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Leucine-Rich Repeat Kinase 2 (LRRK2)

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Attention for Chapter 6: Molecular Insights and Functional Implication of LRRK2 Dimerization
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Chapter title
Molecular Insights and Functional Implication of LRRK2 Dimerization
Chapter number 6
Book title
Leucine-Rich Repeat Kinase 2 (LRRK2)
Published in
Advances in neurobiology, March 2017
DOI 10.1007/978-3-319-49969-7_6
Pubmed ID
Book ISBNs
978-3-31-949967-3, 978-3-31-949969-7
Authors

Laura Civiero, Isabella Russo, Luigi Bubacco, Elisa Greggio, Civiero, Laura, Russo, Isabella, Bubacco, Luigi, Greggio, Elisa

Editors

Hardy J. Rideout

Abstract

The Parkinson's disease protein leucine-rich repeat kinase 2 (LRRK2) is a multidomain protein with an enzymatic core comprising serine-threonine kinase and GTPase activities and a number of protein-protein interaction domains. While the complex domain architecture of LRRK2 has hampered its structural investigation, there is convincing evidence that LRRK2 can form dimers in solution and in the cell and that the GTPase/ROC domain plays a central role in this process. This chapter focuses on recent studies addressing the molecular nature, the functional significance, and the pathological implication of LRRK2 dimerization.

Mendeley readers

Mendeley readers

The data shown below were compiled from readership statistics for 23 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Unknown 23 100%

Demographic breakdown

Readers by professional status Count As %
Researcher 5 22%
Student > Ph. D. Student 4 17%
Student > Doctoral Student 3 13%
Student > Bachelor 3 13%
Professor > Associate Professor 2 9%
Other 1 4%
Unknown 5 22%
Readers by discipline Count As %
Neuroscience 6 26%
Biochemistry, Genetics and Molecular Biology 4 17%
Agricultural and Biological Sciences 3 13%
Medicine and Dentistry 1 4%
Pharmacology, Toxicology and Pharmaceutical Science 1 4%
Other 0 0%
Unknown 8 35%