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Volumn 7, Issue JUNE, 2014, Pages

Parkinson's disease-implicated kinases in the brain; insights into disease pathogenesis

Author keywords

Brain; GAK; JNK; Kinase; LRRK2; MAPK; PINK1; PLK

Indexed keywords

ALPHA SYNUCLEIN; AUXILIN; CASEIN KINASE I; CASEIN KINASE II; CYCLIN DEPENDENT KINASE 5; EPIDERMAL GROWTH FACTOR RECEPTOR; G PROTEIN COUPLED RECEPTOR KINASE; G PROTEIN COUPLED RECEPTOR KINASE 2; G PROTEIN COUPLED RECEPTOR KINASE 3; G PROTEIN COUPLED RECEPTOR KINASE 4; GLIAL CELL LINE DERIVED NEUROTROPHIC FACTOR; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE KINASE; LEUCINE RICH REPEAT KINASE 2; MAMMALIAN TARGET OF RAPAMYCIN; MAMMALIAN TARGET OF RAPAMYCIN COMPLEX 1; MAMMALIAN TARGET OF RAPAMYCIN COMPLEX 2; MESSENGER RNA; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE P38; PHOSPHATIDYLINOSITOL 3 KINASE; PHOSPHATIDYLINOSITOL 3, 4, 5 TRISPHOSPHATE 3 PHOSPHATASE; PHOSPHOINOSITIDE DEPENDENT PROTEIN KINASE 1; PHOSPHOTRANSFERASE; POLO LIKE KINASE 1; POLO LIKE KINASE 2; POLO LIKE KINASE 3; PROTEIN SERINE THREONINE KINASE; RHODOPSIN KINASE; STRESS ACTIVATED PROTEIN KINASE; UNCLASSIFIED DRUG;

EID: 84928499061     PISSN: 16625099     EISSN: None     Source Type: Journal    
DOI: 10.3389/fnmol.2014.00057     Document Type: Article
Times cited : (63)

References (184)
  • 1
    • 33644543761 scopus 로고    scopus 로고
    • Expanding insights of mitochondrial dysfunction in Parkinson's disease
    • doi: 10.1038/nrn1868
    • Abou-Sleiman, P. M., Muqit, M. M., and Wood, N. W. (2006). Expanding insights of mitochondrial dysfunction in Parkinson's disease. Nat. Rev. Neurosci. 7,207-219. doi: 10.1038/nrn1868
    • (2006) Nat. Rev. Neurosci , vol.7 , pp. 207-219
    • Abou-Sleiman, P.M.1    Muqit, M.M.2    Wood, N.W.3
  • 2
    • 42549123597 scopus 로고    scopus 로고
    • LRRK2 is a component of granular alpha-synuclein pathology in the brainstem of Parkinson's disease
    • doi: 10.1111/j.1365-2990.2007.00888.x
    • Alegre-Abarrategui, J., Ansorge, O., Esiri, M., and Wade-Martins, R. (2008). LRRK2 is a component of granular alpha-synuclein pathology in the brainstem of Parkinson's disease. Neuropathol. Appl. Neurobiol. 34, 272-283. doi: 10.1111/j.1365-2990.2007.00888.x
    • (2008) Neuropathol. Appl. Neurobiol , vol.34 , pp. 272-283
    • Alegre-Abarrategui, J.1    Ansorge, O.2    Esiri, M.3    Wade-Martins, R.4
  • 3
    • 78149469728 scopus 로고    scopus 로고
    • Chaperone-mediated autophagy markers in Parkinson disease brains
    • doi: 10.1001/archneurol.2010.198
    • Alvarez-Erviti, L., Rodriguez-Oroz, M. C., Cooper, J. M., Caballero, C., Ferrer, I., Obeso, J. A., et al. (2010). Chaperone-mediated autophagy markers in Parkinson disease brains. Arch. Neurol. 67, 1464-1472. doi: 10.1001/archneurol.2010.198
    • (2010) Arch. Neurol , vol.67 , pp. 1464-1472
