Evidence map›Paper›PMID 24292646›Full record

ArticleNature structural & molecular biology2014

Structural basis for processive DNA synthesis by yeast DNA polymerase ɛ.

Matthew Hogg, Pia Osterman, Göran O Bylund, Rais A Ganai, Else-Britt Lundström, A Elisabeth Sauer-Eriksson, Erik Johansson

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Article in Nature structural & molecular biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 126 papers.

0numbers the graph read from it
0cells of the map it votes in
126citing papers in PubMed
–field-weighted citation impact
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

126 citing papers in PubMed.

  1. Review
  2. Article
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  5. The proofreading mechanism of the human leading-strand DNA polymerase ε holoenzyme.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
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  14. Clamping Pol ε to the leading strand.Nature structural & molecular biology · 2024
    Article
  15. Revised mechanism of hydroxyurea-induced cell cycle arrest and an improved alternative.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

66 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

7 authors.

Matthew HoggDepartment of Medical Biochemistry and Biophysics, Umeå University, Umeå, Sweden.
Pia OstermanDepartment of Medical Biochemistry and Biophysics, Umeå University, Umeå, Sweden.
Göran O BylundDepartment of Medical Biochemistry and Biophysics, Umeå University, Umeå, Sweden.
Rais A GanaiDepartment of Medical Biochemistry and Biophysics, Umeå University, Umeå, Sweden.
Else-Britt LundströmDepartment of Medical Biochemistry and Biophysics, Umeå University, Umeå, Sweden.
A Elisabeth Sauer-ErikssonDepartment of Chemistry, Umeå University, Umeå, Sweden.
Erik JohanssonDepartment of Medical Biochemistry and Biophysics, Umeå University, Umeå, Sweden.ORCID 0000000285266224

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

DNA polymerase ɛ (Pol ɛ) is a high-fidelity polymerase that has been shown to participate in leading-strand synthesis during DNA replication in eukaryotic cells. We present here a ternary structure of the catalytic core of Pol ɛ (142 kDa) from Saccharomyces cerevisiae in complex with DNA and an incoming nucleotide. This structure provides information about the selection of the correct nucleotide and the positions of amino acids that might be critical for proofreading activity. Pol ɛ has the highest fidelity among B-family polymerases despite the absence of an extended β-hairpin loop that is required for high-fidelity replication by other B-family polymerases. Moreover, the catalytic core has a new domain that allows Pol ɛ to encircle the nascent double-stranded DNA. Altogether, the structure provides an explanation for the high processivity and high fidelity of leading-strand DNA synthesis in eukaryotes.

Indexed as

DNA ReplicationCatalytic DomainDNA Polymerase IIModels, MolecularSaccharomyces cerevisiaeDNA Polymerase II

Identifiers

PMID24292646

What OpenQuestion holds

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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.