title: Effects of Intrinsic and Extrinsic Factors on Aggregation of Physiologically Important Intrinsically Disordered Proteins.
abstract: Misfolding and aggregation of proteins and peptides play an important role in a number of diseases as well as in many physiological processes. Many of the proteins that misfold and aggregate in vivo are intrinsically disordered. Protein aggregation is a complex multistep process, and aggregates can significantly differ in morphology, structure, stability, cytotoxicity, and self-propagation ability. The aggregation process is influenced by both intrinsic (e.g., mutations and expression levels) and extrinsic (e.g., polypeptide chain truncation, macromolecular crowding, posttranslational modifications, as well as interaction with metal ions, other small molecules, lipid membranes, and chaperons) factors. This review examines the effect of a variety of these factors on aggregation of physiologically important intrinsically disordered proteins.
authors.affiliation: Byrd Alzheimer's Research Institute, Morsani College of Medicine, University of South Florida, Tampa, FL, United States. Electronic address: lbreydo@health.usf.edu.
authors.forename: L
authors.initials: L
authors.lastname: Breydo
authors.affiliation: Byrd Alzheimer's Research Institute, Morsani College of Medicine, University of South Florida, Tampa, FL, United States.
authors.forename: J M
authors.initials: JM
authors.lastname: Redington
authors.affiliation: Byrd Alzheimer's Research Institute, Morsani College of Medicine, University of South Florida, Tampa, FL, United States; Laboratory of Structural Dynamics, Stability and Folding of Proteins, Institute of Cytology, Russian Academy of Sciences, St. Petersburg, Russia. Electronic address: vuversky@health.usf.edu.
authors.forename: V N
authors.initials: VN
authors.lastname: Uversky
mesh_terms: D000818:Animals; D006801:Humans; D064267:Intrinsically Disordered Proteins / Q000737:chemistry* / Q000378:metabolism*; D046911:Macromolecular Substances / Q000378:metabolism; D008958:Models, Molecular; D066329:Protein Aggregates; D011499:Protein Processing, Post-Translational
chemical_list: D064267:Intrinsically Disordered Proteins; D046911:Macromolecular Substances; D066329:Protein Aggregates
keywords: Binding partner; Crowding; Expression level; Intrinsically disordered protein; Mutation; Posttranslational modification; Protein aggregation