    • Alvarez-Erviti, L.1    Rodriguez-Oroz, M.C.2    Cooper, J.M.3    Caballero, C.4    Ferrer, I.5    Obeso, J.A.6
  • 4
    • 33749570292 scopus 로고    scopus 로고
    • Phosphorylation of Ser-129 is the dominant pathologicalmod- ification of alpha-synuclein in familial and sporadic Lewy body disease
    • doi: 10.1074/jbc.M600933200
    • Anderson, J. P., Walker, D. E., Goldstein, J. M., De Laat, R., Banducci, K., Caccavello, R. J., et al. (2006). Phosphorylation of Ser-129 is the dominant pathologicalmod- ification of alpha-synuclein in familial and sporadic Lewy body disease. J. Biol. Chem. 281, 29739-29752. doi: 10.1074/jbc.M600933200
    • (2006) J. Biol. Chem , vol.281 , pp. 29739-29752
    • Anderson, J.P.1    Walker, D.E.2    Goldstein, J.M.3    de Laat, R.4    Banducci, K.5    Caccavello, R.J.6
  • 5
    • 33748483511 scopus 로고    scopus 로고
    • The role of G-protein-coupled receptor kinase 5 in pathogenesis of sporadic Parkinson's disease
    • doi: 10.1523/JNEUROSCI.0341- 06.2006
    • Arawaka, S., Wada, M., Goto, S., Karube, H., Sakamoto, M., Ren, C. H., et al. (2006). The role of G-protein-coupled receptor kinase 5 in pathogenesis of sporadic Parkinson's disease. J. Neurosci. 26, 9227-9238. doi: 10.1523/JNEUROSCI.0341- 06.2006
    • (2006) J. Neurosci , vol.26 , pp. 9227-9238
    • Arawaka, S.1    Wada, M.2    Goto, S.3    Karube, H.4    Sakamoto, M.5    Ren, C.H.6
  • 6
    • 84874771458 scopus 로고    scopus 로고
    • Ghrelin is neuroprotective in Parkinson's disease: Molecular mechanisms of metabolic neuroprotection
    • doi: 10.1177/2042018813479645
    • Bayliss, J. A., and Andrews, Z. B. (2013). Ghrelin is neuroprotective in Parkinson's disease: molecular mechanisms of metabolic neuroprotection. Ther. Adv. Endocrinol. Metab. 4, 25-36. doi: 10.1177/2042018813479645
    • (2013) Ther. Adv. Endocrinol. Metab , vol.4 , pp. 25-36
    • Bayliss, J.A.1    Andrews, Z.B.2
  • 7
    • 84894322830 scopus 로고    scopus 로고
    • Unbiased screen for interactors ofleucine-rich repeat kinase 2 supports a common pathway for sporadic and familial Parkinson disease
    • doi: 10.1073/pnas.1318306111
    • Beilina, A., Rudenko, I. N., Kaganovich, A., Civiero, L., Chau, H., Kalia, S. K., et al. (2014). Unbiased screen for interactors ofleucine-rich repeat kinase 2 supports a common pathway for sporadic and familial Parkinson disease. Proc. Natl. Acad. Sci. U.S.A. 111,2626-2631. doi: 10.1073/pnas.1318306111
    • (2014) Proc. Natl. Acad. Sci. U.S.A , vol.111 , pp. 2626-2631
    • Beilina, A.1    Rudenko, I.N.2    Kaganovich, A.3    Civiero, L.4    Chau, H.5    Kalia, S.K.6
  • 8
    • 84887510168 scopus 로고    scopus 로고
    • In vivo modulation of polo-like kinases supports a key role for PLK2 in Ser129 alpha-synuclein phosphorylation in mouse brain
    • doi: 10.1016/j.neuroscience.2013.09.061
