The internal workings of a DNA polymerase clamp-loading machine. - Wikidata - awgldk - TriplyDB

The internal workings of a DNA polymerase clamp-loading machine.

The internal workings of a DNA polymerase clamp-loading machine.

http://www.wikidata.org/entity/Q42213856

about

Clamp loader ATPases and the evolution of DNA replication machinery.Open clamp structure in the clamp-loading complex visualized by electron microscopic image analysis.A CAF-1-PCNA-mediated chromatin assembly pathway triggered by sensing DNA damage Crystal structure of an archaeal DNA sliding clamp: proliferating cell nuclear antigen from Pyrococcus furiosus Biochemical characterization of DNA damage checkpoint complexes: clamp loader and clamp complexes with specificity for 5' recessed DNA The RFC clamp loader: structure and function Sliding Clamp–DNA Interactions Are Required for Viability and Contribute to DNA Polymerase Management in Escherichia coli Structure and Biochemical Activities of Escherichia coli MgsA The Escherichia coli Clamp Loader Can Actively Pry Open the -Sliding Clamp How a DNA Polymerase Clamp Loader Opens a Sliding Clamp A proposal: Evolution of PCNA's role as a marker of newly replicated DNA Mechanism of proliferating cell nuclear antigen clamp opening by replication factor C XpsE oligomerization triggered by ATP binding, not hydrolysis, leads to its association with XpsL Rapid mapping of protein structure, interactions, and ligand binding by misincorporation proton-alkyl exchange.ATP utilization by yeast replication factor C. I. ATP-mediated interaction with DNA and with proliferating cell nuclear antigen.Archaeal DNA replication: identifying the pieces to solve a puzzle.Motion of a DNA sliding clamp observed by single molecule fluorescence spectroscopy A slow ATP-induced conformational change limits the rate of DNA binding but not the rate of beta clamp binding by the escherichia coli gamma complex clamp loader.Fission yeast Rad17 associates with chromatin in response to aberrant genomic structures Intrinsic stability and oligomerization dynamics of DNA processivity clamps.On the specificity of interaction between the Saccharomyces cerevisiae clamp loader replication factor C and primed DNA templates during DNA replication.A universal protein-protein interaction motif in the eubacterial DNA replication and repair systems.AAA proteins. Lords of the ring.Out-of-plane motions in open sliding clamps: molecular dynamics simulations of eukaryotic and archaeal proliferating cell nuclear antigen Posttranslational modification of the umuD-encoded subunit of Escherichia coli DNA polymerase V regulates its interactions with the beta processivity clamp Competitive processivity-clamp usage by DNA polymerases during DNA replication and repair.The interplay of primer-template DNA phosphorylation status and single-stranded DNA binding proteins in directing clamp loaders to the appropriate polarity of DNA.Impairment of lagging strand synthesis triggers the formation of a RuvABC substrate at replication forks Rescue of arrested replication forks by homologous recombination Interaction of the beta sliding clamp with MutS, ligase, and DNA polymerase I.Motors and switches: AAA+ machines within the replisome.A dnaN plasmid shuffle strain for rapid in vivo analysis of mutant Escherichia coli β clamps provides insight into the role of clamp in umuDC-mediated cold sensitivity.A central swivel point in the RFC clamp loader controls PCNA opening and loading on DNA ATP-dependent structural change of the eukaryotic clamp-loader protein, replication factor C.Dynamics of Open DNA Sliding Clamps.DNA polymerase clamp loaders and DNA recognition.Replisome architecture and dynamics in Escherichia coli.Proteomic dissection of DNA polymerization.Dynamics of loading the Escherichia coli DNA polymerase processivity clamp.The β sliding clamp closes around DNA prior to release by the Escherichia coli clamp loader γ complex

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P2860

The internal workings of a DNA polymerase clamp-loading machine.

http://www.wikidata.org/entity/Q42213856

description

1999 nî lūn-bûn

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1999年の論文

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1999年論文

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1999年論文

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1999年論文

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1999年論文

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1999年論文

@zh-tw

1999年论文

@wuu

1999年论文

@zh

1999年论文

@zh-cn

name

The internal workings of a DNA polymerase clamp-loading machine.

@en

The internal workings of a DNA polymerase clamp-loading machine.

@nl

type

label

The internal workings of a DNA polymerase clamp-loading machine.

@en

The internal workings of a DNA polymerase clamp-loading machine.

@nl

prefLabel

The internal workings of a DNA polymerase clamp-loading machine.

@en

The internal workings of a DNA polymerase clamp-loading machine.

@nl

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The EMBO Journal

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The internal workings of a DNA polymerase clamp-loading machine.

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J Turner

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

M M Hingorani

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M O'Donnell

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Z Kelman

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P2860

Three-dimensional structure of the beta subunit of E. coli DNA polymerase III holoenzyme: a sliding DNA clamp

Crystal structure of the eukaryotic DNA polymerase processivity factor PCNA

Structure of the C-terminal region of p21(WAF1/CIP1) complexed with human PCNA

Crystal structure of the delta' subunit of the clamp-loader complex of E. coli DNA polymerase III

Characterization of the five replication factor C genes of Saccharomyces cerevisiae

The RFC2 gene, encoding the third-largest subunit of the replication factor C complex, is required for an S-phase checkpoint in Saccharomyces cerevisiae

A complex consisting of human replication factor C p40, p37, and p36 subunits is a DNA-dependent ATPase and an intermediate in the assembly of the holoenzyme

Mechanism of the sliding beta-clamp of DNA polymerase III holoenzyme

Mechanism of elongation of primed DNA by DNA polymerase delta, proliferating cell nuclear antigen, and activator 1

Clamping down on clamps and clamp loaders--the eukaryotic replication factor C

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