{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,12]],"date-time":"2026-07-12T00:18:13Z","timestamp":1783815493712,"version":"3.55.0"},"reference-count":71,"publisher":"American Society for Microbiology","issue":"6","license":[{"start":{"date-parts":[[2012,6,1]],"date-time":"2012-06-01T00:00:00Z","timestamp":1338508800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["Antimicrob Agents Chemother"],"published-print":{"date-parts":[[2012,6]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            The distribution of mutants in the Keio collection of\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">Escherichia coli<\/jats:named-content>\n            gene knockout mutants that display increased sensitivity to the aminoglycosides kanamycin and neomycin indicates that damaged bases resulting from antibiotic action can lead to cell death. Strains lacking one of a number of glycosylases (e.g., AlkA, YzaB, Ogt, KsgA) or other specific repair proteins (AlkB, PhrB, SmbC) are more sensitive to these antibiotics. Mutants lacking AlkB display the strongest sensitivity among the glycosylase- or direct lesion removal-deficient strains. This perhaps suggests the involvement of ethenoadenine adducts, resulting from reactive oxygen species and lipid peroxidation, since AlkB removes this lesion. Other sensitivities displayed by mutants lacking UvrA, polymerase V (Pol V), or components of double-strand break repair indicate that kanamycin results in damaged base pairs that need to be removed or replicated past in order to avoid double-strand breaks that saturate the cellular repair capacity. Caffeine enhances the sensitivities of these repair-deficient strains to kanamycin and neomycin. The gene knockout mutants that display increased sensitivity to caffeine (\n            <jats:italic>dnaQ<\/jats:italic>\n            ,\n            <jats:italic>holC<\/jats:italic>\n            ,\n            <jats:italic>holD<\/jats:italic>\n            , and\n            <jats:italic>priA<\/jats:italic>\n            knockout mutants) indicate that caffeine blocks DNA replication, ultimately leading to double-strand breaks that require recombinational repair by functions encoded by\n            <jats:italic>recA<\/jats:italic>\n            ,\n            <jats:italic>recB<\/jats:italic>\n            , and\n            <jats:italic>recC<\/jats:italic>\n            , among others. Additionally, caffeine partially protects cells of both\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">Escherichia coli<\/jats:named-content>\n            and\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">Bacillus anthracis<\/jats:named-content>\n            from killing by the widely used fluoroquinolone antibiotic ciprofloxacin.\n          <\/jats:p>","DOI":"10.1128\/aac.00066-12","type":"journal-article","created":{"date-parts":[[2012,3,6]],"date-time":"2012-03-06T05:49:51Z","timestamp":1331012991000},"page":"3216-3223","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":42,"title":["The Aminoglycoside Antibiotic Kanamycin Damages DNA Bases in Escherichia coli: Caffeine Potentiates the DNA-Damaging Effects of Kanamycin while Suppressing Cell Killing by Ciprofloxacin in Escherichia coli and Bacillus anthracis"],"prefix":"10.1128","volume":"56","author":[{"given":"Tina Manzhu","family":"Kang","sequence":"first","affiliation":[{"name":"Department of Microbiology, Immunology, and Molecular Genetics and the Molecular Biology Institute, University of California, and the David Geffen School of Medicine, Los Angeles, California, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jessica","family":"Yuan","sequence":"additional","affiliation":[{"name":"Department of Microbiology, Immunology, and Molecular Genetics and the Molecular Biology