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

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

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

http://www.wikidata.org/entity/Q30476604

about

Genome-wide mapping of ORC and Mcm2p binding sites on tiling arrays and identification of essential ARS consensus sequences in S. cerevisiae Hexameric ring structure of human MCM10 DNA replication factor Functional uncoupling of MCM helicase and DNA polymerase activities activates the ATR-dependent checkpoint.The chromosome cycle: coordinating replication and segregation. Second in the cycles review series.Conserved nucleosome positioning defines replication origins Concerted loading of Mcm2-7 double hexamers around DNA during DNA replication origin licensing Preventing re-replication of chromosomal DNA.DNA replication in the archaea DNA binding and helicase actions of mouse MCM4/6/7 helicase.Interactions between the archaeal Cdc6 and MCM proteins modulate their biochemical properties.Archaeal MCM Proteins as an Analog for the Eukaryotic Mcm2-7 Helicase to Reveal Essential Features of Structure and Function Mechanisms for initiating cellular DNA replication The minichromosome maintenance replicative helicase MCM ring hexamerization is a prerequisite for DNA-binding.Structural analysis of the Sulfolobus solfataricus MCM protein N-terminal domain Structure and Mutagenesis Studies of the C-terminal Region of Licensing Factor Cdt1 Enable the Identification of Key Residues for Binding to Replicative Helicase Mcm Proteins 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.Insights into the MCM functional mechanism: lessons learned from the archaeal MCM complex.Origin recognition and the chromosome cycle The structural basis for MCM2-7 helicase activation by GINS and Cdc45.Structure and regulatory role of the C-terminal winged helix domain of the archaeal minichromosome maintenance complex Mutations in subdomain B of the minichromosome maintenance (MCM) helicase affect DNA binding and modulate conformational transitions Two heads are better than one: regulation of DNA replication by hexameric helicases CMG-Pol epsilon dynamics suggests a mechanism for the establishment of leading-strand synthesis in the eukaryotic replisome.Evolution of DNA replication protein complexes in eukaryotes and Archaea.A unique DNA entry gate serves for regulated loading of the eukaryotic replicative helicase MCM2-7 onto DNA Structural insights into the Cdt1-mediated MCM2-7 chromatin loading.The Saccharomyces cerevisiae Mcm6/2 and Mcm5/3 ATPase active sites contribute to the function of the putative Mcm2-7 'gate'.Molecular architecture of a multifunctional MCM complex S-phase sensing of DNA-protein crosslinks triggers TopBP1-independent ATR activation and p53-mediated cell death by formaldehyde.The ATPase activity of MCM2-7 is dispensable for pre-RC assembly but is required for DNA unwinding.Minichromosome maintenance helicase activity is controlled by N- and C-terminal motifs and requires the ATPase domain helix-2 insert.Pre-replication complex proteins assemble at regions of low nucleosome occupancy within the Chinese hamster dihydrofolate reductase initiation zone Characterization of the MCM homohexamer from the thermoacidophilic euryarchaeon Picrophilus torridus.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 DNA topoisomerase I domain interactions impact enzyme activity and sensitivity to camptothecin.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.

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P2860

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

http://www.wikidata.org/entity/Q30476604

description

2003 nî lūn-bûn

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2003 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

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2003 թվականի հոտեմբերին հրատարակված գիտական հոդված

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2003年の論文

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2003年論文

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2003年論文

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2003年論文

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2003年論文

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2003年論文

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2003年论文

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name

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

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

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type

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

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

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prefLabel

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

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

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

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P2093

Giorgia Vicentini

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Hedije Meka

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Marin van Heel

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Shaoxia Chen

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P2860

Crystal structure of T7 gene 4 ring helicase indicates a mechanism for sequential hydrolysis of nucleotides

Structure of the AAA ATPase p97

Structure and mechanism of the RuvB Holliday junction branch migration motor

The structure and function of MCM from archaeal M. Thermoautotrophicum

Structure of the replicative helicase of the oncoprotein SV40 large tumour antigen

Uninterrupted MCM2-7 function required for DNA replication fork progression.

MCM proteins in DNA replication

AAA+: A class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes

A new generation of the IMAGIC image processing system

Interactions between two catalytically distinct MCM subgroups are essential for coordinated ATP hydrolysis and DNA replication

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1079-1083

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10.1038/SJ.EMBOR.7400010

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11

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4

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