PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 29976995-0 2018 Sir-2.1 mediated attenuation of alpha-synuclein expression by Alaskan bog blueberry polyphenols in a transgenic model of Caenorhabditis elegans. Polyphenols 84-95 synuclein alpha Homo sapiens 32-47 21966584-3 2011 Seeded aggregation of alpha-synuclein induced necrotic cell death, which was suppressed by the addition of various polyphenols. Polyphenols 115-126 synuclein alpha Homo sapiens 22-37 26517049-6 2016 Small molecules such as polyphenols, peptides as well as large proteins have proven effective at protecting cells against the cytotoxicity of alpha-synuclein. Polyphenols 24-35 synuclein alpha Homo sapiens 142-157 25498223-0 2015 Tea polyphenols alleviate motor impairments, dopaminergic neuronal injury, and cerebral alpha-synuclein aggregation in MPTP-intoxicated parkinsonian monkeys. Polyphenols 4-15 synuclein alpha Homo sapiens 88-103 23064431-2 2013 In the last decades, a series of compounds, including quinones and polyphenols, has been described as having anti-fibrillogenic action on alpha-synuclein (alpha-syn) whose aggregation is associated to the pathogenesis of Parkinson"s disease (PD). Polyphenols 67-78 synuclein alpha Homo sapiens 138-153 23064431-2 2013 In the last decades, a series of compounds, including quinones and polyphenols, has been described as having anti-fibrillogenic action on alpha-synuclein (alpha-syn) whose aggregation is associated to the pathogenesis of Parkinson"s disease (PD). Polyphenols 67-78 synuclein alpha Homo sapiens 138-147 24835632-7 2014 Moreover, we demonstrated that certain potent inhibitors of alpha-syn fibrillation, such as oxidized catecholamines and polyphenols, undergo spontaneous oxidation in aqueous solution, generating compounds that strongly quench ThT fluorescence. Polyphenols 120-131 synuclein alpha Homo sapiens 60-69 20801100-4 2010 Our data shows a rapid formation of alpha-synuclein amyloid fibrils was stimulated by 1-butyl-3-methylimidazolium bis(trifluoromethylsulfonyl)imide [BIMbF(3)Im], and these fibrils could be disaggregated by polyphenols such as epigallocatechin gallate (EGCG) and baicalein. Polyphenols 206-217 synuclein alpha Homo sapiens 36-51 20385841-2 2010 Recently, we demonstrated that the polyphenol (-)-epi-gallocatechine gallate (EGCG) inhibits alpha-synuclein and amyloid-beta fibrillogenesis. Polyphenols 35-45 synuclein alpha Homo sapiens 93-108 19895818-2 2010 Previous analyses have revealed that several polyphenols inhibit alpha-synuclein assembly with low micromolar IC(50) values, and that SDS-stable, noncytotoxic soluble alpha-synuclein oligomers are formed in their presence. Polyphenols 45-56 synuclein alpha Homo sapiens 65-80 19616561-1 2009 The polyphenol (-)-epigallocatechin-3-gallate (EGCG) has recently attracted much research interest in the field of protein-misfolding diseases because of its potent anti-amyloid activity against amyloid-beta, alpha-synuclein and huntingtin, the amyloid-fibril-forming proteins involved in Alzheimer"s, Parkinson"s and Huntington"s diseases, respectively. Polyphenols 4-14 synuclein alpha Homo sapiens 209-224 19183551-5 2009 We show that the conformations of polyphenol-bound alpha-synuclein monomers and dimers differ from those of unbound monomers and resemble amyloid fibrils. Polyphenols 34-44 synuclein alpha Homo sapiens 51-66 34015214-4 2021 Polyphenols, small molecules, synthetic peptides, and peptide-derived molecules have been considered as potential candidates that inhibit alpha-synuclein oligomerization and its fibrillation, and a few of them are in clinical trials. Polyphenols 0-11 synuclein alpha Homo sapiens 138-153 34948195-5 2021 The present study aimed to assess the role of Ellagic acid (EA), a polyphenol found in many fruits, on alpha-syn aggregation and toxicity. Polyphenols 67-77 synuclein alpha Homo sapiens 103-112 34046949-0 2021 Polyphenol-solubility alters amyloid fibril formation of alpha-synuclein. Polyphenols 0-10 synuclein alpha Homo sapiens 57-72 18511942-4 2008 The polyphenol (-)-epigallocatechin gallate efficiently inhibits the fibrillogenesis of both alpha-synuclein and amyloid-beta by directly binding to the natively unfolded polypeptides and preventing their conversion into toxic, on-pathway aggregation intermediates. Polyphenols 4-14 synuclein alpha Homo sapiens 93-108 16681381-3 2006 Several polyphenols, phenothiazines, porphyrins, polyene macrolides, and Congo red and its derivatives, BSB and FSB, inhibited alpha-synuclein filament assembly with IC(50) values in the low micromolar range. Polyphenols 8-19 synuclein alpha Homo sapiens 127-142 33610557-3 2021 Here we test the effects of Brazilin on both seeded and unseeded alpha-syn fibril formation and show that the natural polyphenol inhibits fibrillogenesis of alpha-syn by a unique mechanism that alters conformational equilibria in two separate points of the assembly mechanism: Brazilin preserves the natively unfolded state of alpha-syn by specifically binding to the compact conformation of the alpha-syn monomer. Polyphenols 118-128 synuclein alpha Homo sapiens 157-166 33610557-3 2021 Here we test the effects of Brazilin on both seeded and unseeded alpha-syn fibril formation and show that the natural polyphenol inhibits fibrillogenesis of alpha-syn by a unique mechanism that alters conformational equilibria in two separate points of the assembly mechanism: Brazilin preserves the natively unfolded state of alpha-syn by specifically binding to the compact conformation of the alpha-syn monomer. Polyphenols 118-128 synuclein alpha Homo sapiens 157-166 33610557-3 2021 Here we test the effects of Brazilin on both seeded and unseeded alpha-syn fibril formation and show that the natural polyphenol inhibits fibrillogenesis of alpha-syn by a unique mechanism that alters conformational equilibria in two separate points of the assembly mechanism: Brazilin preserves the natively unfolded state of alpha-syn by specifically binding to the compact conformation of the alpha-syn monomer. Polyphenols 118-128 synuclein alpha Homo sapiens 157-166 32822152-4 2020 We explore the effectiveness of the polyphenols Epigallocatechin-3-gallate, Oleuropein aglycone, and quercetin on their ability to inhibit aggregation of amyloid-beta, tau, alpha-synuclein, and mitigate other pathological features for AD and PD. Polyphenols 36-47 synuclein alpha Homo sapiens 173-188 33185419-0 2020 Polyphenol Honokiol and Flavone 2",3",4"-Trihydroxyflavone Differentially Interact with alpha-Synuclein at Distinct Phases of Aggregation. Polyphenols 0-10 synuclein alpha Homo sapiens 88-103 33185419-4 2020 This study comprehensively assesses the inhibitory properties of two small molecules, the lignan polyphenol honokiol and the flavonoid 2",3",4"-trihydroxyflavone, in preventing alpha-synuclein fibrilization. Polyphenols 97-107 synuclein alpha Homo sapiens 177-192 33186020-3 2020 Experimental studies reported that epigallocatechin gallate (EGCG), a polyphenol extracted from green tea, can disrupt alpha-syn fibrils into benign amorphous aggregates. Polyphenols 70-80 synuclein alpha Homo sapiens 119-128