Mapping interactions with the chaperone network reveals factors that protect against tau aggregation. [PDF]
, 2018 A network of molecular chaperones is known to bind proteins ('clients') and balance their folding, function and turnover. However, it is often unclear which chaperones are critical for selective recognition of individual clients. It is also not clear why
A Rodina +95 more
core +3 more sources
Nuclear tau and its potential role in Alzheimer’s disease [PDF]
, 2016 Tau protein, found in both neuronal and non-neuronal cells, forms aggregates in neurons that constitutes one of the hallmarks of Alzheimer’s disease (AD).
Al-Hilaly, Youssra +2 more
core +6 more sources
Folding of the Tau Protein on Microtubules
Angewandte Chemie International Edition, 2015 AbstractMicrotubules are regulated by microtubule‐associated proteins. However, little is known about the structure of microtubule‐associated proteins in complex with microtubules. Herein we show that the microtubule‐associated protein Tau, which is intrinsically disordered in solution, locally folds into a stable structure upon binding to microtubules.
Jacek Biernat +8 more
openaire +6 more sources
Interaction of tau with the RNA-Binding Protein TIA1 Regulates tau Pathophysiology and Toxicity
Cell Reports, 2016 Summary: Dendritic mislocalization of microtubule associated protein tau is a hallmark of tauopathies, but the role of dendritic tau is unknown. We now report that tau interacts with the RNA-binding protein (RBP) TIA1 in brain tissue, and we present the ...
Tara Vanderweyde +15 more
doaj +1 more source
The role of p38 MAPK and its substrates in neuronal plasticity and neurodegenerative disease [PDF]
, 2012 A significant amount of evidence suggests that the p38-mitogen-activated protein kinase (MAPK) signalling cascade plays a crucial role in synaptic plasticity and in neurodegenerative diseases.
Corrêa, Sônia A. L. +1 more
core +3 more sources
ALZHEIMER'S DISEASE AND TAU PROTEINS
The Lancet, 1986 info:eu-repo/semantics ...
Brion, Jean Pierre +2 more
openaire +5 more sources
Extracellular Monomeric Tau Protein Is Sufficient to Initiate the Spread of Tau Protein Pathology [PDF]
Journal of Biological Chemistry, 2014 Understanding the formation and propagation of aggregates of the Alzheimer disease-associated Tau protein in vivo is vital for the development of therapeutics for this devastating disorder. Using our recently developed live-cell aggregation sensor in neuron-like cells, we demonstrate that different variants of exogenous monomeric Tau, namely full ...
Eva-Maria Mandelkow +11 more
openaire +4 more sources
Bioengineering, 2020 Tau protein aggregation is identified as one of the key phenomena associated with the onset and progression of Alzheimer’s disease. In the present study, we performed on-chip confocal imaging of tau protein aggregation and tau–drug interactions using a ...
Shubha Jain +6 more
doaj +1 more source
Loss of vesicular dopamine release precedes tauopathy in degenerative dopaminergic neurons in a Drosophila model expressing human tau. [PDF]
, 2013 While a number of genome-wide association studies have identified microtubule-associated protein tau as a strong risk factor for Parkinson's disease (PD), little is known about the mechanism through which human tau can predispose an individual to this ...
Chang, Hui-Yun +6 more
core +2 more sources
Microglial activation arises after aggregation of phosphorylated-tau in a neuron-specific P301S tauopathy mouse model [PDF]
, 2020 Alzheimer's disease, progressive supranuclear palsy and frontotemporal dementia are characterized by neuronal expression of aberrant tau protein, tau hyperphosphorylation (pTAU), tau aggregation and neurofibrillary tangle formation sequentially ...
Carmans, Sofie +13 more
core +1 more source