DNA containing a chemically reduced apurinic site is a high affinity ligand for the E. coli formamidopyrimidine-DNA glycosylase
about
Crystal structure of a repair enzyme of oxidatively damaged DNA, MutM (Fpg), from an extreme thermophile, Thermus thermophilus HB8Structural insights into abasic site for Fpg specific binding and catalysis: comparative high-resolution crystallographic studies of Fpg bound to various models of abasic site analogues-containing DNAStructural Characterization of a Mouse Ortholog of Human NEIL3 with a Marked Preference for Single-Stranded DNAThe oxidative DNA glycosylases of Mycobacterium tuberculosis exhibit different substrate preferences from their Escherichia coli counterpartsCloning and characterization of a mammalian 8-oxoguanine DNA glycosylaseStimulation of human 8-oxoguanine-DNA glycosylase by AP-endonuclease: potential coordination of the initial steps in base excision repairRecent progress in the biology, chemistry and structural biology of DNA glycosylases.The Ogg1 protein of Saccharomyces cerevisiae: a 7,8-dihydro-8-oxoguanine DNA glycosylase/AP lyase whose lysine 241 is a critical residue for catalytic activityInteraction of the recombinant human methylpurine-DNA glycosylase (MPG protein) with oligodeoxyribonucleotides containing either hypoxanthine or abasic sites.Enzymic removal of 5-methylcytosine from DNA by a human DNA-glycosylase.Escherichia coli endonuclease VIII: cloning, sequencing, and overexpression of the nei structural gene and characterization of nei and nei nth mutantsA continuous hyperchromicity assay to characterize the kinetics and thermodynamics of DNA lesion recognition and base excisionCatalytic and DNA-binding properties of the human Ogg1 DNA N-glycosylase/AP lyase: biochemical exploration of H270, Q315 and F319, three amino acids of the 8-oxoguanine-binding pocket.ROS1 5-methylcytosine DNA glycosylase is a slow-turnover catalyst that initiates DNA demethylation in a distributive fashion.Recognition of base J in duplex DNA by J-binding protein.HU protein of Escherichia coli binds specifically to DNA that contains single-strand breaks or gaps.High resolution characterization of formamidopyrimidine-DNA glycosylase interaction with its substrate by chemical cross-linking and mass spectrometry using substrate analogs.Role of the N-terminal proline residue in the catalytic activities of the Escherichia coli Fpg protein.Cleavage and binding of a DNA fragment containing a single 8-oxoguanine by wild type and mutant FPG proteins.Structural requirements of double and single stranded DNA substrates and inhibitors, including a photoaffinity label, of Fpg protein from Escherichia coli.The catalytic mechanism of a pyrimidine dimer-specific glycosylase (pdg)/abasic lyase, Chlorella virus-pdg.Thermodynamic, kinetic and structural basis for recognition and repair of abasic sites in DNA by apurinic/apyrimidinic endonuclease from human placenta.Specific binding of a designed pyrrolidine abasic site analog to multiple DNA glycosylases.Excision of 8-oxoguanine within clustered damage by the yeast OGG1 protein.Zinc finger oxidation of Fpg/Nei DNA glycosylases by 2-thioxanthine: biochemical and X-ray structural characterization.AP site structural determinants for Fpg specific recognitionDNA-Templated Synthesis of Perylenediimide Stacks Utilizing Abasic Sites as Binding Pockets and Reactive Sites.
P2860
Q24630698-6279D490-0A3B-4981-BBE3-59B4AC7763ABQ24816127-019B81A3-8A86-4F46-AE92-BFE51A469105Q27675877-BCF4C3ED-4B31-4A71-B80E-1677B9E04A47Q28487547-72AF9826-DEE1-493F-ACB4-55D146D2C5CBQ28507243-8BCB7314-8A50-482D-9B5D-14512EB6B9A4Q28645611-21860A86-A0F2-4EFF-BF2C-CB125686B2DCQ32063493-5324659C-9B44-4C7C-AAF2-616D598759F8Q34633314-8478D209-A6B3-4E05-8641-B29CC201ADD8Q34674798-DD9944F2-AC56-4C95-A3A2-69EA1D81F546Q35018540-FA0E829A-DF77-4A59-ACEB-7F66ACB503D9Q35624116-D16F0291-CB2A-4156-89C6-3AB8D3AC14C4Q36423601-3A78EA70-8BC4-48F8-94BF-19F34015245DQ37070265-14ADDCEB-CCBD-4165-8D39-654F3B617174Q37273644-5268C85E-7866-41CC-8678-6FD65345399BQ38294915-03C44C99-BA5B-41A1-B724-4D20CFEDF4F0Q38296278-E4EAD147-1457-47F6-B172-2F90C97754A2Q38310377-F600EF73-82E1-4AC9-A394-B7D085513005Q38313827-0837BB43-AA1C-4840-B1A4-6FAB4E8CDB9EQ38318188-21B8D9D0-4E47-4B02-97AF-CF5E1F0841D1Q38318406-AB585A4D-4AE5-463A-AB5D-EAD303FDA9BDQ38326710-237F17E8-4CD7-4F0C-9BC0-C0035CE1E050Q38335880-A4C432FF-3E1B-4B13-B104-F808099C1A8DQ38337800-0009C7E9-65C9-440A-BC41-13B51347095FQ38660216-E701A16E-FB3B-4746-A014-BC7D06C1AA1BQ39142123-E21899DA-37FD-4435-8C05-D91F48F3053AQ39726837-C8D8B45E-405C-4A74-88CF-64A35C161D07Q51138772-D796C361-F794-4D49-85F4-AA69A277EDB8
P2860
DNA containing a chemically reduced apurinic site is a high affinity ligand for the E. coli formamidopyrimidine-DNA glycosylase
description
1992 nî lūn-bûn
@nan
1992 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
1992 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
1992年の論文
@ja
1992年論文
@yue
1992年論文
@zh-hant
1992年論文
@zh-hk
1992年論文
@zh-mo
1992年論文
@zh-tw
1992年论文
@wuu
name
DNA containing a chemically re ...... midopyrimidine-DNA glycosylase
@ast
DNA containing a chemically re ...... midopyrimidine-DNA glycosylase
@en
type
label
DNA containing a chemically re ...... midopyrimidine-DNA glycosylase
@ast
DNA containing a chemically re ...... midopyrimidine-DNA glycosylase
@en
prefLabel
DNA containing a chemically re ...... midopyrimidine-DNA glycosylase
@ast
DNA containing a chemically re ...... midopyrimidine-DNA glycosylase
@en
P2093
P2860
P356
P1476
DNA containing a chemically re ...... midopyrimidine-DNA glycosylase
@en
P2093
P2860
P304
P356
10.1093/NAR/20.3.389
P407
P577
1992-02-01T00:00:00Z