Amyloid-type protein aggregation and prion-like properties of amyloids

D Willbold, B Strodel, GF Schröder, W Hoyer… - Chemical …, 2021 - ACS Publications
This review will focus on the process of amyloid-type protein aggregation. Amyloid fibrils are
an important hallmark of protein misfolding diseases and therefore have been investigated …

Food protein amyloid fibrils: Origin, structure, formation, characterization, applications and health implications

Y Cao, R Mezzenga - Advances in colloid and interface science, 2019 - Elsevier
Amyloid fibrils have traditionally been considered only as pathological aggregates in human
neurodegenerative diseases, but it is increasingly becoming clear that the propensity to form …

Structures of α-synuclein filaments from multiple system atrophy

M Schweighauser, Y Shi, A Tarutani, F Kametani… - Nature, 2020 - nature.com
Synucleinopathies, which include multiple system atrophy (MSA), Parkinson's disease,
Parkinson's disease with dementia and dementia with Lewy bodies (DLB), are human …

Fibril structure of amyloid-β (1–42) by cryo–electron microscopy

L Gremer, D Schölzel, C Schenk, E Reinartz, J Labahn… - Science, 2017 - science.org
Amyloids are implicated in neurodegenerative diseases. Fibrillar aggregates of the amyloid-
β protein (Aβ) are the main component of the senile plaques found in brains of Alzheimer's …

[PDF][PDF] Structure of FUS protein fibrils and its relevance to self-assembly and phase separation of low-complexity domains

DT Murray, M Kato, Y Lin, KR Thurber, I Hung… - Cell, 2017 - cell.com
Polymerization and phase separation of proteins containing low-complexity (LC) domains
are important factors in gene expression, mRNA processing and trafficking, and localization …

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 …

Solid-state NMR structure of a pathogenic fibril of full-length human α-synuclein

MD Tuttle, G Comellas, AJ Nieuwkoop… - Nature structural & …, 2016 - nature.com
Misfolded α-synuclein amyloid fibrils are the principal components of Lewy bodies and
neurites, hallmarks of Parkinson's disease (PD). We present a high-resolution structure of an …

α-Synuclein misfolding and aggregation: Implications in Parkinson's disease pathogenesis

S Mehra, S Sahay, SK Maji - Biochimica et Biophysica Acta (BBA)-Proteins …, 2019 - Elsevier
Abstract α-Synuclein (α-Syn) has been extensively studied for its structural and biophysical
properties owing to its pathophysiological role in Parkinson's disease (PD). Lewy bodies …

Two new polymorphic structures of human full-length alpha-synuclein fibrils solved by cryo-electron microscopy

R Guerrero-Ferreira, NMI Taylor, AA Arteni, P Kumari… - Elife, 2019 - elifesciences.org
Intracellular inclusions rich in alpha-synuclein are a hallmark of several neuropathological
diseases including Parkinson's disease (PD). Previously, we reported the structure of alpha …

[HTML][HTML] Structural and functional characterization of two alpha-synuclein strains

L Bousset, L Pieri, G Ruiz-Arlandis, J Gath… - Nature …, 2013 - nature.com
Abstract α-synuclein aggregation is implicated in a variety of diseases including Parkinson's
disease, dementia with Lewy bodies, pure autonomic failure and multiple system atrophy …