ArticleScientific reports2020
Exploring the effect of nsSNPs in human YPEL3 gene in cellular senescence.
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 10 papers.
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Who cites it
10 citing papers in PubMed, 17 citations in OpenAlex.
- Article
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- Photoinduced chromophore dissociation resulting in aggregation-induced red fluorescence.Communications biology · 2025Article
- Rosemarinic Acid-Induced Destabilization of Aβ Peptides: Insights from Molecular Dynamics Simulations.Foods (Basel, Switzerland) · 2024Article
- Identification of mitochondria-related gene biomarkers associated with immune infiltration in acute myocardial infarction.iScience · 2024Article
- Comprehensive characterization of high-risk coding and non-coding single nucleotide polymorphisms of human CXCR4 gene.PloS one · 2024Article
- Investigation of pathogenic germline variants in gastric cancer and development of "GasCanBase" database.Cancer reports (Hoboken, N.J.) · 2023Article
- Functional and structural analysis of non-synonymous single nucleotide polymorphisms (nsSNPs) in the MYB oncoproteins associated with human cancer.Scientific reports · 2021Article
- Computational and Mass Spectrometry-Based Approach Identify Deleterious Non-Synonymous Single Nucleotide Polymorphisms (nsSNPs) in JMJD6.Molecules (Basel, Switzerland) · 2021Article
- Study of Endogen Substrates, Drug Substrates and Inhibitors Binding Conformations on MRP4 and Its Variants by Molecular Docking and Molecular Dynamics.Molecules (Basel, Switzerland) · 2021Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
YPEL3 that induces cellular senescence in both normal and tumour cells of humans may show altered expression under the influence of incidental mutations. In this study, we proposed the first structure of Native YPEL3 protein and its five possible deleterious mutants-V40M, C61Y, G98R, G108S, and A131T and predicted their deleterious effects to alter stability, flexibility and conformational changes in the protein. The MD simulation (RMSD, RMSF, Rg, h-bond and SASA) analysis revealed that the variants V40M, G98R and G108S increased the flexibility in protein, and variant V40M imparted more compactness to the protein.. In general, variants attributed changes in the native conformation and structure of the YPEL3 protein which might affect the native function of cellular senescence. The study provides opportunities for health professionals and practitioners in formulating précised medicines to effectively cure various cancers. We propose in-vitro or in-vivo studies should consider these reported nsSNPs while examining any malfunction in the YPEL3 protein.
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