Steady-state, pre-steady-state, and single-turnover kinetic measurement for DNA glycosylase activity. - Wikidata - awgldk - TriplyDB

Steady-state, pre-steady-state, and single-turnover kinetic measurement for DNA glycosylase activity.

Steady-state, pre-steady-state, and single-turnover kinetic measurement for DNA glycosylase activity.

http://www.wikidata.org/entity/Q37375102

about

Base excision repair of tandem modifications in a methylated CpG dinucleotide.Enzyme characteristics of pathogen-specific trehalose-6-phosphate phosphatases Mammalian Base Excision Repair: Functional Partnership between PARP-1 and APE1 in AP-Site Repair.Roles of Residues Arg-61 and Gln-38 of Human DNA Polymerase η in Bypass of Deoxyguanosine and 7,8-Dihydro-8-oxo-2'-deoxyguanosine.Pre-Steady-State Kinetic Analysis of Single-Nucleotide Incorporation by DNA Polymerases Biochemical Characterization of AP Lyase and m6A Demethylase Activities of Human AlkB Homologue 1 (ALKBH1).Impact of Ribonucleotide Backbone on Translesion Synthesis and Repair of 7,8-Dihydro-8-oxoguanine.

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Steady-state, pre-steady-state, and single-turnover kinetic measurement for DNA glycosylase activity.

http://www.wikidata.org/entity/Q37375102

description

article científic

@ca

article scientifique

@fr

articolo scientifico

@it

artigo científico

@pt

bilimsel makale

@tr

scientific article published on 19 August 2013

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

Steady-state, pre-steady-state ...... for DNA glycosylase activity.

@en

Steady-state, pre-steady-state ...... for DNA glycosylase activity.

@nl

type

label

Steady-state, pre-steady-state ...... for DNA glycosylase activity.

@en

Steady-state, pre-steady-state ...... for DNA glycosylase activity.

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prefLabel

Steady-state, pre-steady-state ...... for DNA glycosylase activity.

@en

Steady-state, pre-steady-state ...... for DNA glycosylase activity.

@nl

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Journal of Visualized Experiments

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Steady-state, pre-steady-state ...... for DNA glycosylase activity.

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Akira Sassa

http://www.w3.org/2001/XMLSchema#string

David D Shock

http://www.w3.org/2001/XMLSchema#string

Samuel H Wilson

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William A Beard

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P2860

Calculation of protein extinction coefficients from amino acid sequence data

Stimulation of DNA glycosylase activity of OGG1 by NEIL1: functional collaboration between two human DNA glycosylases

Excision of deaminated cytosine from the vertebrate genome: role of the SMUG1 uracil-DNA glycosylase

Stimulation of human 8-oxoguanine-DNA glycosylase by AP-endonuclease: potential coordination of the initial steps in base excision repair

DNA structure and aspartate 276 influence nucleotide binding to human DNA polymerase beta. Implication for the identity of the rate-limiting conformational change.

Mutation versus repair: NEIL1 removal of hydantoin lesions in single-stranded, bulge, bubble, and duplex DNA contexts.

Incidence and persistence of 8-oxo-7,8-dihydroguanine within a hairpin intermediate exacerbates a toxic oxidation cycle associated with trinucleotide repeat expansion

DNA sequence context effects on the glycosylase activity of human 8-oxoguanine DNA glycosylase.

Efficient removal of formamidopyrimidines by 8-oxoguanine glycosylases.

Clostridium acetobutylicum 8-oxoguanine DNA glycosylase (Ogg) differs from eukaryotic Oggs with respect to opposite base discrimination

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e50695

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scholarly article

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10.3791/50695

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78

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2013-08-19T00:00:00Z

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23995844

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3855924

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