Evidence map›Paper›PMID 42589256›Full record

ArticleInternational journal of molecular sciences2026

Poly(ADP-Ribose) polymerase1 Has Potential to Facilitate the Nucleosome Disassembly.

Aleksandr A Alekseev, Mikhail M Kutuzov, Ekaterina A Belousova, Alexander A Ukraintsev, Ivan D Goncharov, Aleksandra A Vasileva, Mikhail A Khodorkovskii, Olga I Lavrik

Abstract read
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Article in International journal of molecular sciences, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0citing papers in PubMed
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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

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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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

8 authors.

Aleksandr A AlekseevPeter the Great St. Petersburg Polytechnic University, Saint Petersburg 195251, Russia.ORCID 0000-0003-4371-265X
Mikhail M KutuzovInstitute of Chemical Biology and Fundamental Medicine, Novosibirsk 630090, Russia.ORCID 0000-0003-0927-4043
Ekaterina A BelousovaInstitute of Chemical Biology and Fundamental Medicine, Novosibirsk 630090, Russia.ORCID 0000-0002-4361-3793
Alexander A UkraintsevInstitute of Chemical Biology and Fundamental Medicine, Novosibirsk 630090, Russia.ORCID 0000-0001-7249-4458
Ivan D GoncharovPeter the Great St. Petersburg Polytechnic University, Saint Petersburg 195251, Russia.
Aleksandra A VasilevaPeter the Great St. Petersburg Polytechnic University, Saint Petersburg 195251, Russia.ORCID 0000-0002-0070-4898
Mikhail A KhodorkovskiiPeter the Great St. Petersburg Polytechnic University, Saint Petersburg 195251, Russia.ORCID 0000-0003-0562-0156
Olga I LavrikInstitute of Chemical Biology and Fundamental Medicine, Novosibirsk 630090, Russia.

Funding

Russian Science Foundation 24-74-00107Russian Science Foundation 25-74-30006Russian state-funded project 125012300658-9
6 · The paper itself

Abstract

Being the basic building blocks of chromatin, nucleosomes and their stability determine the genome accessibility for different DNA-dependent proteins. This characteristic is labile under cell-life processes. One of the abundant DNA-binding proteins, which is important for genome compaction, is poly(ADP-ribose) polymerase1 (PARP1). Despite the extensive experimental data on the chromatin compaction regulation under ADP-ribosylation, the details of the interplay of nucleosome with PARP1 in the absence of protein activation remain unclear. In this study, we discovered unusual changes of the nucleosome wrapping strength upon PARP1 interaction using a single-molecule approach-optical tweezers. We demonstrated that PARP1 binding leads to weakening of the contacts of inner DNA turn in nucleosome.

Indexed as

Chromatin Assembly and DisassemblyNucleosomesPoly (ADP-Ribose) Polymerase-1DNAHumansOptical TweezersProtein BindingDNANucleosomesPoly (ADP-Ribose) Polymerase-1chromatin like particlenucleosomeoptical tweezerspoly(ADP-ribose) polymerase1

Identifiers

PMID42589256
PMCPMC13465022

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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.