ReviewInternational journal of molecular sciences2025
Sialidases as Potential Therapeutic Targets for Treatment of a Number of Human Diseases.
Review in International journal of molecular sciences, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 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
5 citing papers in PubMed.
- Perspectives of Natural Products and Sialic Acid Mimetics as Modulators of Human Sialidases NEU1-3 in Atherosclerosis.Biomolecules · 2026Review
- Sialic Acids in Kidney Disease: Immune Regulation, Complement Activation and Glomerular Injury.Antioxidants (Basel, Switzerland) · 2026Review
- Temporal gut microbiota dysbiosis links metabolic impairment, LDL desialylation, and accelerated atherosclerosis in LDLRFrontiers in medicine · 2026Article
- Decoding sialidase: physiological roles, pathological pathways, and clinical opportunities.Frontiers in cellular and infection microbiology · 2026Review
- Lysosomal membrane permeabilization is involved in CYP2E1-induced apoptosis in hepatocellular carcinoma cells.BBA advances · 2026Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
1 author.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Four human sialidases (hNEUs, E.C 3.2.1.18) have been identified. Each is an exosialidase identified as either NEU1, NEU2, NEU3, or NEU4. They exhibit differences in structure, subcellular distribution, substrate specificity, and the diseases with which they are associated. Similarly, microbial sialidases (NAs) may catalyze the release of sialyl residues from the same sialoglycoconjugates as hNEUs, even though they have low sequence homology with human NEUs. Use of sequence homology, plus the crystalline structure of human NEU2, has provided researchers with the basis for developing inhibitors that may differentiate between them. While microbial-induced diseases that use sialidase to complete their infectious cycle have been the driving force behind interrogation of possible NA inhibitors, errors affecting expression of functional hNEUs and their correlation with clinical problems has led to study of the sialidases per se. Information gained about sialidase structure, function, mechanism of action, mutations affecting expression, and their role(s) in disease, has provided the information about the different sialidases needed for development of specific therapies.
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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.