Evidence map›Paper›PMID 29736333›Full record

ArticlePeerJ2018

From in silico to in vitro: a trip to reveal flavonoid binding on the

Alfonso Trezza, Vittoria Cicaloni, Piera Porciatti, Andrea Langella, Fabio Fusi, Simona Saponara, Ottavia Spiga

Open access · goldAbstract read
In one paragraph

Article in PeerJ, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed, 1 pooled it
1.4field-weighted citation impact, top 18% 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, 1 synthesis or guideline pooled it, 17 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Flavonoids as Modulators of Potassium Channels.International journal of molecular sciences · 2023
    Review
  5. VietnameseMolecules (Basel, Switzerland) · 2022
    Article
  6. The Selective Rat Toxicant Norbormide Blocks KFrontiers in pharmacology · 2019
    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

7 authors at 1 institution in 1 country.

Alfonso TrezzaDepartment of Biotechnology, Chemistry and Pharmacy, University of Siena, Siena, Italy.
Vittoria CicaloniDepartment of Biotechnology, Chemistry and Pharmacy, University of Siena, Siena, Italy.
Piera PorciattiDepartment of Biotechnology, Chemistry and Pharmacy, University of Siena, Siena, Italy.
Andrea LangellaDepartment of Biotechnology, Chemistry and Pharmacy, University of Siena, Siena, Italy.
Fabio FusiDepartment of Life Sciences, University of Siena, Siena, Italy.ORCID 0000-0002-5737-8309
Simona SaponaraDepartment of Life Sciences, University of Siena, Siena, Italy.
Ottavia SpigaDepartment of Biotechnology, Chemistry and Pharmacy, University of Siena, Siena, Italy.ORCID 0000-0002-0263-7107
University of Siena · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundATP-sensitive inward rectifier potassium channels (Kir), are a potassium channel family involved in many physiological processes. K

methodsA broader view of the K

resultsComputational analysis by performing molecular dynamics (MD) and docking simulation on rat 3D modelled structure have been completed, in its closed and open conformation state and in complex with Quercetin, 5-Hydroxyflavone and Rutin flavonoids. Our study showed that only Quercetin and 5-Hydroxyflavone were responsible for a significant down-regulation of the Kir6.1 activity, stabilising it in a closed conformation. This hypothesis was supported by in vitro experiments demonstrating that Quercetin and 5-Hydroxyflavone were capable to inhibit K

conclusionCombined methodological approaches, such as molecular modelling, docking and MD simulations of Kir6.1 channel, used to elucidate flavonoids intrinsic mechanism of action, are introduced, revealing a new potential druggable protein site.

Indexed as

ATP-sensitive inward rectifier potassium channelBinding siteFlavonoidHomology modelingKir6.1Molecular dockingMolecular dynamicsPatch clampPotassium channel

Identifiers

PMID29736333
PMCPMC5936070
OpenAlexW2799773667

What OpenQuestion 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 OpenQuestion graph.