Institute, University of California, and the David Geffen School of Medicine, Los Angeles, California, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Angelyn","family":"Nguyen","sequence":"additional","affiliation":[{"name":"Department of Microbiology, Immunology, and Molecular Genetics and the Molecular Biology Institute, University of California, and the David Geffen School of Medicine, Los Angeles, California, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Elinne","family":"Becket","sequence":"additional","affiliation":[{"name":"Department of Microbiology, Immunology, and Molecular Genetics and the Molecular Biology Institute, University of California, and the David Geffen School of Medicine, Los Angeles, California, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hanjing","family":"Yang","sequence":"additional","affiliation":[{"name":"Department of Microbiology, Immunology, and Molecular Genetics and the Molecular Biology Institute, University of California, and the David Geffen School of Medicine, Los Angeles, California, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jeffrey H.","family":"Miller","sequence":"additional","affiliation":[{"name":"Department of Microbiology, Immunology, and Molecular Genetics and the Molecular Biology Institute, University of California, and the David Geffen School of Medicine, Los Angeles, California, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.cell.2007.03.004"},{"key":"e_1_3_2_3_2","doi-asserted-by":"crossref","first-page":"741","DOI":"10.1016\/S0092-8674(03)00197-1","article-title":"Interchangeable parts of the Escherichia coli recombinational machinery","volume":"112","author":"Amundsen SK","year":"2003","unstructured":"AmundsenSK SmithGR. 2003. Interchangeable parts of the Escherichia coli recombinational machinery. Cell 112:741\u2013744.","journal-title":"Cell"},{"key":"e_1_3_2_4_2","doi-asserted-by":"publisher","DOI":"10.1093\/jac\/48.suppl_1.5"},{"key":"e_1_3_2_5_2","doi-asserted-by":"publisher","DOI":"10.1038\/msb4100050"},{"key":"e_1_3_2_6_2","doi-asserted-by":"publisher","DOI":"10.1016\/0378-1119(82)90023-3"},{"key":"e_1_3_2_7_2","doi-asserted-by":"crossref","first-page":"949","DOI":"10.1016\/j.dnarep.2010.06.008","article-title":"Determination of hypersensitivity to genotoxic agents among Escherichia coli single gene knockout mutants","volume":"9","author":"Becket E","year":"2010","unstructured":"BecketE ChenF TamaeC MillerJH. 2010. Determination of hypersensitivity to genotoxic agents among Escherichia coli single gene knockout mutants. DNA Repair 9:949\u2013957.","journal-title":"DNA Repair"},{"key":"e_1_3_2_8_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0021-9258(18)43840-9"},{"key":"e_1_3_2_9_2","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0006619"},{"key":"e_1_3_2_10_2","unstructured":"CDC. 2008. Centers for Disease Control and Prevention Active Bacterial Core Surveillance Report Emerging Infections Program Network methicillin-resistant Staphylococcus aureus 2008. CDC Atlanta GA. http:\/\/www.cdc.gov\/abcs\/reports-findings\/survreports\/mrsa08.pdf."},{"key":"e_1_3_2_11_2","doi-asserted-by":"crossref","first-page":"971","DOI":"10.1016\/S0140-6736(73)91604-8","article-title":"Synergistic effect of methyl-substituted xanthines and neomycin sulphate on Staphylococcus aureus and Pseudomonas aeruginosa in vitro","author":"Charles BG","year":"1973","unstructured":"CharlesBG RawalBD. 1973. Synergistic effect of methyl-substituted xanthines and neomycin sulphate on Staphylococcus aureus and Pseudomonas aeruginosa in vitro. Lancet i:971\u2013973.","journal-title":"Lancet"},{"key":"e_1_3_2_12_2","doi-asserted-by":"crossref","first-page":"339","DOI":"10.1007\/s00203-003-0598-4","article-title":"Chromosomally encoded gyrase inhibitor GyrI protects against DNA-damaging agents","volume":"180","author":"Chatterji M","year":"2003","unstructured":"ChatterjiM SenguptaS NagarajaV. 