Evidence map›Paper›PMID 23624145›Full record

ReviewMolecular aspects of medicine2013

Poly-ADP-ribose polymerase: machinery for nuclear processes.

Colin Thomas, Alexei V Tulin

Open access · greenAbstract readReview
In one paragraph

Review in Molecular aspects of medicine, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.

0numbers the graph read from it
0cells of the map it votes in
56citing papers in PubMed
5.6field-weighted citation impact, top 3% 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

56 citing papers in PubMed, 99 citations in OpenAlex.

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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.

Colin ThomasFox Chase Cancer Center, Philadelphia, PA 19111, USA.
Alexei V Tulin
Fox Chase Cancer Center · US

Funding

Poly ADP-ribose Polymerase in Chromatin and Transcriptional RegulationR01GM077452 · NIGMS · RESEARCH INST OF FOX CHASE CAN CTR · PI TULIN, ALEXEI V · 2008 to 2012
$1.6M
NIGMS NIH HHS R01 GM077452
6 · The paper itself

Abstract

It is becoming increasingly clear that the nuclear protein, poly-ADP-ribose polymerase 1 (PARP1), plays essential roles in the cell, including DNA repair, translation, transcription, telomere maintenance, and chromatin remodeling. Despite the exciting progress made in understanding the ubiquitous role of poly-ADP-ribose metabolism, a basic mechanism of PARP's activity regulating multiple nuclear processes is yet to be outlined. This review offers a holistic perspective on activity of PARP1, based on empirically observable phenomena. Primary attention is given to mechanisms by which PARP1 regulates a broad range of essential nuclear events, including two complementary processes (1) regulation of protein-nucleic acid interactions by means of protein shuttling and (2) utilizing poly-ADP-ribose as an anionic matrix for trapping, recruiting, and scaffolding proteins.

Indexed as

Adenosine Diphosphate RiboseAnimalsCell NucleusDNADNA RepairGene Expression RegulationHumansNuclear ProteinsPoly Adenosine Diphosphate RibosePoly(ADP-ribose) PolymerasesProtein Processing, Post-TranslationalAdenosine Diphosphate RiboseDNANuclear ProteinsPoly Adenosine Diphosphate RibosePoly(ADP-ribose) PolymerasesChromatinHistonesNucleosomePargPARP1Poly(ADP-ribose)

Identifiers

PMID23624145
PMCPMC3750069
OpenAlexW1975346450

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.