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 …

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 …

[HTML][HTML] Cell-free formation of RNA granules: low complexity sequence domains form dynamic fibers within hydrogels

M Kato, TW Han, S **e, K Shi, X Du, LC Wu, H Mirzaei… - Cell, 2012 - cell.com
Eukaryotic cells contain assemblies of RNAs and proteins termed RNA granules. Many
proteins within these bodies contain KH or RRM RNA-binding domains as well as low …

Amyloid formation as a protein phase transition

TCT Michaels, D Qian, A Šarić, M Vendruscolo… - Nature Reviews …, 2023 - nature.com
The formation of amyloid fibrils is a general class of protein self-assembly behaviour, which
is associated with both functional biology and the development of a number of disorders …

Hierarchically oriented organization in supramolecular peptide crystals

C Yuan, W Ji, R **ng, J Li, E Gazit, X Yan - Nature Reviews Chemistry, 2019 - nature.com
Hierarchical self-assembly and crystallization with long-range ordered spatial arrangement
is ubiquitous in nature and plays an essential role in the regulation of structures and …

Lipid vesicles trigger α-synuclein aggregation by stimulating primary nucleation

C Galvagnion, AK Buell, G Meisl, TCT Michaels… - Nature chemical …, 2015 - nature.com
Abstract α-Synuclein (α-syn) is a 140-residue intrinsically disordered protein that is involved
in neuronal and synaptic vesicle plasticity, but its aggregation to form amyloid fibrils is the …

Functional amyloid–from bacteria to humans

DM Fowler, AV Koulov, WE Balch, JW Kelly - Trends in biochemical …, 2007 - cell.com
Amyloid–a fibrillar, cross β-sheet quaternary structure–was first discovered in the context of
human disease and tissue damage, and was thought to always be detrimental to the host …

Nanomechanics of functional and pathological amyloid materials

TPJ Knowles, MJ Buehler - Nature nanotechnology, 2011 - nature.com
Amyloid or amyloid-like fibrils represent a general class of nanomaterials that can be formed
from many different peptides and proteins. Although these structures have an important role …

Self-assembled peptide nanostructures: the design of molecular building blocks and their technological utilization

E Gazit - Chemical Society Reviews, 2007 - pubs.rsc.org
In this tutorial review the process and applications of peptide self-assembly into nanotubes,
nanospheres, nanofibrils, nanotapes, and other ordered structures at the nano-scale are …

Microglial amyloid beta clearance is driven by PIEZO1 channels

H Jäntti, V Sitnikova, Y Ishchenko… - Journal of …, 2022 - Springer
Background Microglia are the endogenous immune cells of the brain and act as sensors of
pathology to maintain brain homeostasis and eliminate potential threats. In Alzheimer's …