Background: Alzheimer's disease (AD) is a neurodegenerative disorder recognized as the most
common cause of chronic dementia among the ageing population. AD is histopathologically characterized by
progressive loss of neurons and deposits of insoluble proteins, primarily composed of amyloid-β pelaques and
neurofibrillary tangles (NFTs).
Methods: Several molecular processes contribute to the formation of AD cellular hallmarks. Among them,
post-translational modifications (PTMs) represent an attractive mechanism underlying the formation of covalent
bonds between chemical groups/peptides to target proteins, which ultimately result modified in their function.
Most of the proteins related to AD undergo PTMs. Several recent studies show that AD-related proteins
like APP, Aβ, tau, BACE1 undergo post-translational modifications. The effect of PTMs contributes to the
normal function of cells, although aberrant protein modification, which may depend on many factors, can
drive the onset or support the development of AD.
Results: Here we will discuss the effect of several PTMs on the functionality of AD-related proteins potentially
contributing to the development of AD pathology.
Conclusion: We will consider the role of Ubiquitination, Phosphorylation, SUMOylation, Acetylation and
Nitrosylation on specific AD-related proteins and, more interestingly, the possible interactions that may occur
between such different PTMs.