Evidence map›Paper›PMID 9034345›Full record

ArticleThe EMBO journal1997

A role for DNA primase in coupling DNA replication to DNA damage response.

F Marini, A Pellicioli, V Paciotti, G Lucchini, P Plevani, D F Stern, M Foiani

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
4.5field-weighted citation impact, top 4% 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

43 citing papers in PubMed, 118 citations in OpenAlex.

  1. Article
  2. Article
  3. The yeast Dbf4 ZnCurrent genetics · 2022
    Article
  4. Review
  5. Review
  6. Article
  7. Plant DNA Polymerases.International journal of molecular sciences · 2019
    Review
  8. Article
  9. Article
  10. Review
  11. Article
  12. Regulation of Elg1 activity by phosphorylation.Cell cycle (Georgetown, Tex.) · 2015
    Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Review
  19. Yeast telomere capping protein Stn1 overrides DNA replication control through the S phase checkpoint.Proceedings of the National Academy of Sciences of the United States of America · 2009
    Article
  20. Multiple functions of DNA polymerases.Critical reviews in plant sciences · 2007
    Article
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 at 1 institution in 1 country.

F MariniDipartimento di Genetica e di Biologia dei Microrganismi, Università degli Studi di Milano, Italy.
A Pellicioli
V Paciotti
G Lucchini
P Plevani
D F Stern
M Foiani
University of Milan · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The temperature-sensitive yeast DNA primase mutant pri1-M4 fails to execute an early step of DNA replication and exhibits a dominant, allele-specific sensitivity to DNA-damaging agents. pri1-M4 is defective in slowing down the rate of S phase progression and partially delaying the G1-S transition in response to DNA damage. Conversely, the G2 DNA damage response and the S-M checkpoint coupling completion of DNA replication to mitosis are unaffected. The signal transduction pathway leading to Rad53p phosphorylation induced by DNA damage is proficient in pri1-M4, and cell cycle delay caused by Rad53p overexpression is counteracted by the pri1-M4 mutation. Altogether, our results suggest that DNA primase plays an essential role in a subset of the Rad53p-dependent checkpoint pathways controlling cell cycle progression in response to DNA damage.

Indexed as

Cell Cycle ProteinsProtein Serine-Threonine KinasesSaccharomyces cerevisiae ProteinsBlotting, WesternCell CycleCheckpoint Kinase 2DNADNA DamageDNA PrimaseDNA ReplicationEnzyme StabilityFlow CytometryFungal ProteinsGene Expression Regulation, FungalGenes, FungalInterphaseCell Cycle ProteinsCheckpoint Kinase 2DNADNA PrimaseFungal ProteinsMethyl MethanesulfonateMutagensProtein KinasesProtein Serine-Threonine KinasesRAD53 protein, S cerevisiaeRNA NucleotidyltransferasesSaccharomyces cerevisiae Proteins

Identifiers

PMID9034345
PMCPMC1169666
OpenAlexW2037174303

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.