Tau protein is abundant in the central nervous system and involved in microtubule assembly
and stabilization. It is predominantly associated with axonal microtubules and present at …

Alzheimer's disease (AD) belongs to a group of neurodegenerative diseases collectively
designated as “tauopathies”, because they are characterized by the aggregation of …

Tau is a protein that is highly enriched in neurons and was originally defined by its ability to
bind and stabilize microtubules. However, it is now becoming evident that the functions of …

Phosphorylation of proteins on serine or threonine residues preceding proline is a key
signalling mechanism in diverse physiological and pathological processes. Pin1 (peptidyl …

Background Alzheimer's disease (AD) is characterized by a neurodegenerative progression
that alters cognition. On a phenotypical level, cognition is evaluated by means of the …

The molecular chaperone Hsp90 is critical for the maintenance of cellular homeostasis and
represents a promising drug target. Despite increasing knowledge on the structure of Hsp90 …

Peptidyl‐prolyl cis/trans isomerases (PPI ases), a unique family of molecular chaperones,
regulate protein folding at proline residues. These residues are abundant within intrinsically …

The aggregation of amyloid-β (Aβ) peptides into oligomers and fibrils is a key pathological
feature of Alzheimer's disease (AD). An increasing amount of evidence suggests that …

Alzheimer's Disease (AD) is characterized by progressive loss of cognitive function, linked to
marked neuronal loss. Pathological hallmarks of the disease are the accumulation of the …

Alzheimer's disease (AD) is the most common cause of dementia with cognitive decline. The
neuropathology of AD is characterized by intracellular aggregation of neurofibrillary tangles …