Characterization of pairs of toxic and nontoxic misfolded protein oligomers elucidates the structural determinants of oligomer toxicity in protein misfolding diseases

R Limbocker, N Cremades, R Cascella… - Accounts of Chemical …, 2023 - ACS Publications
Conspectus The aberrant misfolding and aggregation of peptides and proteins into amyloid
aggregates occurs in over 50 largely incurable protein misfolding diseases. These …

[HTML][HTML] Disentangling mitochondria in Alzheimer's disease

A Johri - International journal of molecular sciences, 2021 - mdpi.com
Alzheimer's disease (AD) is a major cause of dementia in older adults and is fast becoming
a major societal and economic burden due to an increase in life expectancy. Age seems to …

Imaging Amyloid‐β Membrane Interactions: Ion‐Channel Pores and Lipid‐Bilayer Permeability in Alzheimer's Disease

JH Viles - Angewandte Chemie International Edition, 2023 - Wiley Online Library
The accumulation of the amyloid‐β peptides (Aβ) is central to the development of
Alzheimer's disease. The mechanism by which Aβ triggers a cascade of events that leads to …

[HTML][HTML] Understanding the role of protein glycation in the amyloid aggregation process

I Sirangelo, C Iannuzzi - International Journal of Molecular Sciences, 2021 - mdpi.com
Protein function and flexibility is directly related to the native distribution of its structural
elements and any alteration in protein architecture leads to several abnormalities and …

Protein misfolding and related human diseases: A comprehensive review of toxicity, proteins involved, and current therapeutic strategies

AN Khan, RH Khan - International Journal of Biological Macromolecules, 2022 - Elsevier
Most of the cell's chemical reactions and structural components are facilitated by proteins.
But proteins are highly dynamic molecules, where numerous modifications or changes in the …

Protein misfolding and amyloid nucleation through liquid–liquid phase separation

S Mukherjee, M Poudyal, K Dave, P Kadu… - Chemical Society …, 2024 - pubs.rsc.org
Liquid–liquid phase separation (LLPS) is an emerging phenomenon in cell physiology and
diseases. The weak multivalent interaction prerequisite for LLPS is believed to be facilitated …

[HTML][HTML] Flanking regions, amyloid cores, and polymorphism: the potential interplay underlying structural diversity

AA Bhopatkar, R Kayed - Journal of Biological Chemistry, 2023 - ASBMB
The β-sheet–rich amyloid core is the defining feature of protein aggregates associated with
neurodegenerative disorders. Recent investigations have revealed that there exist multiple …

Quantitative attribution of the protective effects of aminosterols against protein aggregates to their chemical structures and ability to modulate biological membranes

S Errico, G Lucchesi, D Odino, EY Osman… - Journal of Medicinal …, 2023 - ACS Publications
Natural aminosterols are promising drug candidates against neurodegenerative diseases,
like Alzheimer and Parkinson, and one relevant protective mechanism occurs via their …

[HTML][HTML] Modulation of the interactions between α-synuclein and lipid membranes by post-translational modifications

R Bell, M Vendruscolo - Frontiers in neurology, 2021 - frontiersin.org
Parkinson's disease is characterised by the presence in brain tissue of aberrant inclusions
known as Lewy bodies and Lewy neurites, which are deposits composed by α-synuclein …

[HTML][HTML] Significance of oligomeric and fibrillar species in amyloidosis: insights into pathophysiology and treatment

H Koike, Y Iguchi, K Sahashi, M Katsuno - Molecules, 2021 - mdpi.com
Amyloidosis is a term referring to a group of various protein-misfolding diseases wherein
normally soluble proteins form aggregates as insoluble amyloid fibrils. How, or whether …