2003. Chromosomally encoded gyrase inhibitor GyrI protects against DNA-damaging agents. Arch. Microbiol. 180:339\u2013346.","journal-title":"Arch. Microbiol."},{"key":"e_1_3_2_13_2","doi-asserted-by":"crossref","first-page":"261","DOI":"10.1093\/embo-reports\/kvf038","article-title":"GyrI: a counter-defensive strategy against proteinaceous inhibitors of DNA gyrase","volume":"3","author":"Chatterji M","year":"2002","unstructured":"ChatterjiM NagarajaV. 2002. GyrI: a counter-defensive strategy against proteinaceous inhibitors of DNA gyrase. EMBO Rep. 3:261\u2013267.","journal-title":"EMBO Rep."},{"key":"e_1_3_2_14_2","doi-asserted-by":"crossref","first-page":"2105","DOI":"10.1093\/carcin\/17.10.2105","article-title":"Lipid peroxidation as a potential endogenous source for the formation of exocyclic DNA adducts","volume":"17","author":"Chung FL","year":"1996","unstructured":"ChungFL ChenHJ NathRG. 1996. Lipid peroxidation as a potential endogenous source for the formation of exocyclic DNA adducts. Carcinogenesis 17:2105\u20132111.","journal-title":"Carcinogenesis"},{"key":"e_1_3_2_15_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.tibtech.2007.09.004"},{"key":"e_1_3_2_16_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.120163297"},{"key":"e_1_3_2_17_2","doi-asserted-by":"crossref","first-page":"97","DOI":"10.1093\/jac\/22.Supplement_C.97","article-title":"Overview of drug interactions with the quinolones","volume":"22","author":"Davey PG","year":"1988","unstructured":"DaveyPG. 1988. Overview of drug interactions with the quinolones. J. Antimicrob. Chemother. 22:97\u2013107.","journal-title":"J. Antimicrob. Chemother."},{"key":"e_1_3_2_18_2","doi-asserted-by":"crossref","first-page":"616","DOI":"10.1038\/sj.embor.7401022","article-title":"Microbes have the last word","volume":"8","author":"Davies J","year":"2007","unstructured":"DaviesJ. 2007. Microbes have the last word. EMBO Rep. 8:616\u2013621.","journal-title":"EMBO Rep."},{"key":"e_1_3_2_19_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.molcel.2009.11.024"},{"key":"e_1_3_2_20_2","doi-asserted-by":"publisher","DOI":"10.1128\/mr.51.3.341-350.1987"},{"key":"e_1_3_2_21_2","doi-asserted-by":"crossref","first-page":"14051","DOI":"10.1073\/pnas.0403489101","article-title":"Mutagenesis, genotoxicity, and repair of 1-methyladenine, 3-alkylcytosines, 1-methylguanine and 3-methylthymine in alkB Escherichia coli","volume":"101","author":"Delaney JC","year":"2004","unstructured":"DelaneyJC EssigmannJM. 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\u201314056.","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"e_1_3_2_22_2","doi-asserted-by":"crossref","first-page":"855","DOI":"10.1038\/nsmb996","article-title":"AlkB reverses etheno DNA lesions caused by lipid oxidation in vitro and in vivo","volume":"12","author":"Delaney JC","year":"2005","unstructured":"DelaneyJC. 2005. AlkB reverses etheno DNA lesions caused by lipid oxidation in vitro and in vivo. Nat. Struct. Mol. Biol. 12:855\u2013860.","journal-title":"Nat. Struct. Mol. Biol."},{"key":"e_1_3_2_23_2","doi-asserted-by":"publisher","DOI":"10.1128\/mmbr.61.3.377-392.1997"},{"key":"e_1_3_2_24_2","doi-asserted-by":"publisher","DOI":"10.1128\/AEM.66.6.2641-2646.2000"},{"key":"e_1_3_2_25_2","doi-asserted-by":"crossref","first-page":"16660","DOI":"10.1073\/pnas.262589799","article-title":"Reversal of DNA alkylation damage by two human dioxygenases","volume":"99","author":"Duncan T","year":"2002","unstructured":"DuncanT. 