Evidence map›Paper›PMID 37296335›Full record

ArticleBiochemical genetics2024

In Silico Prediction and Molecular Docking of SNPs in NRP1 Gene Associated with SARS-COV-2.

Ebru Özkan Oktay, Tuğba Kaman, Ömer Faruk Karasakal, Vildan Enisoğlu Atalay

Open access · bronzeAbstract read
In one paragraph

Article in Biochemical genetics, 2024. 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
0.6field-weighted citation impact, top 30% 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, 4 citations in OpenAlex.

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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

4 authors at 1 institution in 1 country.

Ebru Özkan OktayVocational School of Health Services, Laboratory Technology, Üsküdar University, Üsküdar, Istanbul, Turkey. ebru.ozkanoktay@uskudar.edu.tr.ORCID http://orcid.org/0000-0002-0395-9845
Tuğba KamanVocational School of Health Services, Medical and Aromatic Plants, Üsküdar University, Üsküdar, Istanbul, Turkey.ORCID http://orcid.org/0000-0002-5885-0193
Ömer Faruk KarasakalVocational School of Health Services, Medical Laboratory Techniques, Üsküdar University, Üsküdar, Istanbul, Turkey.ORCID http://orcid.org/0000-0001-7803-3249
Vildan Enisoğlu AtalayDepartment of Molecular Biology and Genetics, Üsküdar University, Üsküdar, Istanbul, Turkey.ORCID http://orcid.org/0000-0002-9830-9158
Üsküdar University · TR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Neuropilin-1 (NRP1) which is a main transmembrane cell surface receptor acts as a host cell mediator resulting in increasing the SARS-Cov-2 infectivity and also plays a role in neuronal development, angiogenesis and axonal outgrowth. The goal of this study is to estimate the impact of single nucleotide polymorphisms (SNPs) in the NRP1 gene on the function, structure and stabilization of protein as well as on the miRNA-mRNA binding regions using bioinformatical tools. It is also aimed to investigate the changes caused by SNPs in NRP1 on interactions with drug molecule and spike protein. The missense type of SNPs was analyzed using SIFT, PolyPhen-2, SNAP2, PROVEAN, Mutation Assessor, SNPs&GO, PhD-SNP, I-Mutant 3.0, MUpro, STRING, Project HOPE, ConSurf, and PolymiRTS. Docking analyses were conducted by AutoDock Vina program. As a result, a total of 733 missense SNPs were determined within the NRP1 gene and nine SNPs were specified as damaging to the protein. The modelling results showed that wild and mutant type amino acids had some different properties such as size, charge, and hydrophobicity. Additionally, their three-dimensional structures of protein were utilized for confirmation of these differences. After evaluating the results, nine polymorphisms rs141633354, rs142121081, rs145954532, rs200028992, rs200660300, rs369312020, rs370117610, rs370551432, rs370641686 were determined to be damaging on the structure and function of NRP1 protein and located in conserved regions. The results of molecular docking showed that the binding affinity values are nearly the same for wild-type and mutant structures support that the mutations carried out are not in the focus of the binding site, therefore the ligand does not affect the binding energy. It is expected that the results will be useful for future studies.

Indexed as

COVID-19Polymorphism, Single NucleotideBinding SitesHumansMolecular Docking SimulationSARS-CoV-2In silico analysisNeuropilin-1 (NRP1)SARS-CoV-2Single nucleotide polymorphism (SNP)

Identifiers

PMID37296335
PMCPMC10255949
OpenAlexW4379979956

What OpenQuestion holds

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Registered trials

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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.