ArticleActa crystallographica. Section D, Biological crystallography2014
Structural basis of sialidase in complex with geranylated flavonoids as potent natural inhibitors.
Article in Acta crystallographica. Section D, Biological crystallography, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 13 papers.
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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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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
13 citing papers in PubMed, 18 citations in OpenAlex.
- Perspectives of Natural Products and Sialic Acid Mimetics as Modulators of Human Sialidases NEU1-3 in Atherosclerosis.Biomolecules · 2026Review
- Sialidase Inhibitors with Different Mechanisms.Journal of medicinal chemistry · 2022Review
- Sialidase and Sialyltransferase Inhibitors: Targeting Pathogenicity and Disease.Frontiers in molecular biosciences · 2021Review
- Changes in dietary fiber intake in mice reveal associations between colonic mucinGut microbes · 2020Article
- An overview on the role of bioactive α-glucosidase inhibitors in ameliorating diabetic complications.Food and chemical toxicology : an international journal published for the British Industrial Biological Research Association · 2020Review
- Effectiveness of Prenyl Group on Flavonoids fromMolecules (Basel, Switzerland) · 2019Article
- Sialidases FromFrontiers in cellular and infection microbiology · 2019Review
- Design, synthesis, and evaluation of curcumin analogues as potential inhibitors of bacterial sialidase.Journal of enzyme inhibition and medicinal chemistry · 2018Article
- Inhibition of protein tyrosine phosphatase (PTP1B) and α-glucosidase by geranylated flavonoids from Paulownia tomentosa.Journal of enzyme inhibition and medicinal chemistry · 2017Article
- Crystal structure of the catalytic domain of Clostridium perfringens neuraminidase in complex with a non-carbohydrate-based inhibitor, 2-(cyclohexylamino)ethanesulfonic acid.Biochemical and biophysical research communications · 2017Article
- Sialidases from gut bacteria: a mini-review.Biochemical Society transactions · 2016Review
- Structural basis of sialidase in complex with geranylated flavonoids as potent natural inhibitors. Corrigendum.Acta crystallographica. Section D, Biological crystallography · 2015Article
- Phytochemical profile ofPhytochemistry reviews : proceedings of the Phytochemical Society of Europe · 2015Review
Corrections and comments
- Erratum issued
Authors and funding
9 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Sialidase catalyzes the removal of a terminal sialic acid from glycoconjugates and plays a pivotal role in nutrition, cellular interactions and pathogenesis mediating various infectious diseases including cholera, influenza and sepsis. An array of antiviral sialidase agents have been developed and are commercially available, such as zanamivir and oseltamivir for treating influenza. However, the development of bacterial sialidase inhibitors has been much less successful. Here, natural polyphenolic geranylated flavonoids which show significant inhibitory effects against Cp-NanI, a sialidase from Clostridium perfringens, are reported. This bacterium causes various gastrointestinal diseases. The crystal structure of the Cp-NanI catalytic domain in complex with the best inhibitor, diplacone, is also presented. This structure explains how diplacone generates a stable enzyme-inhibitor complex. These results provide a structural framework for understanding the interaction between sialidase and natural flavonoids, which are promising scaffolds on which to discover new anti-sialidase agents.
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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.