2002. Reversal of DNA alkylation damage by two human dioxygenases. Proc. Natl. Acad. Sci. U. S. A. 99:16660\u201316665.","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"e_1_3_2_26_2","doi-asserted-by":"crossref","first-page":"278","DOI":"10.1021\/tx00044a013","article-title":"Formation of 1,N\n                  6-ethenoadenine and 3,N\n                  4-ethenocytosine by lipid peroxidation products and nucleic acid bases","volume":"8","author":"el Ghissassi F","year":"1995","unstructured":"el GhissassiF BarbinA NairJ BartschH. 1995. Formation of 1,N6-ethenoadenine and 3,N4-ethenocytosine by lipid peroxidation products and nucleic acid bases. Chem. Res. Toxicol. 8:278\u2013283.","journal-title":"Chem. Res. Toxicol."},{"key":"e_1_3_2_27_2","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0001619"},{"key":"e_1_3_2_28_2","doi-asserted-by":"publisher","DOI":"10.1128\/mcb.14.12.8071-8077.1994"},{"key":"e_1_3_2_29_2","doi-asserted-by":"crossref","first-page":"755","DOI":"10.1073\/pnas.0607377104","article-title":"Alleviation of 1,N\n                  6-ethanoadenine genotoxicity by the Escherichia coli adaptive response protein AlkB","volume":"104","author":"Frick LE","year":"2007","unstructured":"FrickLE DelaneyJC WongC DrennanCL EssigmannJM. 2007. Alleviation of 1,N6-ethanoadenine genotoxicity by the Escherichia coli adaptive response protein AlkB. Proc. Natl. Acad. Sci. U. S. A. 104:755\u2013760.","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"e_1_3_2_30_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0065-3233(04)69008-5"},{"key":"e_1_3_2_31_2","doi-asserted-by":"crossref","first-page":"99","DOI":"10.7164\/antibiotics.38.99","article-title":"Amplification of the antibiotic effects of the bleomycins and tallysomycins: its dependence on the nature of the variable groups","volume":"38","author":"Grigg GW","year":"1985","unstructured":"GriggGW. 1985. Amplification of the antibiotic effects of the bleomycins and tallysomycins: its dependence on the nature of the variable groups. J. Antibiot. 38:99\u2013110.","journal-title":"J. Antibiot."},{"key":"e_1_3_2_32_2","doi-asserted-by":"crossref","first-page":"1517","DOI":"10.1016\/j.dnarep.2008.05.010","article-title":"DNA double strand break repair and crossing over by RuvABC resolvase and RecG translocase","volume":"7","author":"Grove JI","year":"2008","unstructured":"GroveJI HarrisL NuckmanC LloydRG. 2008. DNA double strand break repair and crossing over by RuvABC resolvase and RecG translocase. DNA Repair 7:1517\u20131530.","journal-title":"DNA Repair"},{"key":"e_1_3_2_33_2","doi-asserted-by":"publisher","DOI":"10.1038\/msb4100184"},{"key":"e_1_3_2_34_2","doi-asserted-by":"crossref","first-page":"18814","DOI":"10.1016\/S0021-9258(17)32239-1","article-title":"New substrates for old enzymes. 5-hydroxy-2\u2032-cytidine and 5-hydroxy-2\u2032-uridine are substrates for Escherichia coli endonuclease III and formamidopyrimidine DNA N-glycosylase, while 5-hydroxy-2\u2032-deoxyuridine is a substrate for uracil DNA N-glycosylase","volume":"269","author":"Hatahet Z","year":"1994","unstructured":"HatahetZ KowYW PurmalAA CunninghamRP WallaceSS. 1994. New substrates for old enzymes. 5-hydroxy-2\u2032-cytidine and 5-hydroxy-2\u2032-uridine are substrates for Escherichia coli endonuclease III and formamidopyrimidine DNA N-glycosylase, while 5-hydroxy-2\u2032-deoxyuridine is a substrate for uracil DNA N-glycosylase. J. Biol. Chem. 269:18814\u201318820.","journal-title":"J. Biol. Chem."},{"key":"e_1_3_2_35_2","doi-asserted-by":"publisher","DOI":"10.1128\/AAC.33.4.474"},{"key":"e_1_3_2_36_2","doi-asserted-by":"publisher","DOI":"10.1126\/science.1150021"},{"key":"e_1_3_2_37_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.272.51.32230"},{"key":"e_1_3_2_38_2","doi-asserted-by":"crossref","first-page":"1579","DOI":"10.1016\/j.dnarep.2004.06.012","article-title":"Role of mismatch-specific uracil-DNA glycosylase in repair of 3,N\n                  4-ethenocytosine in vivo","volume":"3","author":"Jurado J","year":"2004","unstructured":"JuradoJ MaciejewskaA KrawiczJ LavalJ SaparbaevMK. 