Mechanisms and pathology of protein misfolding and aggregation
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 …
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
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 …
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
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 …
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
INTRODUCTION Cells have evolved quality control mechanisms that operate under normal
growth conditions and during stress to maintain protein homeostasis (proteostasis) and …
growth conditions and during stress to maintain protein homeostasis (proteostasis) and …
Self-assembling peptide and protein amyloids: from structure to tailored function in nanotechnology
Self-assembled peptide and protein amyloid nanostructures have traditionally been
considered only as pathological aggregates implicated in human neurodegenerative …
considered only as pathological aggregates implicated in human neurodegenerative …
[HTML][HTML] Phase transition of a disordered nuage protein generates environmentally responsive membraneless organelles
Cells chemically isolate molecules in compartments to both facilitate and regulate their
interactions. In addition to membrane-encapsulated compartments, cells can form …
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 …
rapidly increasing research activities across a wide range of scientific disciplines. Such …
From protein building blocks to functional materials
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 …
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 …
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 …
deposition into insoluble plaques and intracellular inclusions is the hallmark of several …