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Volumn 59, Issue , 2013, Pages 227-254

From human genetics to drug candidates: An industrial perspective on lrrk2 inhibition as a treatment for parkinson's disease

Author keywords

Drug discovery; Familial PD; Kinase activity; Leucine rich repeat kinase 2; Neurodegenerative disease; Parkinson's disease

Indexed keywords


EID: 85017403624     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1002/9783527677252.ch10     Document Type: Chapter
Times cited : (3)

References (104)
  • 3
    • 33744982893 scopus 로고    scopus 로고
    • Etiology of Parkinson's disease
    • Schapira, A.H. (2006) Etiology of Parkinson's disease. Neurology, 66 10 (Suppl. 4), S10-S13.
    • (2006) Neurology , vol.66 , Issue.4 , pp. S10-S13
    • Schapira, A.H.1
  • 4
    • 77952122496 scopus 로고    scopus 로고
    • LRRK2 and Parkinson disease
    • Dachsel, J.C. and Farrer, M.J. (2010) LRRK2 and Parkinson disease. Archives of Neurology, 67 (5), 542-547.
    • (2010) Archives of Neurology , vol.67 , Issue.5 , pp. 542-547
    • Dachsel, J.C.1    Farrer, M.J.2
  • 14
    • 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., and Alessi, D.R. (2007) LRRK2 phosphorylates moesin at threonine-558: characterization of how Parkinson's disease mutants affect kinase activity. The Biochemical Journal, 405 (2), 307-317.
    • (2007) The Biochemical Journal , vol.405 , Issue.2 , 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
  • 16
    • 77950640166 scopus 로고    scopus 로고
    • Differential effects of divalent manganese and magnesium on the kinase activity of leucine-rich repeat kinase 2 (LRRK2)
    • Lovitt, B., Vanderporten, E.C., Sheng, Z., Zhu, H., Drummond, J., and Liu, Y. (2010) Differential effects of divalent manganese and magnesium on the kinase activity of leucine-rich repeat kinase 2 (LRRK2). Biochemistry, 49 (14), 3092-3100.
    • (2010) Biochemistry , vol.49 , Issue.14 , pp. 3092-3100
    • Lovitt, B.1    Vanderporten, E.C.2    Sheng, Z.3    Zhu, H.4    Drummond, J.5    Liu, Y.6
  • 17
    • 57749185024 scopus 로고    scopus 로고
    • Identification of compounds that inhibit the kinase activity of leucine-rich repeat kinase 2
    • Covy, J.P. and Giasson, B.I. (2009) Identification of compounds that inhibit the kinase activity of leucine-rich repeat kinase 2. Biochemical and Biophysical Research Communications, 378 (3), 473-477.
    • (2009) Biochemical and Biophysical Research Communications , vol.378 , Issue.3 , pp. 473-477
    • Covy, J.P.1    Giasson, B.I.2
  • 18
    • 77953395313 scopus 로고    scopus 로고
    • Leucine-rich repeat kinase 2 mutations and Parkinson's disease: three questions
    • Greggio, E. and Cookson, M.R. (2009) Leucine-rich repeat kinase 2 mutations and Parkinson's disease: three questions. ASN Neuroscience, 1 (1), 13-24.
    • (2009) ASN Neuroscience , vol.1 , Issue.1 , pp. 13-24
    • Greggio, E.1    Cookson, M.R.2
  • 21
    • 84860389765 scopus 로고    scopus 로고
    • Autophosphorylation in the leucine-rich repeat kinase 2 (LRRK2) GTPase domain modifies kinase and GTPbinding activities
    • Webber, P.J., Smith, A.D., Sen, S., Renfrow, M.B., Mobley, J.A., and West, A. B. (2011) Autophosphorylation in the leucine-rich repeat kinase 2 (LRRK2) GTPase domain modifies kinase and GTPbinding activities. Journal of Molecular Biology, 412 (1), 94-110.
    • (2011) Journal of Molecular Biology , vol.412 , Issue.1 , pp. 94-110
    • Webber, P.J.1    Smith, A.D.2    Sen, S.3    Renfrow, M.B.4    Mobley, J.A.5    West, A.B.6
  • 23
    • 72749105819 scopus 로고    scopus 로고
    • Identification of the autophosphorylation sites of LRRK2
    • Kamikawaji, S., Ito, G., and Iwatsubo, T. (2009) Identification of the autophosphorylation sites of LRRK2. Biochemistry, 48 (46), 10963-10975.
