Evidence map›Paper›PMID 32884013›Full record

ArticleScientific reports2020

In silico analysis predicting effects of deleterious SNPs of human RASSF5 gene on its structure and functions.

Md Shahadat Hossain, Arpita Singha Roy, Md Sajedul Islam

Open access · goldAbstract 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 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
4.8field-weighted citation impact, top 4% of its field
1 · What the graph read from it

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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

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3 · Its place in the literature

Who cites it

37 citing papers in PubMed, 95 citations in OpenAlex.

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4 · The record

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5 · Who and what money

Authors and funding

3 authors at 2 institutions in 1 country.

Md Shahadat Hossain *Department of Biotechnology and Genetic Engineering, Noakhali Science and Technology University, Noakhali, Bangladesh.
Arpita Singha RoyDepartment of Biotechnology and Genetic Engineering, Noakhali Science and Technology University, Noakhali, Bangladesh.
Md Sajedul Islam *Department of Biochemistry and Biotechnology, University of Barishal, Barishal, Bangladesh. sajedtuhin2203@gmail.com.ORCID http://orcid.org/0000-0002-3649-8037
Noakhali Science and Technology University · BDUniversity of Barishal · BD

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ras association domain-containing protein 5 (RASSF5), one of the prospective biomarkers for tumors, generally plays a crucial role as a tumor suppressor. As deleterious effects can result from functional differences through SNPs, we sought to analyze the most deleterious SNPs of RASSF5 as well as predict the structural changes associated with the mutants that hamper the normal protein-protein interactions. We adopted both sequence and structure based approaches to analyze the SNPs of RASSF5 protein. We also analyzed the putative post translational modification sites as well as the altered protein-protein interactions that encompass various cascades of signals. Out of all the SNPs obtained from the NCBI database, only 25 were considered as highly deleterious by six in silico SNP prediction tools. Among them, upon analyzing the effect of these nsSNPs on the stability of the protein, we found 17 SNPs that decrease the stability. Significant deviation in the energy minimization score was observed in P350R, F321L, and R277W. Besides this, docking analysis confirmed that P350R, A319V, F321L, and R277W reduce the binding affinity of the protein with H-Ras, where P350R shows the most remarkable deviation. Protein-protein interaction analysis revealed that RASSF5 acts as a hub connecting two clusters consisting of 18 proteins and alteration in the RASSF5 may lead to disassociation of several signal cascades. Thus, based on these analyses, our study suggests that the reported functional SNPs may serve as potential targets for different proteomic studies, diagnosis and therapeutic interventions.

Indexed as

Adaptor Proteins, Signal TransducingApoptosis Regulatory ProteinsComputational BiologyHumansPolymorphism, Single NucleotideProtein BindingSystems BiologyAdaptor Proteins, Signal TransducingApoptosis Regulatory ProteinsRASSF5 protein, human

Identifiers

PMID32884013
PMCPMC7471297
OpenAlexW3082144258

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