ReviewGlycoconjugate journal2020
Sialidase substrates for Sialdiase assays - activity, specificity, quantification and inhibition.
Review in Glycoconjugate journal, 2020. 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
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
8 citing papers in PubMed.
- Research Progress and Screening Strategies of Natural Product-Derived Neuraminidase Inhibitors.Biosensors · 2026Review
- Desialylation and sialidase secretion from monocytes and macrophages upon LPS activation.Frontiers in immunology · 2026Article
- A Viral Neuraminidase-Specific Sensor for Taste-Based Detection of Influenza.ACS central science · 2025Article
- Structural and functional insights into metal coordination and substrate recognition of Akkermansia muciniphila sialidase Amuc_1547.Molecular biomedicine · 2025Article
- Efficient Enzymatic Glycan Engineering of Extracellular Vesicles Using Nanomaterial-Interfaced Microfluidics.ACS applied materials & interfaces · 2025Article
- Maintaining sidedness and fluidity in cell membrane coatings supported on nano-particulate and planar surfaces.Bioactive materials · 2024Review
- Molecular approaches for spinal cord injury treatment.Neural regeneration research · 2023Review
- Ultrasensitive chemiluminescent neuraminidase probe for rapid screening and identification of small-molecules with antiviral activity against influenza A virus in mammalian cells.Chemical science · 2022Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Sialidases are glycosidases responsible for the removal of sialic acid (Sia) residues (desialylation) from glycan portions of either glycoproteins or glycolipids. By desialylation, sialidases are able to modulate the functionality and stability of the Sia-containing molecules and are involved in both physiological and pathological pathways. Therefore, evaluation of sialidase activity and specificity is important for understanding the biological significance of desialylation by sialidases and its function and the related molecular mechanisms of the physiological and pathological pathways. In addition, it is essential for developing novel mechanisms and approaches for disease treatment and diagnosis and pathogen detection as well. This review summarizes the most recent sialidase substrates for evaluating sialidase activity and specificity and screening sialidase inhibitors, including (i) general sialidase substrates, (ii) specific sialidase substrates, (iii) native sialidase substrates and (iv) cellular sialidase substrates. This review also provides a brief introduction of recent instrumental methods for quantifying the sialidase activity, such as UV, fluorescence, HPLC and LC-MS methods.
Indexed as
Identifiers
32813176What 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.