    • (2009) Biochemistry , vol.48 , Issue.46 , pp. 10963-10975
    • Kamikawaji, S.1    Ito, G.2    Iwatsubo, T.3
  • 24
    • 77950631558 scopus 로고    scopus 로고
    • Phosphopeptide analysis reveals two discrete clusters of phosphorylation in the N-terminus and the Roc domain of the Parkinson-disease associated protein kinase LRRK2
    • Gloeckner, C.J., Boldt, K., von Zweydorf, F., Helm, S., Wiesent, L., Sarioglu, H., and Ueffing, M. (2010) Phosphopeptide analysis reveals two discrete clusters of phosphorylation in the N-terminus and the Roc domain of the Parkinson-disease associated protein kinase LRRK2. Journal of Proteome Research, 9 (4), 1738-1745.
    • (2010) Journal of Proteome Research , vol.9 , Issue.4 , pp. 1738-1745
    • Gloeckner, C.J.1    Boldt, K.2    von Zweydorf, F.3    Helm, S.4    Wiesent, L.5    Sarioglu, H.6    Ueffing, M.7
  • 25
    • 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., and Chen, S.G. (2007) The Parkinson's disease-associated protein, leucine-rich repeat kinase 2 (LRRK2), is an authentic GTPase that stimulates kinase activity. Experimental Cell Research, 313 (16), 3658-3670.
    • (2007) Experimental Cell Research , vol.313 , Issue.16 , 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
  • 26
    • 34548621385 scopus 로고    scopus 로고
    • Leucinerich 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., and Yue, Z. (2007) Leucinerich repeat kinase 2 (LRRK2)/PARK8 possesses GTPase activity that is altered in familial Parkinson's disease R1441C/G mutants. Journal of Neurochemistry, 103 (1), 238-247.
    • (2007) Journal of Neurochemistry , vol.103 , Issue.1 , pp. 238-247
    • Li, X.1    Tan, Y.C.2    Poulose, S.3    Olanow, C.W.4    Huang, X.Y.5    Yue, Z.6
  • 27
    • 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
    • Ito, G., Okai, T., Fujino, G., Takeda, K., Ichijo, H., Katada, T., and Iwatsubo, T. (2007) GTP binding is essential to the protein kinase activity of LRRK2, a causative gene product for familial Parkinson's disease. Biochemistry, 46 (5), 1380-1388.
    • (2007) Biochemistry , vol.46 , Issue.5 , pp. 1380-1388
    • Ito, G.1    Okai, T.2    Fujino, G.3    Takeda, K.4    Ichijo, H.5    Katada, T.6    Iwatsubo, T.7
  • 30
    • 77749255337 scopus 로고    scopus 로고
    • Kinetic mechanistic studies of wild-type leucinerich repeat kinase 2: characterization of the kinase and GTPase activities
    • Liu, M., Dobson, B., Glicksman, M.A., Yue, Z., and Stein, R.L. (2010) Kinetic mechanistic studies of wild-type leucinerich repeat kinase 2: characterization of the kinase and GTPase activities. Biochemistry,49. (9), 2008-2017.
    • (2010) Biochemistry , vol.49 , Issue.9 , pp. 2008-2017
    • Liu, M.1    Dobson, B.2    Glicksman, M.A.3    Yue, Z.4    Stein, R.L.5
  • 35
    • 59649089328 scopus 로고    scopus 로고
    • The Parkinson disease protein leucine-rich repeat kinase 2 transduces death signals via Fas-associated protein with death domain and caspase-8 in a cellular model of neurodegeneration
    • Ho, C.C., Rideout, H.J., Ribe, E., Troy, C. M., and Dauer, W.T. (2009) The Parkinson disease protein leucine-rich repeat kinase 2 transduces death signals via Fas-associated protein with death domain and caspase-8 in a cellular model of neurodegeneration. The Journal of Neuroscience, 29 (4), 1011-1016.
    • (2009) The Journal of Neuroscience , vol.29 , Issue.4 , pp. 1011-1016
    • Ho, C.C.1    Rideout, H.J.2    Ribe, E.3    Troy, C.M.4    Dauer, W.T.5
  • 36
    • 33751256567 scopus 로고    scopus 로고
    • The familial Parkinsonism gene LRRK2 regulates neurite process morphology
    • MacLeod, D., Dowman, J., Hammond, R., Leete, T., Inoue, K., and Abeliovich, A. (2006) The familial Parkinsonism gene LRRK2 regulates neurite process morphology. Neuron, 52 (4), 587-593.
