DNA Repair by Reversal of DNA Damage
Open accessAbstract
Endogenous and exogenous factors constantly challenge cellular DNA, generating cytotoxic and/or mutagenic DNA adducts. As a result, organisms have evolved different mechanisms to defend against the deleterious effects of DNA damage. Among these diverse repair pathways, direct DNA-repair systems provide cells with simple yet efficient solutions to reverse covalent DNA adducts. In this review, we focus on recent advances in the field of direct DNA repair, namely, photolyase-, alkyltransferase-, and dioxygenase-mediated repair processes. We present specific examples to describe new findings of known enzymes and appealing discoveries of new proteins. At the end of this article, we also briefly discuss the influence of direct DNA repair on other fields of biology and its implication on the discovery of new biology.
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Two classes of CPD photolyases with different electron transfer pathways and different mechanistic properties exist.
“Two classes of CPD photolyases with different pathway of electron transfer, and different mechanistic properties exist.”
From Focus on UV-Induced DNA Damage and Repair—Disease Relevance and Protective Strategies (2020) · cites this paper as [77]
Placental mammals, including humans, lack photolyase activity, and repair of UV-induced damage is probably replaced by NER.
“Placental mammals (including humans) lack photolyase activity, and the repair of UV-induced damage is probably replaced by the activity of NER.”
From Focus on UV-Induced DNA Damage and Repair—Disease Relevance and Protective Strategies (2020) · cites this paper as [77]
CPDs and 6-4PPs are the two main types of photolesions repaired by photolyases.
“CPDs and 6-4PPs are the two main types of photolesions repaired by photolyases.”
From Focus on UV-Induced DNA Damage and Repair—Disease Relevance and Protective Strategies (2020) · cites this paper as [77]
Absorption of light by the class-specific chromophore leads to its excitation.
“The absorption of light by the class specific chromophore (either 5,10-methyl tetrahydrofolate (MTHF) or 8-hydroxy-5-deazaflavin (8-HDF)) leads to its excitation.”
From Focus on UV-Induced DNA Damage and Repair—Disease Relevance and Protective Strategies (2020) · cites this paper as [77]
Energy obtained through excitation of the chromophore is transferred to FADH, and photoexcited FADH provides energy for dimer-splitting.
“The energy obtained through excitation of chormophore is then transferred to important cofactor—reduced flavin adenine dinucleotide (FADH). Consequently, photoexcitated FADH provides energy for the dimer-splitting.”
From Focus on UV-Induced DNA Damage and Repair—Disease Relevance and Protective Strategies (2020) · cites this paper as [77]
There are three major types of direct DNA repair: reversal of UV-induced photolesions by photolyases, repair of O-alkylated DNA by O6-alkylguanine-DNA alkyltransferases, and repair of N-alkylated bases by AlkB family dioxygenase enzymes.
“There are three major types of direct DNA repair: (a) reversal of UV-induced photolesions carried by photolyases, (b) repair of O-alkylated DNA by O6-alkylguanine-DNA alkyltransferases, and (c) repair of N-alkylated bases by AlkB family dioxygenase enzymes [77].”
From Focus on UV-Induced DNA Damage and Repair—Disease Relevance and Protective Strategies (2020) · cites this paper as [77]
Subsequent back electron transfer regenerates FADH, ensuring the proper FAD form for the next reaction.
“Subsequent back electron transfer regenerates the FADH, ensuring the proper FAD form for the next reaction.”
From Focus on UV-Induced DNA Damage and Repair—Disease Relevance and Protective Strategies (2020) · cites this paper as [77]
A thymine pair is flipped back into the DNA duplex, and the hydrogen bond between thymine and adenine is formed.
“A thymine pair is consequently flipped back into the DNA duplex and the hydrogen bond between thymine and adenine is formed.”
From Focus on UV-Induced DNA Damage and Repair—Disease Relevance and Protective Strategies (2020) · cites this paper as [77]
In the absence of blue light, photolyases bind to CPDs and 6-4PPs.
“In the absence of blue light photolyases bind to CPDs, and 6-4PPs.”
From Focus on UV-Induced DNA Damage and Repair—Disease Relevance and Protective Strategies (2020) · cites this paper as [77]
In many organisms, photolyases are the key enzymes that remove photo-damage.
“However, in many organisms, photolyases are the key enzymes that remove photo-damage.”
From Focus on UV-Induced DNA Damage and Repair—Disease Relevance and Protective Strategies (2020) · cites this paper as [77]
Repair of 6-4PPs is different than CPDs and requires (6-4PP) photolyase and involves oxetane intermediate formation.
“The repair of 6-4PPs is different than CPDs and requires (6-4PPs) photolyase and involves oxetane intermediate formation.”
From Focus on UV-Induced DNA Damage and Repair—Disease Relevance and Protective Strategies (2020) · cites this paper as [77]
Conflicting results exist on oxetane formation during repair.
“However, conflicting results exist on the oxetane formation during repair.”
From Focus on UV-Induced DNA Damage and Repair—Disease Relevance and Protective Strategies (2020) · cites this paper as [77]
Covalent links between adjacent pyrimidines in dimers are broken, and proper DNA structure is restored.
“Again, the covalent links between adjacent pyrimidines in the dimers are broken, and the proper structure of DNA molecule is restored [77,78,79,80,81].”
