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Parkinson disease-associated mutation R1441H in LRRK2 prolongs the "active state" of its GTPase domain.
Liao, Jingling; Wu, Chun-Xiang; Burlak, Christopher; Zhang, Sheng; Sahm, Heather; Wang, Mu; Zhang, Zhong-Yin; Vogel, Kurt W; Federici, Mark; Riddle, Steve M; Nichols, R Jeremy; Liu, Dali; Cookson, Mark R; Stone, Todd A; Hoang, Quyen Q.
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  • Liao J; Department of Biochemistry and Molecular Biology and Stark Neurosciences Institute, Indiana University School of Medicine, Indianapolis, IN 46202.
Proc Natl Acad Sci U S A ; 111(11): 4055-60, 2014 Mar 18.
Article in En | MEDLINE | ID: mdl-24591621
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Full text: 1 Database: MEDLINE Main subject: Parkinson Disease / Protein Conformation / Models, Molecular / Protein Serine-Threonine Kinases / Mutation, Missense / GTP Phosphohydrolases Type of study: Risk_factors_studies Limits: Humans Language: En Year: 2014 Type: Article
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Full text: 1 Database: MEDLINE Main subject: Parkinson Disease / Protein Conformation / Models, Molecular / Protein Serine-Threonine Kinases / Mutation, Missense / GTP Phosphohydrolases Type of study: Risk_factors_studies Limits: Humans Language: En Year: 2014 Type: Article