    • (2006) Neuron , vol.52 , Issue.4 , pp. 587-593
    • MacLeod, D.1    Dowman, J.2    Hammond, R.3    Leete, T.4    Inoue, K.5    Abeliovich, A.6
  • 37
    • 39549117093 scopus 로고    scopus 로고
    • Role of autophagy in G2019S-LRRK2-associated neurite shortening in differentiated SH-SY5Y cells
    • Plowey, E.D., Cherra, S.J., III, Liu, Y.J., and Chu, C.T. (2008) Role of autophagy in G2019S-LRRK2-associated neurite shortening in differentiated SH-SY5Y cells. Journal of Neurochemistry, 105 (3), 1048-1056.
    • (2008) Journal of Neurochemistry , vol.105 , Issue.3 , pp. 1048-1056
    • Plowey, E.D.1    Cherra, S.J.2    III Liu, Y.J.3    Chu, C.T.4
  • 39
    • 84859187983 scopus 로고    scopus 로고
    • GTPase activity and neuronal toxicity of Parkinson's disease-associated LRRK2 is regulated by ArfGAP1
    • Stafa, K., Trancikova, A., Webber, P.J., Glauser, L., West, A.B., and Moore, D.J. (2012) GTPase activity and neuronal toxicity of Parkinson's disease-associated LRRK2 is regulated by ArfGAP1. PLoS Genetics, 8 (2), e1002526.
    • (2012) PLoS Genetics , vol.8 , Issue.2 , pp. e1002526
    • Stafa, K.1    Trancikova, A.2    Webber, P.J.3    Glauser, L.4    West, A.B.5    Moore, D.J.6
  • 43
    • 51949090816 scopus 로고    scopus 로고
    • Phosphorylation of 4E-BP by LRRK2 affects the maintenance of dopaminergic neurons in Drosophila
    • Imai, Y., Gehrke, S., Wang, H.Q., Takahashi, R., Hasegawa, K., Oota, E., and Lu, B. (2008) Phosphorylation of 4E-BP by LRRK2 affects the maintenance of dopaminergic neurons in Drosophila. EMBO Journal, 27 (18), 2432-2443.
    • (2008) EMBO Journal , vol.27 , Issue.18 , pp. 2432-2443
    • Imai, Y.1    Gehrke, S.2    Wang, H.Q.3    Takahashi, R.4    Hasegawa, K.5    Oota, E.6    Lu, B.7
  • 44
    • 81555205691 scopus 로고    scopus 로고
    • Leucine-rich repeat kinase 2 (LRRK2) cellular biology: a review of recent advances in identifying physiological substrates and cellular functions
    • Drolet, R.E., Sanders, J.M., and Kern, J.T. (2011) Leucine-rich repeat kinase 2 (LRRK2) cellular biology: a review of recent advances in identifying physiological substrates and cellular functions. Journal of Neurogenetics, 25 (4), 140-151.
    • (2011) Journal of Neurogenetics , vol.25 , Issue.4 , pp. 140-151
    • Drolet, R.E.1    Sanders, J.M.2    Kern, J.T.3
  • 45
    • 77956655427 scopus 로고    scopus 로고
    • Inhibition of LRRK2 kinase activity leads to dephosphorylation of Ser(910)/Ser(935), disruption of 14-3-3 binding and altered cytoplasmic localization
    • Dzamko, N., Deak, M., Hentati, F., Reith, A.D., Prescott, A.R., Alessi, D.R., and Nichols, R.J. (2010) Inhibition of LRRK2 kinase activity leads to dephosphorylation of Ser(910)/Ser(935), disruption of 14-3-3 binding and altered cytoplasmic localization. The Biochemical Journal, 430 (3), 405-413.
    • (2010) The Biochemical Journal , vol.430 , Issue.3 , pp. 405-413
    • Dzamko, N.1    Deak, M.2    Hentati, F.3    Reith, A.D.4    Prescott, A.R.5    Alessi, D.R.6    Nichols, R.J.7
  • 46
    • 79952302007 scopus 로고    scopus 로고
    • Phosphorylation-dependent 14-3-3 binding to LRRK2 is impaired by common mutations of familial Parkinson's disease
    • Li, X.,Wang, Q.J., Pan, N., Lee, S., Zhao, Y., Chait, B.T., and Yue, Z. (2011) Phosphorylation-dependent 14-3-3 binding to LRRK2 is impaired by common mutations of familial Parkinson's disease. PLoS One, 6 (3), e17153.
