Posttranslational Modifications and Clearing of α-Synuclein Aggregates in Yeast
The budding yeast Saccharomyces cerevisiae represents an established model system to study the molecular mechanisms associated to neurodegenerative disorders. A key-feature of Parkinson’s disease is the formation of Lewy bodies, which are cytoplasmic protein inclusions. Misfolded α-synuclein is one...
Main Authors: | Blagovesta Popova, Alexandra Kleinknecht, Gerhard H. Braus |
---|---|
Format: | Article |
Language: | English |
Published: |
MDPI AG
2015-04-01
|
Series: | Biomolecules |
Subjects: | |
Online Access: | http://www.mdpi.com/2218-273X/5/2/617 |
Similar Items
-
Sumoylation Protects Against β-Synuclein Toxicity in Yeast
by: Blagovesta Popova, et al.
Published: (2018-03-01) -
α-Synuclein Decreases the Abundance of Proteasome Subunits and Alters Ubiquitin Conjugates in Yeast
by: Blagovesta Popova, et al.
Published: (2021-08-01) -
Synthetic Proteins and Peptides for the Direct Interrogation of α-Synuclein Posttranslational Modifications
by: Matthew R. Pratt, et al.
Published: (2015-06-01) -
Identification of Two Novel Peptides That Inhibit α-Synuclein Toxicity and Aggregation
by: Blagovesta Popova, et al.
Published: (2021-04-01) -
Mechanisms underlying extensive Ser129-phosphorylation in α-synuclein aggregates
by: Shigeki Arawaka, et al.
Published: (2017-06-01)