From Focus on UV-Induced DNA Damage and Repair—Disease Relevance and Protective Strategies (2020) · cites this paper as [77]
Cites
Conversion of 5-Methylcytosine to 5-Hydroxymethylcytosine in Mammalian DNA by MLL Partner TET1
Tahiliani, M., Koh, K. P., Shen, Y., Pastor, W. A., Bandukwala, H., Brudno, Y., Agarwal, S., Iyer, L. M., Liu, D. R., Aravind, L., et al. (2009) · Science · doi:10.1126/science.1170116 · Cited by 5,836 · see citing works
Friedberg, E. C., Walker, G. C., Siede, W., Wood, R. D., Schultz, R. A., & Ellenberger, T. (2005) · doi:10.1128/9781555816704 · Cited by 5,683 · see citing works
Frayling, T. M., Timpson, N. J., Weedon, M. N., Zeggini, E., Freathy, R. M., Lindgren, C. M., Perry, J. R. B., Elliott, K. S., Lango, H., Rayner, N. W., et al. (2007) · Science · doi:10.1126/science.1141634 · Cited by 4,531 · see citing works
N6-Methyladenosine in nuclear RNA is a major substrate of the obesity-associated FTO
Jia, G., Fu, Y., Zhao, X., Dai, Q., Zheng, G., Yang, Y., Yi, C., Lindahl, T., Pan, T., Yang, Y.-G., et al. (2011) · Nature Chemical Biology · doi:10.1038/nchembio.687 · Cited by 4,106 · see citing works
Self-citationTet proteins can convert 5-methylcytosine to 5-formylcytosine and 5-carboxylcytosine
Ito, S., Shen, L., Dai, Q., Wu, S. C., Collins, L. B., Swenberg, J. A., He, C., & Zhang, Y. (2011) · Science · doi:10.1126/science.1210597 · Cited by 3,451 · see citing works
Self-citationTet-Mediated Formation of 5-Carboxylcytosine and Its Excision by TDG in Mammalian DNA
He, Y., Li, B.-Z., Li, Z., Liu, P., Wang, Y., Tang, Q., Ding, J., Jia, Y., Chen, Z., Li, L., et al. (2011) · Science · doi:10.1126/science.1210944 · Cited by 2,776 · see citing works
Self-citationIto, S., D’Alessio, A. C., Taranova, O., Hong, K., Sowers, L. C., & Zhang, Y. (2010) · Nature · doi:10.1038/nature09303 · Cited by 2,542 · see citing works
Histone demethylation by a family of JmjC domain-containing proteins
Tsukada, Y.-I., Fang, J., Erdjument‐Bromage, H., Warren, M., Borchers, C. H., Tempst, P., & Zhang, Y. (2005) · Nature · doi:10.1038/nature04433 · Cited by 2,171 · see citing works
Scuteri, A., Sanna, S., Chen, W.-M., Uda, M., Albai, G., Strait, J., Najjar, S., Nagaraja, R., Orrú, M., Usala, G., et al. (2007) · PLoS Genetics · doi:10.1371/journal.pgen.0030115 · Cited by 1,724 · see citing works
Variation in FTO contributes to childhood obesity and severe adult obesity
Christian Dina, C., Meyre, D., Gallina, S., Durand, E., Körner, A., Jacobson, P., Carlsson, L. M. S., Kieß, W., Vatin, V., Lecœur, C., et al. (2007) · Nature Genetics · doi:10.1038/ng2048 · Cited by 1,620 · see citing works
The Obesity-Associated FTO Gene Encodes a 2-Oxoglutarate-Dependent Nucleic Acid Demethylase
Gerken, T., Girard, C. A. J., Tung, Y. L., Webby, C. J., Saudek, V., Hewitson, K. S., Yeo, G. S. H., McDonough, M. A., Cunliffe, S. L., McNeill, L. A., et al. (2007) · Science · doi:10.1126/science.1151710 · Cited by 1,519 · see citing works
Huang, H., Chopra, R., Verdine, G. L., & Harrison, S. C. (1998) · Science · doi:10.1126/science.282.5394.1669 · Cited by 1,420 · see citing works
Balancing repair and tolerance of DNA damage caused by alkylating agents
Fu, D., Calvo, J. A., & Samson, L. D. (2012) · Nature reviews. Cancer · doi:10.1038/nrc3185 · Cited by 946 · see citing works
Inactivation of the Fto gene protects from obesity
Fischer, J., Koch, L., Emmerling, C., Vierkotten, J., Peters, T., Brüning, J. C., & Rüther, U. (2009) · Nature · doi:10.1038/nature07848 · Cited by 943 · see citing works
Thymine DNA Glycosylase Can Rapidly Excise 5-Formylcytosine and 5-Carboxylcytosine
Maiti, A., & Drohat, A. C. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.c111.284620 · Cited by 825 · see citing works
Oxidative demethylation by Escherichia coli AlkB directly reverts DNA base damage
Trewick, S. C., Henshaw, T. F., Hausinger, R. P., Lindahl, T. L., & Sedgwick, B. (2002) · Nature · doi:10.1038/nature00908 · Cited by 762 · see citing works
Mechanisms and functions of Tet protein-mediated 5-methylcytosine oxidationPreprint
Wu, H., & Zhang, Y. (2011) · Genes & Development · doi:10.17615/800j-yk16 · Cited by 665 · see citing works
REGULATION AND EXPRESSION OF THE ADAPTIVE RESPONSE TO ALKYLATING AGENTS
Lindahl, T. L., Sedgwick, B., Sekiguchi, M., & Nakabeppu, Y. (1988) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.57.070188.001025 · Cited by 650 · see citing works
Alkylation damage in DNA and RNA—repair mechanisms and medical significance
Drabløs, F., Feyzi, E., Aas, P. A., Vågbø, C. B., Kavli, B., Bratlie, M. S., Peña-Dı́az, J., Otterlei, M., Slupphaug, G., & Krokan, H. E. (2004) · DNA repair · doi:10.1016/j.dnarep.2004.05.004 · Cited by 645 · see citing works
Human and bacterial oxidative demethylases repair alkylation damage in both RNA and DNA
Aas, P. A., Otterlei, M., Falnes, P. Ø., Vågbø, C. B., Skorpen, F., Akbari, M., Sundheim, O., Bjørås, M., Slupphaug, G., Seeberg, E., et al. (2003) · Nature · doi:10.1038/nature01363 · Cited by 638 · see citing works
AlkB-mediated oxidative demethylation reverses DNA damage in Escherichia coli
Falnes, P. Ø., Johansen, R., & Seeberg, E. C. (2002) · Nature · doi:10.1038/nature01048 · Cited by 617 · see citing works
Grand Challenge Commentary: RNA epigenetics?
