Mechanisms and pathology of protein misfolding and aggregation
Despite advances in machine learning-based protein structure prediction, we are still far
from fully understanding how proteins fold into their native conformation. The conventional …
from fully understanding how proteins fold into their native conformation. The conventional …
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 …
Amyloid nomenclature 2022: update, novel proteins, and recommendations by the International Society of Amyloidosis (ISA) Nomenclature Committee
JN Buxbaum, A Dispenzieri, DS Eisenberg, M Fändrich… - Amyloid, 2022 - Taylor & Francis
Abstract The Nomenclature Committee of the International Society of Amyloidosis met at the
XVIII International Symposium on Amyloidosis in September and virtually in October 2022 …
XVIII International Symposium on Amyloidosis in September and virtually in October 2022 …
Amyloid nomenclature 2020: update and recommendations by the International Society of Amyloidosis (ISA) nomenclature committee
MD Benson, JN Buxbaum, DS Eisenberg, G Merlini… - Amyloid, 2020 - Taylor & Francis
Abstract The ISA Nomenclature Committee met electronically before and directly after the
XVII ISA International Symposium on Amyloidosis, which, unfortunately, had to be virtual in …
XVII ISA International Symposium on Amyloidosis, which, unfortunately, had to be virtual in …
[HTML][HTML] Amyloid fibrils in FTLD-TDP are composed of TMEM106B and not TDP-43
Frontotemporal lobar degeneration (FTLD) is the third most common neurodegenerative
condition after Alzheimer's and Parkinson's diseases. FTLD typically presents in 45 to 64 …
condition after Alzheimer's and Parkinson's diseases. FTLD typically presents in 45 to 64 …
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 …
Structural polymorphism of amyloid fibrils in ATTR amyloidosis revealed by cryo-electron microscopy
ATTR amyloidosis is caused by the deposition of transthyretin in the form of amyloid fibrils in
virtually every organ of the body, including the heart. This systemic deposition leads to a …
virtually every organ of the body, including the heart. This systemic deposition leads to a …
Structure-based design of nanobodies that inhibit seeding of Alzheimer's patient–extracted tau fibrils
R Abskharon, H Pan, MR Sawaya… - Proceedings of the …, 2023 - National Acad Sciences
Despite much effort, antibody therapies for Alzheimer's disease (AD) have shown limited
efficacy. Challenges to the rational design of effective antibodies include the difficulty of …
efficacy. Challenges to the rational design of effective antibodies include the difficulty of …
Cryo-EM structure of an ATTRwt amyloid fibril from systemic non-hereditary transthyretin amyloidosis
M Steinebrei, J Gottwald, J Baur, C Röcken… - Nature …, 2022 - nature.com
Wild type transthyretin-derived amyloid (ATTRwt) is the major component of non-hereditary
transthyretin amyloidosis. Its accumulation in the heart of elderly patients is life threatening …
transthyretin amyloidosis. Its accumulation in the heart of elderly patients is life threatening …
Cryo-EM structure of amyloid fibrils formed by the entire low complexity domain of TDP-43
Q Li, WM Babinchak, WK Surewicz - Nature communications, 2021 - nature.com
Amyotrophic lateral sclerosis and several other neurodegenerative diseases are associated
with brain deposits of amyloid-like aggregates formed by the C-terminal fragments of TDP …
with brain deposits of amyloid-like aggregates formed by the C-terminal fragments of TDP …