<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Ziaunys M</submitter><funding>European Commission</funding><pagination>1887</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC9598636</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>11(10)</volume><pubmed_abstract>Amyloidogenic protein/peptide aggregation into fibrillar aggregates is associated with multiple amyloidoses, including widespread neurodegenerative disorders. Despite years of research and a well-understood mechanism, there are still very few treatments available for the increasing number of amyloid-related disorders. In recent years, the search for potential anti-aggregation compounds has shifted toward naturally occurring molecules, with one of the most promising being epigallocatechin-3-gallate (EGCG). This polyphenolic compound was shown to inhibit the aggregation of several amyloidogenic proteins/peptides, including amyloid-beta (related to Alzheimer's disease) and alpha-synuclein (related to Parkinson's disease). However, multiple reports have indicated its limited stability under ph</pubmed_abstract><journal>Antioxidants (Basel, Switzerland)</journal><pubmed_title>Exploring Epigallocatechin-3-Gallate Autoxidation Products: Specific Incubation Times Required for Emergence of Anti-Amyloid Properties.</pubmed_title><pmcid>PMC9598636</pmcid><funding_grant_id>293476</funding_grant_id><pubmed_authors>Ziaunys M</pubmed_authors><pubmed_authors>Smirnovas V</pubmed_authors></additional><is_claimable>false</is_claimable><name>Exploring Epigallocatechin-3-Gallate Autoxidation Products: Specific Incubation Times Required for Emergence of Anti-Amyloid Properties.</name><description>Amyloidogenic protein/peptide aggregation into fibrillar aggregates is associated with multiple amyloidoses, including widespread neurodegenerative disorders. Despite years of research and a well-understood mechanism, there are still very few treatments available for the increasing number of amyloid-related disorders. In recent years, the search for potential anti-aggregation compounds has shifted toward naturally occurring molecules, with one of the most promising being epigallocatechin-3-gallate (EGCG). This polyphenolic compound was shown to inhibit the aggregation of several amyloidogenic proteins/peptides, including amyloid-beta (related to Alzheimer's disease) and alpha-synuclein (related to Parkinson's disease). However, multiple reports have indicated its limited stability under ph</description><dates><release>2022-01-01T00:00:00Z</release><publication>2022 Sep</publication><modification>2025-04-04T11:29:32.135Z</modification><creation>2025-04-04T11:29:32.135Z</creation></dates><accession>S-EPMC9598636</accession><cross_references><pubmed>36290609</pubmed><doi>10.3390/antiox11101887</doi></cross_references></HashMap>