    • 0027984433 scopus 로고
    • The Escherichia coli AlkB protein protects human cells against alkylation-induced toxicity
    • Chen, B. J., Carroll, P., and Samson, L. (1994) The Escherichia coli AlkB protein protects human cells against alkylation-induced toxicity. J. Bacteriol. 176, 6255-6261
    • (1994) J. Bacteriol. , vol.176 , pp. 6255-6261
    • Chen, B.J.1    Carroll, P.2    Samson, L.3
  • 7
    • 0037068446 scopus 로고    scopus 로고
    • Oxidative demethylation by Escherichia coli AlkB directly reverts DNA base damage
    • Trewick, S. C., Henshaw, T. F., Hausinger, R. P., Lindahl, T., and Sedgwick, B. (2002) Oxidative demethylation by Escherichia coli AlkB directly reverts DNA base damage. Nature 419, 174-178
    • (2002) Nature , vol.419 , pp. 174-178
    • Trewick, S.C.1    Henshaw, T.F.2    Hausinger, R.P.3    Lindahl, T.4    Sedgwick, B.5
  • 8
    • 0037068433 scopus 로고    scopus 로고
    • AlkB-mediated oxidative demethylation reverses DNA damage in Escherichia coli
    • Falnes, P. Ø., Johansen, R. F., and Seeberg, E. (2002) AlkB-mediated oxidative demethylation reverses DNA damage in Escherichia coli. Nature 419, 178-182
    • (2002) Nature , vol.419 , pp. 178-182
    • Falnes, P.Ø.1    Johansen, R.F.2    Seeberg, E.3
  • 11
  • 14
    • 75349109431 scopus 로고    scopus 로고
    • Bioinformatics and functional analysis define four distinct groups of AlkB DNA-dioxygenases in bacteria
    • van den Born, E., Bekkelund, A., Moen, M. N., Omelchenko, M. V., Klungland, A., and Falnes, P. Ø. (2009) Bioinformatics and functional analysis define four distinct groups of AlkB DNA-dioxygenases in bacteria. Nucleic Acids Res. 37, 7124-7136
    • (2009) Nucleic Acids Res. , vol.37 , pp. 7124-7136
    • Van Den Born, E.1    Bekkelund, A.2    Moen, M.N.3    Omelchenko, M.V.4    Klungland, A.5    Falnes, P.Ø.6
  • 16
    • 84896708800 scopus 로고    scopus 로고
    • FTO gene variant and risk of overweight and obesity among children and adolescents: A systematic review and meta-analysis
    • Liu, C., Mou, S., and Cai, Y. (2013) FTO gene variant and risk of overweight and obesity among children and adolescents: a systematic review and meta-analysis. PLoS One 8, e82133
    • (2013) PLoS One , vol.8
    • Liu, C.1    Mou, S.2    Cai, Y.3
  • 17
    • 34247173363 scopus 로고    scopus 로고
    • Repair of methyl lesions in DNA and RNA by oxidative demethylation
    • Falnes, P. Ø., Klungland, A., and Alseth, I. (2007) Repair of methyl lesions in DNA and RNA by oxidative demethylation. Neuroscience 145, 1222-1232
    • (2007) Neuroscience , vol.145 , pp. 1222-1232
    • Falnes, P.Ø.1    Klungland, A.2    Alseth, I.3
  • 18
    • 38649130998 scopus 로고    scopus 로고
    • The FTO gene, implicated in human obesity, is found only in vertebrates and marine algae
    • Robbens, S., Rouzé, P., Cock, J. M., Spring, J., Worden, A. Z., and Van de Peer, Y. (2008) The FTO gene, implicated in human obesity, is found only in vertebrates and marine algae. J. Mol. Evol. 66, 80-84
