A sticky situation: Aberrant protein–protein interactions in Parkinson’s disease

The aberrant aggregation of normally soluble proteins into amyloid fibrils is the pathological hallmark of several neurodegenerative disorders, including Alzheimer’s and Parkinson’s diseases. Understanding this process will be key to developing both diagnostic and therapeutic approaches for neurodeg...

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Bibliographic Details
Published inSeminars in cell & developmental biology Vol. 99; pp. 65 - 77
Main Authors Brown, James, Horrocks, Mathew H.
Format Journal Article
LanguageEnglish
Published England Elsevier Ltd 01.03.2020
Subjects
Alpha synuclein
alpha-Synuclein - metabolism
Dementia
Humans
Lewy bodies
Parkinson Disease - metabolism
Parkinson Disease - pathology
Parkinson’s
Protein aggregation
Protein Aggregation, Pathological - metabolism
Protein Binding
Protein aggregation
Alpha synuclein
Dementia
Parkinson’s
Lewy bodies
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Summary:The aberrant aggregation of normally soluble proteins into amyloid fibrils is the pathological hallmark of several neurodegenerative disorders, including Alzheimer’s and Parkinson’s diseases. Understanding this process will be key to developing both diagnostic and therapeutic approaches for neurodegenerative diseases. Recent advances in biophysical techniques, coupled with kinetic analyses have enabled a thorough description of the key molecular steps involved in protein aggregation. In this review, we discuss these advances and how they have been applied to study the ability of one such protein, α-Synuclein, to form neurotoxic oligomers.
ISSN:1084-9521
1096-3634
DOI:10.1016/j.semcdb.2018.05.006