ArticleMolecules (Basel, Switzerland)2015
Quercitrin, an inhibitor of Sortase A, interferes with the adhesion of Staphylococcal aureus.
Article in Molecules (Basel, Switzerland), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 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
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
21 citing papers in PubMed, 43 citations in OpenAlex.
- Chromatographic Determination and Antimicrobial Evaluation of Walnut (Plants (Basel, Switzerland) · 2026Article
- Antibacterial activity and compositional analysis ofVeterinarni medicina · 2025Article
- Epicatechin gallate and its analogues interact with sortase A and β-lactamase to suppressFrontiers in cellular and infection microbiology · 2025Article
- The impacts of animal agriculture on One Health-Bacterial zoonosis, antimicrobial resistance, and beyond.One health (Amsterdam, Netherlands) · 2024Review
- Inhibitory Effects onPlants (Basel, Switzerland) · 2024Article
- Synthesis, In Vivo Anticonvulsant Activity Evaluation and In Silico Studies of Some Quinazolin-4(3H)-One Derivatives.Molecules (Basel, Switzerland) · 2024Article
- Structural and functional insights of sortases and their interactions with antivirulence compounds.Current research in structural biology · 2024Review
- Indonesian MangroveMolecules (Basel, Switzerland) · 2022Article
- Punicalagin, an Inhibitor of Sortase A, Is a Promising Therapeutic Drug to Combat Methicillin-Resistant Staphylococcus aureus Infections.Antimicrobial agents and chemotherapy · 2022Article
- Identification of Novel Antistaphylococcal Hit Compounds Targeting Sortase A.Molecules (Basel, Switzerland) · 2021Article
- Targeting Bacterial Sortases in Search of Anti-Virulence Therapies with Low Risk of Resistance Development.Pharmaceuticals (Basel, Switzerland) · 2021Review
- An In Vitro Study of the Effect ofMolecules (Basel, Switzerland) · 2021Article
- Possible drugs for the treatment of bacterial infections in the future: anti-virulence drugs.The Journal of antibiotics · 2021Review
- Defeating Antibiotic-Resistant Bacteria: Exploring Alternative Therapies for a Post-Antibiotic Era.International journal of molecular sciences · 2020Review
- An overview on anti-biofilm properties of quercetin against bacterial pathogens.World journal of microbiology & biotechnology · 2019Review
- Astilbin Inhibits the Activity of Sortase A fromMolecules (Basel, Switzerland) · 2019Article
- Quercetin impairs Streptococcus pneumoniae biofilm formation by inhibiting sortase A activity.Journal of cellular and molecular medicine · 2018Article
- Molecular Docking and Screening Studies of New Natural Sortase A Inhibitors.International journal of molecular sciences · 2017Article
- Rutin InhibitsFrontiers in pharmacology · 2017Article
- Structural Analysis of Sortase A Inhibitors.Molecules (Basel, Switzerland) · 2016Article
Corrections and comments
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
Abstract
Sortase A (SrtA) is a cysteine transpeptidase of most Gram-positive bacteria that is responsible for the anchorage of many surface protein virulence factors to the cell wall layer. SrtA mutants are unable to display surface proteins and are defective in the establishment of infections without affecting microbial viability. In this study, we report that quercitrin (QEN), a natural compound that does not affect Staphylococcus aureus growth, can inhibit the catalytic activity of SrtA in fibrinogen (Fg) cell-clumping and immobilized fibronectin (Fn) adhesion assays. Molecular dynamics simulations and mutagenesis assays suggest that QEN binds to the binding sites of the SrtA G167A and V193A mutants. These findings indicate that QEN is a potential lead compound for the development of new anti-virulence agents against S. aureus infections.
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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.