Half a century of amyloids: past, present and future

PC Ke, R Zhou, LC Serpell, R Riek… - Chemical Society …, 2020 - pubs.rsc.org
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 …

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 …

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 …

[HTML][HTML] In situ architecture and cellular interactions of PolyQ inclusions

FJB Bäuerlein, I Saha, A Mishra, M Kalemanov… - Cell, 2017 - cell.com
Expression of many disease-related aggregation-prone proteins results in cytotoxicity and
the formation of large intracellular inclusion bodies. To gain insight into the role of inclusions …

NMR spectroscopy captures the essential role of dynamics in regulating biomolecular function

TR Alderson, LE Kay - Cell, 2021 - cell.com
Biomolecules are in constant motion. To understand how they function, and why
malfunctions can cause disease, it is necessary to describe their three-dimensional …

[HTML][HTML] Protein interaction networks in neurodegenerative diseases: From physiological function to aggregation

G Calabrese, C Molzahn, T Mayor - Journal of Biological Chemistry, 2022 - Elsevier
The accumulation of protein inclusions is linked to many neurodegenerative diseases that
typically develop in older individuals, due to a combination of genetic and environmental …

The S/T-rich motif in the DNAJB6 chaperone delays polyglutamine aggregation and the onset of disease in a mouse model

V Kakkar, C Månsson, EP de Mattos, S Bergink… - Molecular cell, 2016 - cell.com
Expanded CAG repeats lead to debilitating neurodegenerative disorders characterized by
aggregation of proteins with expanded polyglutamine (polyQ) tracts. The mechanism of …

Peptide-directed assembly of single-helical gold nanoparticle superstructures exhibiting intense chiroptical activity

AD Merg, JC Boatz, A Mandal, G Zhao… - Journal of the …, 2016 - ACS Publications
Chiral nanoparticle assemblies are an interesting class of materials whose chiroptical
properties make them attractive for a variety of applications. Here, C18-(PEPAuM-ox) 2 …

The structure of pathogenic huntingtin exon 1 defines the bases of its aggregation propensity

CA Elena-Real, A Sagar, A Urbanek… - Nature structural & …, 2023 - nature.com
Huntington's disease is a neurodegenerative disorder caused by a CAG expansion in the
first exon of the HTT gene, resulting in an extended polyglutamine (poly-Q) tract in huntingtin …

Proteins containing expanded polyglutamine tracts and neurodegenerative disease

A Adegbuyiro, F Sedighi, AW Pilkington IV… - Biochemistry, 2017 - ACS Publications
Several hereditary neurological and neuromuscular diseases are caused by an abnormal
expansion of trinucleotide repeats. To date, there have been 10 of these trinucleotide repeat …