1,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.
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Mitochondrial DNA damage and its consequences for mitochondrial gene expressionOxanine DNA glycosylase activity from Mammalian alkyladenine glycosylaseDifferential effects of reactive nitrogen species on DNA base excision repair initiated by the alkyladenine DNA glycosylaseRecognition and processing of a new repertoire of DNA substrates by human 3-methyladenine DNA glycosylase (AAG).Substrate binding pocket residues of human alkyladenine-DNA glycosylase critical for methylating agent survivalChemical biology of mutagenesis and DNA repair: cellular responses to DNA alkylationRecent advances in the structural mechanisms of DNA glycosylasesIdentification of Escherichia coli mismatch-specific uracil DNA glycosylase as a robust xanthine DNA glycosylase.Formation and repair of tobacco carcinogen-derived bulky DNA adductsBase excision repair and lesion-dependent subpathways for repair of oxidative DNA damage.Translesion synthesis across 1,N2-ethenoguanine by human DNA polymerases.A structural determinant in the uracil DNA glycosylase superfamily for the removal of uracil from adenine/uracil base pairsDifferential repair of etheno-DNA adducts by bacterial and human AlkB proteinsThe 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.DNA repair is indispensable for survival after acute inflammation.7,8-Dihydro-8-oxoadenine, a highly mutagenic adduct, is repaired by Escherichia coli and human mismatch-specific uracil/thymine-DNA glycosylases.Discrimination of lesion removal of N-methylpurine-DNA glycosylase revealed by a potent neutralizing monoclonal antibody.An 8-oxo-guanine repair pathway coordinated by MUTYH glycosylase and DNA polymerase lambda.Chemistry and biology of DNA containing 1,N(2)-deoxyguanosine adducts of the alpha,beta-unsaturated aldehydes acrolein, crotonaldehyde, and 4-hydroxynonenal.Analysis of DNA adducts in human samples: acrolein-derived exocyclic DNA adducts as an example.Chemistry and structural biology of DNA damage and biological consequencesDamage of DNA and proteins by major lipid peroxidation products in genome stability.The formation of catalytically competent enzyme-substrate complex is not a bottleneck in lesion excision by human alkyladenine DNA glycosylase.N-terminal extension of N-methylpurine DNA glycosylase is required for turnover in hypoxanthine excision reaction.DNA adduct bypass polymerization by Sulfolobus solfataricus DNA polymerase Dpo4: analysis and crystal structures of multiple base pair substitution and frameshift products with the adduct 1,N2-ethenoguanine.Excised damaged base determines the turnover of human N-methylpurine-DNA glycosylaseThe major human AP endonuclease (Ape1) is involved in the nucleotide incision repair pathway.2'-deoxyribonolactone lesion produces G->A transitions in Escherichia coli.Oxidation and glycolytic cleavage of etheno and propano DNA base adducts.Transcription processing at 1,N2-ethenoguanine by human RNA polymerase II and bacteriophage T7 RNA polymeraseExpression, purification and characterization of codon-optimized human N-methylpurine-DNA glycosylase from Escherichia coli.Differential modes of DNA binding by mismatch uracil DNA glycosylase from Escherichia coli: implications for abasic lesion processing and enzyme communication in the base excision repair pathwayStructure of the 1,N2-etheno-2'-deoxyguanosine adduct in duplex DNA at pH 8.6.Hijacking of the human alkyl-N-purine-DNA glycosylase by 3,N4-ethenocytosine, a lipid peroxidation-induced DNA adduct.Structure of the 1,N2-ethenodeoxyguanosine adduct opposite cytosine in duplex DNA: Hoogsteen base pairing at pH 5.2.Mismatch uracil glycosylase from Escherichia coli: a general mismatch or a specific DNA glycosylase?The crystal structure of mismatch-specific uracil-DNA glycosylase (MUG) from Deinococcus radiodurans reveals a novel catalytic residue and broad substrate specificity.Non-bulky Lesions in Human DNA: the Ways of Formation, Repair, and Replication.
P2860
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P2860
1,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.
description
2002 nî lūn-bûn
@nan
2002年の論文
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2002年学术文章
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2002年学术文章
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2002年学术文章
@zh-hans
2002年学术文章
@zh-my
2002年学术文章
@zh-sg
2002年學術文章
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2002年學術文章
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2002年學術文章
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name
1,N(2)-ethenoguanine, a mutage ...... alkylpurine-DNA-N-glycosylase.
@en
type
label
1,N(2)-ethenoguanine, a mutage ...... alkylpurine-DNA-N-glycosylase.
@en
prefLabel
1,N(2)-ethenoguanine, a mutage ...... alkylpurine-DNA-N-glycosylase.
@en
P2093
P2860
P356
P1476
1,N(2)-ethenoguanine, a mutage ...... alkylpurine-DNA-N-glycosylase.
@en
P2093
Cyril V Privezentzev
F Peter Guengerich
Hongliang Cai
Jacques Laval
Murat Saparbaev
Rhoderick H Elder
Sophie Langouët
P2860
P304
26987-26993
P356
10.1074/JBC.M111100200
P407
P577
2002-05-16T00:00:00Z