He, C. (2010) · Nature Chemical Biology · doi:10.1038/nchembio.482 · Cited by 442 · see citing works
Self-citationCrystal 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., & Chai, J. (2010) · Nature · doi:10.1038/nature08921 · Cited by 426 · see citing works
Jia, G., Yang, C., Yang, S., Jian, X., Yi, C., Zhou, Z., & He, C. (2008) · FEBS Letters · doi:10.1016/j.febslet.2008.08.019 · Cited by 424 · see citing works
Self-citationReversal of DNA alkylation damage by two human dioxygenases
Duncan, T., Trewick, S. C., Koivisto, P., Bates, P. A., Lindahl, T. L., & Sedgwick, B. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.262589799 · Cited by 414 · see citing works
Boissel, S., Reish, O., Proulx, K., Kawagoe-Takaki, H., Sedgwick, B., Yeo, G. S. H., Meyre, D., Golzio, C., Molinari, F., Kadhom, N., et al. (2009) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2009.06.002 · Cited by 393 · see citing works
Repairing DNA-methylation damage
Sedgwick, B. (2004) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1312 · Cited by 387 · see citing works
Identification of a New Cryptochrome Class
Brudler, R., Hitomi, K., Daiyasu, H., Toh, H., Kucho, K., Ishiura, M., Kanehisa, M. I., Roberts, V. A., Todo, T., Tainer, J. A., et al. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00008-x · Cited by 322 · see citing works
Quinn, J. A., Jiang, X. “., Reardon, D. A., Desjardins, A., Vredenburgh, J. J., Rich, J. N., Gururangan, S., Friedman, A. H., Bigner, D. D., Sampson, J. H., et al. (2009) · Journal of Clinical Oncology · doi:10.1200/jco.2008.18.8417 · Cited by 314 · see citing works
Thymine DNA glycosylase specifically recognizes 5-carboxylcytosine-modified DNA
Zhang, L., Lu, X., Lu, J., Liang, H., Dai, Q., Xu, G., Luo, C., Jiang, H., & He, C. (2012) · Nature Chemical Biology · doi:10.1038/nchembio.914 · Cited by 299 · see citing works
Self-citationA cryptochrome/photolyase class of enzymes with single-stranded DNA-specific photolyase activity
Selby, C. P., & Sancar, A. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0607993103 · Cited by 296 · see citing works
DNA binding and nucleotide flipping by the human DNA repair protein AGT
Daniels, D. S., Woo, T. T., Luu, K. X., Noll, D. M., Clarke, N. D., Pegg, A. E., & Tainer, J. A. (2004) · Nature Structural & Molecular Biology · doi:10.1038/nsmb791 · Cited by 294 · see citing works
Chemical biology of mutagenesis and DNA repair: cellular responses to DNA alkylation
Shrivastav, N., Li, D., & Essigmann, J. M. (2009) · Carcinogenesis · doi:10.1093/carcin/bgp262 · Cited by 294 · see citing works
Crystal structures of DNA/RNA repair enzymes AlkB and ABH2 bound to dsDNA
Yang, C., Yi, C., Duguid, E. M., Sullivan, C. T., Jian, X., Rice, P. A., & He, C. (2008) · Nature · doi:10.1038/nature06889 · Cited by 260 · see citing works
Self-citationDirect observation of thymine dimer repair in DNA by photolyase
Kao, Y.-T., Saxena, C., Wang, L., Sancar, A., & Zhong, D. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0506586102 · Cited by 259 · see citing works
Delaney, J. C., & Essigmann, J. M. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0403489101 · Cited by 241 · see citing works
Songe-Møller, L., van den Born, E., Leihne, V., Vågbø, C. B., Andersstuen, T. K., Krokan, H. E., Kirpekar, F., Falnes, P. Ø., & Klungland, A. (2010) · Molecular and Cellular Biology · doi:10.1128/mcb.01602-09 · Cited by 238 · see citing works
Crystal structures of catalytic complexes of the oxidative DNA/RNA repair enzyme AlkB
Yu, B., Edstrom, W. C., Benach, J., Hamuro, L., Weber, P. C., Gibney, B. R., & Hunt, J. F. (2006) · Nature · doi:10.1038/nature04561 · Cited by 234 · see citing works
Pegg, A. E. (2011) · Chemical Research in Toxicology · doi:10.1021/tx200031q · Cited by 223 · see citing works
Gao, X., Shin, Y.-H., Li, M., Wang, F., Tong, Q., & Zhang, P. (2010) · PLoS ONE · doi:10.1371/journal.pone.0014005 · Cited by 222 · see citing works
Dynamics and mechanism of repair of ultraviolet-induced (6–4) photoproduct by photolyase
Li, J., Liu, Z., Tan, C., Guo, X., Wang, L., Sancar, A., & Zhong, D. (2010) · Nature · doi:10.1038/nature09192 · Cited by 220 · see citing works
The intracellular signal for induction of resistance to alkylating agents in E. coli
Teo, I. A., Sedgwick, B., Kilpatrick, M. W., et al. (1986) · Cell · doi:10.1016/0092-8674(86)90396-x · Cited by 219 · see citing works
Demple, B., Sedgwick, B., Robins, P., Totty, N. F., Waterfield, M. D., & Lindahl, T. L. (1985) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.82.9.2688 · Cited by 218 · see citing works
Srivenugopal, K. S., Yuan, X., Friedman, H. S., & Ali‐Osman, F. (1996) · Biochemistry · doi:10.1021/bi9518205 · Cited by 218 · see citing works
Dango, S., Mosammaparast, N., Sowa, M. E., Xiong, L.-J., Wu, F., Park, K., Rubin, M., Gygi, S., Harper, J. W., & Shi, Y. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.08.039 · Cited by 216 · see citing works
Phylogenomic identification of five new human homologs of the DNA repair enzyme AlkB
Kurowski, M. A., Bhagwat, A. S., Papaj, G., & Bujnicki, J. M. (2003) · BMC Genomics · doi:10.1186/1471-2164-4-48 · Cited by 206 · see citing works