    • (2011) PLoS One , vol.6 , Issue.3 , pp. e17153
    • Li X.Wang, Q.J.1    Pan, N.2    Lee, S.3    Zhao, Y.4    Chait, B.T.5    Yue, Z.6
  • 48
    • 26844505808 scopus 로고    scopus 로고
    • Toxin-induced models of Parkinson's disease
    • Bov±e, J., Prou, D., Perier, C., and Przedborski, S. (2005) Toxin-induced models of Parkinson's disease. NeuroRx, 2 (3), 484-494.512. (7), 826-828.
    • (2005) NeuroRx , vol.2 , Issue.3-7
    • Bove, J.1    Prou, D.2    Perier, C.3    Przedborski, S.4
  • 57
    • 66949117423 scopus 로고    scopus 로고
    • The scientific and clinical basis for the treatment of Parkinson disease
    • Olanow, C.W., Stern, M.B., and Sethi, K. (2009) The scientific and clinical basis for the treatment of Parkinson disease. Neurology, 72 (21 Suppl. 4), S1-S136.
    • (2009) Neurology , vol.72 , Issue.21 , pp. S1-S136
    • Olanow, C.W.1    Stern, M.B.2    Sethi, K.3
  • 58
    • 79955560231 scopus 로고    scopus 로고
    • Neuroimaging in Parkinson's disease
    • Stoessl, A.J. (2011) Neuroimaging in Parkinson's disease. Neurotherapeutics, 8 (1), 72-81.
    • (2011) Neurotherapeutics , vol.8 , Issue.1 , pp. 72-81
    • Stoessl, A.J.1
  • 59
    • 68649126827 scopus 로고    scopus 로고
    • Imaging neurodegeneration in Parkinson's disease
    • Pavese, N. and Brooks, D.J. (2009) Imaging neurodegeneration in Parkinson's disease. Biochimica et Biophysica Acta, 1792 (7), 722-729.
    • (2009) Biochimica et Biophysica Acta , vol.1792 , Issue.7 , pp. 722-729
    • Pavese, N.1    Brooks, D.J.2
  • 64
    • 0037432067 scopus 로고    scopus 로고
    • Slowing Parkinson's disease progression: recent dopamine agonist trials
    • Ahlskog, J.E. (2003) Slowing Parkinson's disease progression: recent dopamine agonist trials. Neurology, 60 (3), 381-389.
    • (2003) Neurology , vol.60 , Issue.3 , pp. 381-389
    • Ahlskog, J.E.1
  • 66
    • 8644231592 scopus 로고    scopus 로고
    • Neuroimaging trials of Parkinson's disease progression
    • Seibyl, J., Jennings, D., Tabamo, R., and Marek, K. (2004) Neuroimaging trials of Parkinson's disease progression. Journal of Neurology, 251 (Suppl 7), vii9-vii13.
    • (2004) Journal of Neurology , vol.251 , Issue.7 , pp. 79-713
    • Seibyl, J.1    Jennings, D.2    Tabamo, R.3    Marek, K.4
  • 67
    • 0037012478 scopus 로고    scopus 로고
    • Dopamine transporter brain imaging to assess the effects of pramipexole vs levodopa on Parkinson disease progression
    • Anonymous (2002) Dopamine transporter brain imaging to assess the effects of pramipexole vs levodopa on Parkinson disease progression. JAMA: the journal of the American Medical Association, 287 (13), 1653-1661.
    • (2002) JAMA: the journal of the American Medical Association , vol.287 , Issue.13 , pp. 1653-1661
  • 68
    • 0035225776 scopus 로고    scopus 로고
    • [123I]FP-CIT SPECT is a useful method to monitor the rate of dopaminergic degeneration in early-stage Parkinson's disease
    • Winogrodzka, A., Bergmans, P., Booij, J., van Royen, E.A., Janssen, A.G., and Wolters, E.C. (2001) [123I]FP-CIT SPECT is a useful method to monitor the rate of dopaminergic degeneration in early-stage Parkinson's disease. Journal of Neural Transmission, 108 (8-9), 1011-1019.
