{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Fortin JS"],"funding":["NIA NIH HHS","Purdue University","NINDS NIH HHS","National Institutes of Health","Pharmaceutical Research and Manufacturers of America Foundation"],"pagination":["133574"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9614895"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["1267"],"pubmed_abstract":["In contrast to A<i>β</i> plaques, the spatiotemporal distribution of neurofibrillary tangles of hyperphosphorylated tau (p-tau) predicts cognitive impairment in Alzheimer's disease (AD), underscoring the key pathological role of p-tau and the utmost need to develop AD therapeutics centering upon the control of p-tau aggregation and cytotoxicity. Our drug discovery program is focused on compounds that prevent the aggregation and cytotoxicity of p-tau moieties of the tau isoform 1N4R due to its prevalence (1 N) and long-distance trans-synaptic propagation (4R). We prepared and tested twenty-four newly synthesized small molecules representing the urea (<b>1, 2, 3</b>), sulfonylurea (<b>4</b>), and sulfonamide (<b>5-24</b>) series and evaluated their anti-aggregation effects with biophysical m"],"journal":["Journal of molecular structure"],"pubmed_title":["Anti-fibrillization effects of sulfonamide derivatives on <i>α</i>-synuclein and hyperphosphorylated tau isoform 1N4R."],"pmcid":["PMC9614895"],"funding_grant_id":["R21AG070447-01A1","R21 NS121826","K08 AG071985","P01 AG014449","NS121826","NS099328","P01AG014449","R01 NS099328","R21 AG070447","R44 AG057274","R01 AG062435","R01 AG060731","R01AG060731","R01AG062435","730313","R44AG57274"],"pubmed_authors":["Borhan B","Liu M","Wang KW","Maity S","Kuo MH","Fortin JS","Saraswati AP","Hagar HT","Shimanaka K","Dettmer U","Ellsworth E","Ganegamage SK","Counts SE"],"additional_accession":[]},"is_claimable":false,"name":"Anti-fibrillization effects of sulfonamide derivatives on <i>α</i>-synuclein and hyperphosphorylated tau isoform 1N4R.","description":"In contrast to A<i>β</i> plaques, the spatiotemporal distribution of neurofibrillary tangles of hyperphosphorylated tau (p-tau) predicts cognitive impairment in Alzheimer's disease (AD), underscoring the key pathological role of p-tau and the utmost need to develop AD therapeutics centering upon the control of p-tau aggregation and cytotoxicity. Our drug discovery program is focused on compounds that prevent the aggregation and cytotoxicity of p-tau moieties of the tau isoform 1N4R due to its prevalence (1 N) and long-distance trans-synaptic propagation (4R). We prepared and tested twenty-four newly synthesized small molecules representing the urea (<b>1, 2, 3</b>), sulfonylurea (<b>4</b>), and sulfonamide (<b>5-24</b>) series and evaluated their anti-aggregation effects with biophysical m","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Nov","modification":"2026-05-27T12:06:29.566Z","creation":"2024-11-08T20:15:57.446Z"},"accession":"S-EPMC9614895","cross_references":{"pubmed":["36310922"],"doi":["10.1016/j.molstruc.2022.133574"]}}