Structural analysis of the inactive state of the Escherichia coli DNA polymerase clamp-loader complex
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.Studying protein complexes by the yeast two-hybrid systemSolution structure of Domains IVa and V of the subunit of Escherichia coli DNA polymerase III and interaction with the subunitStructure of the 12-subunit RNA polymerase II refined with the aid of anomalous diffraction data.The Mechanism of ATP-Dependent Primer-Template Recognition by a Clamp Loader ComplexAnalysis of the role of PCNA-DNA contacts during clamp loadingStructure and Biochemical Activities of Escherichia coli MgsAInsights into the structure and assembly of the Bacillus subtilis clamp-loader complex and its interaction with the replicative helicaseMechanism of proliferating cell nuclear antigen clamp opening by replication factor CA 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.Processivity factor of DNA polymerase and its expanding role in normal and translesion DNA synthesisFast and automated functional classification with MED-SuMo: an application on purine-binding proteins.Out-of-plane motions in open sliding clamps: molecular dynamics simulations of eukaryotic and archaeal proliferating cell nuclear antigenStoichiometry and architecture of active DNA replication machinery in Escherichia coli.Architecture and conservation of the bacterial DNA replication machinery, an underexploited drug target.Dynamics of Open DNA Sliding Clamps.Solution study of the Escherichia coli DNA polymerase III clamp loader reveals the location of the dynamic ψχ heterodimerDynamics of loading the Escherichia coli DNA polymerase processivity clamp.Replication clamps and clamp loaders.Loading clamps for DNA replication and repairReview: The lord of the rings: Structure and mechanism of the sliding clamp loader.Assessing heterogeneity in oligomeric AAA+ machines.Hypothesis: bacterial clamp loader ATPase activation through DNA-dependent repositioning of the catalytic base and of a trans-acting catalytic threonineStructure of the active form of human origin recognition complex and its ATPase motor module.Heterogeneous nucleotide occupancy stimulates functionality of phage shock protein F, an AAA+ transcriptional activator.Structure of the large terminase from a hyperthermophilic virus reveals a unique mechanism for oligomerization and ATP hydrolysis.Mapping the interaction of DNA with the Escherichia coli DNA polymerase clamp loader complex.Isomeric control of protein recognition with amino acid- and dipeptide-functionalized gold nanoparticles.A function for the psi subunit in loading the Escherichia coli DNA polymerase sliding clamp.
P2860
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P2860
Structural analysis of the inactive state of the Escherichia coli DNA polymerase clamp-loader complex
description
2004 nî lūn-bûn
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2004年の論文
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2004年学术文章
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2004年学术文章
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2004年学术文章
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2004年学术文章
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name
Structural analysis of the ina ...... olymerase clamp-loader complex
@en
Structural analysis of the ina ...... lymerase clamp-loader complex.
@nl
type
label
Structural analysis of the ina ...... olymerase clamp-loader complex
@en
Structural analysis of the ina ...... lymerase clamp-loader complex.
@nl
prefLabel
Structural analysis of the ina ...... olymerase clamp-loader complex
@en
Structural analysis of the ina ...... lymerase clamp-loader complex.
@nl
P2093
P2860
P356
P1476
Structural analysis of the ina ...... olymerase clamp-loader complex
@en
P2093
John Kuriyan
Marjetka Podobnik
Mike O'Donnell
Steven L Kazmirski
Tanya F Weitze
P2860
P304
16750-16755
P356
10.1073/PNAS.0407904101
P407
P577
2004-11-19T00:00:00Z