Amyloid β oligomers in Alzheimer's disease pathogenesis, treatment, and diagnosis

KL Viola, WL Klein - Acta neuropathologica, 2015 - Springer
Protein aggregation is common to dozens of diseases including prionoses, diabetes,
Parkinson's and Alzheimer's. Over the past 15 years, there has been a paradigm shift in …

Crucial role of protein oligomerization in the pathogenesis of Alzheimer's and Parkinson's diseases

ML Choi, S Gandhi - The FEBS journal, 2018 - Wiley Online Library
Misfolding and aggregation of the proteins amyloid‐β, tau and alpha‐synuclein is the
predominant pathology underlying the neurodegenerative disorders, Alzheimer's and …

Inhibitors and chemical probes for molecular chaperone networks

JE Gestwicki, H Shao - Journal of Biological Chemistry, 2019 - ASBMB
The molecular chaperones are central mediators of protein homeostasis. In that role, they
engage in widespread protein–protein interactions (PPIs) with each other and with their" …

Nuclear functions of prefoldin

G Millán-Zambrano, S Chávez - Open biology, 2014 - royalsocietypublishing.org
Prefoldin is a cochaperone, present in all eukaryotes, that cooperates with the chaperonin
CCT. It is known mainly for its functional relevance in the cytoplasmic folding of actin and …

Prefoldin function in cellular protein homeostasis and human diseases

I Tahmaz, S Shahmoradi Ghahe, U Topf - Frontiers in cell and …, 2022 - frontiersin.org
Cellular functions are largely performed by proteins. Defects in the production, folding, or
removal of proteins from the cell lead to perturbations in cellular functions that can result in …

Prefoldin 2 contributes to mitochondrial morphology and function

I Tahmaz, S Shahmoradi Ghahe, M Stasiak, KP Liput… - BMC biology, 2023 - Springer
Background Prefoldin is an evolutionarily conserved co-chaperone of the tailless complex
polypeptide 1 ring complex (TRiC)/chaperonin containing tailless complex 1 (CCT). The …

Model of the external force field for the protein folding process—the role of prefoldin

I Roterman, K Stapor, L Konieczny - Frontiers in Chemistry, 2024 - frontiersin.org
Introduction: The protein folding process is very sensitive to environmental conditions. Many
possibilities in the form of numerous pathways for this process can—if an incorrect one is …

Chaperones as suppressors of protein misfolded oligomer toxicity

B Mannini, F Chiti - Frontiers in molecular neuroscience, 2017 - frontiersin.org
Chaperones have long been recognized to play well defined functions such as to:(i) assist
protein folding and promote formation and maintenance of multisubunit complexes;(ii) …

The functions and mechanisms of prefoldin complex and prefoldin-subunits

J Liang, L Xia, L Oyang, J Lin, S Tan, P Yi, Y Han… - Cell & bioscience, 2020 - Springer
The correct folding is a key process for a protein to acquire its functional structure and
conformation. Prefoldin is a well-known chaperone protein that regulates the correct folding …

[HTML][HTML] Maintaining essential microtubule bundles in meter-long axons: a role for local tubulin biogenesis?

LM Pinho-Correia, A Prokop - Brain Research Bulletin, 2023 - Elsevier
Axons are the narrow, up-to-meter long cellular processes of neurons that form the
biological cables wiring our nervous system. Most axons must survive for an organism's …