The bacterial helicase-primase interaction: a common structural/functional module.
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Mcm10 and And-1/CTF4 recruit DNA polymerase alpha to chromatin for initiation of DNA replicationThe crystal structure of the Thermus aquaticus DnaB helicase monomerThe structure of a DnaB-family replicative helicase and its interactions with primasePrimase is required for helicase activity and helicase alters the specificity of primase in the enteropathogen Clostridium difficileBiochemical Characterization of a Mycobacteriophage Derived DnaB Ortholog Reveals New Insight into the Evolutionary Origin of DnaB HelicasesAllosteric regulation of the primase (DnaG) activity by the clamp-loader (tau) in vitro.A superfamily 3 DNA helicase encoded by plasmid pSSVi from the hyperthermophilic archaeon Sulfolobus solfataricus unwinds DNA as a higher-order oligomer and interacts with host primase.Essential biological processes of an emerging pathogen: DNA replication, transcription, and cell division in Acinetobacter sppMechanism of sequence-specific template binding by the DNA primase of bacteriophage T7Domain swapping reveals that the C- and N-terminal domains of DnaG and DnaB, respectively, are functional homologues.GINS, a central nexus in the archaeal DNA replication fork.Architecture and conservation of the bacterial DNA replication machinery, an underexploited drug target.Characterization of flavonol inhibition of DnaB helicase: real-time monitoring, structural modeling, and proposed mechanism.Proteomic dissection of DNA polymerization.An in trans interaction at the interface of the helicase and primase domains of the hexameric gene 4 protein of bacteriophage T7 modulates their activities.Loading mechanisms of ring helicases at replication origins.Nutritional control of elongation of DNA replication by (p)ppGppClass-specific restrictions define primase interactions with DNA template and replicative helicase.Staphylococcus aureus helicase but not Escherichia coli helicase stimulates S. aureus primase activity and maintains initiation specificity.Conserved residues of the C-terminal p16 domain of primase are involved in modulating the activity of the bacterial primosome.In the Bacillus stearothermophilus DnaB-DnaG complex, the activities of the two proteins are modulated by distinct but overlapping networks of residues.The Polyphyletic Origins of Primase-Helicase Bifunctional Proteins.DnaC, the indispensable companion of DnaB helicase, controls the accessibility of DnaB helicase by primase.The Macromolecular Machines that Duplicate the Escherichia coli Chromosome as Targets for Drug Discovery.The Escherichia coli UvrD helicase is essential for Tus removal during recombination-dependent replication restart from Ter sites.Rapid determination of protein stability and ligand binding by differential scanning fluorimetry of GFP-tagged proteins
P2860
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P2860
The bacterial helicase-primase interaction: a common structural/functional module.
description
2005 nî lūn-bûn
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2005年の論文
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2005年学术文章
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2005年学术文章
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2005年学术文章
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name
The bacterial helicase-primase interaction: a common structural/functional module.
@ast
The bacterial helicase-primase interaction: a common structural/functional module.
@en
type
label
The bacterial helicase-primase interaction: a common structural/functional module.
@ast
The bacterial helicase-primase interaction: a common structural/functional module.
@en
prefLabel
The bacterial helicase-primase interaction: a common structural/functional module.
@ast
The bacterial helicase-primase interaction: a common structural/functional module.
@en
P2860
P1433
P1476
The bacterial helicase-primase interaction: a common structural/functional module
@en
P2093
Panos Soultanas
P2860
P304
P356
10.1016/J.STR.2005.04.006
P577
2005-06-01T00:00:00Z