DNA lesion recognition by the bacterial repair enzyme MutM - Test2 - elhamkhani - TriplyDB

DNA lesion recognition by the bacterial repair enzyme MutM

DNA lesion recognition by the bacterial repair enzyme MutM

http://www.wikidata.org/entity/Q27642268

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The crystal structure of human endonuclease VIII-like 1 (NEIL1) reveals a zincless finger motif required for glycosylase activity Structure of the uncomplexed DNA repair enzyme endonuclease VIII indicates significant interdomain flexibility.Structural 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 DNA The Fpg/Nei family of DNA glycosylases: substrates, structures, and search for damage DNA damage recognition and repair by 3-methyladenine DNA glycosylase I (TAG)Structure of the E. coli DNA Glycosylase AlkA Bound to the Ends of Duplex DNA: A System for the Structure Determination of Lesion-Containing DNA Structural Characterization of a Viral NEIL1 Ortholog Unliganded and Bound to Abasic Site-containing DNA Structural and Dynamic Features of the MutT Protein in the Recognition of Nucleotides with the Mutagenic 8-Oxoguanine Base Entrapment and Structure of an Extrahelical Guanine Attempting to Enter the Active Site of a Bacterial DNA Glycosylase, MutM Encounter and extrusion of an intrahelical lesion by a DNA repair enzyme Structure of Escherichia coli AlkA in Complex with Undamaged DNA 5-Hydroxy-5-methylhydantoin DNA lesion, a molecular trap for DNA glycosylases Structural and biochemical studies of a plant formamidopyrimidine-DNA glycosylase reveal why eukaryotic Fpg glycosylases do not excise 8-oxoguanine Structural Characterization of a Mouse Ortholog of Human NEIL3 with a Marked Preference for Single-Stranded DNA Structural Characterization of Viral Ortholog of Human DNA Glycosylase NEIL1 Bound to Thymine Glycol or 5-Hydroxyuracil-containing DNA Structural and Biochemical Analysis of DNA Helix Invasion by the Bacterial 8-Oxoguanine DNA Glycosylase MutM Strandwise translocation of a DNA glycosylase on undamaged DNA Sequence-dependent Structural Variation in DNA Undergoing Intrahelical Inspection by the DNA glycosylase MutM NMR Structure of the S-Linked Glycopeptide Sublancin 168 Functional diversification of the RING finger and other binuclear treble clef domains in prokaryotes and the early evolution of the ubiquitin system Base-excision repair of oxidative DNA damage Insights 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 enzymes Biological properties of single chemical-DNA adducts: a twenty year perspective Two glycosylase families diffusively scan DNA using a wedge residue to probe for and identify oxidatively damaged bases.An Improved Reaction Coordinate for Nucleic Acid Base Flipping Studies.A highly conserved family of domains related to the DNA-glycosylase fold helps predict multiple novel pathways for RNA modifications Nucleosomes suppress the formation of double-strand DNA breaks during attempted base excision repair of clustered oxidative damages Analysis of an anomalous mutant of MutM DNA glycosylase leads to new insights into the catalytic mechanism.Recent advances in the structural mechanisms of DNA glycosylases RNA editing changes the lesion specificity for the DNA repair enzyme NEIL1 Molecular mechanics parameters for the FapydG DNA lesion Active destabilization of base pairs by a DNA glycosylase wedge initiates damage recognition A nucleobase lesion remodels the interaction of its normal neighbor in a DNA glycosylase complex.Novel post-synthetic generation, isomeric resolution, and characterization of Fapy-dG within oligodeoxynucleotides: differential anomeric impacts on DNA duplex properties Single Qdot-labeled glycosylase molecules use a wedge amino acid to probe for lesions while scanning along DNA DNA pol λ's extraordinary ability to stabilize misaligned DNA.A base-independent repair mechanism for DNA glycosylase--no discrimination within the active site.Efficient and Reliable Production of Vectors for the Study of the Repair, Mutagenesis, and Phenotypic Consequences of Defined DNA Damage Lesions in Mammalian Cells Surprising repair activities of nonpolar analogs of 8-oxoG expose features of recognition and catalysis by base excision repair glycosylases.

P2860

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P2860

DNA lesion recognition by the bacterial repair enzyme MutM

http://www.wikidata.org/entity/Q27642268

description

2003 nî lūn-bûn

@nan

2003 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2003 թվականի դեկտեմբերին հրատարակված գիտական հոդված

@hy

2003年の論文

@ja

2003年論文

@yue

2003年論文

@zh-hant

2003年論文

@zh-hk

2003年論文

@zh-mo

2003年論文

@zh-tw

2003年论文

@wuu

name

DNA lesion recognition by the bacterial repair enzyme MutM

@ast

DNA lesion recognition by the bacterial repair enzyme MutM

@en

DNA lesion recognition by the bacterial repair enzyme MutM

@nl

type

label

DNA lesion recognition by the bacterial repair enzyme MutM

@ast

DNA lesion recognition by the bacterial repair enzyme MutM

@en

DNA lesion recognition by the bacterial repair enzyme MutM

@nl

prefLabel

DNA lesion recognition by the bacterial repair enzyme MutM

@ast

DNA lesion recognition by the bacterial repair enzyme MutM

@en

DNA lesion recognition by the bacterial repair enzyme MutM

@nl

P1433

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P1433

Journal of Biological Chemistry

P1476

DNA lesion recognition by the bacterial repair enzyme MutM

@en

P2093

Gregory L Verdine

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

P2860

Human DNA glycosylases of the bacterial Fpg/MutM superfamily: an alternative pathway for the repair of 8-oxoguanine and other oxidation products in DNA

Structural analysis of an Escherichia coli endonuclease VIII covalent reaction intermediate.

Crystal structure of a repair enzyme of oxidatively damaged DNA, MutM (Fpg), from an extreme thermophile, Thermus thermophilus HB8

Molecular basis for discriminating between normal and damaged bases by the human alkyladenine glycosylase, AAG

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

PROCHECK: a program to check the stereochemical quality of protein structures

Processing of X-ray diffraction data collected in oscillation mode

Structural basis for recognition and repair of the endogenous mutagen 8-oxoguanine in DNA

Coupling of substrate recognition and catalysis by a human base-excision DNA repair protein

Reciprocal "flipping" underlies substrate recognition and catalytic activation by the human 8-oxo-guanine DNA glycosylase

P304

51543-51548

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P31

scholarly article

P3181

360114

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P356

10.1074/JBC.M307768200

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P407

P433

51

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P478

278

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P50

J Christopher Fromme

P577

2003-10-01T00:00:00Z

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P5875

5596135

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P698

14525999

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