Role of Metal Ions in Aggregation of Intrinsically Disordered Proteins in Neurodegenerative Diseases
Document Type
Article
Publication Date
2011
Digital Object Identifier (DOI)
https://doi.org/10.1039/c1mt00106j
Abstract
Neurodegenerative diseases constitute a set of pathological conditions originating from the slow, irreversible, and systematic cell loss within the various regions of the brain and/or the spinal cord. Depending on the affected region, the outcomes of the neurodegeneration are very broad and diverse, ranging from the problems with movements to dementia. Some neurodegenerative diseases are associated with protein misfolding and aggregation. Many proteins that misfold in human neurodegenerative diseases are intrinsically disordered; i.e., they lack a stable tertiary and/or secondary structure under physiological conditions in vitro. These intrinsically disordered proteins (IDPs) functionally complement ordered proteins, being typically involved in regulation and signaling. There is accumulating evidence that altered metal homeostasis may be related to the progression of neurodegenerative diseases. This review examines the effects of metal ion binding on the aggregation pathways of IDPs found in neurodegenerative diseases.
Was this content written or created while at USF?
Yes
Citation / Publisher Attribution
Metallomics, v. 3, issue 11, p. 1163-1180
Scholar Commons Citation
Breydo, Leonid and Uversky, Vladimir N., "Role of Metal Ions in Aggregation of Intrinsically Disordered Proteins in Neurodegenerative Diseases" (2011). Molecular Medicine Faculty Publications. 487.
https://digitalcommons.usf.edu/mme_facpub/487
