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Protein misfolding is a distinctive characteristic feature of a large group of diseases known as protein conformational diseases as well as aging [1-2]. Proteins may misfold due to inherent mutations [1], mistranslation [3], post-translational modifications (ie oxidation, nitration, phosphorylation, glycation, proteolytic cleavage)[4-6], and upon denaturing stress (ie heat, heavy metals, acidic pH)[7]. Protein misfolding results in loss of native structure and exposure of hydrophobic stretches that are normally buried within the native globular fold. These sticky misfolded species tend to associate with each other via hydrogen bonding and result in soluble oligomers with a cross β-sheet structure [8]. The process of nucleation-dependent polymerization and aggregation goes on until large inclusion bodies and the so-called aggresomes [9] are formed at distinct cellular locations. Therefore, protein aggregation can be considered as a complex multi-step process starting from single monomers and ending in large bodies of insoluble protein aggregates [8].

Protein misfolding is implicated in the postmitotic compartment and in aging. Conformational diseases arise from misfolding and aggregation of specific proteins in postmitotic tissues including the liver, skeletal muscle, eye lens and the brain [10]. Our knowledge on protein aggregation comes largely from studies on neurodegenerative disease models. Although specific abnormal proteins responsible for the pathogenesis are completely different in sequence, structure and function, all neurodegenerative disorders share the common end-stage of protein aggregation and deposition, which take place at various …