{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["15(8)"],"submitter":["Marchesani F"],"pubmed_abstract":["The intricate signaling network within the central nervous system (CNS) involving <i>N</i>-methyl-d-aspartate receptors (NMDARs) has been recognized as a key player in severe neurodegenerative diseases. The indirect modulation of NMDAR-mediated neurotransmission through inhibition of serine racemase (SR)-the enzyme responsible for the synthesis of the NMDAR coagonist d-serine-has been suggested as a therapeutic strategy to treat these conditions. Despite the inherent challenges posed by SR conformational flexibility, a ligand-based drug design strategy has successfully produced a series of potent covalent inhibitors structurally related to amino acid analogues. Among these inhibitors, O-(2-([1,1'-biphenyl]-4-yl)-1-carboxyethyl)hydroxylammonium chloride (<b>28</b>) has emerged as a valuable"],"journal":["ACS medicinal chemistry letters"],"pagination":["1298-1305"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11318019"],"repository":["biostudies-literature"],"pubmed_title":["Chemical Probes to Investigate Central Nervous System Disorders: Design, Synthesis and Mechanism of Action of a Potent Human Serine Racemase Inhibitor."],"pmcid":["PMC11318019"],"pubmed_authors":["Bruno S","Rinaldi S","Faggiano S","Annunziato G","Costantino G","Marchesani F","Pieroni M","Campanini B","Giaccari R","Rebecchi F","Spaggiari C"],"additional_accession":[]},"is_claimable":false,"name":"Chemical Probes to Investigate Central Nervous System Disorders: Design, Synthesis and Mechanism of Action of a Potent Human Serine Racemase Inhibitor.","description":"The intricate signaling network within the central nervous system (CNS) involving <i>N</i>-methyl-d-aspartate receptors (NMDARs) has been recognized as a key player in severe neurodegenerative diseases. The indirect modulation of NMDAR-mediated neurotransmission through inhibition of serine racemase (SR)-the enzyme responsible for the synthesis of the NMDAR coagonist d-serine-has been suggested as a therapeutic strategy to treat these conditions. Despite the inherent challenges posed by SR conformational flexibility, a ligand-based drug design strategy has successfully produced a series of potent covalent inhibitors structurally related to amino acid analogues. Among these inhibitors, O-(2-([1,1'-biphenyl]-4-yl)-1-carboxyethyl)hydroxylammonium chloride (<b>28</b>) has emerged as a valuable","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Aug","modification":"2026-04-12T19:16:20.193Z","creation":"2026-04-07T13:18:06.626Z"},"accession":"S-EPMC11318019","cross_references":{"pubmed":["39140049"],"doi":["10.1021/acsmedchemlett.4c00174"]}}