Protein misfolding and aggregation is observed in many amyloidogenic diseases affecting
either the central nervous system or a variety of peripheral tissues. Structural and dynamic …

Protein phosphorylation is a crucial regulator of protein and cellular function, yet, despite
identifying an enormous number of phosphorylation sites, the role of most is still unclear …

The functions of the neuronal microtubule-associated protein Tau in the central nervous
system are regulated by manifold posttranslational modifications at more than 50 sites. Tau …

Converging evidence continues to point towards Tau aggregation and pathology formation
as central events in the pathogenesis of Alzheimer's disease and other Tauopathies …

Post‐translational modifications (PTMs) have emerged as key modulators of protein phase
separation and have been linked to protein aggregation in neurodegenerative disorders …

Intrinsically disordered proteins (IDPs) play many biological roles in the human proteome
ranging from vesicular transport, signal transduction to neurodegenerative diseases. The Aβ …

Amyloid proteins are involved in many neurodegenerative disorders such as Alzheimer's
disease [Tau, Amyloid β (Aβ)], Parkinson's disease [alpha-synuclein (αSyn)], and …

Nature has developed a plethora of protein machinery to operate and maintain nearly every
task of cellular life. These processes are tightly regulated via post‐expression modifications …

Neurodegenerative proteinopathies are characterized by the intracellular formation of
insoluble and toxic protein aggregates in the brain that are closely linked to disease …

Total chemical protein synthesis provides access to entire D‐protein enantiomers enabling
unique applications in molecular biology, structural biology, and bioactive compound …