Evidence map›Paper›PMID 34830005›Full record

ArticleInternational journal of molecular sciences2021

Mechanisms of Nucleosome Reorganization by PARP1.

Natalya V Maluchenko, Dmitry K Nilov, Sergey V Pushkarev, Elena Y Kotova, Nadezhda S Gerasimova, Mikhail P Kirpichnikov, Marie-France Langelier, John M Pascal, Md Sohail Akhtar, Alexey V Feofanov and 1 more

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.3field-weighted citation impact, top 9% 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

17 citing papers in PubMed, 38 citations in OpenAlex.

  1. PARP1 Exhibits an Enzymatically Inactive Chromatin Binding Mode.bioRxiv : the preprint server for biology · 2026
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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

11 authors at 4 institutions in 4 countries.

Natalya V MaluchenkoFaculty of Biology, Lomonosov Moscow State University, 119234 Moscow, Russia.ORCID 0000-0003-4129-4984
Dmitry K NilovBelozersky Institute of Physicochemical Biology, Lomonosov Moscow State University, 119991 Moscow, Russia.ORCID 0000-0002-5067-7939
Sergey V PushkarevFaculty of Bioengineering and Bioinformatics, Lomonosov Moscow State University, 119991 Moscow, Russia.
Elena Y KotovaFox Chase Cancer Center, Philadelphia, PA 19111-2497, USA.
Nadezhda S GerasimovaFaculty of Biology, Lomonosov Moscow State University, 119234 Moscow, Russia.ORCID 0000-0002-5048-0378
Mikhail P KirpichnikovFaculty of Biology, Lomonosov Moscow State University, 119234 Moscow, Russia.
Marie-France LangelierDepartment of Biochemistry and Molecular Medicine, Université de Montréal, 2900 Boulevard Edouard-Montpetit, Montreal, QC H3T 1J4, Canada.
John M PascalDepartment of Biochemistry and Molecular Medicine, Université de Montréal, 2900 Boulevard Edouard-Montpetit, Montreal, QC H3T 1J4, Canada.
Md Sohail AkhtarMolecular and Structural Biology Division, CSIR-Central Drug Research Institute, Lucknow 226031, Uttar Pradesh, India.
Alexey V FeofanovFaculty of Biology, Lomonosov Moscow State University, 119234 Moscow, Russia.ORCID 0000-0002-1596-9506
Vasily M StuditskyFaculty of Biology, Lomonosov Moscow State University, 119234 Moscow, Russia.
Lomonosov Moscow State University · RUFox Chase Cancer Center · USUniversité de Montréal · CACentral Drug Research Institute · IN

Funding

Mechanisms of PARP-1 interaction with chromatinR21CA220151 · NCI · RESEARCH INST OF FOX CHASE CAN CTR · PI STUDITSKY, VASILY M · 2017 to 2019
$435k
Department of Science and Technology DST/INT/RUS/RSF/P27NCI NIH HHS R21 CA220151NIH HHS CA220151NIH HHS GM087282Russian Science Foundation 19-44-02013
6 · The paper itself

Abstract

Poly(ADP-ribose) polymerase 1 (PARP1) is an enzyme involved in DNA repair, chromatin organization and transcription. During transcription initiation, PARP1 interacts with gene promoters where it binds to nucleosomes, replaces linker histone H1 and participates in gene regulation. However, the mechanisms of PARP1-nucleosome interaction remain unknown. Here, using spFRET microscopy, molecular dynamics and biochemical approaches we identified several different PARP1-nucleosome complexes and two types of PARP1 binding to mononucleosomes: at DNA ends and end-independent. Two or three molecules of PARP1 can bind to a nucleosome depending on the presence of linker DNA and can induce reorganization of the entire nucleosome that is independent of catalytic activity of PARP1. Nucleosome reorganization depends upon binding of PARP1 to nucleosomal DNA, likely near the binding site of linker histone H1. The data suggest that PARP1 can induce the formation of an alternative nucleosome state that is likely involved in gene regulation and DNA repair.

Indexed as

ChromatinDNA-Binding ProteinsDNA RepairGene Expression RegulationHistonesHumansMolecular Dynamics SimulationNucleosomesPoly (ADP-Ribose) Polymerase-1Promoter Regions, GeneticChromatinDNA-Binding ProteinsHistonesNucleosomesPoly (ADP-Ribose) Polymerase-1molecular dynamicsnucleosomepoly(ADP-ribose) polymerase 1spFRET microscopy

Identifiers

PMID34830005
PMCPMC8620739
OpenAlexW3213781114

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.