    • (2001) Journal of Neural Transmission , vol.108 , Issue.8-9 , pp. 1011-1019
    • Winogrodzka, A.1    Bergmans, P.2    Booij, J.3    van Royen, E.A.4    Janssen, A.G.5    Wolters, E.C.6
  • 70
    • 0027530638 scopus 로고
    • Effects of tocopherol and deprenyl on the progression of disability in early Parkinson's disease
    • Anonymous (1993) Effects of tocopherol and deprenyl on the progression of disability in early Parkinson's disease. The Parkinson Study Group. The New England Journal of Medicine, 328 (3), 176-183.
    • (1993) The Parkinson Study Group. The New England Journal of Medicine , vol.328 , Issue.3 , pp. 176-183
  • 73
    • 0037032835 scopus 로고    scopus 로고
    • The protein kinase complement of the human genome
    • Manning, G., Whyte, D.B., Martinez, R., Hunter, T., and Sudarsanam, S. (2002) The protein kinase complement of the human genome. Science, 298 (5600), 1912-1934.
    • (2002) Science , vol.298 , Issue.5600 , pp. 1912-1934
    • Manning, G.1    Whyte, D.B.2    Martinez, R.3    Hunter, T.4    Sudarsanam, S.5
  • 74
    • 80054979896 scopus 로고    scopus 로고
    • Kinetic, mechanistic, and structural modeling studies of truncated wild-type leucinerich repeat kinase 2 and the G2019S mutant
    • Liu, M., Kang, S., Ray, S., Jackson, J., Zaitsev, A.D., Gerber, S.A., Cuny, G.D., and Glicksman, M.A. (2011) Kinetic, mechanistic, and structural modeling studies of truncated wild-type leucinerich repeat kinase 2 and the G2019S mutant. Biochemistry, 50 (43), 9399-9408.
    • (2011) Biochemistry , vol.50 , Issue.43 , pp. 9399-9408
    • Liu, M.1    Kang, S.2    Ray, S.3    Jackson, J.4    Zaitsev, A.D.5    Gerber, S.A.6    Cuny, G.D.7    Glicksman, M.A.8
  • 75
    • 33750931271 scopus 로고    scopus 로고
    • The Parkinson disease gene LRRK2: evolutionary and structural insights
    • Marin, I. (2006) The Parkinson disease gene LRRK2: evolutionary and structural insights. Molecular Biology and Evolution,23. (12), 2423-2433.
    • (2006) Molecular Biology and Evolution , vol.23 , Issue.12 , pp. 2423-2433
    • Marin, I.1
  • 76
    • 79955567288 scopus 로고    scopus 로고
    • Identification of chemicals to inhibit the kinase activity of leucine-rich repeat kinase 2 (LRRK2), a Parkinson's disease-associated protein
    • Yun, H., Heo, H.Y., Kim, H.H., DooKim, N., and Seol, W. (2011) Identification of chemicals to inhibit the kinase activity of leucine-rich repeat kinase 2 (LRRK2), a Parkinson's disease-associated protein. Bioorganic & Medicinal Chemistry Letters,21. (10), 2953-2957.
    • (2011) Bioorganic & Medicinal Chemistry Letters , vol.21 , Issue.10 , pp. 2953-2957
    • Yun, H.1    Heo, H.Y.2    Kim, H.H.3    DooKim, N.4    Seol, W.5
  • 82
    • 84858791638 scopus 로고    scopus 로고
    • Small molecule kinase inhibitors for LRRK2 and their application to Parkinson's disease models
    • Kramer, T., Lo Monte, F., Goring, S., Okala Amombo, G.M., and Schmidt, B. (2012) Small molecule kinase inhibitors for LRRK2 and their application to Parkinson's disease models. ACS Chemical Neuroscience, 3 (3), 151-160.
    • (2012) ACS Chemical Neuroscience , vol.3 , Issue.3 , pp. 151-160
    • Kramer, T.1    Lo Monte, F.2    Goring, S.3    Okala Amombo, G.M.4    Schmidt, B.5
  • 84
    • 80053152848 scopus 로고    scopus 로고
    • Inhibitors of LRRK2 kinase attenuate neurodegeneration and Parkinson-like phenotypes in Caenorhabditis elegans and Drosophila Parkinson's disease models
    • Liu, Z., Hamamichi, S., Lee, B.D., Yang, D., Ray, A., Caldwell, G.A., Caldwell, K. A., Dawson, T.M., Smith, W.W., and Dawson, V.L. (2011) Inhibitors of LRRK2 kinase attenuate neurodegeneration and Parkinson-like phenotypes in Caenorhabditis elegans and Drosophila Parkinson's disease models. Human Molecular Genetics, 20 (20), 3933-3942.
