[HTML][HTML] Small molecule therapeutics for tauopathy in Alzheimer's disease: walking on the path of most resistance
Alzheimer's disease (AD) is the most common form of dementia characterized by presence
of extracellular amyloid plaques and intracellular neurofibrillary tangles composed of tau …
of extracellular amyloid plaques and intracellular neurofibrillary tangles composed of tau …
HSPA8/HSC70 in immune disorders: a molecular rheostat that adjusts chaperone-mediated autophagy substrates
SR Bonam, M Ruff, S Muller - Cells, 2019 - mdpi.com
HSPA8/HSC70 is a molecular chaperone involved in a wide variety of cellular processes. It
plays a crucial role in protein quality control, ensuring the correct folding and re-folding of …
plays a crucial role in protein quality control, ensuring the correct folding and re-folding of …
Pathogenic tau impairs axon initial segment plasticity and excitability homeostasis
Dysregulation of neuronal excitability underlies the pathogenesis of tauopathies, including
frontotemporal dementia (FTD) with tau inclusions. A majority of FTD-causing tau mutations …
frontotemporal dementia (FTD) with tau inclusions. A majority of FTD-causing tau mutations …
Map** interactions with the chaperone network reveals factors that protect against tau aggregation
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 …
folding, function and turnover. However, it is often unclear which chaperones are critical for …
Function, therapeutic potential, and inhibition of Hsp70 chaperones
Hsp70s are among the most highly conserved proteins in all of biology. Through an iterative
binding and release of exposed hydrophobic residues on client proteins, Hsp70s can …
binding and release of exposed hydrophobic residues on client proteins, Hsp70s can …
Bromo-protopine, a novel protopine derivative, alleviates tau pathology by activating chaperone-mediated autophagy for Alzheimer's disease therapy
SG Sreenivasmurthy, A Iyaswamy… - Frontiers in Molecular …, 2022 - frontiersin.org
Emerging evidence from Alzheimer's disease (AD) patients suggests that reducing tau
pathology can restore cognitive and memory loss. To reduce tau pathology, it is critical to …
pathology can restore cognitive and memory loss. To reduce tau pathology, it is critical to …
HSP70 and HSP90 in neurodegenerative diseases
Molecular chaperones have a role to stabilize proteins or assist them in reaching their native
fold. Heat shock proteins (HSPs) are a family of molecular chaperons that protect proteins …
fold. Heat shock proteins (HSPs) are a family of molecular chaperons that protect proteins …
Protein–protein interactions in the molecular chaperone network
Conspectus Molecular chaperones play a central role in protein homeostasis (aka
proteostasis) by balancing protein folding, quality control, and turnover. To perform these …
proteostasis) by balancing protein folding, quality control, and turnover. To perform these …
Exploration of benzothiazole rhodacyanines as allosteric inhibitors of protein–protein interactions with heat shock protein 70 (Hsp70)
Cancer cells rely on the chaperone heat shock protein 70 (Hsp70) for survival and
proliferation. Recently, benzothiazole rhodacyanines have been shown to bind an allosteric …
proliferation. Recently, benzothiazole rhodacyanines have been shown to bind an allosteric …
Hsp70 inhibits the nucleation and elongation of tau and sequesters tau aggregates with high affinity
As a key player of the protein quality control network of the cell, the molecular chaperone
Hsp70 inhibits the aggregation of the amyloid protein tau. To date, the mechanism of this …
Hsp70 inhibits the aggregation of the amyloid protein tau. To date, the mechanism of this …