ArticleJournal of medicinal chemistry2013
Substrate-based fragment identification for the development of selective, nonpeptidic inhibitors of striatal-enriched protein tyrosine phosphatase.
Article in Journal of medicinal chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 33 citations in OpenAlex.
- Article
- Advances on the Merger of Electrochemistry and Transition Metal Catalysis for Organic Synthesis.Chemical reviews · 2022Review
- The Implication of STEP in Synaptic Plasticity and Cognitive Impairments in Alzheimer's Disease and Other Neurological Disorders.Frontiers in cell and developmental biology · 2021Review
- Inhibition of striatal-enriched protein tyrosine phosphatase by targeting computationally revealed cryptic pockets.European journal of medicinal chemistry · 2020Article
- Altered Intracellular Calcium Homeostasis Underlying Enhanced Glutamatergic Transmission in Striatal-Enriched Tyrosine Phosphatase (STEP) Knockout Mice.Molecular neurobiology · 2018Article
- Synthesis and Reactions of α-Hydroxyphosphonates.Molecules (Basel, Switzerland) · 2018Review
- Glutathione-Responsive Selenosulfide Prodrugs as a Platform Strategy for Potent and Selective Mechanism-Based Inhibition of Protein Tyrosine Phosphatases.ACS central science · 2017Article
- X-ray Characterization and Structure-Based Optimization of Striatal-Enriched Protein Tyrosine Phosphatase Inhibitors.Journal of medicinal chemistry · 2017Article
- Identification of multiple structurally distinct, nonpeptidic small molecule inhibitors of protein arginine deiminase 3 using a substrate-based fragment method.Journal of the American Chemical Society · 2015Article
- Synthesis of benzopentathiepin analogs and their evaluation as inhibitors of the phosphatase STEP.Bioorganic & medicinal chemistry letters · 2015Article
- Small molecule substrate phosphorylation site inhibitors of protein kinases: approaches and challenges.ACS chemical biology · 2015Review
- Striatal-enriched protein tyrosine phosphatase controls responses to aversive stimuli: implication for ethanol drinking.PloS one · 2015Article
- Disruption of striatal-enriched protein tyrosine phosphatase (STEP) function in neuropsychiatric disorders.Neuroscience research · 2014Review
- Substrate deconstruction and the nonadditivity of enzyme recognition.Journal of the American Chemical Society · 2014Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
High levels of striatal-enriched protein tyrosine phosphatase (STEP) activity are observed in a number of neuropsychiatric disorders such as Alzheimer's disease. Overexpression of STEP results in the dephosphorylation and inactivation of many key neuronal signaling molecules, including ionotropic glutamate receptors. Moreover, genetically reducing STEP levels in AD mouse models significantly reversed cognitive deficits and decreased glutamate receptor internalization. These results support STEP as a potential target for drug discovery for the treatment of Alzheimer's disease. Herein, a substrate-based approach for the discovery and optimization of fragments called substrate activity screening (SAS) has been applied to the development of low molecular weight (<450 Da) and nonpeptidic, single-digit micromolar mechanism-based STEP inhibitors with greater than 20-fold selectivity across multiple tyrosine and dual specificity phosphatases. Significant levels of STEP inhibition in rat cortical neurons are also observed.
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Registered trials
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