Evidence map›Paper›PMID 33649352›Full record

ArticleScientific reports2021

The contribution of PARP1, PARP2 and poly(ADP-ribosyl)ation to base excision repair in the nucleosomal context.

M M Kutuzov, E A Belousova, T A Kurgina, A A Ukraintsev, I A Vasil'eva, S N Khodyreva, O I Lavrik

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
3.3field-weighted citation impact, top 5% 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

31 citing papers in PubMed, 58 citations in OpenAlex.

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  16. Review
  17. PARP3 Affects Nucleosome Compaction Regulation.International journal of molecular sciences · 2023
    Article
  18. Generation of Recombinant Nucleosomes Containing Site-Specific DNA Damage.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  19. Review
  20. 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

7 authors at 3 institutions in 1 country.

M M Kutuzov *Institute of Chemical Biology and Fundamental Medicine, SB RAS, Novosibirsk, Russia.
E A Belousova *Institute of Chemical Biology and Fundamental Medicine, SB RAS, Novosibirsk, Russia.
T A KurginaInstitute of Chemical Biology and Fundamental Medicine, SB RAS, Novosibirsk, Russia.
A A UkraintsevInstitute of Chemical Biology and Fundamental Medicine, SB RAS, Novosibirsk, Russia.
I A Vasil'evaInstitute of Chemical Biology and Fundamental Medicine, SB RAS, Novosibirsk, Russia.
S N KhodyrevaInstitute of Chemical Biology and Fundamental Medicine, SB RAS, Novosibirsk, Russia.
O I LavrikInstitute of Chemical Biology and Fundamental Medicine, SB RAS, Novosibirsk, Russia. lavrik@niboch.nsc.ru.
Institute of Chemical Biology and Fundamental Medicine · RUSiberian Branch of the Russian Academy of Sciences · RUNovosibirsk State University · RU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The regulation of repair processes including base excision repair (BER) in the presence of DNA damage is implemented by a cellular signal: poly(ADP-ribosyl)ation (PARylation), which is catalysed by PARP1 and PARP2. Despite ample studies, it is far from clear how BER is regulated by PARPs and how the roles are distributed between the PARPs. Here, we investigated the effects of PARP1, PARP2 and PARylation on activities of the main BER enzymes (APE1, DNA polymerase β [Polβ] and DNA ligase IIIα [LigIIIα]) in combination with BER scaffold protein XRCC1 in the nucleosomal context. We constructed nucleosome core particles with midward- or outward-oriented damage. It was concluded that in most cases, the presence of PARP1 leads to the suppression of the activities of APE1, Polβ and to a lesser extent LigIIIα. PARylation by PARP1 attenuated this effect to various degrees depending on the enzyme. PARP2 had an influence predominantly on the last stage of BER: DNA sealing. Nonetheless, PARylation by PARP2 led to Polβ inhibition and to significant stimulation of LigIIIα activities in a NAD

Indexed as

DNA RepairPoly ADP RibosylationDNAHumansNucleosomesPoly (ADP-Ribose) Polymerase-1Poly(ADP-ribose) PolymerasesDNANucleosomesPARP1 protein, humanPARP2 protein, humanPoly (ADP-Ribose) Polymerase-1Poly(ADP-ribose) Polymerases

Identifiers

PMID33649352
PMCPMC7921663
OpenAlexW3135024668

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Registered trials

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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.