Evidence map›Paper›PMID 39802857›Full record

ArticleEuroasian journal of hepato-gastroenterology

Molecular Characterization and Potential Inhibitors Prediction of Protein Arginine Methyltransferase-2 in Carcinoma: An Insight from Molecular Docking, ADMET Profiling and Molecular Dynamics Simulation Studies.

Md Sahadot Hossen, Md Nur Islam, Md Enayet A Pramanik, Md Hasanur Rahman, Md Al Amin, Saraban T Antora, Farzana S Sraboni, Rifah N Chowdhury, Nazia Farha, Amina A Sathi and 17 more

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In one paragraph

Article in Euroasian journal of hepato-gastroenterology. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
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

0 citing papers in PubMed.

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

27 authors.

Md Sahadot HossenDepartment of Biochemistry and Molecular Biology, School of Life Sciences, Shahjalal University of Science and Technology, Sylhet, Bangladesh.
Md Nur IslamNational Laboratory of Biomacromolecules, Chinese Academy of Sciences Center for Excellence in Biomacromolecules, Institute of Biophysics, CAS, Beijing, People's Republic of China; Department of Pharmacy, Manarat International University, Gulshan, Dhaka, Bangladesh.
Md Enayet A PramanikDepartment of Entomology, On-Farm Research Division, Bangladesh Agricultural Research Institute, Terokhadia, Rajshahi, Bangladesh.
Md Hasanur RahmanDepartment of Biotechnology and Genetic Engineering, Faculty of Life Sciences, Bangabandhu Sheikh Mujibur Rahman Science and Technology University, Gopalganj, Bangladesh.
Md Al AminDepartment of Biotechnology and Genetic Engineering, Faculty of Life Sciences, Mawlana Bhashani Science and Technology University, Tangail, Santosh, Bangladesh.
Saraban T AntoraDepartment of Biochemistry and Molecular Biology, Faculty of Life Sciences, Bangabandhu Sheikh Mujibur Rahman Science and Technology University, Gopalganj, Bangladesh.
Farzana S SraboniDepartment of Genetic Engineering and Biotechnology, Faculty of Biological Sciences, University of Rajshahi, Rajshahi, Bangladesh.
Rifah N ChowdhuryDepartment of Pharmacy, Faculty of Pharmacy, University of Dhaka (DU), Mokarram Hussain Khundker Bhaban, University St, Dhaka, Bangladesh.
Nazia FarhaDepartment of Genetic Engineering and Biotechnology, Faculty of Biological Sciences, University of Chittagong, Chittagong, Bangladesh.
Amina A SathiDepartment of Genetic Engineering and Biotechnology, Faculty of Biological Sciences, University of Rajshahi, Rajshahi, Bangladesh.
Samia SadafDepartment of Biology, Development Biology Laboratory, Clarkson University, Potsdam, New York, United States of America.
Farjana BannaDepartment of Biotechnology and Genetic Engineering, Faculty of Science, Islamic University, Kushtia, Bangladesh.
Md Rezaul KarimDepartment of Pharmacy, School of Engineering, Science and Technology, Manarat International University, Gulshan, Dhaka, Bangladesh.
Nasrin AkterDepartment of Biochemistry and Molecular Biology, University of Rajshahi, Rajshahi, Bangladesh.
Md Royhan GofurDepartment of Veterinary and Animal Sciences, University of Rajshahi, Rajshahi, Bangladesh.
Md Shariful IslamDepartment of Veterinary and Animal Sciences, University of Rajshahi, Rajshahi, Bangladesh.
M Morsed Z MiahDepartment of Hematology, Rajshahi Medical College, Rajshahi, Bangladesh.
Mira AkhterDepartment of Clinical Pathology, Rajshahi Medical College Hospital, Rajshahi, Bangladesh.
Md Shariful IslamDepartment of Ortho-Surgery, Rajshahi Medical College, Rajshahi, Bangladesh.
Md Sharif HasanDepartment of Cardiology, Mymensingh Medical College Hospital, Mymensingh, Bangladesh.
Fahmida FahminDepartment of Paediatric, Mymensingh Medical College Hospital, Mymensingh, Bangladesh.
Mohammad M RahmanDepartment of Medicine, Rajshahi Medical College, Rajshahi, Bangladesh.
Prabir M BasakDepartment of Medicine, Rajshahi Medical College, Rajshahi, Bangladesh.
Amio K SonnyashiDepartment of Medicine, Rajshahi Medical College, Rajshahi, Bangladesh.
Haimanti S DasDepartment of Virology, Rajshahi Medical College, Rajshahi, Bangladesh.
Mamun Al MahtabDepartment of Interventional Hepatology, Bangabandhu Sheikh Mujib Medical University, Shahbagh, Dhaka, Bangladesh.
Sheikh Mf AkbarDepartment of Gastroenterology and Metabology, Ehime University Graduate School of Medicine, Ehime, Japan.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Objectives: To predict and characterize the three-dimensional (3D) structure of protein arginine methyltransferase 2 (PRMT2) using homology modeling, besides, the identification of potent inhibitors for enhanced comprehension of the biological function of this protein arginine methyltransferase (PRMT) family protein in carcinogenesis. Materials and methods: An Results: Protein arginine methyltransferases are associated with a range of physiological processes, including as splicing, proliferation, regulation of the cell cycle, differentiation, and signaling of DNA damage. These functional capacities are also related to carcinogenesis and metastasis-several forms of PRMT have been cited in the literature. These include PRMT-1, PRMT-2, and PRMT-5. Among these, the role of PRMT-2 has been shown in breast cancer and hepatocellular carcinoma. To gain more insights into the role of PRMT2 in cancer pathogenesis, we opted to characterize tertiary structure utilizing an Conclusion: Three strong inhibitory compounds that were non-carcinogenic also have drug-like properties. By using desirable parameters in root mean square deviation (RMSD), root mean square fluctuation (RMSF), radius of gyration (Rg), solvent accessible surface area (SASA), molecular surface area (MolSA), and intermolecular hydrogen bonding, complexes verified structural stability and compactness over the 100 ns time frame. How to cite this article: Hossen MS, Islam MN, Pramanik MEA

Indexed as

Computer-aided drug designHomology modelingInhibitor's predictionMolecular dockingMolecular dynamics simulationProtein arginine methyltransferase 2

Identifiers

PMID39802857
PMCPMC11714102

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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.