Amyloid oligomers: A joint experimental/computational perspective on Alzheimer's disease, Parkinson's disease, type II diabetes, and amyotrophic lateral sclerosis
PH Nguyen, A Ramamoorthy, BR Sahoo… - Chemical …, 2021 - ACS Publications
Protein misfolding and aggregation is observed in many amyloidogenic diseases affecting
either the central nervous system or a variety of peripheral tissues. Structural and dynamic …
either the central nervous system or a variety of peripheral tissues. Structural and dynamic …
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 …
Machine learned coarse-grained protein force-fields: Are we there yet?
The successful recent application of machine learning methods to scientific problems
includes the learning of flexible and accurate atomic-level force-fields for materials and …
includes the learning of flexible and accurate atomic-level force-fields for materials and …
[HTML][HTML] Visualizing and trapping transient oligomers in amyloid assembly pathways
Oligomers which form during amyloid fibril assembly are considered to be key contributors
towards amyloid disease. However, understanding how such intermediates form, their …
towards amyloid disease. However, understanding how such intermediates form, their …
Computational and theoretical advances in studies of intrinsically disordered proteins
RB Best - Current opinion in structural biology, 2017 - Elsevier
Highlights•Improvements in all-atom simulations and implicit solvent models now allow IDP
simulations with realistic dimensions to be performed.•Native-centric coarse-grained …
simulations with realistic dimensions to be performed.•Native-centric coarse-grained …
General principles underpinning amyloid structure
AIP Taylor, RA Staniforth - Frontiers in Neuroscience, 2022 - frontiersin.org
Amyloid fibrils are a pathologically and functionally relevant state of protein folding, which is
generally accessible to polypeptide chains and differs fundamentally from the globular state …
generally accessible to polypeptide chains and differs fundamentally from the globular state …
High-resolution probing of early events in amyloid-β aggregation related to Alzheimer's disease
In Alzheimer's disease (AD), soluble oligomers of amyloid-β (Aβ) are emerging as a crucial
entity in driving disease progression as compared to insoluble amyloid deposits. The lacuna …
entity in driving disease progression as compared to insoluble amyloid deposits. The lacuna …
Free gangliosides can alter amyloid-β aggregation
A Chakravorty, SD McCalpin, BR Sahoo… - The journal of …, 2022 - ACS Publications
A recently proposed lipid-chaperone hypothesis suggests that free lipid molecules, not
bound to membranes, affect the aggregation of amyloidogenic peptides such as amyloid-β …
bound to membranes, affect the aggregation of amyloidogenic peptides such as amyloid-β …
Mesoscopic protein-rich clusters host the nucleation of mutant p53 amyloid fibrils
The protein p53 is a crucial tumor suppressor, often called “the guardian of the genome”;
however, mutations transform p53 into a powerful cancer promoter. The oncogenic capacity …
however, mutations transform p53 into a powerful cancer promoter. The oncogenic capacity …
Comparing the aggregation free energy landscapes of amyloid beta (1–42) and amyloid beta (1–40)
Using a predictive coarse-grained protein force field, we compute and compare the free
energy landscapes and relative stabilities of amyloid-β protein (1–42) and amyloid-β protein …
energy landscapes and relative stabilities of amyloid-β protein (1–42) and amyloid-β protein …