Evidence map›Paper›PMID 22474384›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2012

Properties of the human Cdc45/Mcm2-7/GINS helicase complex and its action with DNA polymerase epsilon in rolling circle DNA synthesis.

Young-Hoon Kang, Wiebke Chemnitz Galal, Andrea Farina, Inger Tappin, Jerard Hurwitz

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 87 papers.

0numbers the graph read from it
0cells of the map it votes in
87citing papers in PubMed
6.0field-weighted citation impact, top 3% 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

87 citing papers in PubMed, 137 citations in OpenAlex.

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  10. Mechanism of eukaryotic origin unwinding is a dual helicase DNA shearing process.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  11. Article
  12. Review
  13. SV40 T-antigen uses a DNA shearing mechanism to initiate origin unwinding.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  14. Article
  15. Article
  16. CMG helicase can use ATPγS to unwind DNA: Implications for the rate-limiting step in the reaction mechanism.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  17. Article
  18. Article
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  20. Article

27 more citing papers are in PubMed but not listed here.

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

5 authors at 1 institution in 1 country.

Young-Hoon KangProgram of Molecular Biology, Memorial Sloan-Kettering Cancer Center, New York, NY 10065, USA.
Wiebke Chemnitz Galal
Andrea Farina
Inger Tappin
Jerard Hurwitz
Memorial Sloan Kettering Cancer Center · US

Funding

Studies on Eukaryotic ReplicationR01GM034559 · NIGMS · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI HURWITZ, JERARD · 1985 to 2011
$9.3M
NIGMS NIH HHS R01 GM034559PHS HHS GMS R01 GM034559
6 · The paper itself

Abstract

In eukaryotes, although the Mcm2-7 complex is a key component of the replicative DNA helicase, its association with Cdc45 and GINS (the CMG complex) is required for the activation of the DNA helicase. Here, we show that the CMG complex is localized to chromatin in human cells and describe the biochemical properties of the human CMG complex purified from baculovirus-infected Sf9 cells. The isolated complex binds to ssDNA regions in the presence of magnesium and ATP (or a nonhydrolyzable ATP analog), contains maximal DNA helicase in the presence of forked DNA structures, and translocates along the leading strand (3' to 5' direction). The complex hydrolyses ATP in the absence of DNA; unwinds duplex regions up to 500 bp; and either replication protein A or Escherichia coli single stranded binding protein increases the efficiency of displacement of long duplex regions. Using a 200-nt primed circular DNA substrate, the combined action of human DNA polymerase ε and the human CMG complex leads to the formation of products >10 kb in length. These findings suggest that the coordinated action of these replication complexes supports leading strand synthesis.

Indexed as

Adenosine TriphosphateAnimalsBlotting, WesternCell Cycle ProteinsCell LineChromatinChromosomal Proteins, Non-HistoneDNADNA HelicasesDNA Polymerase IIDNA, Single-StrandedElectrophoretic Mobility Shift AssayHEK293 CellsHeLa CellsHumansKineticsAdenosine TriphosphateCDC45 protein, humanCell Cycle ProteinsChromatinChromosomal Proteins, Non-HistoneDNADNA HelicasesDNA Polymerase IIDNA, Single-StrandedGINS2 protein, humanMCM2 protein, humanMinichromosome Maintenance Complex Component 2Nuclear ProteinsOligonucleotidesOrigin Recognition Complex

Identifiers

PMID22474384
PMCPMC3341058
OpenAlexW2158074805

What OpenQuestion holds

Textmetadata
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.