Evidence map›Paper›PMID 32769996›Full record

ArticleScientific reports2020

Effect of allosteric inhibition of non-muscle myosin 2 on its intracellular diffusion.

Ádám I Horváth, Máté Gyimesi, Boglárka H Várkuti, Miklós Képiró, Gábor Szegvári, István Lőrincz, György Hegyi, Mihály Kovács, András Málnási-Csizmadia

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.4field-weighted citation impact, top 41% 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

5 citing papers in PubMed, 6 citations in OpenAlex.

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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

9 authors at 1 institution in 1 country.

Ádám I HorváthMTA-ELTE Motor Pharmacology Research Group, Department of Biochemistry, Eötvös Loránd University, Pázmány Péter sétány 1/c, 1117, Budapest, Hungary.
Máté GyimesiMTA-ELTE Motor Pharmacology Research Group, Department of Biochemistry, Eötvös Loránd University, Pázmány Péter sétány 1/c, 1117, Budapest, Hungary.
Boglárka H VárkutiMTA-ELTE Motor Pharmacology Research Group, Department of Biochemistry, Eötvös Loránd University, Pázmány Péter sétány 1/c, 1117, Budapest, Hungary.
Miklós KépiróMTA-ELTE Motor Pharmacology Research Group, Department of Biochemistry, Eötvös Loránd University, Pázmány Péter sétány 1/c, 1117, Budapest, Hungary.
Gábor SzegváriMTA-ELTE Motor Pharmacology Research Group, Department of Biochemistry, Eötvös Loránd University, Pázmány Péter sétány 1/c, 1117, Budapest, Hungary.ORCID https://orcid.org/0000-0001-5265-8662
István LőrinczMTA-ELTE Motor Pharmacology Research Group, Department of Biochemistry, Eötvös Loránd University, Pázmány Péter sétány 1/c, 1117, Budapest, Hungary.
György HegyiMTA-ELTE Motor Pharmacology Research Group, Department of Biochemistry, Eötvös Loránd University, Pázmány Péter sétány 1/c, 1117, Budapest, Hungary.
Mihály KovácsMTA-ELTE Motor Pharmacology Research Group, Department of Biochemistry, Eötvös Loránd University, Pázmány Péter sétány 1/c, 1117, Budapest, Hungary. mihaly.kovacs@ttk.elte.hu.
András Málnási-CsizmadiaMTA-ELTE Motor Pharmacology Research Group, Department of Biochemistry, Eötvös Loránd University, Pázmány Péter sétány 1/c, 1117, Budapest, Hungary. malna@elte.hu.
Eötvös Loránd University · HU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Subcellular dynamics of non-muscle myosin 2 (NM2) is crucial for a broad-array of cellular functions. To unveil mechanisms of NM2 pharmacological control, we determined how the dynamics of NM2 diffusion is affected by NM2's allosteric inhibitors, i.e. blebbistatin derivatives, as compared to Y-27632 inhibiting ROCK, NM2's upstream regulator. We found that NM2 diffusion is markedly faster in central fibers than in peripheral stress fibers. Y-27632 accelerated NM2 diffusion in both peripheral and central fibers, whereas in peripheral fibers blebbistatin derivatives slightly accelerated NM2 diffusion at low, but markedly slowed it at high inhibitor concentrations. In contrast, rapid NM2 diffusion in central fibers was unaffected by direct NM2 inhibition. Using our optopharmacological tool, Molecular Tattoo, sub-effective concentrations of a photo-crosslinkable blebbistatin derivative were increased to effective levels in a small, irradiated area of peripheral fibers. These findings suggest that direct allosteric inhibition affects the diffusion profile of NM2 in a markedly different manner compared to the disruption of the upstream control of NM2. The pharmacological action of myosin inhibitors is channeled through autonomous molecular processes and might be affected by the load acting on the NM2 proteins.

Indexed as

Allosteric RegulationAnimalsCell Line, TumorDiffusionHeLa CellsHeterocyclic Compounds, 4 or More RingsHumansMyosin Type IIRatsblebbistatinHeterocyclic Compounds, 4 or More RingsMyosin Type II

Identifiers

PMID32769996
PMCPMC7415145
OpenAlexW3047886988

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.