We discuss protein post‐translational modification (PTM) from an information processing
perspective. PTM at multiple sites on a protein creates a combinatorial explosion in the …

Hyperphosphorylation of microtubule-associated protein tau is one of the major pathological
events in Alzheimer's disease (AD) and other related neurodegenerative diseases, including …

Abnormal phosphorylation (" hyperphosphorylation") and aggregation of Tau protein are
hallmarks of Alzheimer disease and other tauopathies, but their causative connection is still …

Phosphorylation of the neuronal microtubule-associated Tau protein plays a critical role in
the aggregation process leading to the formation of insoluble intraneuronal fibrils within …

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 …

Phosphorylation of the microtubule-associated Tau protein plays a major role in the
regulation of its activity of tubulin polymerization and/or stabilization of microtubule …

Lysine acetylation of the neuronal Tau protein was described as a novel mechanism of
posttranslational regulation of Tau functions with important outcomes in microtubule binding …

The aggregation of hyperphosphorylated tau into amyloid fibrils is closely linked to the
progression of Alzheimer's disease. To gain insight into the link between amyloid structure …

Protein aggregation into highly ordered, regularly repeated cross-β sheet structures called
amyloid fibrils is closely associated to human disorders such as neurodegenerative …

The formation of intraneuronal fibrillar inclusions of tau protein is associated with several
neurodegenerative diseases referred to as tauopathies including Alzheimer's disease (AD) …