Protein aggregation in neurodegeneration

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Guest Editors
Prof. Vittorio Gentile
Prof. Clara Iannuzzi
Department of Precision Medicine, CIRN - Interuniversity Center of Neuroscience Researches, University of Campania "Luigi Vanvitelli"

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.

Submitted papers should not have been previously published nor be currently under consideration for publication elsewhere. All manuscripts will be peer-reviewed before their acceptance for publication. AIMS Biophysics charges 300 USD Article Processing Charge (APC) for accepted paper after peer review. AIMS Biophysics waive the charges for these article types: Review, Editorial, Letter, Conference Reports, Commentary, Corrections, and Erratum.
The deadline for manuscript submission is March 15, 2019.

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Ivana Sirangelo, Margherita Borriello, Gaetano Irace, Clara Iannuzzi
AIMS Biophysics, 2018, 5(2): 155-165. doi: 10.3934/biophy.2018.2.155
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