Archaeal MCM has separable processivity, substrate choice and helicase domains. - Wikidata - wikimedia - TriplyDB

Archaeal MCM has separable processivity, substrate choice and helicase domains.

Archaeal MCM has separable processivity, substrate choice and helicase domains.

http://www.wikidata.org/entity/Q42942774

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Archaeal MCM Proteins as an Analog for the Eukaryotic Mcm2-7 Helicase to Reveal Essential Features of Structure and Function The minichromosome maintenance replicative helicase Structural analysis of the Sulfolobus solfataricus MCM protein N-terminal domain Crystal structure of a near-full-length archaeal MCM: Functional insights for an AAA+ hexameric helicase A conserved MCM single-stranded DNA binding element is essential for replication initiation Differences in the single-stranded DNA binding activities of MCM2-7 and MCM467: MCM2 and MCM5 define a slow ATP-dependent step.Fundamental Characteristics of AAA+ Protein Family Structure and Function Insights into the MCM functional mechanism: lessons learned from the archaeal MCM complex.Archaeal orthologs of Cdc45 and GINS form a stable complex that stimulates the helicase activity of MCM Structure and regulatory role of the C-terminal winged helix domain of the archaeal minichromosome maintenance complex Dbf4-Cdc7 phosphorylation of Mcm2 is required for cell growth.CMG-Pol epsilon dynamics suggests a mechanism for the establishment of leading-strand synthesis in the eukaryotic replisome.Mechanism and substrate specificity of telomeric protein POT1 stimulation of the Werner syndrome helicase Mcm4 C-terminal domain of MCM helicase prevents excessive formation of single-stranded DNA at stalled replication forks Eukaryotic Replicative Helicase Subunit Interaction with DNA and Its Role in DNA Replication.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.Steric exclusion and wrapping of the excluded DNA strand occurs along discrete external binding paths during MCM helicase unwinding.Analysis of the crystal structure of an active MCM hexamer The Sulfolobus solfataricus GINS Complex Stimulates DNA Binding and Processive DNA Unwinding by Minichromosome Maintenance Helicase The Helicase Activity of Hyperthermophilic Archaeal MCM is Enhanced at High Temperatures by Lysine Methylation Coupling of DNA binding and helicase activity is mediated by a conserved loop in the MCM protein.Cryo-electron microscopy reveals a novel DNA-binding site on the MCM helicase.Intersubunit allosteric communication mediated by a conserved loop in the MCM helicase A biochemically active MCM-like helicase in Bacillus cereus The Mcm complex: unwinding the mechanism of a replicative helicase.Ligand-induced and small-molecule control of substrate loading in a hexameric helicase Structural biology of MCM helicases.Modular organization of the Sulfolobus solfataricus mini-chromosome maintenance protein.Preparing to unwind.Mechanisms and regulation of DNA replication initiation in eukaryotes.Expression, purification and biochemical characterization of Schizosaccharomyces pombe Mcm4, 6 and 7.Mechanism of Archaeal MCM Helicase Recruitment to DNA Replication Origins.Potent DNA strand annealing activity associated with mouse Mcm2∼7 heterohexameric complex.¹H, ¹⁵N, and ¹³C chemical shift assignments for the winged helix domains of two archeal MCM C-termini.The ring-shaped hexameric helicases that function at DNA replication forks.The Eukaryotic CMG Helicase at the Replication Fork: Emerging Architecture Reveals an Unexpected Mechanism.The interplay of DNA binding, ATP hydrolysis and helicase activities of the archaeal MCM helicase.The solution structure of full-length dodecameric MCM by SANS and molecular modeling

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P2860

Archaeal MCM has separable processivity, substrate choice and helicase domains.

http://www.wikidata.org/entity/Q42942774

description

2007 nî lūn-bûn

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2007年の論文

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2007年論文

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2007年論文

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2007年論文

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2007年论文

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2007年论文

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2007年论文

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name

Archaeal MCM has separable processivity, substrate choice and helicase domains.

@en

Archaeal MCM has separable processivity, substrate choice and helicase domains.

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type

label

Archaeal MCM has separable processivity, substrate choice and helicase domains.

@en

Archaeal MCM has separable processivity, substrate choice and helicase domains.

@nl

prefLabel

Archaeal MCM has separable processivity, substrate choice and helicase domains.

@en

Archaeal MCM has separable processivity, substrate choice and helicase domains.

@nl

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P1476

Archaeal MCM has separable processivity, substrate choice and helicase domains.

@en

P2093

Adam T McGeoch

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

Elizabeth R Barry

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

Zvi Kelman

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

P2860

A DNA helicase activity is associated with an MCM4, -6, and -7 protein complex

A new member of the MCM protein family encoded by the human MCM8 gene, located contrapodal to GCD10 at chromosome band 20p12.3-13

The structure and function of MCM from archaeal M. Thermoautotrophicum

MCM proteins in DNA replication

The Methanobacterium thermoautotrophicum MCM protein can form heptameric rings.

Structural polymorphism of Methanothermobacter thermautotrophicus MCM.

Hexameric ring structure of the full-length archaeal MCM protein complex.

Is the MCM2-7 complex the eukaryotic DNA replication fork helicase?

Archaea: an archetype for replication initiation studies?

Minichromosome maintenance helicase activity is controlled by N- and C-terminal motifs and requires the ATPase domain helix-2 insert.

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988-998

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scholarly article

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10.1093/NAR/GKL1117

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3

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35

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Stephen D. Bell

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2007-01-26T00:00:00Z

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6545347

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17259218

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1807962

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