Evidence map›Paper›PMID 26181362›Full record

ArticleBioscience reports2015

Poly(ADP-ribose)polymerase 1 stimulates the AP-site cleavage activity of tyrosyl-DNA phosphodiesterase 1.

Natalia A Lebedeva, Rashid O Anarbaev, Maria Sukhanova, Inna A Vasil'eva, Nadejda I Rechkunova, Olga I Lavrik

Open access · goldAbstract read
In one paragraph

Article in Bioscience reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.9field-weighted citation impact, top 25% 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

6 citing papers in PubMed, 14 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Coordination of DNA single strand break repair.Free radical biology & medicine · 2017
    Review
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

6 authors at 2 institutions in 1 country.

Natalia A LebedevaInstitute of Chemical Biology and Fundamental Medicine, Lavrentiev av. 8, Novosibirsk 630090, Russia Department of Natural Sciences, Novosibirsk State University, 2 Pirogov Street, Novosibirsk 630090, Russia.
Rashid O AnarbaevInstitute of Chemical Biology and Fundamental Medicine, Lavrentiev av. 8, Novosibirsk 630090, Russia Department of Natural Sciences, Novosibirsk State University, 2 Pirogov Street, Novosibirsk 630090, Russia.
Maria SukhanovaInstitute of Chemical Biology and Fundamental Medicine, Lavrentiev av. 8, Novosibirsk 630090, Russia Department of Natural Sciences, Novosibirsk State University, 2 Pirogov Street, Novosibirsk 630090, Russia.
Inna A Vasil'evaInstitute of Chemical Biology and Fundamental Medicine, Lavrentiev av. 8, Novosibirsk 630090, Russia.
Nadejda I RechkunovaInstitute of Chemical Biology and Fundamental Medicine, Lavrentiev av. 8, Novosibirsk 630090, Russia Department of Natural Sciences, Novosibirsk State University, 2 Pirogov Street, Novosibirsk 630090, Russia.
Olga I LavrikInstitute of Chemical Biology and Fundamental Medicine, Lavrentiev av. 8, Novosibirsk 630090, Russia Department of Natural Sciences, Novosibirsk State University, 2 Pirogov Street, Novosibirsk 630090, Russia lavrik@niboch.nsc.ru.
Institute of Chemical Biology and Fundamental Medicine · RUNovosibirsk State University · RU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The influence of poly(ADP-ribose)polymerase 1 (PARP1) on the apurinic/apyrimidinic (AP)-site cleavage activity of tyrosyl-DNA phosphodiesterase 1 (TDP1) and interaction of PARP1 and TDP1 were studied. The efficiency of single or clustered AP-site hydrolysis catalysed by TDP1 was estimated. It was shown that the efficiency of AP-site cleavage increases in the presence of an additional AP-site in the opposite DNA strand depending on its position. PARP1 stimulates TDP1; the stimulation effect was abolished in the presence of NAD(+). The interaction of these two proteins was characterized quantitatively by measuring the dissociation constant for the TDP1-PARP1 complex using fluorescently-labelled proteins. The distance between the N-termini of the proteins within the complex was estimated using FRET. The data obtained suggest that PARP1 and TDP1 bind in an antiparallel orientation; the N-terminus of the former protein interacts with the C-terminal domain of the latter. The functional significance of PARP1 and TDP1 interaction in the process of DNA repair was demonstrated for the first time.

Indexed as

DNAHumansMultienzyme ComplexesNADPhosphoric Diester HydrolasesPoly (ADP-Ribose) Polymerase-1Poly(ADP-ribose) PolymerasesProtein Structure, TertiaryDNAMultienzyme ComplexesNADPARP1 protein, humanPhosphoric Diester HydrolasesPoly (ADP-Ribose) Polymerase-1Poly(ADP-ribose) PolymerasesTDP1 protein, humanclustered damagesfluorescently-labelled proteinspoly(ADP-ribose)polymerase 1protein–protein interactiontyrosyl-DNA phosphodiesterase 1

Identifiers

PMID26181362
PMCPMC4721542
OpenAlexW2341578220

What OpenQuestion holds

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LicenceCC BY
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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.