Mechanisms and pathology of protein misfolding and aggregation

N Louros, J Schymkowitz, F Rousseau - Nature Reviews Molecular Cell …, 2023 - nature.com
Despite advances in machine learning-based protein structure prediction, we are still far
from fully understanding how proteins fold into their native conformation. The conventional …

Protein misfolding, amyloid formation, and human disease: a summary of progress over the last decade

F Chiti, CM Dobson - Annual review of biochemistry, 2017 - annualreviews.org
Peptides and proteins have been found to possess an inherent tendency to convert from
their native functional states into intractable amyloid aggregates. This phenomenon is …

The release of toxic oligomers from α-synuclein fibrils induces dysfunction in neuronal cells

R Cascella, SW Chen, A Bigi, JD Camino… - Nature …, 2021 - nature.com
The self-assembly of α-synuclein (αS) into intraneuronal inclusion bodies is a key
characteristic of Parkinson's disease. To define the nature of the species giving rise to …

The nucleolus functions as a phase-separated protein quality control compartment

F Frottin, F Schueder, S Tiwary, R Gupta, R Körner… - Science, 2019 - science.org
INTRODUCTION Cells have evolved quality control mechanisms that operate under normal
growth conditions and during stress to maintain protein homeostasis (proteostasis) and …

Self-assembling peptide and protein amyloids: from structure to tailored function in nanotechnology

G Wei, Z Su, NP Reynolds, P Arosio… - Chemical Society …, 2017 - pubs.rsc.org
Self-assembled peptide and protein amyloid nanostructures have traditionally been
considered only as pathological aggregates implicated in human neurodegenerative …

[HTML][HTML] Phase transition of a disordered nuage protein generates environmentally responsive membraneless organelles

TJ Nott, E Petsalaki, P Farber, D Jervis, E Fussner… - Molecular cell, 2015 - cell.com
Cells chemically isolate molecules in compartments to both facilitate and regulate their
interactions. In addition to membrane-encapsulated compartments, cells can form …

The amyloid state and its association with protein misfolding diseases

TPJ Knowles, M Vendruscolo… - Nature reviews Molecular …, 2014 - nature.com
The phenomenon of protein aggregation and amyloid formation has become the subject of
rapidly increasing research activities across a wide range of scientific disciplines. Such …

From protein building blocks to functional materials

Y Shen, A Levin, A Kamada, Z Toprakcioglu… - ACS …, 2021 - ACS Publications
Proteins are the fundamental building blocks for high-performance materials in nature. Such
materials fulfill structural roles, as in the case of silk and collagen, and can generate active …

Amyloid polymorphism in the protein folding and aggregation energy landscape

J Adamcik, R Mezzenga - Angewandte Chemie International …, 2018 - Wiley Online Library
Protein folding involves a large number of steps and conformations in which the folding
protein samples different thermodynamic states characterized by local minima. Kinetically …

Structure and aggregation mechanisms in amyloids

ZL Almeida, RMM Brito - Molecules, 2020 - mdpi.com
The aggregation of a polypeptide chain into amyloid fibrils and their accumulation and
deposition into insoluble plaques and intracellular inclusions is the hallmark of several …