    • Bergeron, M., Motter, R., Tanaka, P., Fauss, D., Babcock, M., Chiou, S.S., et al. (2014). In vivo modulation of polo-like kinases supports a key role for PLK2 in Ser129 alpha-synuclein phosphorylation in mouse brain. Neuroscience 256, 72-82. doi: 10.1016/j.neuroscience.2013.09.061
    • (2014) Neuroscience , vol.256 , pp. 72-82
    • Bergeron, M.1    Motter, R.2    Tanaka, P.3    Fauss, D.4    Babcock, M.5    Chiou, S.S.6
  • 9
    • 41649083587 scopus 로고    scopus 로고
    • Dynamic and redundant regulation of LRRK2 and LRRK1 expression
    • doi: 10.1186/1471-2202-8-102
    • Biskup, S., Moore, D. J., Rea, A., Lorenz-Deperieux, B., Coombes, C. E., Dawson, V. L., et al. (2007). Dynamic and redundant regulation of LRRK2 and LRRK1 expression. BMCNeurosci. 8:102. doi: 10.1186/1471-2202-8-102
    • (2007) BMCNeurosci , vol.8 , pp. 102
    • Biskup, S.1    Moore, D.J.2    Rea, A.3    Lorenz-Deperieux, B.4    Coombes, C.E.5    Dawson, V.L.6
  • 10
    • 36448932411 scopus 로고    scopus 로고
    • Expression of PINK1 mRNA in human and rodent brain and in Parkinson's disease
    • doi: 10.1016/j.brainres.2007.09.056
    • Blackinton, J. G., Anvret, A., Beilina, A., Olson, L., Cookson, M. R., and Galter, D. (2007). Expression of PINK1 mRNA in human and rodent brain and in Parkinson's disease. Brain Res. 1184, 10-16. doi: 10.1016/j.brainres.2007.09.056
    • (2007) Brain Res , vol.1184 , pp. 10-16
    • Blackinton, J.G.1    Anvret, A.2    Beilina, A.3    Olson, L.4    Cookson, M.R.5    Galter, D.6
  • 11
    • 84876137430 scopus 로고    scopus 로고
    • Design and synthesis of highly selective, orally active Polo-like kinase-2 (Plk-2) inhibitors
    • doi: 10.1016/j.bmcl.2013.02.065
    • Bowers, S., Truong, A. P., Ye, M., Aubele, D. L., Sealy, J. M., Neitz, R. J., et al. (2013). Design and synthesis of highly selective, orally active Polo-like kinase-2 (Plk-2) inhibitors. Bioorg. Med. Chem. Lett. 23, 2743-2749. doi: 10.1016/j.bmcl.2013.02.065
    • (2013) Bioorg. Med. Chem. Lett , vol.23 , pp. 2743-2749
    • Bowers, S.1    Truong, A.P.2    Ye, M.3    Aubele, D.L.4    Sealy, J.M.5    Neitz, R.J.6
  • 12
    • 0037333666 scopus 로고    scopus 로고
    • Staging of brain pathology related to sporadic Parkinson's disease
    • doi: 10.1016/S0197-4580(02)00065-9
    • Braak, H., Del Tredici, K., Rub, U., De Vos, R. A., Jansen Steur, E. N., and Braak, E. (2003). Staging of brain pathology related to sporadic Parkinson's disease. Neurobiol. Aging 24,197-211. doi: 10.1016/S0197-4580(02)00065-9
    • (2003) Neurobiol. Aging , vol.24 , pp. 197-211
    • Braak, H.1    Del Tredici, K.2    Rub, U.3    de Vos, R.A.4    Jansen, S.E.N.5    Braak, E.6
  • 13
    • 0028828550 scopus 로고
    • Cortical and brainstem-type Lewy bodies are immunoreactive for the cyclin-dependent kinase 5
    • Brion, J. P., and Couck, A. M. (1995). Cortical and brainstem-type Lewy bodies are immunoreactive for the cyclin-dependent kinase 5. Am. J. Pathol. 147,1465-1476.