2004. Role of mismatch-specific uracil-DNA glycosylase in repair of 3,N4-ethenocytosine in vivo. DNA Repair 3:1579\u20131590.","journal-title":"DNA Repair"},{"key":"e_1_3_2_39_2","doi-asserted-by":"crossref","first-page":"67","DOI":"10.1016\/S1383-5742(02)00025-X","article-title":"Molecular mechanisms of adaptive response to alkylating agents in Escherichia coli and some remarks on O\n                  6-methylguanine DNA-methyltransferase in other organisms","volume":"512","author":"Kleibl K","year":"2002","unstructured":"KleiblK. 2002. Molecular mechanisms of adaptive response to alkylating agents in Escherichia coli and some remarks on O6-methylguanine DNA-methyltransferase in other organisms. Mutat. Res. 512:67\u201384.","journal-title":"Mutat. Res."},{"key":"e_1_3_2_40_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.cell.2007.06.049"},{"key":"e_1_3_2_41_2","doi-asserted-by":"publisher","DOI":"10.1038\/nrmicro2333"},{"key":"e_1_3_2_42_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.cell.2008.09.038"},{"key":"e_1_3_2_43_2","doi-asserted-by":"crossref","first-page":"40470","DOI":"10.1074\/jbc.M407960200","article-title":"Demethylation of 3-methylthymine in DNA by bacterial and human dioxygenases","volume":"279","author":"Koivisto P","year":"2004","unstructured":"KoivistoP RobinsP LindahlT SedgewickB. 2004. Demethylation of 3-methylthymine in DNA by bacterial and human dioxygenases. J. Biol. Chem. 279:40470\u201340474.","journal-title":"J. Biol. Chem."},{"key":"e_1_3_2_44_2","doi-asserted-by":"publisher","DOI":"10.1101\/gad.13.3.345"},{"key":"e_1_3_2_45_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.0903619106"},{"key":"e_1_3_2_46_2","doi-asserted-by":"publisher","DOI":"10.1128\/AAC.00906-09"},{"key":"e_1_3_2_47_2","doi-asserted-by":"crossref","first-page":"9331","DOI":"10.1073\/pnas.89.19.9331","article-title":"Release of N\n                  2,3-ethenoguanine from chloroacetaldehyde-treated DNA by Escherichia coli 3-methyladenine DNA glycosylase II","volume":"89","author":"Matijasevic Sekiguchi SM","year":"1992","unstructured":"Matijasevic SekiguchiSM LudlumDB. 1992. Release of N2,3-ethenoguanine from chloroacetaldehyde-treated DNA by Escherichia coli 3-methyladenine DNA glycosylase II. Proc. Natl. Acad. Sci. U. S. A. 89:9331\u20139334.","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"e_1_3_2_48_2","doi-asserted-by":"crossref","first-page":"18050","DOI":"10.1073\/pnas.1008635107","article-title":"Alkyltransferase-like protein (eATL) prevents mismatch repair-mediated toxicity induced by O\n                  6-alkyl adducts in Escherichia coli","volume":"107","author":"Mazon G","year":"2010","unstructured":"MazonG. 2010. Alkyltransferase-like protein (eATL) prevents mismatch repair-mediated toxicity induced by O6-alkyl adducts in Escherichia coli. Proc. Natl. Acad. Sci. U. S. A. 107:18050\u201318055.","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"e_1_3_2_49_2","doi-asserted-by":"publisher","DOI":"10.1021\/bi00171a028"},{"key":"e_1_3_2_50_2","unstructured":"MillerJH. 1992. A short course in bacterial genetics: a laboratory manual and handbook for Escherichia coli and related bacteria p 194\u2013195. Cold Spring Harbor Laboratory Press Cold Spring Harbor NY."},{"key":"e_1_3_2_51_2","doi-asserted-by":"crossref","first-page":"12741","DOI":"10.1074\/jbc.M700575200","article-title":"DNA polymerase V allows bypass of toxic guanine oxidation products in vivo","volume":"282","author":"Neely WL","year":"2007","unstructured":"NeelyWL. 2007. DNA polymerase V allows bypass of toxic guanine oxidation products in vivo. J. Biol. Chem. 282:12741\u201312748.","journal-title":"J. Biol. Chem."