ArticleJournal of molecular graphics & modelling2022
Molecular dynamics simulations of the flexibility and inhibition of SARS-CoV-2 NSP 13 helicase.
Article in Journal of molecular graphics & modelling, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 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
3 citing papers in PubMed, 6 citations in OpenAlex.
- Natural products from Streptomyces spp. as potential inhibitors of the major factors (holoRdRp and nsp13) for SARS-CoV-2 replication: an in silico approach.Archives of microbiology · 2024Article
- Generalized open-source workflows for atomistic molecular dynamics simulations of viral helicases.GigaScience · 2024Article
- Recent advances in the exploration and discovery of SARS-CoV-2 inhibitory peptides from edible animal proteins.Frontiers in nutrition · 2024Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The helicase protein of the Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2) is both a good potential drug target and very flexible. The flexibility, and therefore its function, could be reduced through knowledge of these motions and identification of allosteric pockets. Using molecular dynamics simulations with enhanced sampling, we determined key modes of motion and sites on the protein that are at the interface between flexible domains of the proteins. We developed an approach to map the principal components of motion onto the surface of a potential binding pocket to help in the identification of allosteric sites.
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Registered trials
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