ArticleScientific reports2016
New Insights into Molecular Organization of Human Neuraminidase-1: Transmembrane Topology and Dimerization Ability.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers, 1 of them a synthesis that pooled it.
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Who cites it
26 citing papers in PubMed, 1 synthesis or guideline pooled it, 56 citations in OpenAlex.
- Mammalian Neuraminidases in Immune-Mediated Diseases: Mucins and Beyond.Frontiers in immunology · 2022Pooled it
- A non-enzymatic function of neuraminidase 1 restrains hepatic glucagon response in mice.Nature communications · 2026Article
- Desialylation and sialidase secretion from monocytes and macrophages upon LPS activation.Frontiers in immunology · 2026Article
- Identification of novel neuraminidase 1 modulators as potential therapeutics for Alzheimer's disease using virtual screening and molecular dynamics simulations.Scientific reports · 2025Article
- Structure and Function of the Extracellular Matrix in Normal and Pathological Conditions: Looking at the Bicuspid Aortic Valve.International journal of molecular sciences · 2025Review
- Sialidases as Potential Therapeutic Targets for Treatment of a Number of Human Diseases.International journal of molecular sciences · 2025Review
- Growth factor-triggered de-sialylation controls glycolipid-lectin-driven endocytosis.Nature cell biology · 2025Article
- Neuraminidase as a novel therapeutic management strategy for Alzheimer's disease: evidenced through molecular docking, molecular dynamic simulation and gene expression analysis.Frontiers in chemistry · 2025Article
- Sialic acids cleavage induced by elastin-derived peptides impairs the interaction between insulin and its receptor in adipocytes 3T3-L1.Journal of physiology and biochemistry · 2024Article
- Structure of the immunoregulatory sialidase NEU1.Science advances · 2023Article
- Sialidase Inhibitors with Different Mechanisms.Journal of medicinal chemistry · 2022Review
- The Elastin Receptor Complex: An Emerging Therapeutic Target Against Age-Related Vascular Diseases.Frontiers in endocrinology · 2022Review
- Flipping the Switch: Innovations in Inducible Probes for Protein Profiling.ACS chemical biology · 2021Review
- Depolarization-dependent Induction of Site-specific Changes in Sialylation onMolecular & cellular proteomics : MCP · 2020Article
- The role of neuraminidase 1 and 2 in glycoprotein Ibα-mediated integrin αIIbβ3 activation.Haematologica · 2020Article
- Review
- Transmembrane Peptides as Inhibitors of Protein-Protein Interactions: An Efficient Strategy to Target Cancer Cells?Frontiers in oncology · 2020Review
- Transmembrane Peptides as a New Strategy to Inhibit Neuraminidase-1 Activation.Frontiers in cell and developmental biology · 2020Article
- Relevance of platelet desialylation and thrombocytopenia in type 2B von Willebrand disease: preclinical and clinical evidence.Haematologica · 2019Article
- Identification of CD36 as a new interaction partner of membrane NEU1: potential implication in the pro-atherogenic effects of the elastin receptor complex.Cellular and molecular life sciences : CMLS · 2019Article
Corrections and comments
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Authors and funding
16 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Neuraminidase 1 (NEU1) is a lysosomal sialidase catalyzing the removal of terminal sialic acids from sialyloconjugates. A plasma membrane-bound NEU1 modulating a plethora of receptors by desialylation, has been consistently documented from the last ten years. Despite a growing interest of the scientific community to NEU1, its membrane organization is not understood and current structural and biochemical data cannot account for such membrane localization. By combining molecular biology and biochemical analyses with structural biophysics and computational approaches, we identified here two regions in human NEU1 - segments 139-159 (TM1) and 316-333 (TM2) - as potential transmembrane (TM) domains. In membrane mimicking environments, the corresponding peptides form stable α-helices and TM2 is suited for self-association. This was confirmed with full-size NEU1 by co-immunoprecipitations from membrane preparations and split-ubiquitin yeast two hybrids. The TM2 region was shown to be critical for dimerization since introduction of point mutations within TM2 leads to disruption of NEU1 dimerization and decrease of sialidase activity in membrane. In conclusion, these results bring new insights in the molecular organization of membrane-bound NEU1 and demonstrate, for the first time, the presence of two potential TM domains that may anchor NEU1 in the membrane, control its dimerization and sialidase activity.
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