AlkB restores the biological function of mRNA and tRNA inactivated by chemical methylation
Ougland, R., Zhang, C.-M., Liiv, A., Johansen, R. F., Seeberg, E., Hou, Y.-M., Remme, J., & Falnes, P. Ø. (2004) · Molecular Cell · doi:10.1016/j.molcel.2004.09.002 · Cited by 205 · see citing works
Fu, D., Brophy, J. A. N., Chan, C. T. Y., Atmore, K. A., Begley, U., Paules, R. S., Dedon, P. C., Begley, T. J., & Samson, L. D. (2010) · Molecular and Cellular Biology · doi:10.1128/mcb.01604-09 · Cited by 204 · see citing works
Reaction mechanisms of DNA photolyase
Brettel, K., & Byrdin, M. (2010) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2010.07.003 · Cited by 201 · see citing works
Sánchez‐Pulido, L., & Andrade-Navarro, M. A. (2007) · BMC Biochemistry · doi:10.1186/1471-2091-8-23 · Cited by 197 · see citing works
Crystal Structure and Mechanism of a DNA (6‐4) Photolyase
Maul, M. J., Barends, T. R. M., Glas, A. F., Cryle, M. J., Domratcheva, T. M., Schneider, S., Schlichting, I., & Carell, T. (2008) · Angewandte Chemie International Edition · doi:10.1002/anie.200804268 · Cited by 197 · see citing works
AlkB reverses etheno DNA lesions caused by lipid oxidation in vitro and in vivo
Delaney, J. C., Smeester, L., Wong, C., Frick, L. E., Taghizadeh, K., Wishnok, J. S., Drennan, C. L., Samson, L. D., & Essigmann, J. M. (2005) · Nature Structural & Molecular Biology · doi:10.1038/nsmb996 · Cited by 194 · see citing works
Human AlkB Homolog 1 Is a Mitochondrial Protein That Demethylates 3-Methylcytosine in DNA and RNA
Westbye, M. P., Feyzi, E., Aas, P. A., Vågbø, C. B., Monsen, V. T., Kavli, B., Hagen, L., Sundheim, O., Akbari, M., Liabakk, N., et al. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m803776200 · Cited by 187 · see citing works
Ringvoll, J., Nordstrand, L. M., Vågbø, C. B., Monsen, V. T., Reite, K., Aas, P. A., Lauritzen, K. H., Liabakk, N., Bjørk, A., Doughty, R. W., et al. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601109 · Cited by 187 · see citing works
Variability and regulation of O6-alkylguanine-DNA alkyltransferase
Margison, G. P. (2003) · Carcinogenesis · doi:10.1093/carcin/bgg005 · Cited by 182 · see citing works
Tung, Y.-C., Ayuso, E., Shan, X., Bosch, F., O’Rahilly, S., Coll, A. P., & Yeo, G. S. H. (2010) · PLoS ONE · doi:10.1371/journal.pone.0008771 · Cited by 180 · see citing works
Recognition and repair of UV lesions in loop structures of duplex DNA by DASH-type cryptochrome
Pokorny, R., Klar, T., Hennecke, U., Carell, T., Batschauer, A., & Essen, L. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0805830106 · Cited by 179 · see citing works
Tubbs, J. L., Pegg, A. E., & Tainer, J. A. (2007) · DNA repair · doi:10.1016/j.dnarep.2007.03.011 · Cited by 175 · see citing works
Human ABH3 structure and key residues for oxidative demethylation to reverse DNA/RNA damage
Sundheim, O., Vågbø, C. B., Bjørås, M., de Sousa, M. M. L., Monsen, V. T., Aas, P. A., Drabløs, F., Krokan, H. E., Tainer, J. A., & Slupphaug, G. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601219 · Cited by 174 · see citing works
ALKBH8-mediated formation of a novel diastereomeric pair of wobble nucleosides in mammalian tRNA
van den Born, E., Vågbø, C. B., Songe-Møller, L., Leihne, V., Lien, G. F., Leszczyńska, G., Małkiewicz, A. J., Krokan, H. E., Kirpekar, F., Klungland, A., et al. (2011) · Nature Communications · doi:10.1038/ncomms1173 · Cited by 174 · see citing works
Dynamics and mechanism of cyclobutane pyrimidine dimer repair by DNA photolyase
Liu, Z., Tan, C., Guo, X., Kao, Y., Li, J., Wang, L., Sancar, A., & Zhong, D. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1110927108 · Cited by 173 · see citing works
Identification of a novel, widespread, and functionally important PCNA-binding motif
Gilljam, K. M., Feyzi, E., Aas, P. A., de Sousa, M. M. L., Müller, R., Vågbø, C. B., Catterall, T., Liabakk, N., Slupphaug, G., Drabløs, F., et al. (2009) · The Journal of Cell Biology · doi:10.1083/jcb.200903138 · Cited by 169 · see citing works
A Novel Human AlkB Homologue, ALKBH8, Contributes to Human Bladder Cancer Progression
Shimada, K., Nakamura, M., Anai, S., Velasco, M. A. D., Tanaka, M., Tsujikawa, K., Ouji, Y., & Konishi, N. (2009) · Cancer Research · doi:10.1158/0008-5472.can-08-3530 · Cited by 156 · see citing works
Fu, Y., Dai, Q., Zhang, W., Jin, R., Pan, T., & He, C. (2010) · Angewandte Chemie International Edition · doi:10.1002/anie.201001242 · Cited by 155 · see citing works
Self-citationThalhammer, A., Bencokova, Z., Poole, R., Loenarz, C., Adam, J., O′Flaherty, L., Schödel, J., Mole, D. R., Giaslakiotis, K., Schofield, C. J., et al. (2011) · PLoS ONE · doi:10.1371/journal.pone.0016210 · Cited by 151 · see citing works
Repair of DNA Methylphosphotriesters Through a Metalloactivated Cysteine Nucleophile
Myers, L. C., Terranova, M. P., Ferentz, A. E., Wagner, G., & Verdine, G. L. (1993) · Science · doi:10.1126/science.8395079 · Cited by 150 · see citing works
Tet Proteins Can Convert 5-Methylcytosine to 5-Formylcytosine and 5-Carboxylcytosine
