Evidence map›Paper›PMID 35410409›Full record

ArticleJournal of molecular modeling2022

Identification of novel protein kinase C-βII inhibitors: virtual screening, molecular docking and molecular dynamics simulation studies.

Bharat Kumar Reddy Sanapalli, Vidyasrilekha Yele, Lalji Baldaniya, Veera Venkata Satyanarayana Reddy Karri

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Article in Journal of molecular modeling, 2022. 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
0.6field-weighted citation impact, top 37% 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, 8 citations in OpenAlex.

  1. Therapeutic potential ofFrontiers in chemistry · 2025
    Article
  2. 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

4 authors at 2 institutions in 1 country.

Bharat Kumar Reddy SanapalliDepartment of Pharmacology, Faculty of Pharmacy, Marwadi University, Rajkot, Gujarat, 360003, India. bharathsanapalli@yahoo.in.ORCID http://orcid.org/0000-0002-9162-5553
Vidyasrilekha YeleDepartment of Pharmaceutical Chemistry, Faculty of Pharmacy, Marwadi University, Rajkot, Gujarat, 360003, India. vidyasrilekha16@gmail.com.
Lalji BaldaniyaDepartment of Pharmaceutics, Faculty of Pharmacy, Marwadi University, Rajkot, Gujarat, 360003, India.
Veera Venkata Satyanarayana Reddy KarriDepartment of Pharmaceutics, JSS College of Pharmacy, JSS Academy of Higher Education & Research, Ooty, Tamil Nadu, 643001, India.
Marwadi University · INJSS Academy of Higher Education and Research · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Diabetic wounds (DWs) are the major end-stage manifestation encountered in diabetic patients. The two major pathways involved in the pathogenesis of DW are impaired angiogenesis and unnecessary NETosis, which are regulated by a common enzyme called protein kinase C (PKC)-βII. PKC-βII is a conventional isoform of PKC family that can be activated by calcium and diacylglycerol. PKC-βII possesses a specific expression profile and plays a distinct role in various cellular and molecular functions. The pathogenic role of PKC-βII and its involvement in the impairment of wound healing suggested that PKC-βII plays a potential role in DW progression. Hence, there is a renewed interest in developing specific inhibitors of PKC-βII. In the present study, receptor-based virtual screening was performed for the identification of potential PKC-βII inhibitors using TimTec, Enamine, Zinc and Specs databases. A total of 595 candidate compounds were evaluated based on absorption, distribution, metabolism, excretion and toxicity, standard precision docking. Further, extra-precision docking and binding free energy calculations were carried out for top-ranked compounds. Based on Glide score and protein-ligand interactions, we have identified compound 1 as a potential inhibitor. Finally, molecular dynamics (MD) simulation was performed for top compound 1 using the Desmond module (Schrödinger suite) to identify the structural stability of the protein-ligand complex. Gratifyingly, MD trajectory analysis demonstrated the stable binding conformation of compound 1 with PKC-βII enzyme. In silico approaches incorporated in this study provide a set of new putative PKC-βII inhibitors which could be potential leads to develop DW therapeutics.

Indexed as

Molecular Dynamics SimulationHumansLigandsMolecular Docking SimulationProtein Kinase C betaLigandsProtein Kinase C betaADMET calculationsDiabetic woundMolecular dockingMolecular dynamics simulation studiesProtein kinase C-βIIReceptor-based virtual screening

Identifiers

PMID35410409
OpenAlexW4223430356

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.