Evidence map›Paper›PMID 22842922›Full record

ArticleNature cell biology2012

Dissecting DNA damage response pathways by analysing protein localization and abundance changes during DNA replication stress.

Johnny M Tkach, Askar Yimit, Anna Y Lee, Michael Riffle, Michael Costanzo, Daniel Jaschob, Jason A Hendry, Jiongwen Ou, Jason Moffat, Charles Boone and 3 more

Open access · greenAbstract read
In one paragraph

Article in Nature cell biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 297 papers.

0numbers the graph read from it
0cells of the map it votes in
297citing papers in PubMed
16.4field-weighted citation impact, top 1% 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

297 citing papers in PubMed, 527 citations in OpenAlex.

  1. Article
  2. Article
  3. The role of the nucleus in the control of mitochondrial precursor proteins in yeast.Protein science : a publication of the Protein Society · 2026
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  4. Truncation ofSynthetic and systems biotechnology · 2026
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  17. Structure of the yeast ceramide synthase.Nature structural & molecular biology · 2025
    Article
  18. Biological Amyloids Chemically Damage DNA.ACS chemical neuroscience · 2025
    Article
  19. Article
  20. Article

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

13 authors at 3 institutions in 2 countries.

Johnny M TkachDepartment of Biochemistry, University of Toronto, Toronto, Ontario M5S 1A8, Canada.
Askar Yimit
Anna Y Lee
Michael Riffle
Michael Costanzo
Daniel Jaschob
Jason A Hendry
Jiongwen Ou
Jason Moffat
Charles Boone
Trisha N Davis
Corey Nislow
Grant W Brown
University of Toronto · CAUniversity of Washington · USCanada Research Chairs · CA

Funding

ZDS2P REGULATES SWE1P-DEPENDENT POLARIZED CELL GROWTH IN S CEREVISIAEP41RR011823 · NCRR · UNIVERSITY OF WASHINGTON · PI DAVIS, TRACY · 1996 to 2011
$24.7M
TrainingP41GM103533 · NIGMS · UNIVERSITY OF WASHINGTON · PI MACCOSS, MICHAEL · 2012 to 2021
$20.7M
Mapping the reference genetic network of a eukaryotic cellR01HG005853 · NHGRI · UNIVERSITY OF TORONTO · PI ANDREWS, BRENDA JEAN, BOONE, CHARLES · 2010 to 2025
$7.6M
CIHR MOP-102629CIHR MOP-97939NCRR NIH HHS P41 RR011823NCRR NIH HHS P41 RR11823NHGRI NIH HHS 1R01HG005853NHGRI NIH HHS R01 HG005853NIGMS NIH HHS P41 GM103533
6 · The paper itself

Abstract

Relocalization of proteins is a hallmark of the DNA damage response. We use high-throughput microscopic screening of the yeast GFP fusion collection to develop a systems-level view of protein reorganization following drug-induced DNA replication stress. Changes in protein localization and abundance reveal drug-specific patterns of functional enrichments. Classification of proteins by subcellular destination enables the identification of pathways that respond to replication stress. We analysed pairwise combinations of GFP fusions and gene deletion mutants to define and order two previously unknown DNA damage responses. In the first, Cmr1 forms subnuclear foci that are regulated by the histone deacetylase Hos2 and are distinct from the typical Rad52 repair foci. In a second example, we find that the checkpoint kinases Mec1/Tel1 and the translation regulator Asc1 regulate P-body formation. This method identifies response pathways that were not detected in genetic and protein interaction screens, and can be readily applied to any form of chemical or genetic stress to reveal cellular response pathways.

Indexed as

DNA DamageAdaptor Proteins, Signal TransducingDNA-Binding ProteinsDNA ReplicationGene DeletionGTP-Binding ProteinsHistone DeacetylasesIntracellular Signaling Peptides and ProteinsProtein Serine-Threonine KinasesProtein TransportSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence DeletionAdaptor Proteins, Signal TransducingASC1 protein, S cerevisiaeCmr1 protein, S cerevisiaeDNA-Binding ProteinsGTP-Binding ProteinsHistone DeacetylasesIntracellular Signaling Peptides and ProteinsMEC1 protein, S cerevisiaeProtein Serine-Threonine KinasesSaccharomyces cerevisiae ProteinsTEL1 protein, S cerevisiae

Identifiers

PMID22842922
PMCPMC3434236
OpenAlexW2058274661

What OpenQuestion holds

Textmetadata
LicenceTDM
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.