Adaptation to alkylation resistance involves the induction of a DNA glycosylase.
about
Repair deficient mice reveal mABH2 as the primary oxidative demethylase for repairing 1meA and 3meC lesions in DNABiochemical characterization and DNA repair pathway interactions of Mag1-mediated base excision repair in Schizosaccharomyces pombeSynthesis and Structure of Duplex DNA Containing the Genotoxic Nucleobase Lesion N7-MethylguanineStructure of Escherichia coli AlkA in Complex with Undamaged DNAFlavin-Induced Oligomerization in Escherichia coli Adaptive Response Protein AidBTransition-state destabilization reveals how human DNA polymerase β proceeds across the chemically unstable lesion N7-methylguanineCloning and expression in Escherichia coli of a gene for an alkylbase DNA glycosylase from Saccharomyces cerevisiae; a homologue to the bacterial alkA gene.Cloning a eukaryotic DNA glycosylase repair gene by the suppression of a DNA repair defect in Escherichia coli.Saccharomyces cerevisiae 3-methyladenine DNA glycosylase has homology to the AlkA glycosylase of E. coli and is induced in response to DNA alkylation damage.Molecular cloning and functional analysis of a human cDNA encoding an Escherichia coli AlkB homolog, a protein involved in DNA alkylation damage repairIncreased spontaneous mutation and alkylation sensitivity of Escherichia coli strains lacking the ogt O6-methylguanine DNA repair methyltransferaseAmplified expression of the tag+ and alkA+ genes in Escherichia coli: identification of gene products and effects on alkylation resistanceExcision of hypoxanthine from DNA containing dIMP residues by the Escherichia coli, yeast, rat, and human alkylpurine DNA glycosylasesA new protein superfamily includes two novel 3-methyladenine DNA glycosylases from Bacillus cereus, AlkC and AlkD.Systems based mapping demonstrates that recovery from alkylation damage requires DNA repair, RNA processing, and translation associated networks.A second DNA methyltransferase repair enzyme in Escherichia coli.Chemical biology of mutagenesis and DNA repair: cellular responses to DNA alkylationLinkage map of Escherichia coli K-12, edition 7.Schizosaccharomyces pombe Swi1, Swi3, and Hsk1 are components of a novel S-phase response pathway to alkylation damage.Radioadaptive response: responses to the five questions.Complementation of sensitivity to alkylating agents in Escherichia coli and Chinese hamster ovary cells by expression of a cloned bacterial DNA repair gene.Release of normal bases from intact DNA by a native DNA repair enzyme.3-Methyladenine residues in DNA induce the SOS function sfiA in Escherichia coli.Imbalanced base excision repair increases spontaneous mutation and alkylation sensitivity in Escherichia coli.Interplay between base excision repair activity and toxicity of 3-methyladenine DNA glycosylases in an E. coli complementation systemDNA polymerase α (swi7) and the flap endonuclease Fen1 (rad2) act together in the S-phase alkylation damage response in S. pombe.Loss of an apurinic/apyrimidinic site endonuclease increases the mutagenicity of N-methyl-N'-nitro-N-nitrosoguanidine to Escherichia coli.Kinetic mechanism for the flipping and excision of 1,N(6)-ethenoadenine by AlkA.Cloning of a 3-methyladenine-DNA glycosylase from Arabidopsis thalianaAdaptive response of Micrococcus luteus to alkylating chemicals.Chemical adaptation of M. luteus induces repair functions for O-alkylated DNA pyrimidines.Alteration of lysine 178 in the hinge region of the Escherichia coli ada protein interferes with activation of ada, but not alkA, transcription.Suppression of Escherichia coli alkB mutants by Saccharomyces cerevisiae genes.Induction of S.cerevisiae MAG 3-methyladenine DNA glycosylase transcript levels in response to DNA damage.The Ada protein acts as both a positive and a negative modulator of Escherichia coli's response to methylating agents.Repair-deficient 3-methyladenine DNA glycosylase homozygous mutant mouse cells have increased sensitivity to alkylation-induced chromosome damage and cell killing.Molecular cloning and characterization of a genetic region from Serratia marcescens involved in DNA repair.Alternative pathways for the in vivo repair of O6-alkylguanine and O4-alkylthymine in Escherichia coli: the adaptive response and nucleotide excision repair.Ring-opened 7-methylguanine residues in DNA are a block to in vitro DNA synthesis.Cross-Talk between Carbon Metabolism and the DNA Damage Response in S. cerevisiae.
