Quantitative analysis of nucleotide modulation of DNA binding by DnaC protein of Escherichia coli. - Wikidata - wikimedia - TriplyDB

Quantitative analysis of nucleotide modulation of DNA binding by DnaC protein of Escherichia coli.

Quantitative analysis of nucleotide modulation of DNA binding by DnaC protein of Escherichia coli.

http://www.wikidata.org/entity/Q42264197

about

Primase directs the release of DnaC from DnaB Mechanisms for initiating cellular DNA replication Structural Synergy and Molecular Crosstalk between Bacterial Helicase Loaders and Replication Initiators Helicase loading at chromosomal origins of replication Viral hijacking of a replicative helicase loader and its implications for helicase loading control and phage replication Replication initiation at the Escherichia coli chromosomal origin Genetic method to analyze essential genes of Escherichia coli DnaC traps DnaB as an open ring and remodels the domain that binds primase.Substitutions of Conserved Residues in the C-terminal Region of DnaC Cause Thermolability in Helicase Loading.The bacterial DnaC helicase loader is a DnaB ring breaker.Replication Initiation in Bacteria.DNA structure specificity conferred on a replicative helicase by its loader.The Macromolecular Machines that Duplicate the Escherichia coli Chromosome as Targets for Drug Discovery.

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P2860

Quantitative analysis of nucleotide modulation of DNA binding by DnaC protein of Escherichia coli.

http://www.wikidata.org/entity/Q42264197

description

2004 nî lūn-bûn

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2004年の論文

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2004年論文

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2004年論文

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2004年論文

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name

Quantitative analysis of nucle ...... C protein of Escherichia coli.

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Quantitative analysis of nucle ...... C protein of Escherichia coli.

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type

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Quantitative analysis of nucle ...... C protein of Escherichia coli.

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Quantitative analysis of nucle ...... C protein of Escherichia coli.

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Quantitative analysis of nucle ...... C protein of Escherichia coli.

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Quantitative analysis of nucle ...... C protein of Escherichia coli.

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Biochemical Journal

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Quantitative analysis of nucle ...... C protein of Escherichia coli.

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P2093

Esther E Biswas-Fiss

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Stephen Flowers

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

Subhasis B Biswas

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

P2860

Chromatin association of human origin recognition complex, cdc6, and minichromosome maintenance proteins during the cell cycle: assembly of prereplication complexes in late mitosis

Dual functions of CDC6: a yeast protein required for DNA replication also inhibits nuclear division

Cdc6 is regulated by E2F and is essential for DNA replication in mammalian cells

Architecture of the human origin recognition complex

ATP-dependent recognition of eukaryotic origins of DNA replication by a multiprotein complex

The multidomain structure of Orc1p reveals similarity to regulators of DNA replication and transcriptional silencing

DNA replication and the cell cycle.

DnaC protein contains a modified ATP-binding motif and belongs to a novel family of ATPases including also DnaA.

Numerical analysis of binding data: advantages, practical aspects, and implications.

Binding of XPA and RPA to damaged DNA investigated by fluorescence anisotropy.

P304

553-562

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scholarly article

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10.1042/BJ20031255

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P433

Pt 3

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379

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2004-05-01T00:00:00Z

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8926038

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14715083

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1224104

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