Evidence map›Paper›PMID 32678193›Full record

ArticleScientific reports2020

Mutational analysis on predicting the impact of high-risk SNPs in human secretary phospholipase A2 receptor (PLA2R1).

Zoya Khalid, Omar Almaghrabi

Abstract read
In one paragraph

Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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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

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3 · Its place in the literature

Who cites it

6 citing papers in PubMed.

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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

2 authors.

Zoya KhalidComputational Biology Research Lab, Department of Computer Science, National University of Computing and Emerging Sciences, NUCES-FAST, Islamabad, Pakistan. zoya.khalid@nu.edu.pk.
Omar AlmaghrabiDepartment of Biology, College of Science, University of Jeddah, Jeddah, Saudi Arabia.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

PLA2R1 is a transmembrane glycoprotein that acts as an endogenous ligand which stimulates the processes including cell proliferation and cell migration. The SNPs in PLA2R1 is associated with idiopathic membranous nephropathy which is an autoimmune kidney disorder. The present study aimed to explore the structure-function analysis of high risk SNPs in PLA2R1 by using 12 different computational tools. First the functional annotation of SNPs were carried out by sequence based tools which were further subjected to evolutionary conservation analysis. Those SNPs which were predicted as deleterious in both categories were further considered for structure based analysis. The resultant SNPs were C1096S, C545S, C664S, F1257L, F734S, I1174T, I1114T, P177S, P384S, W1198G, W1328G, W692C, W692L, W962R, Y499H. One functional domain of PLA2R1 is already modelled in PDB (6JLI), the full 3D structure of the protein was predicted using I-TASSER homology modelling tool. The stability analysis, structure superimposition, RMSD calculation and docking studies were carried out. The structural analysis predicted four mutations F734S, F1246L, I1174T, W1198G as damaging to the structure of the protein. All these mutations are occurring at the conserved region of CTL domain hence are more likely to abolish the function of the protein. Up to the best of our knowledge, this is the first study that provides in-depth and in-silico analysis of deleterious mutations on structure and function of PLA2R1.

Indexed as

Genetic Association StudiesGenetic Predisposition to DiseasePolymorphism, Single NucleotideComputational BiologyDatabases, GeneticHumansModels, MolecularMolecular Sequence AnnotationMutationReceptors, Phospholipase A2Reproducibility of ResultsStructure-Activity RelationshipPLA2R1 protein, humanReceptors, Phospholipase A2

Identifiers

PMID32678193
PMCPMC7366643

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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.