Manuscript Topics

Most neurodegenerative diseases are sporadic thus suggesting that many factors must contribute to the onset and progression of these disorders. In particular, post-translational modifications are known to affect protein structure and function and might trigger protein misfolding and accumulation in vivo. Between them, both glycation and transglutamination have been shown to promote protein cross-linking and have a key role in amyloid aggregation in vivo. Proteins in amyloid deposits are often found glycated suggesting a direct correlation between protein glycation and amyloidosis. Interestingly, neurodegenerative diseases, such as Alzheimer’s Disease, Parkinson’s Disease, supranuclear palsy, Huntington’s Disease and other polyglutamine diseases, are characterized in part by aberrant cerebral transglutaminase activity and by increased cross-linked proteins in affected brains. In this special issue we will focus on the molecular determinants of amyloid aggregation and the role of these post-translational modifications in amyloidosis. In addition, possible molecular mechanisms responsible for such diseases will be proposed as well as the possible use of aggregation inhibitors for patients with diseases characterized by aberrant protein aggregation.

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