ArticleACS medicinal chemistry letters2013
Development of Unsymmetrical Dyads As Potent Noncarbohydrate-Based Inhibitors against Human β-N-Acetyl-d-hexosaminidase.
Article in ACS medicinal chemistry letters, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 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
7 citing papers in PubMed, 30 citations in OpenAlex.
- Mechanical macrocyclic effects: stimuli-responsive dual emission by self-inclusion and mutual exclusion.Chemical science · 2026Article
- Twisting, Hydrogen Bonding, Exciplex Formation, and Charge Transfer. What Makes a Bright Fluorophore Not So Bright?The Journal of organic chemistry · 2025Article
- spJournal of enzyme inhibition and medicinal chemistry · 2022Article
- Computational Studies on the Potency and Selectivity of PUGNAc Derivatives Against GH3, GH20, and GH84 β-N-acetyl-D-hexosaminidases.Frontiers in chemistry · 2019Article
- Modification of the Thioglycosyl-Naphthalimides as Potent and Selective Human O-GlcNAcase Inhibitors.ACS medicinal chemistry letters · 2018Article
- Design and synthesis of naphthalimide group-bearing thioglycosides as novel β-N-acetylhexosaminidases inhibitors.Journal of enzyme inhibition and medicinal chemistry · 2018Article
- A crystal structure-guided rational design switching non-carbohydrate inhibitors' specificity between two β-GlcNAcase homologs.Scientific reports · 2014Article
Corrections and comments
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Authors and funding
6 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Human β-N-acetyl-d-hexosaminidase has gained much attention due to its roles in several pathological processes and been considered as potential targets for disease therapy. A novel and efficient skeleton, which was an unsymmetrical dyad containing naphthalimide and methoxyphenyl moieties with an alkylamine spacer linkage as a noncarbohydrate-based inhibitor, was synthesized, and the activities were valuated against human β-N-acetyl-d-hexosaminidase. The most potent inhibitor exhibits high inhibitory activity with K i values of 0.63 μM. The straightforward synthetic manners of these unsymmetrical dyads and understanding of the binding model could be advantageous for further structure optimization and development of new therapeutic agents for Hex-related diseases.
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Registered trials
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