Evidence map›Paper›PMID 11726693›Full record

ArticleNucleic acids research2001

Nearest neighbour analysis of MCM protein complexes in Drosophila melanogaster.

G Crevel, A Ivetic, K Ohno, M Yamaguchi, S Cotterill

Open access · bronzeAbstract read
In one paragraph

Article in Nucleic acids research, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
0.6field-weighted citation impact, top 34% 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

20 citing papers in PubMed, 37 citations in OpenAlex.

  1. Article
  2. Mechanisms and regulation of DNA replication initiation in eukaryotes.Critical reviews in biochemistry and molecular biology · 2017
    Review
  3. Article
  4. Article
  5. Article
  6. Examining Nek2 as a better proliferation marker in non-small cell lung cancer prognosis.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2014
    Article
  7. The minichromosome maintenance replicative helicase.Cold Spring Harbor perspectives in biology · 2013
    Review
  8. Mechanisms for initiating cellular DNA replication.Annual review of biochemistry · 2013
    Review
  9. Functional analysis of Drosophila DNA polymerase ε p58 subunit.American journal of cancer research · 2013
    Article
  10. Article
  11. Article
  12. Article
  13. The Mcm complex: unwinding the mechanism of a replicative helicase.Microbiology and molecular biology reviews : MMBR · 2009
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Cell cycle regulation of DNA replication.Annual review of genetics · 2007
    Review
  19. Article
  20. Eukaryotic MCM proteins: beyond replication initiation.Microbiology and molecular biology reviews : MMBR · 2004
    Review
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.

G CrevelDepartment of Biochemistry, St Georges Hospital Medical School, Cranmer Terrace, London SW17 0RE, UK.
A Ivetic
K Ohno
M Yamaguchi
S Cotterill
St George's Hospital · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The MCM proteins are a group of six proteins whose action is vital for DNA replication in eukaryotes. It has been suggested that they constitute the replicative helicase, with a subset of the proteins forming the catalytic helicase (MCM4,6,7) while the others have a loading or control function. In this paper we show that all six MCM proteins are present in equivalent amounts in soluble extracts and on chromatin. We have also analysed soluble and chromatin-associated MCM protein complexes under different conditions. This suggests that all six MCM proteins are always found in a complex with each other, although the interaction between the individual MCM proteins is not equivalent as stringent salt conditions are able to break the intact complex into a number of stable subcomplexes. These data contribute to the ongoing debate about the nature of MCM complexes, supporting the hypothesis that they act as a heterohexamer rather than as a number of different subcomplexes. Finally, using protein-protein cross-linking we have shown that MCM2 interacts directly with MCM5 and MCM6; MCM5 with MCM3 and MCM2; and MCM6 with MCM2 and MCM4. This provides the first direct information about specific subunit contacts in the MCM complex.

Indexed as

Saccharomyces cerevisiae ProteinsAnimalsCell Cycle ProteinsCell ExtractsCell FractionationChromatinChromosomal Proteins, Non-HistoneCross-Linking ReagentsCytoplasmDNA-Binding ProteinsDrosophila melanogasterDrosophila ProteinsMacromolecular SubstancesMinichromosome Maintenance Complex Component 4Minichromosome Maintenance Complex Component 6Minichromosome Maintenance Complex Component 7Cell Cycle ProteinsCell ExtractsChromatinChromosomal Proteins, Non-HistoneCross-Linking Reagentsdithiobis(succinimidylpropionate)DNA-Binding ProteinsDrosophila ProteinsMacromolecular SubstancesMCM4 protein, S cerevisiaemcm5 protein, S pombeMcm6 protein, DrosophilaMCM6 protein, S cerevisiaeMcm7 protein, DrosophilaMCM7 protein, S cerevisiaeMinichromosome Maintenance Complex Component 4Minichromosome Maintenance Complex Component 6Minichromosome Maintenance Complex Component 7Nuclear ProteinsSaccharomyces cerevisiae ProteinsSchizosaccharomyces pombe ProteinsSuccinimides

Identifiers

PMID11726693
PMCPMC96677
OpenAlexW2104368366

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.