    • (2008) J. Mol. Evol. , vol.66 , pp. 80-84
    • Robbens, S.1    Rouzé, P.2    Cock, J.M.3    Spring, J.4    Worden, A.Z.5    Van De Peer, Y.6
  • 19
    • 84883275141 scopus 로고    scopus 로고
    • ABH2 couples regulation of ribosomal DNA transcription with DNA alkylation repair
    • Li, P., Gao, S., Wang, L., Yu, F., Li, J., Wang, C., Li, J., and Wong, J. (2013) ABH2 couples regulation of ribosomal DNA transcription with DNA alkylation repair. Cell Rep. 4, 817-829
    • (2013) Cell Rep. , vol.4 , pp. 817-829
    • Li, P.1    Gao, S.2    Wang, L.3    Yu, F.4    Li, J.5    Wang, C.6    Li, J.7    Wong, J.8
  • 20
    • 84897404290 scopus 로고    scopus 로고
    • Switching demethylation activities between AlkB family RNA/DNA demethylases through exchange of active-site residues
    • Zhu, C., and Yi, C. (2014) Switching demethylation activities between AlkB family RNA/DNA demethylases through exchange of active-site residues. Angew. Chem. Int. Ed. Engl. 53, 3659-3662
    • (2014) Angew. Chem. Int. Ed. Engl. , vol.53 , pp. 3659-3662
    • Zhu, C.1    Yi, C.2
  • 21
    • 77957905714 scopus 로고    scopus 로고
    • Mechanistic insight into the recognition of single-stranded and double-stranded DNA substrates by ABH2 and ABH3
    • Chen, B., Liu, H., Sun, X., and Yang, C.-G. (2010) Mechanistic insight into the recognition of single-stranded and double-stranded DNA substrates by ABH2 and ABH3. Mol. Biosyst. 6, 2143-2149
    • (2010) Mol. Biosyst. , vol.6 , pp. 2143-2149
    • Chen, B.1    Liu, H.2    Sun, X.3    Yang, C.-G.4
  • 22
    • 84855352358 scopus 로고    scopus 로고
    • 4-ethenocytosine by the human ALKBH2 dioxygenase is blocked by the AAG/MPG glycosylase
    • 4-ethenocytosine by the human ALKBH2 dioxygenase is blocked by the AAG/MPG glycosylase. DNA Repair (Amst.) 11, 46-52, 10.1016/j.dnarep.2011.10.004
    • (2012) DNA Repair (Amst.) , vol.11 , pp. 46-52
    • Fu, D.1    Samson, L.D.2
  • 23
    • 84862808452 scopus 로고    scopus 로고
    • Alkbh2 protects against lethality and mutation in primary mouse embryonic fibroblasts
    • Nay, S. L., Lee, D.-H., Bates, S. E., and O'Connor, T. R. (2012) Alkbh2 protects against lethality and mutation in primary mouse embryonic fibroblasts. DNA Repair (Amst.) 11, 502-510, 10.1016/j.dnarep.2012.02.005
    • (2012) DNA Repair (Amst.) , vol.11 , pp. 502-510
    • Nay, S.L.1    Lee, D.-H.2    Bates, S.E.3    O'Connor, T.R.4
  • 24
    • 68949136580 scopus 로고    scopus 로고
    • Pediatric brain tumors: Mutations of two dioxygenases (hABH2 and hABH3) that directly repair alkylation damage
    • Cetica, V., Genitori, L., Giunti, L., Sanzo, M., Bernini, G., Massimino, M., and Sardi, I. (2009) Pediatric brain tumors: mutations of two dioxygenases (hABH2 and hABH3) that directly repair alkylation damage. J. Neurooncol. 94, 195-201
    • (2009) J. Neurooncol. , vol.94 , pp. 195-201
    • Cetica, V.1    Genitori, L.2    Giunti, L.3    Sanzo, M.4    Bernini, G.5    Massimino, M.6    Sardi, I.7
  • 26
