ArticleScientific reports2019
Analysis of mutations leading to para-aminosalicylic acid resistance in Mycobacterium tuberculosis.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 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.
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Who cites it
8 citing papers in PubMed, 22 citations in OpenAlex.
- Computational Mutagenesis and Inhibition ofBioMed research international · 2024Article
- Gated Calcium Ion Channel and Mutation Mechanisms in Multidrug-Resistant Tuberculosis.International journal of molecular sciences · 2023Review
- Progress Report: Antimicrobial Drug Discovery in the Resistance Era.Pharmaceuticals (Basel, Switzerland) · 2022Review
- Ionic liquid/TiORSC advances · 2022Article
- Computer-aided screening for potential TMPRSS2 inhibitors: a combination of pharmacophore modeling, molecular docking and molecular dynamics simulation approaches.Journal of biomolecular structure & dynamics · 2021Article
- Novel Approaches for the Treatment of Pulmonary Tuberculosis.Pharmaceutics · 2020Review
- Computer-aided synthesis of dapsone-phytochemical conjugates against dapsone-resistant Mycobacterium leprae.Scientific reports · 2020Article
- Combining structure and genomics to understand antimicrobial resistance.Computational and structural biotechnology journal · 2020Review
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Thymidylate synthase A (ThyA) is the key enzyme involved in the folate pathway in Mycobacterium tuberculosis. Mutation of key residues of ThyA enzyme which are involved in interaction with substrate 2'-deoxyuridine-5'-monophosphate (dUMP), cofactor 5,10-methylenetetrahydrofolate (MTHF), and catalytic site have caused para-aminosalicylic acid (PAS) resistance in TB patients. Focusing on R127L, L143P, C146R, L172P, A182P, and V261G mutations, including wild-type, we performed long molecular dynamics (MD) simulations in explicit solvent to investigate the molecular principles underlying PAS resistance due to missense mutations. We found that these mutations lead to (i) extensive changes in the dUMP and MTHF binding sites, (ii) weak interaction of ThyA enzyme with dUMP and MTHF by inducing conformational changes in the structure, (iii) loss of the hydrogen bond and other atomic interactions and (iv) enhanced movement of protein atoms indicated by principal component analysis (PCA). In this study, MD simulations framework has provided considerable insight into mutation induced conformational changes in the ThyA enzyme of Mycobacterium.
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Registered trials
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