ArticleFEBS letters2015
Benserazide, the first allosteric inhibitor of Coxsackievirus B3 3C protease.
Article in FEBS letters, 2015. 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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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
8 citing papers in PubMed, 14 citations in OpenAlex.
- Baicalein suppresses Coxsackievirus B3 replication by inhibiting caspase-1 and viral protease 2A.Virologica Sinica · 2024Article
- Development of FRET and Stress Granule Dual-Based System to Screen for Viral 3C Protease Inhibitors.Molecules (Basel, Switzerland) · 2023Article
- Dual-Reporter System for Real-Time Monitoring of SARS-CoV-2 Main Protease Activity in Live Cells Enables Identification of an Allosteric Inhibition Path.ACS bio & med chem Au · 2022Article
- Antiviral Effects of Novel 2-Benzoxyl-Phenylpyridine Derivatives.Molecules (Basel, Switzerland) · 2020Article
- Coxsackievirus B3 Responds to Polyamine Depletion via Enhancement of 2A and 3C Protease Activity.Viruses · 2019Article
- Cardiovascular Involvement in Chronic Hepatitis C Virus Infections - Insight from Novel Antiviral Therapies.Journal of clinical and translational hepatology · 2018Review
- Benserazide, a dopadecarboxylase inhibitor, suppresses tumor growth by targeting hexokinase 2.Journal of experimental & clinical cancer research : CR · 2017Article
- Review
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Coxsackievirus B3 is the main cause of human viral myocarditis and cardiomyopathy. Virally encoded Coxsackievirus 3C protease (3C(pro)) plays an essential role in viral proliferation. Here, benserazide was discovered as a novel inhibitor from a drug library screen targeting Coxsackievirus 3C(pro) using a FRET-based enzyme assay. Benserazide, whose chemical structure has no electrophilic functional groups, was characterized as a non-competitive inhibitor by enzyme kinetic studies. A molecular docking study with benserazide and its analogs indicated that a novel putative allosteric binding site was involved. Specifically, a 2,3,4-trihydroxybenzyl moiety was determined to be a key pharmacophore for the enzyme's inhibitory activity. We suggest that the putative allosteric binding site may be a novel target for future therapeutic strategies.
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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.