Half a century of amyloids: past, present and future
Amyloid diseases are global epidemics with profound health, social and economic
implications and yet remain without a cure. This dire situation calls for research into the …
implications and yet remain without a cure. This dire situation calls for research into the …
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 …
Secondary nucleation in amyloid formation
M Törnquist, TCT Michaels, K Sanagavarapu… - Chemical …, 2018 - pubs.rsc.org
Nucleation of new peptide and protein aggregates on the surfaces of amyloid fibrils of the
same peptide or protein has emerged in the past two decades as a major pathway for both …
same peptide or protein has emerged in the past two decades as a major pathway for both …
Atomic Resolution Structure of Monomorphic Aβ42 Amyloid Fibrils
Amyloid-β (Aβ) is a 39–42 residue protein produced by the cleavage of the amyloid
precursor protein (APP), which subsequently aggregates to form cross-β amyloid fibrils that …
precursor protein (APP), which subsequently aggregates to form cross-β amyloid fibrils that …
Interrogating amyloid aggregates using fluorescent probes
Amyloids are a broad class of proteins and peptides that can misfold and assemble into long
unbranched fibrils with a cross-β conformation. These misfolding and aggregation events …
unbranched fibrils with a cross-β conformation. These misfolding and aggregation events …
Molecular mechanisms of protein aggregation from global fitting of kinetic models
The elucidation of the molecular mechanisms by which soluble proteins convert into their
amyloid forms is a fundamental prerequisite for understanding and controlling disorders that …
amyloid forms is a fundamental prerequisite for understanding and controlling disorders that …
On the lag phase in amyloid fibril formation
P Arosio, TPJ Knowles, S Linse - Physical Chemistry Chemical Physics, 2015 - pubs.rsc.org
The formation of nanoscale amyloid fibrils from normally soluble peptides and proteins is a
common form of self-assembly phenomenon that has fundamental connections with …
common form of self-assembly phenomenon that has fundamental connections with …
Acceleration of α-synuclein aggregation by exosomes
Exosomes are small vesicles released from cells into extracellular space. We have isolated
exosomes from neuroblastoma cells and investigated their influence on the aggregation of α …
exosomes from neuroblastoma cells and investigated their influence on the aggregation of α …
A molecular chaperone breaks the catalytic cycle that generates toxic Aβ oligomers
SIA Cohen, P Arosio, J Presto… - Nature structural & …, 2015 - nature.com
Alzheimer's disease is an increasingly prevalent neurodegenerative disorder whose
pathogenesis has been associated with aggregation of the amyloid-β peptide (Aβ42) …
pathogenesis has been associated with aggregation of the amyloid-β peptide (Aβ42) …
Secondary nucleation of monomers on fibril surface dominates α-synuclein aggregation and provides autocatalytic amyloid amplification
Parkinson's disease (PD) is characterized by proteinaceous aggregates named Lewy
Bodies and Lewy Neurites containing α-synuclein fibrils. The underlying aggregation …
Bodies and Lewy Neurites containing α-synuclein fibrils. The underlying aggregation …