Mutation versus repair: NEIL1 removal of hydantoin lesions in single-stranded, bulge, bubble, and duplex DNA contexts.
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The current state of eukaryotic DNA base damage and repairThe Fpg/Nei family of DNA glycosylases: substrates, structures, and search for damageBase excision repair and cancerSubstitution of Ala for Tyr567 in RB69 DNA Polymerase Allows dAMP and dGMP To Be Inserted opposite Guanidinohydantoin,Structural Characterization of a Mouse Ortholog of Human NEIL3 with a Marked Preference for Single-Stranded DNAStructural investigation of a viral ortholog of human NEIL2/3 DNA glycosylasesGenome and cancer single nucleotide polymorphisms of the human NEIL1 DNA glycosylase: Activity, structure, and the effect of editingCrystal Structure of DNA Polymerase β with DNA Containing the Base Lesion Spiroiminodihydantoin in a Templating PositionBase excision repairThermodynamic profiles and nuclear magnetic resonance studies of oligonucleotide duplexes containing single diastereomeric spiroiminodihydantoin lesions.Reconciliation of chemical, enzymatic, spectroscopic and computational data to assign the absolute configuration of the DNA base lesion spiroiminodihydantoin.New insights in the removal of the hydantoins, oxidation product of pyrimidines, via the base excision and nucleotide incision repair pathways.Destabilization of the PCNA trimer mediated by its interaction with the NEIL1 DNA glycosylaseHuman base excision repair creates a bias toward -1 frameshift mutationsEffect of the multifunctional proteins RPA, YB-1, and XPC repair factor on AP site cleavage by DNA glycosylase NEIL1.Recent advances in the structural mechanisms of DNA glycosylasesPrereplicative repair of oxidized bases in the human genome is mediated by NEIL1 DNA glycosylase together with replication proteins.RNA editing changes the lesion specificity for the DNA repair enzyme NEIL1Probing the DNA structural requirements for facilitated diffusion.New paradigms in the repair of oxidative damage in human genome: mechanisms ensuring repair of mutagenic base lesions during replication and involvement of accessory proteins.Base and Nucleotide Excision Repair of Oxidatively Generated Guanine Lesions in DNA.Phosphorylation Sites Identified in the NEIL1 DNA Glycosylase Are Potential Targets for the JNK1 Kinase.Thermodynamic consequences of the hyperoxidized guanine lesion guanidinohydantoin in duplex DNApH-Dependent Equilibrium between 5-Guanidinohydantoin and Iminoallantoin Affects Nucleotide Insertion Opposite the DNA Lesion.Guanine oxidation product 5-carboxamido-5-formamido-2-iminohydantoin induces mutations when bypassed by DNA polymerases and is a substrate for base excision repair.Neil3, the final frontier for the DNA glycosylases that recognize oxidative damage.Klenow Fragment Discriminates against the Incorporation of the Hyperoxidized dGTP Lesion Spiroiminodihydantoin into DNA.Tautomerization-dependent recognition and excision of oxidation damage in base-excision DNA repair.Steady-state, pre-steady-state, and single-turnover kinetic measurement for DNA glycosylase activity.Repair of hydantoin lesions and their amine adducts in DNA by base and nucleotide excision repair.Endonuclease and Exonuclease Activities on Oligodeoxynucleotides Containing Spiroiminodihydantoin Depend on the Sequence Context and the Lesion Stereochemistry.Cockayne Syndrome group B protein stimulates NEIL2 DNA glycosylase activity.Base Excision Repair of N6-Deoxyadenosine Adducts of 1,3-Butadiene.A chemical and kinetic perspective on base excision repair of DNA.Removal of oxidatively generated DNA damage by overlapping repair pathways.Formation and processing of DNA damage substrates for the hNEIL enzymes.G-quadruplex folds of the human telomere sequence alter the site reactivity and reaction pathway of guanine oxidation compared to duplex DNA.Structural context effects in the oxidation of 8-oxo-7,8-dihydro-2'-deoxyguanosine to hydantoin products: electrostatics, base stacking, and base pairingVisualizing the Search for Radiation-damaged DNA Bases in Real Time.8-Oxo-7,8-dihydro-2'-deoxyguanosine and abasic site tandem lesions are oxidation prone yielding hydantoin products that strongly destabilize duplex DNA.
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P2860
Mutation versus repair: NEIL1 removal of hydantoin lesions in single-stranded, bulge, bubble, and duplex DNA contexts.
description
2010 nî lūn-bûn
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2010 թուականի Մարտին հրատարակուած գիտական յօդուած
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2010 թվականի մարտին հրատարակված գիտական հոդված
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2010年の論文
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2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
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2010年论文
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name
Mutation versus repair: NEIL1 ...... bble, and duplex DNA contexts.
@ast
Mutation versus repair: NEIL1 ...... bble, and duplex DNA contexts.
@en
type
label
Mutation versus repair: NEIL1 ...... bble, and duplex DNA contexts.
@ast
Mutation versus repair: NEIL1 ...... bble, and duplex DNA contexts.
@en
prefLabel
Mutation versus repair: NEIL1 ...... bble, and duplex DNA contexts.
@ast
Mutation versus repair: NEIL1 ...... bble, and duplex DNA contexts.
@en
P2093
P2860
P356
P1433
P1476
Mutation versus repair: NEIL1 ...... bble, and duplex DNA contexts.
@en
P2093
Cynthia J Burrows
Nirmala Krishnamurthy
Sheila S David
Xiaobei Zhao
P2860
P304
P356
10.1021/BI901852Q
P407
P577
2010-03-01T00:00:00Z