Wu, S. C., Zhang, Y., Collins, L. B., et al. (2020) · Carolina Digital Repository (University of North Carolina at Chapel Hill) · doi:10.17615/w7hh-zy88 · Cited by 145 · see citing works
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., Cui, Q., & He, C. (2010) · Nature · doi:10.1038/nature09497 · Cited by 138 · see citing works
Self-citationHuang, Y., Baxter, R. H. G., Smith, B. S., Partch, C. L., Colbert, C. L., & Deisenhofer, J. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0608554103 · Cited by 133 · see citing works
Flipping of alkylated DNA damage bridges base and nucleotide excision repair
Tubbs, J. L., Latypov, V., Kanugula, S., Butt, A., Melikishvili, M., Kraehenbuehl, R., Fleck, O., Marriott, A. S., Watson, A. J., Verbeek, B., et al. (2009) · Nature · doi:10.1038/nature08076 · Cited by 132 · see citing works
A proteome chip approach reveals new DNA damage recognition activities in Escherichia coli
Chen, C., Korobkova, E. A., Chen, H., Zhu, J. K., Jian, X., Tao, S., He, C., & Zhu, H. (2007) · Nature Methods · doi:10.1038/nmeth1148 · Cited by 127 · see citing works
Self-citationALKBH3, a human AlkB homologue, contributes to cell survival in human non-small-cell lung cancer
Tasaki, M., Shimada, K., Kimurâ, H., Tsujikawa, K., & Konishi, N. (2011) · British Journal of Cancer · doi:10.1038/sj.bjc.6606012 · Cited by 126 · see citing works
Hitomi, K. (2000) · Nucleic Acids Research · doi:10.1093/nar/28.12.2353 · Cited by 125 · see citing works
Structural biology of DNA photolyases and cryptochromes
Müller, M., & Carell, T. (2009) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2009.05.003 · Cited by 125 · see citing works
Defective processing of methylated single-stranded DNA by E. coli alkB mutantsPreprint
Dinglay, S., Trewick, S. C., Lindahl, T. L., & Sedgwick, B. (2000) · Genes & Development · doi:10.1101/gad.14.16.2097 · Cited by 125 · see citing works
Hitomi, K., DiTacchio, L., Arvai, A. S., Yamamoto, J., Kim, S., Todo, T., Tainer, J. A., Iwai, S., Panda, S., & Getzoff, E. D. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0809180106 · Cited by 123 · see citing works
A Non-Heme Iron-Mediated Chemical Demethylation in DNA and RNA
Yi, C., Yang, C., & He, C. (2009) · Accounts of Chemical Research · doi:10.1021/ar800178j · Cited by 117 · see citing works
Self-citationTaguchi, T. (1995) · PubMed · Cited by 117 · see citing works
Identification of cryptochrome DASH from vertebrates
Daiyasu, H., Ishikawa, T., Kuma, K., Iwai, S., Todo, T., & Toh, H. (2004) · Genes to Cells · doi:10.1111/j.1356-9597.2004.00738.x · Cited by 114 · see citing works
Covalent Trapping of Protein-DNA Complexes
Verdine, G. L., & Norman, D. P. G. (2003) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.72.121801.161447 · Cited by 114 · see citing works
Repair of 3-methylthymine and 1-methylguanine lesions by bacterial and human AlkB proteins
Falnes, P. Ø. (2004) · Nucleic Acids Research · doi:10.1093/nar/gkh964 · Cited by 112 · see citing works
Direct Repair of the Exocyclic DNA Adduct 1,N6-Ethenoadenine by the DNA Repair AlkB Proteins
Mishina, Y., Yang, C., & He, C. (2005) · Journal of the American Chemical Society · doi:10.1021/ja055957m · Cited by 109 · see citing works
Self-citationFunctional domains and methyl acceptor sites of the Escherichia coli ada protein.
Sedgwick, B., Robins, P., Totty, N. F., et al. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)68944-6 · Cited by 106 · see citing works
Prevalence of Loss-of-Function FTO Mutations in Lean and Obese Individuals
Eyre, S., Proulx, K., Kawagoe-Takaki, H., et al. (2009) · Diabetes · doi:10.2337/db09-0703 · Cited by 106 · see citing works
Shimada, K., Nakamura, M., Ishida, E., Higuchi, T., Yamamoto, H., Tsujikawa, K., & Konishi, N. (2007) · Cancer Science · doi:10.1111/j.1349-7006.2007.00655.x · Cited by 101 · see citing works
Demethylation of 3-Methylthymine in DNA by Bacterial and Human DNA Dioxygenases
Koivisto, P., Robins, P., Lindahl, T. L., & Sedgwick, B. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m407960200 · Cited by 101 · see citing works
Crystal structures of an archaeal class II DNA photolyase and its complex with UV‐damaged duplex DNA
Kiontke, S., Geisselbrecht, Y., Pokorny, R., Carell, T., Batschauer, A., & Essen, L. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.313 · Cited by 98 · see citing works
The Structure of the Human AGT Protein Bound to DNA and its Implications for Damage Detection
Duguid, E. M., Rice, P. A., & He, C. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2005.05.028 · Cited by 96 · see citing works
Self-citationFrom GWAS to biology: lessons from FTO
Tung, Y. L., & Yeo, G. S. H. (2011) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2010.05903.x · Cited by 95 · see citing works
Sowers, L. C., Ito, S., Taranova, O., Hong, K., D’Alessio, A. C., & Zhang, Y. (2020) · Carolina Digital Repository (University of North Carolina at Chapel Hill) · doi:10.17615/mdef-cm08 · Cited by 95 · see citing works
Inactivation of O6-alkylguanine DNA alkyltransferase as a means to enhance chemotherapy.
