Evidence map›Paper›PMID 30280322›Full record

ArticleJournal of molecular modeling2018

Interactions of cantharidin-like inhibitors with human protein phosphatase-5 in a Mg

Letícia C Assis, Alexandre A de Castro, Ingrid G Prandi, Daiana T Mancini, Juliana O S de Giacoppo, Ranylson M L Savedra, Tamiris M de Assis, Juliano B Carregal, Elaine F F da Cunha, Teodorico Castro Ramalho

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Article in Journal of molecular modeling, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0citing papers in PubMed
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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

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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

0 citing papers in PubMed, 0 citations in OpenAlex.

No citing paper in PubMed yet.

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

10 authors at 4 institutions in 2 countries.

Letícia C AssisLaboratory of Computational Chemistry, Department of Chemistry, Federal University of Lavras (UFLA), 3027, Campus Universitario, Lavras, 37200000, Minas Gerais, Brazil.
Alexandre A de CastroLaboratory of Computational Chemistry, Department of Chemistry, Federal University of Lavras (UFLA), 3027, Campus Universitario, Lavras, 37200000, Minas Gerais, Brazil.
Ingrid G PrandiLaboratory of Computational Chemistry, Department of Chemistry, Federal University of Lavras (UFLA), 3027, Campus Universitario, Lavras, 37200000, Minas Gerais, Brazil.
Daiana T ManciniLaboratory of Computational Chemistry, Department of Chemistry, Federal University of Lavras (UFLA), 3027, Campus Universitario, Lavras, 37200000, Minas Gerais, Brazil.
Juliana O S de GiacoppoLaboratory of Computational Chemistry, Department of Chemistry, Federal University of Lavras (UFLA), 3027, Campus Universitario, Lavras, 37200000, Minas Gerais, Brazil.
Ranylson M L SavedraLaboratory of Molecular Simulation of Material, Department of Physics, Federal University of Ouro Preto, Campus Universitário Morro do Cruzeiro, Ouro Preto, MG, CEP 35400-000, Brazil.
Tamiris M de AssisLaboratory of Computational Chemistry, Department of Chemistry, Federal University of Lavras (UFLA), 3027, Campus Universitario, Lavras, 37200000, Minas Gerais, Brazil.
Juliano B CarregalLaboratory of Molecular Modeling, Department of Chemistry, Federal University of São João del Rei (UFSJ), Rua Sebastião Gonçalves Coelho 400, Divinópolis, MG, 35501-296, Brazil.
Elaine F F da CunhaLaboratory of Computational Chemistry, Department of Chemistry, Federal University of Lavras (UFLA), 3027, Campus Universitario, Lavras, 37200000, Minas Gerais, Brazil.
Teodorico Castro RamalhoLaboratory of Computational Chemistry, Department of Chemistry, Federal University of Lavras (UFLA), 3027, Campus Universitario, Lavras, 37200000, Minas Gerais, Brazil. teo@dqi.ufla.br.
Universidade Federal de Lavras · BRFederal University of São João del-Rei · BRUniversidade Federal de Ouro Preto · BRUniversity of Hradec Králové · CZ

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The serine/threonine protein phosphatase type 5 (PP5) is a promising target for designing new antitumor drugs. This enzyme is a member of the PPP phosphatases gene family, which catalyzes a dephosphorylation reaction: a regulatory process in the signal transduction pathway that controls various biological processes. The aim of this work is to study and compare the inhibition of PP5 by ten cantharidin-like inhibitors in order to bring about contributions relevant to the better comprehension of their inhibitory activity. In this theoretical investigation, we used molecular dynamics techniques to understand the role of key interactions that occur in the protein active site; QM calculations were employed to study the interaction mode of these inhibitors in the enzyme. In addition, atoms in molecules (AIM) calculations were carried out to characterize the chemical bonds among the atoms involved and investigate the orbital interactions with their respective energy values. The obtained results suggest that the Arg275, Asn303, His304, His352, Arg400, His427, Glu428, Val429, Tyr451, and Phe446 residues favorably contribute to the interactions between inhibitors and PP5. However, the Asp271 and Asp244 amino acid residues do not favor such interactions for some inhibitors. Through the QM calculations, we can suggest that the reactional energy of the coordination mechanism of these inhibitors in the PP5 active site is quite important and is responsible for the inhibitory activity. The AIM technique employed in this work was essential to get a better comprehension of the transition states acquired from the mechanism simulation. This work offers insights of how cantharidin-like inhibitors interact with human PP5, potentially allowing the design of more specific and even less cytotoxic drugs for cancer treatments. Graphical Abstract Interactions of cantharidin-like inhibitors with human protein phosphatase-5 in a Mg

Indexed as

Molecular Dynamics SimulationCantharidinCatalytic DomainCations, DivalentDrug DesignEnzyme InhibitorsHumansMagnesiumNuclear ProteinsPhosphoprotein PhosphatasesCantharidinCations, DivalentEnzyme InhibitorsMagnesiumNuclear ProteinsPhosphoprotein Phosphatasesprotein phosphatase 5AIMCantharidin-like inhibitorsMolecular dynamicsQM/MMSerine/threonine phosphatase 5

Identifiers

PMID30280322
OpenAlexW2894612476

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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.