    • 80555127349 scopus 로고    scopus 로고
    • DNA unwinding by ASCC3 helicase is coupled to ALKBH3-dependent DNA alkylation repair and cancer cell proliferation
    • Dango, S., Mosammaparast, N., Sowa, M. E., Xiong, L.-J., Wu, F., Park, K., Rubin, M., Gygi, S., Harper, J. W., and Shi, Y. (2011) DNA unwinding by ASCC3 helicase is coupled to ALKBH3-dependent DNA alkylation repair and cancer cell proliferation. Mol. Cell 44, 373-384
    • (2011) Mol. Cell , vol.44 , pp. 373-384
    • Dango, S.1    Mosammaparast, N.2    Sowa, M.E.3    Xiong, L.-J.4    Wu, F.5    Park, K.6    Rubin, M.7    Gygi, S.8    Harper, J.W.9    Shi, Y.10
  • 32
    • 84878419555 scopus 로고    scopus 로고
    • A covalent protein-DNA 5ô-product adduct is generated following AP lyase activity of human ALKBH1 (AlkB homologue 1)
    • Müller, T. A., Andrzejak, M. M., and Hausinger, R. P. (2013) A covalent protein-DNA 5ô-product adduct is generated following AP lyase activity of human ALKBH1 (AlkB homologue 1). Biochem. J. 452, 509-518
    • (2013) Biochem. J. , vol.452 , pp. 509-518
    • Müller, T.A.1    Andrzejak, M.M.2    Hausinger, R.P.3
  • 33
    • 84879347620 scopus 로고    scopus 로고
    • ALKBH1 is dispensable for abasic site cleavage during base excision repair and class switch recombination
    • Müller, T. A., Yu, K., Hausinger, R. P., and Meek, K. (2013) ALKBH1 is dispensable for abasic site cleavage during base excision repair and class switch recombination. PLoS One 8, e67403
    • (2013) PLoS One , vol.8
    • Müller, T.A.1    Yu, K.2    Hausinger, R.P.3    Meek, K.4
  • 34
    • 84908590974 scopus 로고    scopus 로고
    • Homology modeling, molecular dynamics, and site-directed mutagenesis study of AlkB human homolog 1 (ALKBH1)
    • Silvestrov, P., Müller, T. A., Clark, K. N., Hausinger, R. P., and Cisneros, G. A. (2014) Homology modeling, molecular dynamics, and site-directed mutagenesis study of AlkB human homolog 1 (ALKBH1). J. Mol. Graph. Model. 54, 123-130
    • (2014) J. Mol. Graph. Model. , vol.54 , pp. 123-130
    • Silvestrov, P.1    Müller, T.A.2    Clark, K.N.3    Hausinger, R.P.4    Cisneros, G.A.5
  • 35
    • 84860255141 scopus 로고    scopus 로고
    • The Schizosaccharomyces pombe AlkB homolog Abh1 exhibits AP lyase activity but no demethylase activity
    • Korvald, H., Falnes, P. Ø., Laerdahl, J. K., Bjørås, M., and Alseth, I. (2012) The Schizosaccharomyces pombe AlkB homolog Abh1 exhibits AP lyase activity but no demethylase activity. DNA Repair (Amst.) 11, 453-462, 10.1016/j.dnarep.2012.01.014
    • (2012) DNA Repair (Amst.) , vol.11 , pp. 453-462
    • Korvald, H.1    Falnes, P.Ø.2    Laerdahl, J.K.3    Bjørås, M.4    Alseth, I.5
  • 40
    • 84938290567 scopus 로고    scopus 로고
    • 6-methyladenosine RNA mark in gene regulation and its implications on development and disease
    • 6-methyladenosine RNA mark in gene regulation and its implications on development and disease. Brief Funct. Genomics 14, 169-179
    • (2015) Brief Funct. Genomics , vol.14 , pp. 169-179
