Evidence map›Paper›PMID 30475809›Full record

ArticlePloS one2018

A study on endonuclease BspD6I and its stimulus-responsive switching by modified oligonucleotides.

Liudmila A Abrosimova, Anzhela Yu Migur, Elena A Kubareva, Timofei S Zatsepin, Aleksandra V Gavshina, Alfiya K Yunusova, Tatiana A Perevyazova, Alfred Pingoud, Tatiana S Oretskaya

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in PloS one, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.4field-weighted citation impact, top 38% 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

2 citing papers in PubMed, 6 citations in OpenAlex.

  1. Types and Applications of Nicking Enzyme-Combined Isothermal Amplification.International journal of molecular sciences · 2022
    Review
  2. 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

9 authors at 4 institutions in 2 countries.

Liudmila A AbrosimovaDepartment of Chemistry and A.N. Belozersky Institute of Physico-Chemical Biology, M.V. Lomonosov Moscow State University, Moscow, Russia.ORCID 0000-0002-8975-8285
Anzhela Yu MigurDepartment of Chemistry and A.N. Belozersky Institute of Physico-Chemical Biology, M.V. Lomonosov Moscow State University, Moscow, Russia.
Elena A KubarevaDepartment of Chemistry and A.N. Belozersky Institute of Physico-Chemical Biology, M.V. Lomonosov Moscow State University, Moscow, Russia.
Timofei S ZatsepinDepartment of Chemistry and A.N. Belozersky Institute of Physico-Chemical Biology, M.V. Lomonosov Moscow State University, Moscow, Russia.
Aleksandra V GavshinaDepartment of Chemistry and A.N. Belozersky Institute of Physico-Chemical Biology, M.V. Lomonosov Moscow State University, Moscow, Russia.
Alfiya K YunusovaInstitute of Theoretical and Experimental Biophysics of Russian Academy of Sciences, Pushchino, Moscow region, Russia.
Tatiana A PerevyazovaInstitute of Theoretical and Experimental Biophysics of Russian Academy of Sciences, Pushchino, Moscow region, Russia.
Alfred PingoudInstitute of Biochemistry, Justus-Liebig University, Giessen, Germany.
Tatiana S OretskayaDepartment of Chemistry and A.N. Belozersky Institute of Physico-Chemical Biology, M.V. Lomonosov Moscow State University, Moscow, Russia.
Lomonosov Moscow State University · RUInstitute of Theoretical and Experimental Biophysics · RUJustus-Liebig-Universität Gießen · DESkolkovo Institute of Science and Technology · RU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Nicking endonucleases (NEases) selectively cleave single DNA strands in double-stranded DNAs at a specific site. They are widely used in bioanalytical applications and in genome editing; however, the peculiarities of DNA-protein interactions for most of them are still poorly studied. Previously, it has been shown that the large subunit of heterodimeric restriction endonuclease BspD6I (Nt.BstD6I) acts as a NEase. Here we present a study of interaction of restriction endonuclease BspD6I with modified DNA containing single non-nucleotide insertion with an azobenzene moiety in the enzyme cleavage sites or in positions of sugar-phosphate backbone nearby. According to these data, we designed a number of effective stimulus-responsive oligonucleotide inhibitors bearing azobenzene or triethylene glycol residues. These modified oligonucleotides modulated the functional activity of Nt.BspD6I after cooling or heating. We were able to block the cleavage of T7 phage DNA by this enzyme in the presence of such inhibitors at 20-25°C, whereas the Nt.BspD6I ability to hydrolyze DNA was completely restored after heating to 45°C. The observed effects can serve as a basis for the development of a platform for regulation of NEase activity in vitro or in vivo by external signals.

Indexed as

Azo CompoundsBacteriophage T7Deoxyribonuclease IDNA, ViralEscherichia coliEscherichia coli ProteinsOligodeoxyribonucleotidesPolyethylene GlycolsazobenzeneAzo CompoundsBspD6I protein, E coliDeoxyribonuclease IDNA, ViralEscherichia coli ProteinsOligodeoxyribonucleotidesPolyethylene Glycolstriethylene glycol

Identifiers

PMID30475809
PMCPMC6261011
OpenAlexW2903146490

What Socratic 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 Socratic graph.