    • (1995) Am. J. Pathol , vol.147 , pp. 1465-1476
    • Brion, J.P.1    Couck, A.M.2
  • 14
    • 38949138075 scopus 로고    scopus 로고
    • Arrestins and two receptor kinases are upregulated in Parkinson's disease with dementia
    • doi: 10.1016/j.neurobiolaging.2006.10.012
    • Bychkov, E. R., Gurevich, V. V., Joyce, J. N., Benovic, J. L., and Gurevich, E. V. (2008). Arrestins and two receptor kinases are upregulated in Parkinson's disease with dementia. Neurobiol. Aging 29, 379-396. doi: 10.1016/j.neurobiolaging.2006.10.012
    • (2008) Neurobiol. Aging , vol.29 , pp. 379-396
    • Bychkov, E.R.1    Gurevich, V.V.2    Joyce, J.N.3    Benovic, J.L.4    Gurevich, E.V.5
  • 15
    • 0000015266 scopus 로고
    • The occurrence, distribution and physiological role of catecholamines in the nervous system
    • Carlsson, A. (1959). The occurrence, distribution and physiological role of catecholamines in the nervous system. Pharmacol. Rev. 11, 490-493.
    • (1959) Pharmacol. Rev , vol.11 , pp. 490-493
    • Carlsson, A.1
  • 16
    • 84891600042 scopus 로고    scopus 로고
    • PPAR-gamma: Therapeutic prospects in Parkinson's disease
    • doi: 10.2174/1389450111314070004
    • Carta, A. R. (2013). PPAR-gamma: therapeutic prospects in Parkinson's disease. Curr. DrugTargets 14, 743-751. doi: 10.2174/1389450111314070004
    • (2013) Curr. DrugTargets , vol.14 , pp. 743-751
    • Carta, A.R.1
  • 17
    • 84868089556 scopus 로고    scopus 로고
    • Tauroursodeoxycholic acid prevents MPTP- induced dopaminergic cell death in a mouse model of Parkinson's disease
    • doi: 10.1007/s12035-012-8295-4
    • Castro-Caldas, M., Carvalho, A. N., Rodrigues, E., Henderson, C. J., Wolf, C. R., Rodrigues, C. M., et al. (2012). Tauroursodeoxycholic acid prevents MPTP- induced dopaminergic cell death in a mouse model of Parkinson's disease. Mol. Neurobiol. 46, 475-486. doi: 10.1007/s12035-012-8295-4
    • (2012) Mol. Neurobiol , vol.46 , pp. 475-486
    • Castro-Caldas, M.1    Carvalho, A.N.2    Rodrigues, E.3    Henderson, C.J.4    Wolf, C.R.5    Rodrigues, C.M.6
  • 18
    • 84872356254 scopus 로고    scopus 로고
    • Blocking c-Jun N-terminal kinase (JNK) translocation to the mitochondria prevents 6-hydroxydopamine- induced toxicity in vitro and in vivo
    • doi: 10.1074/jbc.M112.421354
    • Chambers, J. W., Howard, S., and Lograsso, P.V. (2013). Blocking c-Jun N-terminal kinase (JNK) translocation to the mitochondria prevents 6-hydroxydopamine- induced toxicity in vitro and in vivo. J. Biol. Chem. 288, 1079-1087. doi: 10.1074/jbc.M112.421354
    • (2013) J. Biol. Chem , vol.288 , pp. 1079-1087
    • Chambers, J.W.1    Howard, S.2    Lograsso, P.V.3
  • 19
    • 79955111737 scopus 로고    scopus 로고
    • Small molecule c-jun-N-terminal kinase (JNK) inhibitors protect dopaminergic neurons in a model of Parkinson's disease
    • doi: 10.1021/cn100109k
    • Chambers, J.W., Pachori, A., Howard, S., Ganno, M., Hansen, D. Jr., Kamenecka, T., et al. (2011). Small molecule c-jun-N-terminal kinase (JNK) inhibitors protect dopaminergic neurons in a model of Parkinson's disease. ACS Chem. Neurosci. 2, 198-206. doi: 10.1021/cn100109k
    • (2011) ACS. Chem. Neurosci , vol.2 , pp. 198-206
