biostudies-literatureAlmeida ZLFundação para a Ciência e a TecnologiaFundação para a Ciência e Tecnologia3276https://www.ebi.ac.uk/biostudies/studies/S-EPMC9776232biostudies-literatureUnknown10(12)Protein aggregation and subsequent accumulation of insoluble amyloid fibrils with cross-β structure is an intrinsic characteristic of amyloid diseases, i.e., amyloidoses. Amyloid formation involves a series of on-pathway and off-pathway protein aggregation events, leading to mature insoluble fibrils that eventually accumulate in multiple tissues. In this cascade of events, soluble oligomeric species are formed, which are among the most cytotoxic molecular entities along the amyloid cascade. The direct or indirect action of these amyloid soluble oligomers and amyloid protofibrils and fibrils in several tissues and organs lead to cell death in some cases and organ disfunction in general. There are dozens of different proteins and peptides causing multiple amyloid pathologies, chief among theBiomedicinesAmyloid Disassembly: What Can We Learn from Chaperones?PMC9776232SFRH/BD/137991/2018UID/QUI/00313/2019Brito RMMAlmeida ZLfalseAmyloid Disassembly: What Can We Learn from Chaperones?Protein aggregation and subsequent accumulation of insoluble amyloid fibrils with cross-β structure is an intrinsic characteristic of amyloid diseases, i.e., amyloidoses. Amyloid formation involves a series of on-pathway and off-pathway protein aggregation events, leading to mature insoluble fibrils that eventually accumulate in multiple tissues. In this cascade of events, soluble oligomeric species are formed, which are among the most cytotoxic molecular entities along the amyloid cascade. The direct or indirect action of these amyloid soluble oligomers and amyloid protofibrils and fibrils in several tissues and organs lead to cell death in some cases and organ disfunction in general. There are dozens of different proteins and peptides causing multiple amyloid pathologies, chief among the2022-01-01T00:00:00Z2022 Dec2025-04-19T22:47:28.473Z2025-04-19T22:47:28.473ZS-EPMC97762323655203210.3390/biomedicines10123276