{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["6"],"submitter":["Soeda Y"],"pubmed_abstract":["Neurofibrillary tangles, composed of hyperphosphorylated tau fibrils, are a pathological hallmark of Alzheimer's disease; the neurofibrillary tangle load correlates strongly with clinical progression of the disease. A growing body of evidence indicates that tau oligomer formation precedes the appearance of neurofibrillary tangles and contributes to neuronal loss. Here we show that tau oligomer formation can be inhibited by compounds whose chemical backbone includes 1,2-dihydroxybenzene. Specifically, we demonstrate that 1,2-dihydroxybenzene-containing compounds bind to and cap cysteine residues of tau and prevent its aggregation by hindering interactions between tau molecules. Further, we show that orally administered DL-isoproterenol, an adrenergic receptor agonist whose skeleton includes"],"journal":["Nature communications"],"pagination":["10216"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC4703892"],"repository":["biostudies-literature"],"pubmed_title":["Toxic tau oligomer formation blocked by capping of cysteine residues with 1,2-dihydroxybenzene groups."],"pmcid":["PMC4703892"],"pubmed_authors":["Almeida OF","Ihara Y","Suzuki M","Maeda S","Miyasaka T","Kimura T","Takashima A","Osada H","Yoshikawa M","Soeda Y","Sumioka A","Yoshiike Y","Koyama H","Sugimoto H","Kondoh Y","Saito A"],"additional_accession":[]},"is_claimable":false,"name":"Toxic tau oligomer formation blocked by capping of cysteine residues with 1,2-dihydroxybenzene groups.","description":"Neurofibrillary tangles, composed of hyperphosphorylated tau fibrils, are a pathological hallmark of Alzheimer's disease; the neurofibrillary tangle load correlates strongly with clinical progression of the disease. A growing body of evidence indicates that tau oligomer formation precedes the appearance of neurofibrillary tangles and contributes to neuronal loss. Here we show that tau oligomer formation can be inhibited by compounds whose chemical backbone includes 1,2-dihydroxybenzene. Specifically, we demonstrate that 1,2-dihydroxybenzene-containing compounds bind to and cap cysteine residues of tau and prevent its aggregation by hindering interactions between tau molecules. Further, we show that orally administered DL-isoproterenol, an adrenergic receptor agonist whose skeleton includes","dates":{"release":"2015-01-01T00:00:00Z","publication":"2015 Dec","modification":"2026-05-05T17:26:35.994Z","creation":"2026-04-07T21:53:54.86Z"},"accession":"S-EPMC4703892","cross_references":{"pubmed":["26671725"],"doi":["10.1038/ncomms10216"]}}