    • Chandola, U.1    Das, R.2    Panda, B.3
  • 48
    • 84899425559 scopus 로고    scopus 로고
    • Crystal structures of the human RNA demethylase Alkbh5 reveal basis for substrate recognition
    • Feng, C., Liu, Y., Wang, G., Deng, Z., Zhang, Q., Wu, W., Tong, Y., Cheng, C., and Chen, Z. (2014) Crystal structures of the human RNA demethylase Alkbh5 reveal basis for substrate recognition. J. Biol. Chem. 289, 11571-11583
    • (2014) J. Biol. Chem. , vol.289 , pp. 11571-11583
    • Feng, C.1    Liu, Y.2    Wang, G.3    Deng, Z.4    Zhang, Q.5    Wu, W.6    Tong, Y.7    Cheng, C.8    Chen, Z.9
  • 49
    • 54849381000 scopus 로고    scopus 로고
    • Oxidative demethylation of 3-methylthymine and 3-methyluracil in single-stranded DNA and RNA by mouse and human FTO
    • Jia, G., Yang, C.-G., Yang, S., Jian, X., Yi, C., Zhou, Z., and He, C. (2008) Oxidative demethylation of 3-methylthymine and 3-methyluracil in single-stranded DNA and RNA by mouse and human FTO. FEBS Lett. 582, 3313-3319
    • (2008) FEBS Lett. , vol.582 , pp. 3313-3319
    • Jia, G.1    Yang, C.-G.2    Yang, S.3    Jian, X.4    Yi, C.5    Zhou, Z.6    He, C.7
  • 52
    • 78449233126 scopus 로고    scopus 로고
    • The AlkB domain of mammalian ABH8 catalyzes hydroxylation of 5-methoxycarbonylmethyluridine at the wobble position of tRNA
    • Fu, Y., Dai, Q., Zhang, W., Ren, J., Pan, T., and He, C. (2010) The AlkB domain of mammalian ABH8 catalyzes hydroxylation of 5-methoxycarbonylmethyluridine at the wobble position of tRNA. Angew. Chem. Int. Ed. Engl. 49, 8885-8888
    • (2010) Angew. Chem. Int. Ed. Engl. , vol.49 , pp. 8885-8888
    • Fu, Y.1    Dai, Q.2    Zhang, W.3    Ren, J.4    Pan, T.5    He, C.6
  • 53
    • 84855835084 scopus 로고    scopus 로고
    • Crystal structure and RNA binding properties of the RNA recognition motif (RRM) and AlkB domains in human AlkB homolog 8 (ABH8), an enzyme catalyzing tRNA hypermodification
    • Pastore, C., Topalidou, I., Forouhar, F., Yan, A. C., Levy, M., and Hunt, J. F. (2012) Crystal structure and RNA binding properties of the RNA recognition motif (RRM) and AlkB domains in human AlkB homolog 8 (ABH8), an enzyme catalyzing tRNA hypermodification. J. Biol. Chem. 287, 2130-2143
    • (2012) J. Biol. Chem. , vol.287 , pp. 2130-2143
    • Pastore, C.1    Topalidou, I.2    Forouhar, F.3    Yan, A.C.4    Levy, M.5    Hunt, J.F.6
  • 56
    • 79952132872 scopus 로고    scopus 로고
    • Spectroscopic and magnetic studies of wild-type and mutant forms of the Fe(II)- and 2-oxoglutarate-dependent decarboxylase ALKBH4
    • Bjørnstad, L. G., Zoppellaro, G., Tomter, A. B., Falnes, P. Ø., and Andersson, K. K. (2011) Spectroscopic and magnetic studies of wild-type and mutant forms of the Fe(II)- and 2-oxoglutarate-dependent decarboxylase ALKBH4. Biochem. J. 434, 391-398
    • (2011) Biochem. J. , vol.434 , pp. 391-398
    • Bjørnstad, L.G.1    Zoppellaro, G.2    Tomter, A.B.3    Falnes, P.Ø.4    Andersson, K.K.5
  • 58
