Dynamic opening of DNA during the enzymatic search for a damaged base. - Test2 - elhamkhani - TriplyDB

Dynamic opening of DNA during the enzymatic search for a damaged base.

Dynamic opening of DNA during the enzymatic search for a damaged base.

http://www.wikidata.org/entity/Q30976865

about

The Fpg/Nei family of DNA glycosylases: substrates, structures, and search for damage Enzymatic capture of an extrahelical thymine in the search for uracil in DNA Duplex interrogation by a direct DNA repair protein in search of base damage Twist-open mechanism of DNA damage recognition by the Rad4/XPC nucleotide excision repair complex Uracil-DNA glycosylase: Structural, thermodynamic and kinetic aspects of lesion search and recognition Base excision repair A two-step nucleotide-flipping mechanism enables kinetic discrimination of DNA lesions by AGT Molecular dynamics of a kappaB DNA element: base flipping via cross-strand intercalative stacking in a microsecond-scale simulation Nontarget DNA binding shapes the dynamic landscape for enzymatic recognition of DNA damage.Two glycosylase families diffusively scan DNA using a wedge residue to probe for and identify oxidatively damaged bases.Predicting protein-DNA interactions by full search computational docking.Dynamics of spontaneous flipping of a mismatched base in DNA duplex.Mechanism of duplex DNA destabilization by RNA-guided Cas9 nuclease during target interrogation.Solid state 2H NMR analysis of furanose ring dynamics in DNA containing uracil Characterization of DNA with an 8-oxoguanine modification.DNA-Destabilizing Agents as an Alternative Approach for Targeting DNA: Mechanisms of Action and Cellular Consequences On the molecular basis of uracil recognition in DNA: comparative study of T-A versus U-A structure, dynamics and open base pair kinetics.Dynamics of uracil and 5-fluorouracil in DNA.Sequence-dependent enhancement of hydrolytic deamination of cytosines in DNA by the restriction enzyme PspGI.Differential stabilities and sequence-dependent base pair opening dynamics of Watson-Crick base pairs with 5-hydroxymethylcytosine, 5-formylcytosine, or 5-carboxylcytosine.Lesion search and recognition by thymine DNA glycosylase revealed by single molecule imaging.Single Qdot-labeled glycosylase molecules use a wedge amino acid to probe for lesions while scanning along DNA Hidden in plain sight: subtle effects of the 8-oxoguanine lesion on the structure, dynamics, and thermodynamics of a 15-base pair oligodeoxynucleotide duplex.Binding of undamaged double stranded DNA to vaccinia virus uracil-DNA Glycosylase.Thermodynamics and kinetics for base-pair opening in the P1 duplex of the Tetrahymena group I ribozyme Combining H/D exchange mass spectroscopy and computational docking reveals extended DNA-binding surface on uracil-DNA glycosylase.Identification of DNA lesions using a third base pair for amplification and nanopore sequencing.Single-molecule spectroscopic study of dynamic nanoscale DNA bending behavior of HIV-1 nucleocapsid protein.Direct reversal of DNA alkylation damage.Probing enzyme phosphoester interactions by combining mutagenesis and chemical modification of phosphate ester oxygens.Uracil DNA glycosylase uses DNA hopping and short-range sliding to trap extrahelical uracils.Extrahelical damaged base recognition by DNA glycosylase enzymes Uncoupling of nucleotide flipping and DNA bending by the t4 pyrimidine dimer DNA glycosylase.Early steps of active DNA demethylation initiated by ROS1 glycosylase require three putative helix-invading residues.DNA base repair--recognition and initiation of catalysis.Looking for Waldo: a potential thermodynamic signature to DNA damage.Detection of damaged DNA bases by DNA glycosylase enzymes.Recognition of damaged DNA: structure and dynamic markers.Energetic preference of 8-oxoG eversion pathways in a DNA glycosylase.Timing facilitated site transfer of an enzyme on DNA

P2860

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P2860

Dynamic opening of DNA during the enzymatic search for a damaged base.

http://www.wikidata.org/entity/Q30976865

description

2004 nî lūn-bûn

@nan

2004 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

@hyw

2004 թվականի նոյեմբերին հրատարակված գիտական հոդված

@hy

2004年の論文

@ja

2004年論文

@yue

2004年論文

@zh-hant

2004年論文

@zh-hk

2004年論文

@zh-mo

2004年論文

@zh-tw

2004年论文

@wuu

name

Dynamic opening of DNA during the enzymatic search for a damaged base.

@ast

Dynamic opening of DNA during the enzymatic search for a damaged base.

@en

type

label

Dynamic opening of DNA during the enzymatic search for a damaged base.

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Dynamic opening of DNA during the enzymatic search for a damaged base.

@en

prefLabel

Dynamic opening of DNA during the enzymatic search for a damaged base.

@ast

Dynamic opening of DNA during the enzymatic search for a damaged base.

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P1433

Nature Structural & Molecular Biology

P1476

Dynamic opening of DNA during the enzymatic search for a damaged base.

@en

P2093

Chunyang Cao

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

Fenhong Song

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

James T Stivers

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

Yu Lin Jiang

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

P2860

Uracil-DNA glycosylase-DNA substrate and product structures: conformational strain promotes catalytic efficiency by coupled stereoelectronic effects

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

Stressing-out DNA? The contribution of serine-phosphodiester interactions in catalysis by uracil DNA glycosylase

Solution structure and base perturbation studies reveal a novel mode of alkylated base recognition by 3-methyladenine DNA glycosylase I

A nucleotide-flipping mechanism from the structure of human uracil-DNA glycosylase bound to DNA

Crystal structure of a human alkylbase-DNA repair enzyme complexed to DNA: mechanisms for nucleotide flipping and base excision

NMRPipe: a multidimensional spectral processing system based on UNIX pipes

Role of electrophilic and general base catalysis in the mechanism of Escherichia coli uracil DNA glycosylase.

Imino proton exchange and base-pair kinetics in RNA duplexes.

Kinetic mechanism of damage site recognition and uracil flipping by Escherichia coli uracil DNA glycosylase.

P2888

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scholarly article

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10.1038/NSMB864

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12

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11

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2004-11-21T00:00:00Z

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15558051

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