Evidence map›Paper›PMID 27065883›Full record

ArticleFrontiers in physiology2016

Flavonolignans As a Novel Class of Sodium Pump Inhibitors.

Martin Kubala, Petra Čechová, Jaroslava Geletičová, Michal Biler, Tereza Štenclová, Patrick Trouillas, David Biedermann

Open access · goldAbstract read
In one paragraph

Article in Frontiers in physiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
3.8field-weighted citation impact, top 8% 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

6 citing papers in PubMed, 18 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Identification of cisplatin-binding sites on the large cytoplasmic loop of the NaJournal of enzyme inhibition and medicinal chemistry · 2018
    Article
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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 at 3 institutions in 2 countries.

Martin KubalaDepartment of Biophysics, Faculty of Science, Centre of Region Haná for Biotechnological and Agricultural Research, Palacký University Olomouc, Czech Republic.
Petra ČechováDepartment of Biophysics, Faculty of Science, Centre of Region Haná for Biotechnological and Agricultural Research, Palacký University Olomouc, Czech Republic.
Jaroslava GeletičováDepartment of Biophysics, Faculty of Science, Centre of Region Haná for Biotechnological and Agricultural Research, Palacký University Olomouc, Czech Republic.
Michal BilerDepartment of Biophysics, Faculty of Science, Centre of Region Haná for Biotechnological and Agricultural Research, Palacký UniversityOlomouc, Czech Republic; INSERM UMR 850, School of Pharmacy, University LimogesLimoges, France.
Tereza ŠtenclováDepartment of Biophysics, Faculty of Science, Centre of Region Haná for Biotechnological and Agricultural Research, Palacký University Olomouc, Czech Republic.
Patrick TrouillasINSERM UMR 850, School of Pharmacy, University LimogesLimoges, France; Department of Physical Chemistry, Faculty of Science, Regional Centre of Advanced Technologies and Materials, Palacký UniversityOlomouc, Czech Republic.
David BiedermannLaboratory of Biotransformation, Institute of Microbiology, Czech Academy of Sciences Prague, Czech Republic.
Palacký University Olomouc · CZCzech Academy of Sciences · CZInserm · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We examined the inhibitory effects of three flavonolignans and their dehydro- derivatives, taxifolin and quercetin on the activity of the Na(+)/K(+)-ATPase (NKA). The flavonolignans silychristin, dehydrosilychristin and dehydrosilydianin inhibited NKA with IC50 of 110 ± 40 μM, 38 ± 8 μM, and 36 ± 14 μM, respectively. Using the methods of molecular modeling, we identified several possible binding sites for these species on NKA and proposed the possible mechanisms of inhibition. The binding to the extracellular- or cytoplasmic C-terminal sites can block the transport of cations through the plasma membrane, while the binding on the interface of cytoplasmic domains can inhibit the enzyme allosterically. Fluorescence spectroscopy experiments confirmed the interaction of these three species with the large cytoplasmic segment connecting transmembrane helices 4 and 5 (C45). The flavonolignans are distinct from the cardiac glycosides that are currently used in NKA treatment. Because their binding sites are different, the mechanism of inhibition is different as well as the range of active concentrations, one can expect that these new NKA inhibitors would exhibit also a different biomedical actions than cardiac glycosides.

Indexed as

binding sitesflavonolignansinhibitionNa+/K+-ATPasesodium pump

Identifiers

PMID27065883
PMCPMC4812144
OpenAlexW2324865675

What OpenQuestion holds

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Registered trials

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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.