P2860
Q24544017-38D6D30F-64C7-413B-AC18-6220C1220ED9Q24556623-A543D033-D485-4303-A0A7-03039FD8247FQ27651448-97044BE6-0A98-4856-9345-B8A66EA33DFBQ27664515-F7A73B54-A4DA-4E7F-90C9-F6A889248579Q27675105-FCB9AC61-E41C-4AD3-AD13-F36D288981B0Q27684466-2B7467BA-068E-4144-A293-BBFF22DD48B0Q27935462-0C634352-3F18-4EA4-BAD7-ECB85B92DF7BQ27937308-BDC98C7B-92BF-488E-A4E0-E740B126EFFAQ27938394-FA68701C-CAAF-4025-8B6B-397AAB358296Q28116035-96A2F50B-DC37-4054-B5C1-22A600436E95Q28268090-B8025ACE-DBCA-4CE8-A22D-634B8E67ADB7Q28493053-2228BEEC-F01A-46FE-A0A4-703B882C437DQ28610597-70DC6619-A5F5-4593-A314-44B3092B5E6CQ30807594-F9B1952B-8A37-42EE-AD75-97D35E298A71Q33372645-3CF3506E-17FB-4D02-AEFD-5109FD4C0E23Q33570243-BB832F45-7CBA-4D50-BB32-46064703853BQ33575712-64022FBE-93DC-454B-86F4-81A4F55E1950Q33627756-2ABBDD22-E6A8-4331-AEDE-4FB17D0ABDC6Q33707715-FA6DAED0-4DB4-4926-A988-15761EF1AD1AQ33715991-17F7A348-4126-4051-A7B8-9BA3BD38DBB2Q33880958-49CE6485-5CF0-4073-9FD7-46458B829736Q33888049-3DA65375-1F6F-432B-BE81-8F65B23A33FAQ33940054-0B53AB98-E628-4DB3-BBA7-C3B79F7FA57BQ33993117-CF416E1E-B947-405A-A274-98D73CB16E5AQ34332668-D1D20404-6AB8-4035-86F7-16244EE9266BQ34447883-C055E9BB-3CBB-4332-B0B1-6B52DD92BEAAQ34619157-CEFE31B5-5AD7-4A4C-8A0A-F698C6A19738Q35027137-5099F017-887E-4EDC-A707-9712BB5B796BQ35101884-4754D43E-2853-4B39-B385-76BBEF132180Q35266983-8D22430C-A96C-4E83-B6C8-D2E4D2BF920DQ35562002-6B1AD3AE-C3E4-4B98-9B7B-46B86DEADE00Q35580334-39040A65-7184-4CDD-B60C-EF34B9BF6A28Q35593508-864DE88F-23E4-483D-8582-E8FABF5785B4Q35795438-94D3AECA-C6FD-4731-98AF-FE33AE0F775AQ35809531-05D5DEBD-6C74-45B5-99F1-0F12DDBFF4C9Q35853590-320113F7-3148-431D-B278-2B8072C3872BQ35873674-AE9D6477-8D08-4AB7-B238-B28F7606756BQ35985879-8BE8A17E-E06B-497D-97A6-CD2884EDCA1CQ36011520-506B746E-7D00-4A3A-A0D1-73F6303577C5Q36090408-92F1CA66-E3F8-4FFA-9694-FD3C0976E1E8
P2860
Adaptation to alkylation resistance involves the induction of a DNA glycosylase.
description
1982 nî lūn-bûn
@nan
1982 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
1982 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
1982年の論文
@ja
1982年論文
@yue
1982年論文
@zh-hant
1982年論文
@zh-hk
1982年論文
@zh-mo
1982年論文
@zh-tw
1982年论文
@wuu
name
Adaptation to alkylation resistance involves the induction of a DNA glycosylase.
@ast
Adaptation to alkylation resistance involves the induction of a DNA glycosylase.
@en
Adaptation to alkylation resistance involves the induction of a DNA glycosylase.
@nl
type
label
Adaptation to alkylation resistance involves the induction of a DNA glycosylase.
@ast
Adaptation to alkylation resistance involves the induction of a DNA glycosylase.
@en
Adaptation to alkylation resistance involves the induction of a DNA glycosylase.
@nl
prefLabel
Adaptation to alkylation resistance involves the induction of a DNA glycosylase.
@ast
Adaptation to alkylation resistance involves the induction of a DNA glycosylase.
@en
Adaptation to alkylation resistance involves the induction of a DNA glycosylase.
@nl
P356
P1433
P1476
Adaptation to alkylation resistance involves the induction of a DNA glycosylase.
@en
P2093
P2888
P304
P356
10.1038/296773A0
P407
P577
1982-04-01T00:00:00Z
P6179
1024527273