Evidence map›Paper›PMID 22615993›Full record

ArticlePloS one2012

Identification of novel human damage response proteins targeted through yeast orthology.

J Peter Svensson, Rebecca C Fry, Emma Wang, Luis A Somoza, Leona D Samson

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
0.4field-weighted citation impact, top 37% 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

8 citing papers in PubMed, 10 citations in OpenAlex.

  1. Article
  2. Evolution-based screening enables genome-wide prioritization and discovery of DNA repair genes.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  3. Article
  4. Article
  5. Autophagy and p53.Cold Spring Harbor perspectives in medicine · 2016
    Review
  6. Article
  7. Article
  8. 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

5 authors at 2 institutions in 1 country.

J Peter SvenssonBiological Engineering Department, Center for Environmental Health Sciences, Massachusetts Institute of Technology, Cambridge, Massachusetts, United States of America.
Rebecca C Fry
Emma Wang
Luis A Somoza
Leona D Samson
Center for Environmental Health · USMassachusetts Institute of Technology · US

Funding

Tumor Cell Networks CenterU54CA112967 · NCI · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI LAUFFENBURGER, DOUGLAS A · 2004 to 2015
$26.2M
TOXICOLOGY CORE UNITP30ES002109 · NIEHS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI LEVINE, STUART S · 1985 to 2020
$25.6M
EUKARYTIC DNA ALKYLATION REPAIRR01CA055042 · NCI · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI SAMSON, LEONA D. · 1991 to 2010
$4.8M
NCI NIH HHS CA112967NCI NIH HHS CA55042NCI NIH HHS R01 CA055042NCI NIH HHS U54 CA112967NIEHS NIH HHS ES02109NIEHS NIH HHS P30 ES002109
6 · The paper itself

Abstract

Studies in Saccharomyces cerevisiae show that many proteins influence cellular survival upon exposure to DNA damaging agents. We hypothesized that human orthologs of these S. cerevisiae proteins would also be required for cellular survival after treatment with DNA damaging agents. For this purpose, human homologs of S. cerevisiae proteins were identified and mapped onto the human protein-protein interaction network. The resulting human network was highly modular and a series of selection rules were implemented to identify 45 candidates for human toxicity-modulating proteins. The corresponding transcripts were targeted by RNA interference in human cells. The cell lines with depleted target expression were challenged with three DNA damaging agents: the alkylating agents MMS and 4-NQO, and the oxidizing agent t-BuOOH. A comparison of the survival revealed that the majority (74%) of proteins conferred either sensitivity or resistance. The identified human toxicity-modulating proteins represent a variety of biological functions: autophagy, chromatin modifications, RNA and protein metabolism, and telomere maintenance. Further studies revealed that MMS-induced autophagy increase the survival of cells treated with DNA damaging agents. In summary, we show that damage recovery proteins in humans can be identified through homology to S. cerevisiae and that many of the same pathways are represented among the toxicity modulators.

Indexed as

Protein Interaction MapsSequence Homology, Amino Acid4-Nitroquinoline-1-oxideAlkylating AgentsAutophagyCell LineChromatin Assembly and DisassemblyDNA DamageDNA RepairHumansMethyl MethanesulfonateMutagensQuinolonesSaccharomyces cerevisiaeSaccharomyces cerevisiae Proteinstert-Butylhydroperoxide4-Nitroquinoline-1-oxide4-nitroquinolone-1-oxideAlkylating AgentsMethyl MethanesulfonateMutagensQuinolonesRBSN protein, humanSaccharomyces cerevisiae Proteinstert-ButylhydroperoxideVesicular Transport Proteins

Identifiers

PMID22615993
PMCPMC3353887
OpenAlexW2140017874

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.