    • (2011) Human Molecular Genetics , vol.20 , Issue.20 , pp. 3933-3942
    • Liu, Z.1    Hamamichi, S.2    Lee, B.D.3    Yang, D.4    Ray, A.5    Caldwell, G.A.6    Caldwell, K.A.7    Dawson, T.M.8    Smith, W.W.9    Dawson, V.L.10
  • 85
    • 85017383160 scopus 로고    scopus 로고
    • Methods for the identification of LRRK2 interacting molecules
    • US 8,163,511 B2 (Apr. 24, 2012)
    • Gerard, D., Hopf, C., and Reader, V. (2012) Methods for the identification of LRRK2 interacting molecules. US 8,163,511 B2 (Apr. 24, 2012).
    • (2012)
    • Gerard, D.1    Hopf, C.2    Reader, V.3
  • 86
    • 85017406359 scopus 로고    scopus 로고
    • The use of LRRK2 inhibitors for neurodegenerative diseases
    • WO 2009/127642 A2
    • Ramsden, N. (2009) The use of LRRK2 inhibitors for neurodegenerative diseases. WO 2009/127642 A2.
    • (2009)
    • Ramsden, N.1
  • 87
    • 42949150113 scopus 로고    scopus 로고
    • High-throughput kinase profiling as a platform for drug discovery
    • Goldstein, D.M., Gray, N.S., and Zarrinkar, P.P. (2008) High-throughput kinase profiling as a platform for drug discovery. Nature Reviews. Drug Discovery, 7 (5), 391-397.
    • (2008) Nature Reviews. Drug Discovery , vol.7 , Issue.5 , pp. 391-397
    • Goldstein, D.M.1    Gray, N.S.2    Zarrinkar, P.P.3
  • 90
  • 93
    • 83855160771 scopus 로고    scopus 로고
    • Phosphorylation of LRRK2 serines 955 and is disrupted by Parkinson's disease mutations and LRRK2 pharmacological inhibition
    • Doggett, E.A., Zhao, J., Mork, C.N., Hu, D., and Nichols, R.J. (2011) Phosphorylation of LRRK2 serines 955 and is disrupted by Parkinson's disease mutations and LRRK2 pharmacological inhibition. Journal of Neurochemistry,120. (1), 37-45.
    • (2011) Journal of Neurochemistry , vol.120 , Issue.1 , pp. 37-45
    • Doggett, E.A.1    Zhao, J.2    Mork, C.N.3    Hu, D.4    Nichols, R.J.5
  • 98
    • 84858760185 scopus 로고    scopus 로고
    • Pyrazolopyridines as inhibitors of the kinase LRRK2
    • WO 2012/038743 A1
    • Chan, B., Chen, H., Estrada, A., Shore, D., Sweeney, Z., and McIver, E. (2012) Pyrazolopyridines as inhibitors of the kinase LRRK2. WO 2012/038743 A1.
    • (2012)
    • Chan, B.1    Chen, H.2    Estrada, A.3    Shore, D.4    Sweeney, Z.5    McIver, E.6
  • 99
    • 84858760185 scopus 로고    scopus 로고
    • Pyrazolopyridines as inhibitors of the kinase LRRK2
    • WO 2011/141756. A1
    • Chan, B., Estrada, A., Sweeney, Z., and McIver, E. (2011) Pyrazolopyridines as inhibitors of the kinase LRRK2. WO 2011/141756. A1.
    • (2011)
    • Chan, B.1    Estrada, A.2    Sweeney, Z.3    McIver, E.4
  • 104
    • 84856070973 scopus 로고    scopus 로고
    • LRRK2 and human disease: a complicated question or a question of complexes
    • pe2
    • Lewis, P.A. and Manzoni, C. (2012) LRRK2 and human disease: a complicated question or a question of complexes? Science Signaling, 5 (207), pe2.
    • (2012) Science Signaling , vol.5 , Issue.207
    • Lewis, P.A.1    Manzoni, C.2


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