Evidence map›Paper›PMID 30624775›Full record

ArticleJournal of cellular physiology2019

Protein modeling, molecular network and molecular dynamics study of newly sequenced interleukin-18 (IL-18) gene in Mus musculus.

Brijesh S Yadav, Navaneet Chaturvedi, Pavan K Yadav, Ninoslav Marina, Magdah Ganash, George E Barreto, Ghulam Md Ashraf, Khurshid Ahmad, Mohammad H Baig

Abstract read
In one paragraph

Article in Journal of cellular physiology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.3field-weighted citation impact, top 42% 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

3 citing papers in PubMed, 5 citations in OpenAlex.

  1. Role of Non-Binding T63 Alteration in IL-18 Binding.International journal of molecular sciences · 2024
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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

9 authors at 5 institutions in 8 countries.

Brijesh S YadavDepartment of Bioengineering, University of Information Science and Technology, Republic of Macedonia.ORCID http://orcid.org/0000-0002-3095-3369
Navaneet ChaturvediSchool of Biochemical Engineering, Indian Institute of Technology, Banaras Hindu University, Varanasi, Uttar Pradesh, India.
Pavan K YadavDepartment of Veterinary Physiology & Biochemistry, Faculty of Veterinary and Animal Sciences, Banaras Hindu University, Varanasi, Uttar Pradesh, India.
Ninoslav MarinaDepartment of Bioengineering, University of Information Science and Technology, Republic of Macedonia.
Magdah GanashDepartment of Biology, Faculty of Science, King Abdulaziz University, Jeddah, Saudi Arabia.
George E BarretoDepartamento de Nutrición y Bioquímica, Facultad de Ciencias, Pontificia Universidad Javeriana, Bogotá DC, Colombia.ORCID http://orcid.org/0000-0002-6644-1971
Ghulam Md AshrafKing Fahd Medical Research Center, King Abdulaziz University, Jeddah, Saudi Arabia.
Khurshid AhmadDepartment of Medical Biotechnology, Yeungnam University, Gyeongsan, South Korea.
Mohammad H BaigDepartment of Medical Biotechnology, Yeungnam University, Gyeongsan, South Korea.
King Abdulaziz University · SAUniversity of Macedonia · GRYeungnam University · KRZero to Three · USPontificia Universidad Javeriana · CO

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Interleukin-18 (IL-18) belongs to the superfamily of IL-1 protein and exerts a pleiotropic pro-inflammatory effect on the body. Generally, this protein is significantly involved in immune defense during infection in cells, but sometimes its anomalous activities produce some inflammatory diseases like rheumatoid arthritis and Crohn's disease. In the present study, the IL-18 gene was isolated from mice and was subsequently cloned and sequenced. Further, the network analysis was carried out to explore the functional role of IL-18 protein in animals. The 3D protein structure of the IL-18 protein was generated and docked with appropriate 3-([3-cholamidopropyl]dimethylammonio)-1-propanesulfonate (CPS) ligand. Later the complex structure of the protein was subjected to molecular dynamics simulation (MDS) for 50 ns to determine the effect of ligand on protein. The network analysis explored the correlation of IL-18 protein with others proteins and their involvement in the different significant pathway to defend the cell from various diseases. As confirmed by MDS, the CPS:IL-18 complex was found to be highly stable. Our results further indicated that CPS ligand has the potential to act as a drug molecule, in future, for counteracting IL-18 activity. To date, no structural details were available for animal IL-18. Hence, the finding of this study will be useful in broadening the horizon towards a better understanding of the functional and structural aspects of IL-18 in animals.

Indexed as

Molecular ConformationStructure-Activity RelationshipAlkanesulfonic AcidsAmino Acid SequenceAnimalsArthritis, RheumatoidCloning, MolecularCrohn DiseaseHumansInterleukin-18LigandsMiceMolecular Dynamics SimulationProtein BindingProtein ConformationAlkanesulfonic AcidsInterleukin-18Ligandspropylsulfonic acidcloning and sequencingfunctional enrichmentinterleukin-18molecular dynamicsnetwork analysis

Identifiers

PMID30624775
PMCPMC13483002
OpenAlexW2910125992

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.