Evidence map›Paper›PMID 20484375›Full record

ArticleNucleic acids research2010

The Saccharomyces cerevisiae Mcm6/2 and Mcm5/3 ATPase active sites contribute to the function of the putative Mcm2-7 'gate'.

Matthew L Bochman, Anthony Schwacha

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
2.5field-weighted citation impact, top 11% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

40 citing papers in PubMed, 61 citations in OpenAlex.

  1. Article
  2. Mechanisms of hexameric helicases.Critical reviews in biochemistry and molecular biology · 2021
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  11. Molecular mechanisms of substrate-controlled ring dynamics and substepping in a nucleic acid-dependent hexameric motor.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Matthew L BochmanDepartment of Biological Sciences, University of Pittsburgh, Pittsburgh, PA 15260, USA.
Anthony Schwacha
University of Pittsburgh · US

Funding

The Role of the MCM2-7 Complex in the Replication Fork ProcessivityR01GM083985 · NIGMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI SCHWACHA, ANTHONY · 2009 to 2013
$1.3M
NIGMS NIH HHS 1R01GM83985-1A1NIGMS NIH HHS R01 GM083985
6 · The paper itself

Abstract

The Mcm2-7 complex is the eukaryotic replicative helicase, a toroidal AAA(+) molecular motor that uses adenosine triphosphate (ATP) binding and hydrolysis to separate duplex DNA strands during replication. This heterohexameric helicase contains six different and essential subunits (Mcm2 through Mcm7), with the corresponding dimer interfaces forming ATPase active sites from conserved motifs of adjacent subunits. As all other known hexameric helicases are formed from six identical subunits, the function of the unique heterohexameric organization of Mcm2-7 is of particular interest. Indeed, prior work using mutations in the conserved Walker A box ATPase structural motif strongly suggests that individual ATPase active sites contribute differentially to Mcm2-7 activity. Although only a specific subset of active sites is required for helicase activity, another ATPase active site (Mcm2/5) may serve as a reversible ATP-dependent discontinuity ('gate') within the hexameric ring structure. This study analyzes the contribution that two other structural motifs, the Walker B box and arginine finger, make to each Mcm2-7 ATPase active site. Mutational analysis of these motifs not only confirms that Mcm ATPase active sites contribute unequally to activity but implicates the involvement of at least two additional active sites (Mcm5/3 and 6/2) in modulating the activity of the putative Mcm2/5 gate.

Indexed as

Adenosine TriphosphatasesCatalytic DomainCell Cycle ProteinsChromosomal Proteins, Non-HistoneDNADNA-Binding ProteinsDNA, CircularDNA HelicasesDNA, Single-StrandedKineticsMinichromosome Maintenance Complex Component 3Minichromosome Maintenance Complex Component 6Minichromosome Maintenance Complex Component 7MutationNuclear ProteinsProtein SubunitsAdenosine TriphosphatasesCell Cycle ProteinsChromosomal Proteins, Non-HistoneDNADNA-Binding ProteinsDNA, CircularDNA HelicasesDNA, Single-StrandedMCM2 protein, S cerevisiaeMCM3 protein, S cerevisiaeMCM5 protein, S cerevisiaeMCM6 protein, S cerevisiaeMCM7 protein, S cerevisiaeMinichromosome Maintenance Complex Component 3Minichromosome Maintenance Complex Component 6Minichromosome Maintenance Complex Component 7Nuclear ProteinsProtein SubunitsSaccharomyces cerevisiae Proteins

Identifiers

PMID20484375
PMCPMC2952866
OpenAlexW2167165923

What OpenQuestion holds

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LicenceCC BY-NC
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.