    • Chambers, J.W.1    Pachori, A.2    Howard, S.3    Ganno, M.4    Hansen Jr., D.5    Kamenecka, T.6
  • 20
    • 17844406856 scopus 로고    scopus 로고
    • Alpha-synuclein phosphorylation controls neurotoxicity and inclusion formation in a Drosophila model of Parkinson disease
    • doi: 10.1038/nn1443
    • Chen, L., and Feany, M. B. (2005). Alpha-synuclein phosphorylation controls neurotoxicity and inclusion formation in a Drosophila model of Parkinson disease. Nat. Neurosci. 8, 657-663. doi: 10.1038/nn1443
    • (2005) Nat. Neurosci , vol.8 , pp. 657-663
    • Chen, L.1    Feany, M.B.2
  • 21
    • 79952101339 scopus 로고    scopus 로고
    • Casein kinase 1:Complexityin thefamily
    • doi: 10.1016/j.biocel.2010.12.004
    • Cheong, J. K., and Virshup, D. M. (2011). Casein kinase 1:complexityin thefamily. Int. J. Biochem. Cell Biol. 43, 465-469. doi: 10.1016/j.biocel.2010.12.004
    • (2011) Int. J. Biochem. Cell Biol , vol.43 , pp. 465-469
    • Cheong, J.K.1    Virshup, D.M.2
  • 22
    • 84872394361 scopus 로고    scopus 로고
    • MicroRNA-205 regulates the expression of Parkinson's disease-related leucine- rich repeat kinase 2 protein
    • doi: 10.1093/hmg/ dds470
    • Cho, H. J., Liu, G., Jin, S. M., Parisiadou, L., Xie, C., Yu, J., et al. (2013). MicroRNA-205 regulates the expression of Parkinson's disease-related leucine- rich repeat kinase 2 protein. Hum. Mol. Genet. 22, 608-620. doi: 10.1093/hmg/ dds470
    • (2013) Hum. Mol. Genet , vol.22 , pp. 608-620
    • Cho, H.J.1    Liu, G.2    Jin, S.M.3    Parisiadou, L.4    Xie, C.5    Yu, J.6
  • 23
    • 84892670789 scopus 로고    scopus 로고
    • Celas- trol from 'Thunder God Vine' protects SH-SY5Y cells through the preservation of mitochondrial function and inhibition of p38 MAPK in a rotenone model of Parkinson's disease
    • doi: 10.1007/s11064-013-1193-y
    • Choi, B. S., Kim, H., Lee, H. J., Sapkota, K., Park, S. E., Kim, S., et al. (2014). Celas- trol from 'Thunder God Vine' protects SH-SY5Y cells through the preservation of mitochondrial function and inhibition of p38 MAPK in a rotenone model of Parkinson's disease. Neurochem. Res. 39, 84-96. doi: 10.1007/s11064-013-1193-y
    • (2014) Neurochem. Res , vol.39 , pp. 84-96
    • Choi, B.S.1    Kim, H.2    Lee, H.J.3    Sapkota, K.4    Park, S.E.5    Kim, S.6
  • 24
    • 0033168508 scopus 로고    scopus 로고
    • Two distinct mechanisms are involved in 6-hydroxydopamine- and MPP+- induced dopaminergic neuronal cell death: Role of caspases, ROS, and JNK
    • doi: 10.1002/(SICI)1097-4547(19990701)57:1<86::AID- JNR9>3.0.CO;2-E
    • Choi, W. S., Yoon, S. Y., Oh, T. H., Choi, E. J., O'malley, K. L., and Oh, Y. J. (1999). Two distinct mechanisms are involved in 6-hydroxydopamine- and MPP+- induced dopaminergic neuronal cell death: role of caspases, ROS, and JNK. J.Neurosci. Res. 57, 86-94. doi: 10.1002/(SICI)1097-4547(19990701)57:1<86::AID- JNR9>3.0.CO;2-E
    • (1999) J.Neurosci. Res , vol.57 , pp. 86-94
    • Choi, W.S.1    Yoon, S.Y.2    Oh, T.H.3    Choi, E.J.4    O'Malley, K.L.5    Oh, Y.J.6
  • 25
    • 2942517676 scopus 로고    scopus 로고
    • Oxidative neuronal injury. The darkside ofERK1/2
    • doi: 10.1111/j.1432-1033.2004.04132.x
