| dc.creator |
Athanasopoulos, Panagiotis S. |
|
| dc.creator |
Heumann, Rolf |
|
| dc.creator |
Kortholt, Arjan |
|
| dc.date |
2018-07-01T00:00:00Z |
|
| dc.date.accessioned |
2023-01-09T12:02:33Z |
|
| dc.date.available |
2023-01-09T12:02:33Z |
|
| dc.identifier |
4e60dbd1-fd5a-487d-9e82-c126ca2abddd |
|
| dc.identifier |
10.1515/hsz-2017-0332 |
|
| dc.identifier |
https://avesis.sdu.edu.tr/publication/details/4e60dbd1-fd5a-487d-9e82-c126ca2abddd/oai |
|
| dc.identifier.uri |
http://acikerisim.sdu.edu.tr/xmlui/handle/123456789/97833 |
|
| dc.description |
Mutations in human leucine-rich-repeat kinase 2 (LRRK2) have been found to be the most frequent cause of late-onset Parkinson's Disease (PD). LRRK2 is a large protein with two enzymatic domains, a GTPase and a kinase domain. A cluster of (auto)-phosphorylation sites within the N-terminus of LRRK2 have been shown to be crucial for the localization of LRRK2 and is important for PD pathogenesis. In addition, phosphorylation of sites within the G-domain of the protein affect GTPase activity. Here we discuss the role of these (auto)-phosphorylation sites of LRRK2 and their regulation by phosphatases and upstream kinases. |
|
| dc.language |
eng |
|
| dc.rights |
info:eu-repo/semantics/openAccess |
|
| dc.title |
The role of (auto)-phosphorylation in the complex activation mechanism of LRRK2 |
|
| dc.type |
info:eu-repo/semantics/article |
|