},{"key":"e_1_3_2_52_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.cell.2010.11.052"},{"key":"e_1_3_2_53_2","doi-asserted-by":"crossref","first-page":"431","DOI":"10.1007\/BF01612988","article-title":"Potentiation of cisplatin cytotoxicity by methylxanthines in vitro","volume":"116","author":"Petru E","year":"1990","unstructured":"PetruE BoikeG SevinBU. 1990. Potentiation of cisplatin cytotoxicity by methylxanthines in vitro. J. Cancer Res. Clin. Oncol. 116:431\u2013433.","journal-title":"J. Cancer Res. Clin. Oncol."},{"key":"e_1_3_2_54_2","doi-asserted-by":"publisher","DOI":"10.1038\/nrmicro1265"},{"key":"e_1_3_2_55_2","doi-asserted-by":"crossref","first-page":"173","DOI":"10.1093\/mutage\/5.2.173","article-title":"Induction of frameshift mutations by caffeine in Escherichia coli","volume":"5","author":"Pons FW","year":"1990","unstructured":"PonsFW M\u00fcllerP. 1990. Induction of frameshift mutations by caffeine in Escherichia coli. Mutagenesis 5:173\u2013177.","journal-title":"Mutagenesis"},{"key":"e_1_3_2_56_2","doi-asserted-by":"crossref","first-page":"1438","DOI":"10.1016\/S0021-9258(17)33759-6","article-title":"An endonuclease from Escherichia coli that introduces single polynucleotide chain scissions in ultraviolet-irradiated DNA","volume":"251","author":"Radman M","year":"1976","unstructured":"RadmanM. 1976. An endonuclease from Escherichia coli that introduces single polynucleotide chain scissions in ultraviolet-irradiated DNA. J. Biol. Chem. 251:1438\u20131445.","journal-title":"J. Biol. Chem."},{"key":"e_1_3_2_57_2","doi-asserted-by":"crossref","first-page":"31763","DOI":"10.1074\/jbc.274.45.31763","article-title":"The mutagenesis protein UmuC is a DNA polymerase activated by UmuD\u2032, RecA, and SSB, and specialized for translesion synthesis","volume":"274","author":"Reuven NB","year":"1999","unstructured":"ReuvenNB AradG Maor-ShoshaniA LivnehZ. 1999. The mutagenesis protein UmuC is a DNA polymerase activated by UmuD\u2032, RecA, and SSB, and specialized for translesion synthesis. J. Biol. Chem. 274:31763\u201331766.","journal-title":"J. Biol. Chem."},{"key":"e_1_3_2_58_2","doi-asserted-by":"publisher","DOI":"10.1021\/cr0204348"},{"key":"e_1_3_2_59_2","doi-asserted-by":"crossref","first-page":"237","DOI":"10.1016\/0014-5793(83)80077-5","article-title":"Mechanism of caffeine-induced inhibition of DNA synthesis in Escherichia coli","volume":"151","author":"Sandlie I","year":"1983","unstructured":"SandlieI LossiusI Sj\u00e5stadK KleppeK. 1983. Mechanism of caffeine-induced inhibition of DNA synthesis in Escherichia coli. FEBS Lett. 151:237\u2013242.","journal-title":"FEBS Lett."},{"key":"e_1_3_2_60_2","doi-asserted-by":"crossref","first-page":"26987","DOI":"10.1074\/jbc.M111100200","article-title":"1,N\n                  2-Ethenoguanine, a mutagenic DNA adduct, is a primary substrate of Escherichia coli mismatch-specific uracil-DNA glycosylase and human alkylpurine-DNA-N-glycosylase","volume":"277","author":"Saparbaev M","year":"2002","unstructured":"SaparbaevM. 2002. 1,N2-Ethenoguanine, a mutagenic DNA adduct, is a primary substrate of Escherichia coli mismatch-specific uracil-DNA glycosylase and human alkylpurine-DNA-N-glycosylase. J. Biol. Chem. 277:26987\u201326993.","journal-title":"J. Biol. Chem."},{"key":"e_1_3_2_61_2","doi-asserted-by":"crossref","first-page":"3522","DOI":"10.1073\/pnas.87.9.3522","article-title":"Molecular mechanisms of DNA repair inhibition by caffeine","volume":"87","author":"Selby CP","year":"1990","unstructured":"SelbyCP SancarA. 