Evidence map›Paper›PMID 30284191›Full record

ArticleMolecular and cellular biochemistry2019

Molecular modeling investigation of the potential mechanism for phytochemical-induced skin collagen biosynthesis by inhibition of the protein phosphatase 1 holoenzyme.

Pathomwat Wongrattanakamon, Piyarat Nimmanpipug, Busaban Sirithunyalug, Chalermpong Saenjum, Supat Jiranusornkul

Abstract read
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In one paragraph

Article in Molecular and cellular biochemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.7field-weighted citation impact, top 26% 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

2 citing papers in PubMed, 4 citations in OpenAlex.

  1. Review
  2. Review
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

5 authors at 1 institution in 1 country.

Pathomwat WongrattanakamonLaboratory for Molecular Design and Simulation (LMDS), Faculty of Pharmacy, Department of Pharmaceutical Sciences, Chiang Mai University, Chiang Mai, 50200, Thailand. pathomwat@yahoo.com.ORCID http://orcid.org/0000-0001-6619-1557
Piyarat NimmanpipugComputational Simulation and Modelling Laboratory (CSML), Faculty of Science, Department of Chemistry, Chiang Mai University, Chiang Mai, 50200, Thailand.
Busaban SirithunyalugFaculty of Pharmacy, Department of Pharmaceutical Sciences, Chiang Mai University, Chiang Mai, 50200, Thailand.
Chalermpong SaenjumFaculty of Pharmacy, Department of Pharmaceutical Sciences, Chiang Mai University, Chiang Mai, 50200, Thailand.
Supat JiranusornkulLaboratory for Molecular Design and Simulation (LMDS), Faculty of Pharmacy, Department of Pharmaceutical Sciences, Chiang Mai University, Chiang Mai, 50200, Thailand. supat.jira@cmu.ac.th.
Chiang Mai University · TH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The most prominent feature of UV-induced photoaged skin is decreased type 1 procollagen. Increase of the TGF-β/Smad signaling through inhibition of the TβRI dephosphorylation by the GADD34-PP1c phosphatase complex represents a promising strategy for the increase in type 1 collagen production and prevention of UV-induced skin photoaging. In this study, the molecular docking and dynamics simulations, and pharmacophore modeling method were run to investigate a possible binding site as well as binding modes between apigenin, daidzein, asiaticoside, obovatol, and astragaloside IV and PP1c. Through docking study, the possible binding site for these phytochemicals was predicted as the hydrophobic (PP1-substrate binding) groove. The result indicates that PP1 is the significant target of these compounds. Moreover, the 20,000-ps MD simulations present that the binding locations and modes predicted by the docking have been slightly changed considering that the MD simulations proffer more reliable details upon the protein-ligand recognition. The MM-GBSA binding free energy calculations and pharmacophore modeling rationally identify that the highly hydrophobic surfaces/pockets at close proximity of the catalytic core are the most favorable binding locations of the herbal compounds, and that some experimental facts upon a possible mechanism of increase in collagen biosynthesis can be explained. The present study theoretically offers the reliable binding target of the herbal compounds, and therefore helps to understanding the action mechanism for natural small molecules that enhance collagen production.

Indexed as

Binding SitesBiphenyl CompoundsCatalytic DomainCollagenEnzyme InhibitorsHumansIsoflavonesMolecular Docking SimulationMolecular Dynamics SimulationPhenyl EthersPhytochemicalsProtein Phosphatase 1SaponinsSkinTriterpenesasiaticosideastragaloside ABiphenyl CompoundsCollagendaidzeinEnzyme InhibitorsIsoflavonesobovatolPhenyl EthersPhytochemicalsProtein Phosphatase 1SaponinsTriterpenesCollagenHerbal compoundsMolecular dockingMolecular dynamics simulationPhotoagingPP1TGF-β

Identifiers

PMID30284191
OpenAlexW2894667033

What OpenQuestion holds

Textmetadata
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.