    • 84877948815 scopus 로고    scopus 로고
    • Human ALKBH7 is required for alkylation and oxidation-induced programmed necrosis
    • Fu, D., Jordan, J. J., and Samson, L. D. (2013) Human ALKBH7 is required for alkylation and oxidation-induced programmed necrosis. Genes Dev. 27, 1089-1100
    • (2013) Genes Dev. , vol.27 , pp. 1089-1100
    • Fu, D.1    Jordan, J.J.2    Samson, L.D.3
  • 59
    • 84907482246 scopus 로고    scopus 로고
    • The atomic resolution structure of human AlkB homolog 7 (ALKBH7), a key protein for programmed necrosis and fat metabolism
    • Wang, G., He, Q., Feng, C., Liu, Y., Deng, Z., Qi, X., Wu, W., Mei, P., and Chen, Z. (2014) The atomic resolution structure of human AlkB homolog 7 (ALKBH7), a key protein for programmed necrosis and fat metabolism. J. Biol. Chem. 289, 27924-27936
    • (2014) J. Biol. Chem. , vol.289 , pp. 27924-27936
    • Wang, G.1    He, Q.2    Feng, C.3    Liu, Y.4    Deng, Z.5    Qi, X.6    Wu, W.7    Mei, P.8    Chen, Z.9
  • 60
    • 84923132296 scopus 로고    scopus 로고
    • DNA demethylation, Tet proteins and 5-hydroxymethylcytosine in epigenetic reprogramming: An emerging complex story
    • Hill, P. W. S., Amouroux, R., and Hajkova, P. (2014) DNA demethylation, Tet proteins and 5-hydroxymethylcytosine in epigenetic reprogramming: an emerging complex story. Genomics 104, 324-333
    • (2014) Genomics , vol.104 , pp. 324-333
    • Hill, P.W.S.1    Amouroux, R.2    Hajkova, P.3
  • 61
    • 32844455577 scopus 로고    scopus 로고
    • Crystal structures of catalytic complexes of the oxidative DNA/RNA repair enzyme AlkB
    • Yu, B., Edstrom, W. C., Benach, J., Hamuro, Y., Weber, P. C., Gibney, B. R., and Hunt, J. F. (2006) Crystal structures of catalytic complexes of the oxidative DNA/RNA repair enzyme AlkB. Nature 439, 879-884
    • (2006) Nature , vol.439 , pp. 879-884
    • Yu, B.1    Edstrom, W.C.2    Benach, J.3    Hamuro, Y.4    Weber, P.C.5    Gibney, B.R.6    Hunt, J.F.7
  • 62
    • 42549128712 scopus 로고    scopus 로고
    • Crystal structures of DNA/RNA repair enzymes AlkB and ABH2 bound to dsDNA
    • Yang, C.-G., Yi, C., Duguid, E. M., Sullivan, C. T., Jian, X., Rice, P. A., and He, C. (2008) Crystal structures of DNA/RNA repair enzymes AlkB and ABH2 bound to dsDNA. Nature 452, 961-965
    • (2008) Nature , vol.452 , pp. 961-965
    • Yang, C.-G.1    Yi, C.2    Duguid, E.M.3    Sullivan, C.T.4    Jian, X.5    Rice, P.A.6    He, C.7
  • 63
    • 70149118360 scopus 로고    scopus 로고
    • Enzymological and structural studies of the mechanism of promiscuous substrate recognition by the oxidative DNA repair enzyme AlkB
    • Yu, B., and Hunt, J. F. (2009) Enzymological and structural studies of the mechanism of promiscuous substrate recognition by the oxidative DNA repair enzyme AlkB. Proc. Natl. Acad. Sci. U.S.A. 106, 14315-14320
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 14315-14320
    • Yu, B.1    Hunt, J.F.2
  • 64
    • 78149460370 scopus 로고    scopus 로고
