ArticleCurrent issues in molecular biology2023
In Silico Analysis of SARS-CoV-2 Non-Structural Proteins Reveals an Interaction with the Host's Heat Shock Proteins That May Contribute to Viral Replications and Development.
Article in Current issues in molecular biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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.
The trial behind it
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Who cites it
4 citing papers in PubMed, 4 citations in OpenAlex.
- SARS-CoV-2 Helicase (NSP13) Interacts with Mammalian Polyamine and HSP Partners in Promoting Viral Replication.Current issues in molecular biology · 2026Article
- From Protein Structure to Drug Discovery: Bioinformatics Breakthroughs in 2024-2025.Current issues in molecular biology · 2025Article
- Two sides of the same coin: heat shock proteins as biomarkers and therapeutic targets for some complex diseases.Frontiers in molecular biosciences · 2025Review
- Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The non-structural protein 2 (NSP2) is an RNA-binding protein involved in coronavirus genome replication, and it often decreases human immune response to promote viral invasion and development. It is believed that the NSP2 associates itself with polyamines and heat shock proteins inside the host cell to proceed with viral development. This study aimed to investigate how the SARS-CoV-2 virus' key non-structural proteins (NSP2) utilize polyamines and heat shock proteins using a molecular docking approach and molecular dynamics (MD). ClusPro and HADDOCK servers were used for the docking and Discovery Studio, chimera, and PyMOL were used for analysis. Docking of the heat shock proteins 40 (HSP40), 70 (HSP70), and 90 (HSP90) with SARS-CoV-2 NSP2 resulted in 32, 28, and 19 interactions, respectively. Molecular dynamics revealed Arg458, Asn508, Met297, Arg301, and Trp417 as active residues, and pharmacophore modeling indicated ZINC395648, ZINC01150525, and ZINC85324008 from the zinc database as possible inhibitors for this NSP2.
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What OpenQuestion holds
Registered trials
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.