Capturing Differences in the Regulation of LRRK2 Dynamics and Conformational States by Small Molecule Kinase Inhibitors
Author:
Affiliation:
1. Department of Pharmacology, University of California, San Diego, California 92093, United States
2. Department of Chemistry and Biochemistry, University of California, San Diego, California 92093, United States
Funder
Michael J. Fox Foundation for Parkinson's Research
National Institutes of Health
U.S. Department of Health and Human Services
Publisher
American Chemical Society (ACS)
Subject
Molecular Medicine,General Medicine,Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/acschembio.2c00868
Reference50 articles.
1. Mutations in LRRK2 Cause Autosomal-Dominant Parkinsonism with Pleomorphic Pathology
2. From The Cover: Parkinson's disease-associated mutations in leucine-rich repeat kinase 2 augment kinase activity
3. Kinase activity is required for the toxic effects of mutant LRRK2/dardarin
4. LRRK2 in Parkinson's disease: protein domains and functional insights
5. GTPase activity regulates kinase activity and cellular phenotypes of Parkinson's disease-associated LRRK2
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