1990. Molecular mechanisms of DNA repair inhibition by caffeine. Proc. Natl. Acad. Sci. U. S. A. 87:3522\u20133525.","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"e_1_3_2_62_2","doi-asserted-by":"publisher","DOI":"10.1128\/mr.57.1.138-163.1993"},{"key":"e_1_3_2_63_2","doi-asserted-by":"crossref","first-page":"1997","DOI":"10.1073\/pnas.72.6.1997","article-title":"Endonucleolytic incision of X-irradiated deoxyribonucleic acid by extracts of Escherichia coli","volume":"72","author":"Strniste G","year":"1975","unstructured":"StrnisteG WallaceSS. 1975. Endonucleolytic incision of X-irradiated deoxyribonucleic acid by extracts of Escherichia coli. Proc. Natl. Acad. Sci. U. S. A. 72:1997\u20132001.","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"e_1_3_2_64_2","doi-asserted-by":"publisher","DOI":"10.1128\/JB.01982-07"},{"key":"e_1_3_2_65_2","doi-asserted-by":"crossref","first-page":"8919","DOI":"10.1073\/pnas.96.16.8919","article-title":"UmuD\u20322C is an error-prone DNA polymerase, Escherichia coli Pol V","volume":"96","author":"Tang M","year":"1999","unstructured":"TangM. 1999. UmuD\u20322C is an error-prone DNA polymerase, Escherichia coli Pol V. Proc. Natl. Acad. Sci. U. S. A. 96:8919\u20138924.","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"e_1_3_2_66_2","doi-asserted-by":"crossref","first-page":"112","DOI":"10.1016\/0167-4781(89)90138-3","article-title":"Studies on DNA binding of caffeine and derivatives: evidence of intercalation by DNA-unwinding experiments","volume":"1007","author":"Tornaletti S","year":"1989","unstructured":"TornalettiS RussoP ParodiS PedriniAM. 1989. Studies on DNA binding of caffeine and derivatives: evidence of intercalation by DNA-unwinding experiments. Biochim. Biophys. Acta 1007:112\u2013115.","journal-title":"Biochim. Biophys. Acta"},{"key":"e_1_3_2_67_2","doi-asserted-by":"publisher","DOI":"10.1016\/S1097-2765(00)80376-7"},{"key":"e_1_3_2_68_2","doi-asserted-by":"publisher","DOI":"10.1128\/AAC.01087-08"},{"key":"e_1_3_2_69_2","doi-asserted-by":"publisher","DOI":"10.1038\/msb.2009.92"},{"key":"e_1_3_2_70_2","doi-asserted-by":"publisher","DOI":"10.1038\/ng1755"},{"key":"e_1_3_2_71_2","doi-asserted-by":"crossref","first-page":"879","DOI":"10.1038\/nature04561","article-title":"Crystal structure of catalytic complexes of the oxidative DNA\/RNA repair enzyme AlkB","volume":"439","author":"Yu B","year":"2006","unstructured":"YuB. 2006. Crystal structure of catalytic complexes of the oxidative DNA\/RNA repair enzyme AlkB. Nature 439:879\u2013884.","journal-title":"Nature"},{"key":"e_1_3_2_72_2","doi-asserted-by":"publisher","DOI":"10.1093\/nar\/gkp057"}],"container-title":["Antimicrobial Agents and Chemotherapy"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/journals.asm.org\/doi\/pdf\/10.1128\/AAC.00066-12","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/journals.asm.org\/doi\/pdf\/10.1128\/AAC.00066-12","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,2,21]],"date-time":"2022-02-21T22:14:30Z","timestamp":1645481670000},"score":1,"resource":{"primary":{"URL":"https:\/\/journals.asm.org\/doi\/10.1128\/AAC.00066-12"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2012,6]]},"references-count":71,"journal-issue":{"issue":"6","published-print":{"date-parts":[[2012,6]]}},"alternative-id":["10.1128\/AAC.00066-12"],"URL":"https:\/\/doi.org\/10.1128\/aac.00066-12","relation":{},"ISSN":["0066-4804","1098-6596"],"issn-type":[{"value":"0066-4804","type":"print"},{"value":"1098-6596","type":"electronic"}],"subject":[],"published":{"date-parts":[[2012,6]]},"assertion":[{"value":"2012-01-12","order":0,"name":"received","label":"Received","group":{"name":"publication_history","label":"Publication History"}},{"value":"2012-02-22","order":1,"name":"accepted","label":"Accepted","group":{"name":"publication_history","label":"Publication History"}},{"value":"2012-05-13","order":2,"name":"published","label":"Published","group":{"name":"publication_history","label":"Publication History"}}]}}