메뉴 건너뛰기




Volumn 404, Issue 2, 2010, Pages 186-192

Development of a mechanism-based high-throughput screen assay for leucine-rich repeat kinase 2-Discovery of LRRK2 inhibitors

Author keywords

Assay and analysis; LRRK2 kinase

Indexed keywords

PEPTIDES;

EID: 77954457246     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2010.05.033     Document Type: Article
Times cited : (26)

References (23)
  • 11
    • 76149134717 scopus 로고    scopus 로고
    • Enhanced striatal dopamine transmission and motor performance with LRRK2 overexpression in mice is eliminated by familial Parkinson's disease mutation G2019S
    • Li X., Patel J.C., Wang J., Avshalumov M.V., Nicholson C., Buxbaum J.D., Elder G.A., Rice M.E., Yue Z. Enhanced striatal dopamine transmission and motor performance with LRRK2 overexpression in mice is eliminated by familial Parkinson's disease mutation G2019S. J. Neurosci. 2010, 30:1788-1797.
    • (2010) J. Neurosci. , vol.30 , pp. 1788-1797
    • Li, X.1    Patel, J.C.2    Wang, J.3    Avshalumov, M.V.4    Nicholson, C.5    Buxbaum, J.D.6    Elder, G.A.7    Rice, M.E.8    Yue, Z.9
  • 12
    • 34447118788 scopus 로고    scopus 로고
    • LRRK2 phosphorylates moesin at threonine-558: characterization of how Parkinson's disease mutants affect kinase activity
    • Jaleel M., Nichols R.J., Deak M., Campbell D.G., Gillardon F., Knebel A., Alessi D.R. LRRK2 phosphorylates moesin at threonine-558: characterization of how Parkinson's disease mutants affect kinase activity. Biochem. J. 2007, 405:307-317.
    • (2007) Biochem. J. , vol.405 , pp. 307-317
    • Jaleel, M.1    Nichols, R.J.2    Deak, M.3    Campbell, D.G.4    Gillardon, F.5    Knebel, A.6    Alessi, D.R.7
  • 15
    • 34548604567 scopus 로고    scopus 로고
    • The Parkinson's disease-associated protein, leucine-rich repeat kinase 2 (LRRK2), is an authentic GTPase that stimulates kinase activity
    • Guo L., Gandhi P.N., Wang W., Petersen R.B., Wilson-Delfosse A.L., Chen S.G. The Parkinson's disease-associated protein, leucine-rich repeat kinase 2 (LRRK2), is an authentic GTPase that stimulates kinase activity. Exp. Cell Res. 2007, 313:3658-3670.
    • (2007) Exp. Cell Res. , vol.313 , pp. 3658-3670
    • Guo, L.1    Gandhi, P.N.2    Wang, W.3    Petersen, R.B.4    Wilson-Delfosse, A.L.5    Chen, S.G.6
  • 16
    • 33846818834 scopus 로고    scopus 로고
    • GTP binding is essential to the protein kinase activity of LRRK2, a causative gene product for familial Parkinsons's disease
    • Ito G., Okai T., Fujino G., Takeda K., Ichijo H., Katada T., Iwatsubo T. GTP binding is essential to the protein kinase activity of LRRK2, a causative gene product for familial Parkinsons's disease. Biochemistry 2007, 46:1380-1388.
    • (2007) Biochemistry , vol.46 , pp. 1380-1388
    • Ito, G.1    Okai, T.2    Fujino, G.3    Takeda, K.4    Ichijo, H.5    Katada, T.6    Iwatsubo, T.7
  • 20
    • 34548621385 scopus 로고    scopus 로고
    • Leucine- rich repeat kinase 2 (LRRK2)/PARK8 possesses GTPase activity that is altered in familial Parkinson's disease R1441C/G mutants
    • Li X., Tan Y.C., Poulose S., Olanow C.W., Huang X.Y., Yue Z. Leucine- rich repeat kinase 2 (LRRK2)/PARK8 possesses GTPase activity that is altered in familial Parkinson's disease R1441C/G mutants. J. Neurochem. 2007, 103:238-247.
    • (2007) J. Neurochem. , vol.103 , pp. 238-247
    • Li, X.1    Tan, Y.C.2    Poulose, S.3    Olanow, C.W.4    Huang, X.Y.5    Yue, Z.6
  • 21
    • 77749255337 scopus 로고    scopus 로고
    • Kinetic mechanistic studies of WT leucine-rich repeat kinase2: characterization of the kinase and GTPase activities
    • Liu M., Dobson B., Glicksman M.A., Yue Z., Stein R.L. Kinetic mechanistic studies of WT leucine-rich repeat kinase2: characterization of the kinase and GTPase activities. Biochemistry 2010, 49:2008-2017.
    • (2010) Biochemistry , vol.49 , pp. 2008-2017
    • Liu, M.1    Dobson, B.2    Glicksman, M.A.3    Yue, Z.4    Stein, R.L.5
  • 22
    • 33846818834 scopus 로고    scopus 로고
    • GTP binding is essential to the protein kinase activity of LRRK2, a causative gene product for familial Parkinson's disease
    • Manning G., Whyte D.B., Martinex R., Hunter T., Sudarsanam S. GTP binding is essential to the protein kinase activity of LRRK2, a causative gene product for familial Parkinson's disease. Biochemsitry 2002, 46:1380-1388.
    • (2002) Biochemsitry , vol.46 , pp. 1380-1388
    • Manning, G.1    Whyte, D.B.2    Martinex, R.3    Hunter, T.4    Sudarsanam, S.5
  • 23
    • 49449101644 scopus 로고    scopus 로고
    • Kinetic studies of Cdk5/p25 kinase: phosphorylation of tau and complex inhibition by two prototype inhibitors
    • Liu M., Choi S., Cuny G.D., Ding K., Dobson B.C., Glicksman M.A., Auerbach K., Stein R.L. Kinetic studies of Cdk5/p25 kinase: phosphorylation of tau and complex inhibition by two prototype inhibitors. Biochemistry 2008, 47:8367-8377.
    • (2008) Biochemistry , vol.47 , pp. 8367-8377
    • Liu, M.1    Choi, S.2    Cuny, G.D.3    Ding, K.4    Dobson, B.C.5    Glicksman, M.A.6    Auerbach, K.7    Stein, R.L.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.