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 …
Implications of peptide assemblies in amyloid diseases
Neurodegenerative disorders and type 2 diabetes are global epidemics compromising the
quality of life of millions worldwide, with profound social and economic implications. Despite …
quality of life of millions worldwide, with profound social and economic implications. Despite …
Aβ (1–42) fibril structure illuminates self-recognition and replication of amyloid in Alzheimer's disease
Increasing evidence has suggested that formation and propagation of misfolded aggregates
of 42-residue human amyloid β (Aβ (1–42)), rather than of the more abundant Aβ (1–40) …
of 42-residue human amyloid β (Aβ (1–42)), rather than of the more abundant Aβ (1–40) …
[HTML][HTML] Amyloid polymorphism: structural basis and neurobiological relevance
R Tycko - Neuron, 2015 - cell.com
Our understanding of the molecular structures of amyloid fibrils that are associated with
neurodegenerative diseases, of mechanisms by which disease-associated peptides and …
neurodegenerative diseases, of mechanisms by which disease-associated peptides and …
Protein misfolding, functional amyloid, and human disease
Peptides or proteins convert under some conditions from their soluble forms into highly
ordered fibrillar aggregates. Such transitions can give rise to pathological conditions ranging …
ordered fibrillar aggregates. Such transitions can give rise to pathological conditions ranging …
Atomic structures of amyloid cross-β spines reveal varied steric zippers
MR Sawaya, S Sambashivan, R Nelson, MI Ivanova… - Nature, 2007 - nature.com
Amyloid fibrils formed from different proteins, each associated with a particular disease,
contain a common cross-β spine. The atomic architecture of a spine, from the fibril-forming …
contain a common cross-β spine. The atomic architecture of a spine, from the fibril-forming …
Exogenous induction of cerebral β-amyloidogenesis is governed by agent and host
M Meyer-Luehmann, J Coomaraswamy, T Bolmont… - Science, 2006 - science.org
Protein aggregation is an established pathogenic mechanism in Alzheimer's disease, but
little is known about the initiation of this process in vivo. Intracerebral injection of dilute …
little is known about the initiation of this process in vivo. Intracerebral injection of dilute …
Amyloid cross-seeding: Mechanism, implication, and inhibition
Most neurodegenerative diseases such as Alzheimer's disease, type 2 diabetes, Parkinson's
disease, etc. are caused by inclusions and plaques containing misfolded protein …
disease, etc. are caused by inclusions and plaques containing misfolded protein …
Physical and structural basis for polymorphism in amyloid fibrils
R Tycko - Protein Science, 2014 - Wiley Online Library
As our understanding of the molecular structures of amyloid fibrils has matured over the past
15 years, it has become clear that, while amyloid fibrils do have well‐defined molecular …
15 years, it has become clear that, while amyloid fibrils do have well‐defined molecular …
Protein misfolded oligomers: experimental approaches, mechanism of formation, and structure-toxicity relationships
F Bemporad, F Chiti - Chemistry & biology, 2012 - cell.com
The conversion of proteins from their native state to misfolded oligomers is associated with,
and thought to be the cause of, a number of human diseases, including Alzheimer's disease …
and thought to be the cause of, a number of human diseases, including Alzheimer's disease …