Asset Details
Do you wish to reserve the book?
The many faces of α-synuclein: from structure and toxicity to therapeutic target
Hey, we have placed the reservation for you!
By the way, why not check out events that you can attend while you pick your title.
Oops! Something went wrong.
Looks like we were not able to place the reservation. Kindly try again later.
Are you sure you want to remove the book from the shelf?
The many faces of α-synuclein: from structure and toxicity to therapeutic target
Do you wish to request the book?
The many faces of α-synuclein: from structure and toxicity to therapeutic target
Please be aware that the book you have requested cannot be checked out. If you would like to checkout this book, you can reserve another copy
We have requested the book for you!
Your request is successful and it will be processed during the Library working hours. Please check the status of your request in My Requests.
Oops! Something went wrong.
Looks like we were not able to place your request. Kindly try again later.
Journal Article
The many faces of α-synuclein: from structure and toxicity to therapeutic target
2013
Overview
Key Points
Recent studies of the structural and functional roles of α-synuclein show that this protein participates in synaptic vesicle transport.
Increased expression and/or accumulation of α-synuclein owing to genetic duplication, mutations or a failure in clearance may have roles in Parkinson's disease and related disorders.
Different conformers of α-synuclein, including oligomers, protofibrils and fibrils, may contribute to α-synuclein-mediated toxicity.
Recent studies suggest that the propagation and transmission of α-synuclein participate in the pathogenesis of Parkinson's disease.
Reducing α-synuclein expression, aggregation or propagation, or increasing the clearance of this protein all represent viable therapeutic strategies for combating Parkinson's disease and related disorders.
The abnormal accumulation of α-synuclein seems to have a central role in the pathophysiology of Parkinson's disease and related disorders. Masliah and colleagues review current knowledge regarding the conformational, oligomerization and aggregation states of this protein and how they influence α-synuclein function in health and disease.
Disorders characterized by α-synuclein (α-syn) accumulation, Lewy body formation and parkinsonism (and in some cases dementia) are collectively known as Lewy body diseases. The molecular mechanism (or mechanisms) through which α-syn abnormally accumulates and contributes to neurodegeneration in these disorders remains unknown. Here, we provide an overview of current knowledge and prevailing hypotheses regarding the conformational, oligomerization and aggregation states of α-syn and their role in regulating α-syn function in health and disease. Understanding the nature of the various α-syn structures, how they are formed and their relative contributions to α-syn-mediated toxicity may inform future studies aiming to develop therapeutic prevention and intervention.
Publisher
Nature Publishing Group UK,Nature Publishing Group
