Evidence map›Paper›PMID 38698556›Full record

ReviewExpert reviews in molecular medicine2024

Specific and shared biological functions of PARP2 - is PARP2 really a lil' brother of PARP1?

Magdolna Szántó, José Yélamos, Péter Bai

Abstract readReview
In one paragraph

Review in Expert reviews in molecular medicine, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
–field-weighted citation impact
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

16 citing papers in PubMed.

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  16. Leveraging PARP-1/2 to Target Distant Metastasis.International journal of molecular sciences · 2024
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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

3 authors.

Magdolna SzántóDepartment of Medical Chemistry, Faculty of Medicine, University of Debrecen, Debrecen, 4032, Hungary.
José YélamosHospital del Mar Research Institute, Barcelona, Spain.ORCID 0000-0003-1195-1496
Péter BaiHUN-REN-UD Cell Biology and Signaling Research Group, Debrecen, 4032, Hungary.ORCID 0000-0002-6191-6616

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

PARP2, that belongs to the family of ADP-ribosyl transferase enzymes (ART), is a discovery of the millennium, as it was identified in 1999. Although PARP2 was described initially as a DNA repair factor, it is now evident that PARP2 partakes in the regulation or execution of multiple biological processes as inflammation, carcinogenesis and cancer progression, metabolism or oxidative stress-related diseases. Hereby, we review the involvement of PARP2 in these processes with the aim of understanding which processes are specific for PARP2, but not for other members of the ART family. A better understanding of the specific functions of PARP2 in all of these biological processes is crucial for the development of new PARP-centred selective therapies.

Indexed as

NeoplasmsPoly (ADP-Ribose) Polymerase-1Poly(ADP-ribose) PolymerasesAnimalsCarcinogenesisDNA RepairHumansInflammationOxidative StressPARP1 protein, humanPARP2 protein, humanPoly (ADP-Ribose) Polymerase-1Poly(ADP-ribose) PolymerasesagingATRDcancercell deathinflammationmetabolismmitochondriaPARP

Identifiers

PMID38698556
PMCPMC11140550

What Socratic holds

Textmetadata
LicenceCC BY-NC-ND
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 Socratic graph.