    • Iron-catalysed oxidation intermediates captured in a DNA repair dioxygenase
    • Yi, C., Jia, G., Hou, G., Dai, Q., Zhang, W., Zheng, G., Jian, X., Yang, C.-G., Cui, Q., and He, C. (2010) Iron-catalysed oxidation intermediates captured in a DNA repair dioxygenase. Nature 468, 330-333
    • (2010) Nature , vol.468 , pp. 330-333
    • Yi, C.1    Jia, G.2    Hou, G.3    Dai, Q.4    Zhang, W.5    Zheng, G.6    Jian, X.7    Yang, C.-G.8    Cui, Q.9    He, C.10
  • 66
    • 77951623073 scopus 로고    scopus 로고
    • Crystal structure of the FTO protein reveals basis for its substrate specificity
    • Han, Z., Niu, T., Chang, J., Lei, X., Zhao, M., Wang, Q., Cheng, W., Wang, J., Feng, Y., and Chai, J. (2010) Crystal structure of the FTO protein reveals basis for its substrate specificity. Nature 464, 1205-1209
    • (2010) Nature , vol.464 , pp. 1205-1209
    • Han, Z.1    Niu, T.2    Chang, J.3    Lei, X.4    Zhao, M.5    Wang, Q.6    Cheng, W.7    Wang, J.8    Feng, Y.9    Chai, J.10
  • 69
    • 0032760945 scopus 로고    scopus 로고
    • Structural and mechanistic studies on 2-oxoglutarate-dependent oxygenases and related enzymes
    • Schofield, C. J., and Zhang, Z. (1999) Structural and mechanistic studies on 2-oxoglutarate-dependent oxygenases and related enzymes. Curr. Opin. Struct. Biol. 9, 722-731
    • (1999) Curr. Opin. Struct. Biol. , vol.9 , pp. 722-731
    • Schofield, C.J.1    Zhang, Z.2
  • 70
    • 0033554854 scopus 로고    scopus 로고
    • Herbicide-degrading α-keto acid-dependent enzyme TfdA: Metal coordination environment and mechanistic insights
    • Hegg, E. L., Whiting, A. K., Saari, R. E., McCracken, J., Hausinger, R. P., and Que, L. (1999) Herbicide-degrading α-keto acid-dependent enzyme TfdA: metal coordination environment and mechanistic insights. Biochemistry 38, 16714-16726
    • (1999) Biochemistry , vol.38 , pp. 16714-16726
    • Hegg, E.L.1    Whiting, A.K.2    Saari, R.E.3    McCracken, J.4    Hausinger, R.P.5    Que, L.6
  • 73
    • 65349114389 scopus 로고    scopus 로고
    • A DFT study of nucleobase dealkylation by the DNA repair enzyme AlkB
    • Liu, H., Llano, J., and Gauld, J. W. (2009) A DFT study of nucleobase dealkylation by the DNA repair enzyme AlkB. J. Phys. Chem. B. 113, 4887-4898
    • (2009) J. Phys. Chem. B. , vol.113 , pp. 4887-4898
    • Liu, H.1    Llano, J.2    Gauld, J.W.3
  • 74
    • 77956625845 scopus 로고    scopus 로고
    • DFT study of a model system for the dealkylation step catalyzed by AlkB
    • Cisneros, G. A. (2010) DFT study of a model system for the dealkylation step catalyzed by AlkB. Interdiscip. Sci. 2, 70-77
    • (2010) Interdiscip. Sci. , vol.2 , pp. 70-77
    • Cisneros, G.A.1
  • 75
    • 84909592198 scopus 로고    scopus 로고
    • Alternative pathway for the reaction catalyzed by DNA dealkylase AlkB from ab initio QM/MM calculations
    • Fang, D., and Cisneros, G. A. (2014) Alternative pathway for the reaction catalyzed by DNA dealkylase AlkB from ab initio QM/MM calculations. J. Chem. Theory Comput. 10, 5136-5148