Rabik, C., Njoku, M., & Dolan, M. (2006) · Cancer Treatment Reviews · doi:10.1016/j.ctrv.2006.03.004 · Cited by 92 · see citing works
Yu, B., & Hunt, J. F. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0812938106 · Cited by 91 · see citing works
Kinetics of cyclobutane thymine dimer splitting by DNA photolyase directly monitored in the UV
Thiagarajan, V., Byrdin, M., Eker, A. P. M., Müller, P., & Brettel, K. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1101026108 · Cited by 90 · see citing works
Impaired placental trophoblast lineage differentiation in Alkbh1−/− mice
Pan, Z., Sikandar, S. S., Witherspoon, M., Dizon, D., Nguyen, T., Benirschke, K., Wiley, C. D., Vrana, P. B., & Lipkin, S. M. (2007) · Developmental Dynamics · doi:10.1002/dvdy.21418 · Cited by 85 · see citing works
Repair of methyl lesions in DNA and RNA by oxidative demethylation
Falnes, P. Ø., Klungland, A., & Alseth, I. (2006) · Neuroscience · doi:10.1016/j.neuroscience.2006.11.018 · Cited by 84 · see citing works
He, C., Hus, J., Sun, L., Zhou, P., Norman, D. P. G., Dötsch, V., Wei, H., Gross, J. D., Lane, W. S., Wagner, G., et al. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.08.013 · Cited by 81 · see citing works
Self-citationPastore, C., Topalidou, I., Forouhar, F., Yan, A. C., Levy, M., & Hunt, J. F. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.286187 · Cited by 78 · see citing works
A two-step nucleotide-flipping mechanism enables kinetic discrimination of DNA lesions by AGT
Hu, J., Ma, A., & Dinner, A. R. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0708058105 · Cited by 78 · see citing works
Two proteolytic pathways regulate DNA repair by cotargeting the Mgt1 alkylguanine transferase
Hwang, C., Shemorry, A., & Varshavsky, A. J. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0812316106 · Cited by 77 · see citing works
Duplex interrogation by a direct DNA repair protein in search of base damage
Yi, C., Chen, B., Qi, B., Zhang, W., Jia, G., Zhang, L., Li, C. J., Dinner, A. R., Yang, C., & He, C. (2012) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2320 · Cited by 76 · see citing works
Self-citationMice Lacking Alkbh1 Display Sex-Ratio Distortion and Unilateral Eye Defects
Nordstrand, L. M., Svärd, J., Larsen, E., Nilsen, A., Ougland, R., Furu, K., Lien, G. F., Rognes, T., Namekawa, S. H., Lee, J. T., et al. (2010) · PLoS ONE · doi:10.1371/journal.pone.0013827 · Cited by 75 · see citing works
Human AlkB homologue 1 (ABH1) exhibits DNA lyase activity at abasic sites
Müller, T., Meek, K., & Hausinger, R. P. (2009) · DNA repair · doi:10.1016/j.dnarep.2009.10.011 · Cited by 70 · see citing works
Kinetic Analysis of Steps in the Repair of Damaged DNA by Human O6-Alkylguanine-DNA Alkyltransferase
Zang, H., Fang, Q., Pegg, A. E., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m505283200 · Cited by 69 · see citing works
Structural studies of human alkyladenine glycosylase and E. coli 3-methyladenine glycosylase
Hollis, T., Lau, A. Y., & Ellenberger, T. (2000) · Mutation Research/DNA Repair · doi:10.1016/s0921-8777(00)00027-6 · Cited by 68 · see citing works
Frick, L. E., Delaney, J. C., Wong, C., Drennan, C. L., & Essigmann, J. M. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0607377104 · Cited by 62 · see citing works
Dynamic states of the DNA repair enzyme AlkB regulate product release
Bleijlevens, B., Shivarattan, T., Flashman, E., Yang, Y., Simpson, P. J., Koivisto, P., Sedgwick, B., Schofield, C. J., & Matthews, S. (2008) · EMBO Reports · doi:10.1038/embor.2008.120 · Cited by 60 · see citing works
Holland, P. J., & Hollis, T. (2010) · PLoS ONE · doi:10.1371/journal.pone.0008680 · Cited by 59 · see citing works
Chen, B., Liu, H., Sun, X., & Yang, C. (2010) · Molecular BioSystems · doi:10.1039/c005148a · Cited by 58 · see citing works
Mishina, Y., & He, C. (2003) · Journal of the American Chemical Society · doi:10.1021/ja034636c · Cited by 54 · see citing works
Self-citationRegulation of expression of the ada gene controlling the adaptive response
Sakumi, K., & Sekiguchi, M. (1989) · Journal of Molecular Biology · doi:10.1016/0022-2836(89)90348-3 · Cited by 51 · see citing works
Repair of O6-G-Alkyl-O6-G Interstrand Cross-Links by Human O6-Alkylguanine-DNA Alkyltransferase
Fang, Q., Noronha, A. M., Murphy, S. P., Wilds, C. J., Tubbs, J. L., Tainer, J. A., Chowdhury, G., Guengerich, F. P., & Pegg, A. E. (2008) · Biochemistry · doi:10.1021/bi8008664 · Cited by 49 · see citing works
Mazón, G., Philippin, G., Cadet, J., et al. (2009) · DNA repair · doi:10.1016/j.dnarep.2009.01.022 · Cited by 48 · see citing works
Alkyltransferase-like proteins
Margison, G. P., Butt, A., Pearson, S. J., et al. (2007) · DNA repair · doi:10.1016/j.dnarep.2007.03.014 · Cited by 47 · see citing works
Alkbh2 protects against lethality and mutation in primary mouse embryonic fibroblasts
