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CNS & Neurological Disorders - Drug Targets


ISSN (Print): 1871-5273
ISSN (Online): 1996-3181

Review Article

Deciphering the Role of Aberrant Protein Post-Translational Modification in the Pathology of Neurodegeneration

Author(s): Sadat Shafi, Archu Singh, Paras Gupta, Pooja A. Chawla, Faizana Fayaz, Anjali Sharma and Faheem H. Pottoo*

Volume 20, Issue 1, 2021

Published on: 03 September, 2020

Page: [54 - 67] Pages: 14

DOI: 10.2174/1871527319666200903162200

Price: $65


Neurodegenerative diseases, including Alzheimer’s Disease (AD), Parkinson’s Disease (PD), Amyotrophic Lateral Sclerosis (ALS) and Huntington's Disease (HD), are characterized by progressive neuronal dysfunction and death. Recent studies have established detrimental modifications in the structure and function of brain proteins, which stimulate their aggregation, misfolding and deposition in and around the neurons an important hallmark of neurodegenerative diseases. Post-Translational Modification (PTM) of proteins, including phosphorylation, acetylation, glycosylation, palmitoylation, SUMOylation, and ubiquitination, are important regulators of protein characteristics, including stability, intracellular distribution, activity, interactions, aggregation and clearance. Despite clear evidence that altered protein modifications emerging from impromptu chemical modifications to side chains of amino acid are associated with neurodegeneration, the underlying mechanisms that promote aberrant PTM remain poorly understood. Therefore, elucidating PTM of specific disease-associated proteins can prove to be a significant step in evaluating the functional alteration of proteins and their association with neurodegeneration. This review describes how aberrant PTM of various proteins is linked with the neurodegenerative disease pathogenesis, as well as molecular strategies targeting these modifications for treating such diseases, which are yet incurable.

Keywords: Neurodegenerative diseases, post-translational modification, neuronal dysfunction, phosphorylation, acetylation, palmitoylation, SUMOylation, ubiquitination.

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