ATP binding and hydrolysis by Mcm2 regulate DNA binding by Mcm complexes. - Wikidata - awgldk - TriplyDB

ATP binding and hydrolysis by Mcm2 regulate DNA binding by Mcm complexes.

ATP binding and hydrolysis by Mcm2 regulate DNA binding by Mcm complexes.

http://www.wikidata.org/entity/Q37500135

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The effects of oligomerization on Saccharomyces cerevisiae Mcm4/6/7 function Phosphorylation of Mcm2 modulates Mcm2-7 activity and affects the cell's response to DNA damage The Saccharomyces cerevisiae Mcm6/2 and Mcm5/3 ATPase active sites contribute to the function of the putative Mcm2-7 'gate'.The PS1 hairpin of Mcm3 is essential for viability and for DNA unwinding in vitro.The Mcm complex: unwinding the mechanism of a replicative helicase.Mcm2-7 Is an Active Player in the DNA Replication Checkpoint Signaling Cascade via Proposed Modulation of Its DNA Gate.Dbf4 and Cdc7 proteins promote DNA replication through interactions with distinct Mcm2-7 protein subunits.MCM3 could be a better marker than Ki-67 for evaluation of dysplastic oral lesions: an immunohistochemical study.

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ATP binding and hydrolysis by Mcm2 regulate DNA binding by Mcm complexes.

http://www.wikidata.org/entity/Q37500135

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article científic

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article scientifique

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articolo scientifico

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artigo científico

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bilimsel makale

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scientific article published on 21 June 2009

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vedecký článok

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vetenskaplig artikel

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videnskabelig artikel

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vědecký článek

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name

ATP binding and hydrolysis by Mcm2 regulate DNA binding by Mcm complexes.

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ATP binding and hydrolysis by Mcm2 regulate DNA binding by Mcm complexes.

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type

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ATP binding and hydrolysis by Mcm2 regulate DNA binding by Mcm complexes.

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ATP binding and hydrolysis by Mcm2 regulate DNA binding by Mcm complexes.

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prefLabel

ATP binding and hydrolysis by Mcm2 regulate DNA binding by Mcm complexes.

@en

ATP binding and hydrolysis by Mcm2 regulate DNA binding by Mcm complexes.

@nl

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J.JMB.2009.06.038

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Journal of Molecular Biology

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ATP binding and hydrolysis by Mcm2 regulate DNA binding by Mcm complexes.

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Brent E Stead

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Catherine D Sorbara

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Christopher J Brandl

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Megan J Davey

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P2860

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

Distinct roles for Sld3 and GINS during establishment and progression of eukaryotic DNA replication forks

Processive DNA helicase activity of the minichromosome maintenance proteins 4, 6, and 7 complex requires forked DNA structures

Isolation of the Cdc45/Mcm2-7/GINS (CMG) complex, a candidate for the eukaryotic DNA replication fork helicase

Biochemical analysis of the intrinsic Mcm4-Mcm6-mcm7 DNA helicase activity

Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold

DNA binding and helicase actions of mouse MCM4/6/7 helicase.

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

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

Differences in the single-stranded DNA binding activities of MCM2-7 and MCM467: MCM2 and MCM5 define a slow ATP-dependent step.

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301-313

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scholarly article

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10.1016/J.JMB.2009.06.038

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2

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391

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2009-06-21T00:00:00Z

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19540846

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5154746

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