Nay, S. L., Lee, D.-H., Bates, S., & O'Connor, T. R. (2012) · DNA repair · doi:10.1016/j.dnarep.2012.02.005 · Cited by 46 · see citing works
Interactions of Human O6-Alkylguanine-DNA Alkyltransferase (AGT) with Short Single-stranded DNAs
Rasimas, J. J., Kar, S. R., Pegg, A. E., & Fried, M. G. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m608876200 · Cited by 45 · see citing works
Anti-Tumor Effect of AlkB Homolog 3 Knockdown in Hormone- Independent Prostate Cancer Cells
Koike, K., Ueda, Y., Hase, H., et al. (2012) · Current Cancer Drug Targets · doi:10.2174/156800912802429283 · Cited by 45 · see citing works
Warren, K. E., Aikin, A. A., Libucha, M., Widemann, B. C., Fox, E., Packer, R. J., & Balis, F. M. (2005) · Journal of Clinical Oncology · doi:10.1200/jco.2005.02.0024 · Cited by 43 · see citing works
Phase I trial of temozolomide plus O6-benzylguanine 5-day regimen with recurrent malignant glioma
Quinn, J. A., Jiang, X. “., Reardon, D. A., Desjardins, A., Vredenburgh, J. J., Rich, J. N., Gururangan, S., Friedman, A. H., Bigner, D. D., Sampson, J. H., et al. (2009) · Neuro-Oncology · doi:10.1215/15228517-2009-007 · Cited by 42 · see citing works
Bleijlevens, B., Shivarattan, T., van den Boom, K. S., de Haan, A., van der Zwan, G., Simpson, P. J., & Matthews, S. (2012) · Biochemistry · doi:10.1021/bi201699e · Cited by 42 · see citing works
Monsen, V. T., Sundheim, O., Aas, P. A., Westbye, M. P., de Sousa, M. M. L., Slupphaug, G., & Krokan, H. E. (2010) · Nucleic Acids Research · doi:10.1093/nar/gkq518 · Cited by 41 · see citing works
The DNA dioxygenase ALKBH2 protects Arabidopsis thaliana against methylation damage
Meza, T. J., Moen, M. N., Vågbø, C. B., Krokan, H. E., Klungland, A., Grini, P. E., & Falnes, P. Ø. (2012) · Nucleic Acids Research · doi:10.1093/nar/gks327 · Cited by 40 · see citing works
Turriziani, M., Caporaso, P., Bonmassar, L., Buccisano, F., Amadori, S., Venditti, A., Cantonetti, M., D’Atri, S., & Bonmassar, E. (2006) · Pharmacological Research · doi:10.1016/j.phrs.2005.12.001 · Cited by 39 · see citing works
Mishina, Y., Chen, L. X., & He, C. (2004) · Journal of the American Chemical Society · doi:10.1021/ja045066z · Cited by 39 · see citing works
Self-citationMorita, R., Nakagawa, N., Kuramitsu, S., & Masui, R. (2008) · The Journal of Biochemistry · doi:10.1093/jb/mvn065 · Cited by 39 · see citing works
Pearson, S. J. (2005) · Nucleic Acids Research · doi:10.1093/nar/gki696 · Cited by 38 · see citing works
Hitomi, K., Arvai, A. S., Yamamoto, J., Hitomi, C., Teranishi, M., Hirouchi, T., Yamamoto, K., Iwai, S., Tainer, J. A., Hidema, J., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.244020 · Cited by 37 · see citing works
Rohankhedkar, M. S., Mulrooney, S. B., Wedemeyer, W. J., et al. (2005) · Journal of Bacteriology · doi:10.1128/jb.188.1.223-230.2006 · Cited by 37 · see citing works
Light-induced activation of class II cyclobutane pyrimidine dimer photolyases
Okafuji, A., Biskup, T., Hitomi, K., Getzoff, E. D., Kaiser, G., Batschauer, A., Bacher, A., Hidema, J., Teranishi, M., Yamamoto, K., et al. (2010) · DNA repair · doi:10.1016/j.dnarep.2010.01.014 · Cited by 35 · see citing works
Hammond, L. A., Eckardt, J. R., Kuhn, J. G., et al. (2004) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-03-0174 · Cited by 30 · see citing works
Mishina, Y. M. (2004) · Nucleic Acids Research · doi:10.1093/nar/gkh319 · Cited by 30 · see citing works
Topologies of Complexes Containing O6-Alkylguanine–DNA Alkyltransferase and DNA
Adams, C., Melikishvili, M., Rodgers, D. W., Rasimas, J. J., Pegg, A. E., & Fried, M. G. (2009) · Journal of Molecular Biology · doi:10.1016/j.jmb.2009.03.067 · Cited by 29 · see citing works
Aramini, J. M., Tubbs, J. L., Kanugula, S., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.093591 · Cited by 29 · see citing works
Frequent down‐regulation of hABH2 in gastric cancer and its involvement in growth of cancer cells
Gao, W., Li, L., Xu, P., et al. (2010) · Journal of Gastroenterology and Hepatology · doi:10.1111/j.1440-1746.2010.06531.x · Cited by 27 · see citing works
Structure and DNA binding of alkylation response protein AidB
Bowles, T. M., Metz, A. H., O'Quin, J., et al. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0806521105 · Cited by 27 · see citing works
Rippa, V., Duilio, A., Pasquale, P. D., Amoresano, A., Landini, P., & Volkert, M. R. (2011) · DNA repair · doi:10.1016/j.dnarep.2011.06.001 · Cited by 27 · see citing works
A novel DNA damage recognition protein in Schizosaccharomyces pombe
Pearson, S. J. (2006) · Nucleic Acids Research · doi:10.1093/nar/gkl270 · Cited by 27 · see citing works
FTIR Study of Light-Dependent Activation and DNA Repair Processes of (6–4) Photolyase
Zhang, Y., Iwata, T., Yamamoto, J., et al. (2011) · Biochemistry · doi:10.1021/bi1019397 · Cited by 26 · see citing works
