Evidence map›Paper›PMID 30682825›Full record

ArticleBiomolecules2019

Putative Mechanisms Underlying High Inhibitory Activities of Bimodular DNA Aptamers to Thrombin.

Elena G Zavyalova, Valeriia A Legatova, Rugiya Sh Alieva, Arthur O Zalevsky, Vadim N Tashlitsky, Alexander M Arutyunyan, Alexey M Kopylov

Abstract read
In one paragraph

Article in Biomolecules, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
–field-weighted citation impact
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

12 citing papers in PubMed.

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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

7 authors.

Elena G ZavyalovaChemistry Department, Lomonosov Moscow State University, 119991 Moscow, Russia. zlenka2006@gmail.com.ORCID 0000-0001-5260-1973
Valeriia A LegatovaChemistry Department, Lomonosov Moscow State University, 119991 Moscow, Russia. lera000006@gmail.com.
Rugiya Sh AlievaChemistry Department, Lomonosov Moscow State University, 119991 Moscow, Russia. ruqiwa_eva@mail.ru.
Arthur O ZalevskyFaculty of Bioengineering and Bioinformatics, Lomonosov Moscow State University, 119234 Moscow, Russia. aozalevsky@gmail.com.ORCID 0000-0001-6987-8119
Vadim N TashlitskyChemistry Department, Lomonosov Moscow State University, 119991 Moscow, Russia. tashlitsky@belozersky.msu.ru.
Alexander M ArutyunyanBelozersky Research Institute of Physico-Chemical Biology, Lomonosov Moscow State University, 119991 Moscow, Russia. alarut@genebee.msu.ru.
Alexey M KopylovChemistry Department, Lomonosov Moscow State University, 119991 Moscow, Russia. kopylov.alex@gmail.com.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Nucleic acid aptamers are prospective molecular recognizing elements. Similar to antibodies, aptamers are capable of providing specific recognition due to their spatial structure. However, the apparent simplicity of oligonucleotide folding is often elusive, as there is a balance between several conformations and, in some cases, oligomeric structures. This research is focused on establishing a thermodynamic background and the conformational heterogeneity of aptamers taking a series of thrombin DNA aptamers having G-quadruplex and duplex modules as an example. A series of aptamers with similar modular structures was characterized with spectroscopic and chromatographic techniques, providing examples of the conformational homogeneity of aptamers with high inhibitory activity, as well as a mixture of monomeric and oligomeric species for aptamers with low inhibitory activity. Thermodynamic parameters for aptamer unfolding were calculated, and their correlation with aptamer functional activity was found. Detailed analysis of thrombin complexes with G-quadruplex aptamers bound to exosite I revealed the similarity of the interfaces of aptamers with drastically different affinities to thrombin. It could be suggested that there are some events during complex formation that have a larger impact on the affinity than the states of initial and final macromolecules. Possible mechanisms of the complex formation and a role of the duplex module in the association process are discussed.

Indexed as

Aptamers, NucleotideOligonucleotidesProtein UnfoldingSerine Proteinase InhibitorsThermodynamicsThrombinAptamers, NucleotideOligonucleotidesSerine Proteinase InhibitorsThrombinconformational polymorphismDNA aptamerG-quadruplexstructure–activity relationshipthermodynamicsthrombin

Identifiers

PMID30682825
PMCPMC6406280

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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.