    • (2014) J. Chem. Theory Comput. , vol.10 , pp. 5136-5148
    • Fang, D.1    Cisneros, G.A.2
  • 76
    • 84907487616 scopus 로고    scopus 로고
    • Theory uncovers an unusual mechanism of DNA repair of a lesioned adenine by AlkB enzymes
    • Wang, B., Usharani, D., Li, C., and Shaik, S. (2014) Theory uncovers an unusual mechanism of DNA repair of a lesioned adenine by AlkB enzymes. J. Am. Chem. Soc. 136, 13895-13901
    • (2014) J. Am. Chem. Soc. , vol.136 , pp. 13895-13901
    • Wang, B.1    Usharani, D.2    Li, C.3    Shaik, S.4
  • 77
    • 4644282150 scopus 로고    scopus 로고
    • Mutagenesis, genotoxicity, and repair of 1-methyladenine, 3-alkylcytosines, 1-methylguanine, and 3-methylthymine in alkB Escherichia coli
    • Delaney, J. C., and Essigmann, J. M. (2004) Mutagenesis, genotoxicity, and repair of 1-methyladenine, 3-alkylcytosines, 1-methylguanine, and 3-methylthymine in alkB Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 101, 14051-14056
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 14051-14056
    • Delaney, J.C.1    Essigmann, J.M.2
  • 78
    • 4644343184 scopus 로고    scopus 로고
    • Demethylation of 3-methylthymine in DNA by bacterial and human DNA dioxygenases
    • Koivisto, P., Robins, P., Lindahl, T., and Sedgwick, B. (2004) Demethylation of 3-methylthymine in DNA by bacterial and human DNA dioxygenases. J. Biol. Chem. 279, 40470-40474
    • (2004) J. Biol. Chem. , vol.279 , pp. 40470-40474
    • Koivisto, P.1    Robins, P.2    Lindahl, T.3    Sedgwick, B.4
  • 79
    • 84861649618 scopus 로고    scopus 로고
    • Repair of DNA alkylation damage by the Escherichia coli adaptive response protein AlkB as studied by ESI-TOF mass spectrometry
    • Li, D., Delaney, J. C., Page, C. M., Chen, A. S., Wong, C., Drennan, C. L., and Essigmann, J. M. (2010) Repair of DNA alkylation damage by the Escherichia coli adaptive response protein AlkB as studied by ESI-TOF mass spectrometry. J. Nucleic Acids. 2010, 369434
    • (2010) J. Nucleic Acids. , vol.2010 , pp. 369434
    • Li, D.1    Delaney, J.C.2    Page, C.M.3    Chen, A.S.4    Wong, C.5    Drennan, C.L.6    Essigmann, J.M.7
  • 82
    • 0029163078 scopus 로고
    • Structure and function of DNA methyltransferases
    • Cheng, X. (1995) Structure and function of DNA methyltransferases. Annu. Rev. Biophys. Biomol. Struct. 24, 293-318
    • (1995) Annu. Rev. Biophys. Biomol. Struct. , vol.24 , pp. 293-318
    • Cheng, X.1
  • 89
    • 84918594407 scopus 로고    scopus 로고
    • Mechanism of repair of acrolein- and malondialdehyde-derived exocyclic guanine adducts by the α-ketoglutarate/Fe(II) dioxygenase AlkB
    • Singh, V., Fedeles, B. I., Li, D., Delaney, J. C., Kozekov, I. D., Kozekova, A., Marnett, L. J., Rizzo, C. J., and Essigmann, J. M. (2014) Mechanism of repair of acrolein- and malondialdehyde-derived exocyclic guanine adducts by the α-ketoglutarate/Fe(II) dioxygenase AlkB. Chem. Res. Toxicol. 27, 1619-1631
    • (2014) Chem. Res. Toxicol. , vol.27 , pp. 1619-1631
