ArticlePloS one2011
Mechanism of inhibition of enveloped virus membrane fusion by the antiviral drug arbidol.
Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers, 1 of them a synthesis that pooled it.
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
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
59 citing papers in PubMed, 1 synthesis or guideline pooled it, 135 citations in OpenAlex.
- Meta-analysis of arbidol versus lopinavir/ritonavir in the treatment of coronavirus disease 2019.Journal of medical virology · 2022Pooled it
- Multicenter, randomized controlled, open label evaluation of the efficacy and safety of arbidol hydrochloride tablets in the treatment of influenza-like cases.BMC infectious diseases · 2023Trial
- Pharmacokinetics, metabolism, and excretion of the antiviral drug arbidol in humans.Antimicrobial agents and chemotherapy · 2013Trial
- Effect of Cationic Surfactants on the Molecular Organization of the Simplified Model Lipid Envelope of SARS-CoV-2 Virus─Insights from the Langmuir Monolayer and Liposome Studies.Langmuir : the ACS journal of surfaces and colloids · 2026Article
- One-pot synthesis, characterization and antiviral properties of new benzenesulfonamide-based spirothiazolidinones.Molecular diversity · 2024Article
- Arbidol: The current demand, strategies, and antiviral mechanisms.Immunity, inflammation and disease · 2023Review
- Virucidal Activity of the Pyridobenzothiazolone Derivative HeE1-17Y against Enveloped RNA Viruses.Viruses · 2022Article
- Drug Repurposing for COVID-19: A Review and a Novel Strategy to Identify New Targets and Potential Drug Candidates.Molecules (Basel, Switzerland) · 2022Review
- Approaches to the Potential Therapy of COVID-19: A General Overview from the Medicinal Chemistry Perspective.Molecules (Basel, Switzerland) · 2022Review
- Modeling the Structure-Activity Relationship of Arbidol Derivatives and Other SARS-CoV-2 Fusion Inhibitors Targeting the S2 Segment of the Spike Protein.Journal of chemical information and modeling · 2021Article
- Pharmacological Treatment for the Management of COVID 19: A Narrative Review.JNMA; journal of the Nepal Medical Association · 2021Review
- The Antiviral and Virucidal Activities of Voacangine and Structural Analogs Extracted fromPlants (Basel, Switzerland) · 2021Article
- Brief review on repurposed drugs and vaccines for possible treatment of COVID-19.European journal of pharmacology · 2021Review
- Insights into SARS-CoV-2: Medicinal Chemistry Approaches to Combat Its Structural and Functional Biology.Topics in current chemistry (Cham) · 2021Review
- Unraveling the mechanism of arbidol binding and inhibition of SARS-CoV-2: Insights from atomistic simulations.European journal of pharmacology · 2021Article
- Dimer Organization of Membrane-Associated NS5A of Hepatitis C Virus as Determined by Highly SensitiveAngewandte Chemie (International ed. in English) · 2021Article
- Therapeutics and Vaccines: Strengthening Our Fight Against the Global Pandemic COVID-19.Current microbiology · 2021Review
- Emerging therapeutics in the management of COVID-19.World journal of virology · 2021Review
- Recent Developments on Therapeutic and Diagnostic Approaches for COVID-19.The AAPS journal · 2021Review
- Current Trends and Future Approaches in Small-Molecule Therapeutics for COVID-19.Current medicinal chemistry · 2021Review
Corrections and comments
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Authors and funding
11 authors at 6 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The broad-spectrum antiviral arbidol (Arb) inhibits cell entry of enveloped viruses by blocking viral fusion with host cell membrane. To better understand Arb mechanism of action, we investigated its interactions with phospholipids and membrane peptides. We demonstrate that Arb associates with phospholipids in the micromolar range. NMR reveals that Arb interacts with the polar head-group of phospholipid at the membrane interface. Fluorescence studies of interactions between Arb and either tryptophan derivatives or membrane peptides reconstituted into liposomes show that Arb interacts with tryptophan in the micromolar range. Interestingly, apparent binding affinities between lipids and tryptophan residues are comparable with those of Arb IC50 of the hepatitis C virus (HCV) membrane fusion. Since tryptophan residues of membrane proteins are known to bind preferentially at the membrane interface, these data suggest that Arb could increase the strength of virus glycoprotein's interactions with the membrane, due to a dual binding mode involving aromatic residues and phospholipids. The resulting complexation would inhibit the expected viral glycoprotein conformational changes required during the fusion process. Our findings pave the way towards the design of new drugs exhibiting Arb-like interfacial membrane binding properties to inhibit early steps of virus entry, i.e., attractive targets to combat viral infection.
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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.