Evidence map›Paper›PMID 25460733›Full record

ReviewRedox biology2014

Inputs and outputs of poly(ADP-ribosyl)ation: Relevance to oxidative stress.

Csaba Hegedűs, László Virág

Open access · goldAbstract readReview
In one paragraph

Review in Redox biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
2.8field-weighted citation impact, top 8% 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

32 citing papers in PubMed, 60 citations in OpenAlex.

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  18. Targeting Nuclear NADCancers · 2020
    Article
  19. Article
  20. The role of poly(ADP-ribose) polymerases in manganese exposed Caenorhabditis elegans.Journal of trace elements in medicine and biology : organ of the Society for Minerals and Trace Elements (GMS) · 2020
    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

2 authors at 1 institution in 1 country.

Csaba HegedűsDepartment of Medical Chemistry, Faculty of Medicine, University of Debrecen, Nagyerdei Krt. 98., H-4032 Debrecen, Hungary.
László VirágDepartment of Medical Chemistry, Faculty of Medicine, University of Debrecen, Nagyerdei Krt. 98., H-4032 Debrecen, Hungary; MTA-DE Cell Biology and Signaling Research Group, Debrecen, Hungary. Electronic address: lvirag@med.unideb.hu.
University of Debrecen · HU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Oxidative stress can cause DNA breaks which induce activation of the DNA nick sensor enzyme poly(ADP-ribose) polymerase-1 (PARP-1), part of the 17 member PARP enzyme family. PARP-1 modifies target proteins by attaching to them several NAD-derived ADP-ribose units forming poly(ADP-ribose) (PAR) polymers. PARylation controls many cellular processes while intense PARylation may also lead to cell death by various mechanisms. Here we summarize the modes of activation, inhibitors and modulators of PARP-1 and review the cellular functions regulated by the enzyme.

Indexed as

AnimalsHumansOxidative StressPoly Adenosine Diphosphate RibosePoly (ADP-Ribose) Polymerase-1Poly ADP RibosylationPARP1 protein, humanPoly Adenosine Diphosphate RibosePoly (ADP-Ribose) Polymerase-1ApoptosisCell deathNecroptosisOxidative stressPARP1Poly(ADP-ribosyl)ation

Identifiers

PMID25460733
PMCPMC4215470
OpenAlexW2010022018

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.