Molecular pathology of neurodegenerative diseases by cryo-EM of amyloids
Abnormal assembly of tau, α-synuclein, TDP-43 and amyloid-β proteins into amyloid
filaments defines most human neurodegenerative diseases. Genetics provides a direct link …
filaments defines most human neurodegenerative diseases. Genetics provides a direct link …
Amyloid oligomers: A joint experimental/computational perspective on Alzheimer's disease, Parkinson's disease, type II diabetes, and amyotrophic lateral sclerosis
PH Nguyen, A Ramamoorthy, BR Sahoo… - Chemical …, 2021 - ACS Publications
Protein misfolding and aggregation is observed in many amyloidogenic diseases affecting
either the central nervous system or a variety of peripheral tissues. Structural and dynamic …
either the central nervous system or a variety of peripheral tissues. Structural and dynamic …
Assembly of recombinant tau into filaments identical to those of Alzheimer's disease and chronic traumatic encephalopathy
Abundant filamentous inclusions of tau are characteristic of more than 20
neurodegenerative diseases that are collectively termed tauopathies. Electron cryo …
neurodegenerative diseases that are collectively termed tauopathies. Electron cryo …
Pathological mechanisms and therapeutic strategies for Alzheimer's disease
Y Ju, KY Tam - Neural regeneration research, 2022 - journals.lww.com
Alzheimer's disease is a rather complex neurodegenerative disease, which is attributed to a
combination of multiple factors. Among the many pathological pathways, synaptic …
combination of multiple factors. Among the many pathological pathways, synaptic …
A new era for understanding amyloid structures and disease
MG Iadanza, MP Jackson, EW Hewitt… - … reviews Molecular cell …, 2018 - nature.com
The aggregation of proteins into amyloid fibrils and their deposition into plaques and
intracellular inclusions is the hallmark of amyloid disease. The accumulation and deposition …
intracellular inclusions is the hallmark of amyloid disease. The accumulation and deposition …
Electrostatic interactions in protein structure, folding, binding, and condensation
Charged and polar groups, through forming ion pairs, hydrogen bonds, and other less
specific electrostatic interactions, impart important properties to proteins. Modulation of the …
specific electrostatic interactions, impart important properties to proteins. Modulation of the …
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 …
β protein (Aβ) are the main component of the senile plaques found in brains of Alzheimer's …
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 …
neurodegenerative diseases, but it is increasingly becoming clear that the propensity to form …
Structure of FUS protein fibrils and its relevance to self-assembly and phase separation of low-complexity domains
Polymerization and phase separation of proteins containing low-complexity (LC) domains
are important factors in gene expression, mRNA processing and trafficking, and localization …
are important factors in gene expression, mRNA processing and trafficking, and localization …
Amyloid-type protein aggregation and prion-like properties of amyloids
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 …
an important hallmark of protein misfolding diseases and therefore have been investigated …