<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>13</volume><submitter>Raimundo AF</submitter><pubmed_abstract>&lt;h4>Introduction&lt;/h4>Diabetes is one of the major metabolic diseases worldwide. Despite being a complex systemic pathology, the aggregation and deposition of Islet Amyloid Polypeptide (IAPP), or amylin, is a recognized histopathological marker of the disease. Although IAPP proteotoxicity represents an important trigger of β-cell dysfunction and ultimately death, its exploitation as a therapeutic tool remains underdeveloped. The bioactivity of (poly)phenols towards inhibition of pathological protein aggregation is well known, however, most of the identified molecules have limited bioavailability.&lt;h4>Methods&lt;/h4>Using a strategy combining in silico, cell-free and cell studies, we scrutinized a unique in-house collection of (poly)phenol metabolites predicted to appear in the human circulation</pubmed_abstract><journal>Frontiers in endocrinology</journal><pagination>1008418</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC9797523</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>Urolithin B: Two-way attack on IAPP proteotoxicity with implications for diabetes.</pubmed_title><pmcid>PMC9797523</pmcid><pubmed_authors>Dos Santos DJVA</pubmed_authors><pubmed_authors>Ferreira S</pubmed_authors><pubmed_authors>Menezes R</pubmed_authors><pubmed_authors>Brito JA</pubmed_authors><pubmed_authors>Raimundo AF</pubmed_authors><pubmed_authors>Saraiva N</pubmed_authors><pubmed_authors>Lopes-da-Silva M</pubmed_authors><pubmed_authors>Pobre V</pubmed_authors><pubmed_authors>Dos Santos CN</pubmed_authors></additional><is_claimable>false</is_claimable><name>Urolithin B: Two-way attack on IAPP proteotoxicity with implications for diabetes.</name><description>&lt;h4>Introduction&lt;/h4>Diabetes is one of the major metabolic diseases worldwide. Despite being a complex systemic pathology, the aggregation and deposition of Islet Amyloid Polypeptide (IAPP), or amylin, is a recognized histopathological marker of the disease. Although IAPP proteotoxicity represents an important trigger of β-cell dysfunction and ultimately death, its exploitation as a therapeutic tool remains underdeveloped. The bioactivity of (poly)phenols towards inhibition of pathological protein aggregation is well known, however, most of the identified molecules have limited bioavailability.&lt;h4>Methods&lt;/h4>Using a strategy combining in silico, cell-free and cell studies, we scrutinized a unique in-house collection of (poly)phenol metabolites predicted to appear in the human circulation</description><dates><release>2022-01-01T00:00:00Z</release><publication>2022</publication><modification>2025-04-26T05:19:19.069Z</modification><creation>2025-02-19T01:57:12.027Z</creation></dates><accession>S-EPMC9797523</accession><cross_references><pubmed>36589826</pubmed><doi>10.3389/fendo.2022.1008418</doi></cross_references></HashMap>