Structural analysis of an Escherichia coli endonuclease VIII covalent reaction intermediate.
about
Human DNA glycosylases of the bacterial Fpg/MutM superfamily: an alternative pathway for the repair of 8-oxoguanine and other oxidation products in DNACrystal structure of the Lactococcus lactis formamidopyrimidine-DNA glycosylase bound to an abasic site analogue-containing DNA.Acetylation of the human DNA glycosylase NEIL2 and inhibition of its activityThe crystal structure of human endonuclease VIII-like 1 (NEIL1) reveals a zincless finger motif required for glycosylase activityEarly steps in the DNA base excision/single-strand interruption repair pathway in mammalian cellsStructure of the uncomplexed DNA repair enzyme endonuclease VIII indicates significant interdomain flexibility.NEIL1 excises 3' end proximal oxidative DNA lesions resistant to cleavage by NTH1 and OGG1.Repair of oxidative DNA damage and cancer: recent progress in DNA base excision repairDNA glycosylases: in DNA repair and beyondThe Fpg/Nei family of DNA glycosylases: substrates, structures, and search for damageStructure of formamidopyrimidine-DNA glycosylase covalently complexed to DNAStructure of the topoisomerase VI-B subunit: implications for type II topoisomerase mechanism and evolution.Structure of a trapped endonuclease III-DNA covalent intermediateDNA lesion recognition by the bacterial repair enzyme MutMStructure of the E. coli DNA Glycosylase AlkA Bound to the Ends of Duplex DNA: A System for the Structure Determination of Lesion-Containing DNAStructural Characterization of a Viral NEIL1 Ortholog Unliganded and Bound to Abasic Site-containing DNAStructural and biochemical studies of a plant formamidopyrimidine-DNA glycosylase reveal why eukaryotic Fpg glycosylases do not excise 8-oxoguanineSculpting of DNA at Abasic Sites by DNA Glycosylase Homolog Mag2Structural Characterization of a Mouse Ortholog of Human NEIL3 with a Marked Preference for Single-Stranded DNAStructural Characterization of Viral Ortholog of Human DNA Glycosylase NEIL1 Bound to Thymine Glycol or 5-Hydroxyuracil-containing DNAA novel nucleoid-associated protein specific to the actinobacteriaStructural investigation of a viral ortholog of human NEIL2/3 DNA glycosylasesRepair of oxidized bases in DNA bubble structures by human DNA glycosylases NEIL1 and NEIL2Differential specificity of human and Escherichia coli endonuclease III and VIII homologues for oxidative base lesionsIdentification of a zinc finger domain in the human NEIL2 (Nei-like-2) proteinThe oxidative DNA glycosylases of Mycobacterium tuberculosis exhibit different substrate preferences from their Escherichia coli counterpartsInsights into the glycosylase search for damage from single-molecule fluorescence microscopy.Using shifts in amino acid frequency and substitution rate to identify latent structural characters in base-excision repair enzymesTwo glycosylase families diffusively scan DNA using a wedge residue to probe for and identify oxidatively damaged bases.Non-specific DNA binding interferes with the efficient excision of oxidative lesions from chromatin by the human DNA glycosylase, NEIL1.A highly conserved family of domains related to the DNA-glycosylase fold helps predict multiple novel pathways for RNA modificationsRequirements for 5'dRP/AP lyase activity in Ku.Recent advances in the structural mechanisms of DNA glycosylasesActive destabilization of base pairs by a DNA glycosylase wedge initiates damage recognitionLesion search and recognition by thymine DNA glycosylase revealed by single molecule imaging.New environment-sensitive multichannel DNA fluorescent label for investigation of the protein-DNA interactionsSingle Qdot-labeled glycosylase molecules use a wedge amino acid to probe for lesions while scanning along DNAModulation of the turnover of formamidopyrimidine DNA glycosylase.Simple sequence repeats in prokaryotic genomesOxidatively Generated Guanine(C8)-Thymine(N3) Intrastrand Cross-links in Double-stranded DNA Are Repaired by Base Excision Repair Pathways.
P2860
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P2860
Structural analysis of an Escherichia coli endonuclease VIII covalent reaction intermediate.
description
2002 nî lūn-bûn
@nan
2002 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
name
Structural analysis of an Esch ...... covalent reaction intermediate
@nl
Structural analysis of an Esch ...... ovalent reaction intermediate.
@ast
Structural analysis of an Esch ...... ovalent reaction intermediate.
@en
Structural analysis of an Esch ...... ovalent reaction intermediate.
@en-gb
type
label
Structural analysis of an Esch ...... covalent reaction intermediate
@nl
Structural analysis of an Esch ...... ovalent reaction intermediate.
@ast
Structural analysis of an Esch ...... ovalent reaction intermediate.
@en
Structural analysis of an Esch ...... ovalent reaction intermediate.
@en-gb
prefLabel
Structural analysis of an Esch ...... covalent reaction intermediate
@nl
Structural analysis of an Esch ...... ovalent reaction intermediate.
@ast
Structural analysis of an Esch ...... ovalent reaction intermediate.
@en
Structural analysis of an Esch ...... ovalent reaction intermediate.
@en-gb
P2093
P2860
P356
P1433
P1476
Structural analysis of an Esch ...... ovalent reaction intermediate.
@en
P2093
Andrea S Fernandes
Arthur P Grollman
Dmitry O Zharkov
Gali Golan
Gil Shoham
Jadwiga H Kycia
Robert A Rieger
Rotem Gilboa
Sue Ellen Gerchman
P2860
P304
P356
10.1093/EMBOJ/21.4.789
P407
P577
2002-02-01T00:00:00Z