    • Singh, V.1    Fedeles, B.I.2    Li, D.3    Delaney, J.C.4    Kozekov, I.D.5    Kozekova, A.6    Marnett, L.J.7    Rizzo, C.J.8    Essigmann, J.M.9
  • 90
    • 33745198667 scopus 로고    scopus 로고
    • Assays for determining lesion bypass efficiency and mutagenicity of site-specific DNA lesions in vivo
    • Delaney, J. C., and Essigmann, J. M. (2006) Assays for determining lesion bypass efficiency and mutagenicity of site-specific DNA lesions in vivo. Methods Enzymol. 408, 1-15
    • (2006) Methods Enzymol. , vol.408 , pp. 1-15
    • Delaney, J.C.1    Essigmann, J.M.2
  • 92
    • 79951662917 scopus 로고    scopus 로고
    • Frequent down-regulation of hABH2 in gastric cancer and its involvement in growth of cancer cells
    • Gao, W., Li, L., Xu, P., Fang, J., Xiao, S., and Chen, S. (2011) Frequent down-regulation of hABH2 in gastric cancer and its involvement in growth of cancer cells. J. Gastroenterol. Hepatol. 26, 577-584
    • (2011) J. Gastroenterol. Hepatol. , vol.26 , pp. 577-584
    • Gao, W.1    Li, L.2    Xu, P.3    Fang, J.4    Xiao, S.5    Chen, S.6
  • 93
    • 52049125943 scopus 로고    scopus 로고
    • Advances in chemical carcinogenesis: A historical review and prospective
    • Loeb, L. A., and Harris, C. C. (2008) Advances in chemical carcinogenesis: a historical review and prospective. Cancer Res. 68, 6863-6872
    • (2008) Cancer Res. , vol.68 , pp. 6863-6872
    • Loeb, L.A.1    Harris, C.C.2
  • 94
    • 74049108712 scopus 로고    scopus 로고
    • Chemical biology of mutagenesis and DNA repair: Cellular responses to DNA alkylation
    • Shrivastav, N., Li, D., and Essigmann, J. M. (2010) Chemical biology of mutagenesis and DNA repair: cellular responses to DNA alkylation. Carcinogenesis. 31, 59-70
    • (2010) Carcinogenesis. , vol.31 , pp. 59-70
    • Shrivastav, N.1    Li, D.2    Essigmann, J.M.3
  • 95
    • 27544467955 scopus 로고    scopus 로고
    • Kinetic and spectroscopic investigation of CoII, NiII, and N-oxalylglycine inhibition of the FeII/α-ketoglutarate dioxygenase
    • Kalliri, E., Grzyska, P. K., and Hausinger, R. P. (2005) Kinetic and spectroscopic investigation of CoII, NiII, and N-oxalylglycine inhibition of the FeII/α-ketoglutarate dioxygenase, TauD. Biochem. Biophys. Res. Commun. 338, 191-197
    • (2005) TauD. Biochem. Biophys. Res. Commun. , vol.338 , pp. 191-197
    • Kalliri, E.1    Grzyska, P.K.2    Hausinger, R.P.3
  • 97
    • 84859787197 scopus 로고    scopus 로고
    • Mechanistic studies on the application of DNA aptamers as inhibitors of 2-oxoglutarate-dependent oxygenases
    • Krylova, S. M., Koshkin, V., Bagg, E., Schofield, C. J., and Krylov, S. N. (2012) Mechanistic studies on the application of DNA aptamers as inhibitors of 2-oxoglutarate-dependent oxygenases. J. Med. Chem. 55, 3546-3552
    • (2012) J. Med. Chem. , vol.55 , pp. 3546-3552
    • Krylova, S.M.1    Koshkin, V.2    Bagg, E.3    Schofield, C.J.4    Krylov, S.N.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.