Using the Bias from Flow to Elucidate Single DNA Repair Protein Sliding and Interactions with DNA
Lin, Y., Zhao, T., Jian, X., et al. (2009) · Biophysical Journal · doi:10.1016/j.bpj.2008.11.021 · Cited by 25 · see citing works
Alkyltransferase-like proteins: molecular switches between DNA repair pathways
Tubbs, J. L., & Tainer, J. A. (2010) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-010-0405-8 · Cited by 24 · see citing works
Light-Induced Conformational Change and Product Release in DNA Repair by (6−4) Photolyase
Kondoh, M., Hitomi, K., Yamamoto, J., Todo, T., Iwai, S., Getzoff, E. D., & Terazima, M. (2011) · Journal of the American Chemical Society · doi:10.1021/ja107691w · Cited by 23 · see citing works
Guza, R., Rajesh, M. P., Fang, Q., Pegg, A. E., & Tretyakova, N. Y. (2006) · Chemical Research in Toxicology · doi:10.1021/tx050348d · Cited by 20 · see citing works
Regulation And Expression Of The Adaptive Response To Alkylating Agents
Lindahl, T. (1988) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.57.1.133 · Cited by 20 · see citing works
Korvald, H., Falnes, P. Ø., Laerdahl, J. K., Bjørås, M., & Alseth, I. (2012) · DNA repair · doi:10.1016/j.dnarep.2012.01.014 · Cited by 18 · see citing works
A cryptochrome/photolyase class of enzymes with single-stranded DNA-specific photolyase activity
Sancar, A., & Selby, C. P. (2020) · Carolina Digital Repository (University of North Carolina at Chapel Hill) · doi:10.17615/m1p8-n307 · Cited by 15 · see citing works
Fu, Y., Dai, Q., Zhang, W., Jin, R., Pan, T., & He, C. (2010) · Angewandte Chemie · doi:10.1002/ange.201001242 · Cited by 12 · see citing works
Self-citationDynamics and mechanism of repair of ultraviolet-induced (6–4) photoproduct by photolyase
Li, J., Wang, L., Liu, Z., et al. (2020) · Carolina Digital Repository (University of North Carolina at Chapel Hill) · doi:10.17615/43qb-az27 · Cited by 10 · see citing works
Prostate cancer antigen-1 as a potential novel marker for prostate cancer
Liu, B., Wu, Y., Li, P.-H., Wei, J., Zhang, T., & Liu, R. (2007) · Asian Journal of Andrology · doi:10.1111/j.1745-7262.2007.00279.x · Cited by 6 · see citing works
Dynamics and mechanism of cyclobutane pyrimidine dimer repair by DNA photolyase
Sancar, A., Wang, L., Li, J., et al. (2020) · Carolina Digital Repository (University of North Carolina at Chapel Hill) · doi:10.17615/wc3g-4049 · Cited by 2 · see citing works
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Mechanisms of DNA damage, repair, and mutagenesis
Chatterjee, N., & Walker, G. C. (2017) · Environmental and Molecular Mutagenesis · doi:10.1002/em.22087 · Cited by 2,039 · see citing works
Fedeles, B. I., Singh, V., Delaney, J. C., Li, D., & Essigmann, J. M. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.r115.656462 · Cited by 416 · see citing works
Focus on UV-Induced DNA Damage and Repair—Disease Relevance and Protective Strategies
Kciuk, M., Marciniak, B., Mojzych, M., & Kontek, R. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21197264 · Cited by 168 · see citing works
“There are three major types of direct DNA repair: (a) reversal of UV-induced photolesions carried by photolyases, (b) repair of O-alkylated DNA by O6-alkylguanine-DNA alkyltransferases, and (c) repair of N-alkylated bases by AlkB family dioxygenase enzymes [77].”
BackgroundMitkus, R. J., Hess, M. A., & Schwartz, S. L. (2013) · Vaccine · doi:10.1016/j.vaccine.2013.03.071 · Cited by 35 · see citing works
Non-bulky Lesions in Human DNA: The Ways of Formation, Repair, and Replication
Ignatov, А. V., Bondarenko, K. A., & Makarova, A. V. (2017) · Acta Naturae · doi:10.32607/20758251-2017-9-3-12-26 · Cited by 31 · see citing works
- Authors
- Yi, C., & He, C.
- Affiliations
- Peking University (CN)
- University of Chicago (US)
- Venue
- Cold Spring Harbor Perspectives in Biology
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 2013-01-01
- Volume
- 5
- Issue
- 1
- Pages
- a012575-a012575
- ISSN
- 1943-0264 (ISSN-L)
- PMC
- PMC3579392
- OpenAlex
- W2112528865
- Cited by
- 161
- References
- 149
- Citations by year
- 2026: 9 · 2025: 11 · 2024: 14 · 2023: 11 · 2022: 12 · 2021: 21 · 2020: 14 · 2019: 13 · 2018: 10 · 2017: 15 · 2016: 6 · 2015: 11 · 2014: 8 · 2013: 6
- Type
- posted content
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Cold Spring Harbor Perspectives in Biology (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA and Nucleic Acid Chemistry
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Keywords
- DNA adducts, photolyase, alkyltransferase, dioxygenase, DNA repair enzymes, mutagenesis, cytotoxicity
- MeSH terms
- Alpha-Ketoglutarate-Dependent Dioxygenase FTO, DNA Damage, Deoxyribodipyrimidine Photo-Lyase, DNA Repair, Humans, Methylation, Models, Genetic, Obesity, Proteins, RNA, Alkyl and Aryl Transferases, DNA Repair Enzymes, Dioxygenases, Cryptochromes
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