    • Chu, C. T., Levinthal, D. J., Kulich, S. M., Chalovich, E. M., and Defranco, D. B. (2004). Oxidative neuronal injury. The darkside ofERK1/2. Eur. J. Biochem. 271, 2060-2066. doi: 10.1111/j.1432-1033.2004.04132.x
    • (2004) Eur. J. Biochem , vol.271 , pp. 2060-2066
    • Chu, C.T.1    Levinthal, D.J.2    Kulich, S.M.3    Chalovich, E.M.4    Defranco, D.B.5
  • 26
    • 68149123529 scopus 로고    scopus 로고
    • Alterations in lysosomal and proteasomal markers in Parkinson's disease: Relationship to alpha-synuclein inclusions
    • doi: 10.1016/j.nbd.2009.05.023
    • Chu, Y., Dodiya, H., Aebischer, P., Olanow, C. W., and Kordower, J. H. (2009). Alterations in lysosomal and proteasomal markers in Parkinson's disease: relationship to alpha-synuclein inclusions. Neurobiol. Dis. 35, 385-398. doi: 10.1016/j.nbd.2009.05.023
    • (2009) Neurobiol. Dis , vol.35 , pp. 385-398
    • Chu, Y.1    Dodiya, H.2    Aebischer, P.3    Olanow, C.W.4    Kordower, J.H.5
  • 27
    • 77949504405 scopus 로고    scopus 로고
    • Selective molecular alterations in the autophagy pathway in patients with Lewy body disease and in models of alpha-synucleinopathy
    • doi: 10.1371/journal.pone.0009313
    • Crews, L., Spencer, B., Desplats, P., Patrick, C., Paulino, A., Rockenstein, E., et al. (2010). Selective molecular alterations in the autophagy pathway in patients with Lewy body disease and in models of alpha-synucleinopathy. PLoS ONE 5:e9313. doi: 10.1371/journal.pone.0009313
    • (2010) PLoS ONE , vol.5
    • Crews, L.1    Spencer, B.2    Desplats, P.3    Patrick, C.4    Paulino, A.5    Rockenstein, E.6
  • 28
    • 77950564697 scopus 로고    scopus 로고
    • STK39 polymorphisms and blood pressure: An association study in British Caucasians and assessment of cis-acting influences on gene expression
    • doi: 10.1186/1471-2350-10-135
    • Cunnington, M. S., Kay, C., Avery, P. J., Mayosi, B. M., Koref, M. S., and Keavney, B. (2009). STK39 polymorphisms and blood pressure: an association study in British Caucasians and assessment of cis-acting influences on gene expression. BMC Med. Genet. 10:135. doi: 10.1186/1471-2350-10-135
    • (2009) BMC Med. Genet , vol.10 , pp. 135
    • Cunnington, M.S.1    Kay, C.2    Avery, P.J.3    Mayosi, B.M.4    Koref, M.S.5    Keavney, B.6
  • 29
    • 84895928813 scopus 로고    scopus 로고
    • Beyond the mitochondrion: Cytosolic PINK1 remodels dendrites through protein kinase
    • doi: 10.1111/jnc.12494
    • Dagda, R. K., Pien, I., Wang, R., Zhu, J., Wang, K. Z., Callio, J., et al. (2014). Beyond the mitochondrion: cytosolic PINK1 remodels dendrites through protein kinase J. Neurochem. 128, 864-877. doi: 10.1111/jnc.12494
    • (2014) J. Neurochem , vol.128 , pp. 864-877
    • Dagda, R.K.1    Pien, I.2    Wang, R.3    Zhu, J.4    Wang, K.Z.5    Callio, J.6
  • 30
    • 84879024830 scopus 로고    scopus 로고
    • Comprehensive characterization and optimization of anti-LRRK2 (leucine-rich repeat kinase 2) monoclonal antibodies
    • doi: 10.1042/BJ20121742
    • Davies, P., Hinkle, K. M., Sukar, N. N., Sepulveda, B., Mesias, R., Serrano, G., et al. (2013). Comprehensive characterization and optimization of anti-LRRK2 (leucine-rich repeat kinase 2) monoclonal antibodies. Biochem. J. 453, 101-113. doi: 10.1042/BJ20121742
    • (2013) Biochem. J , vol.453 , pp. 101-113
    • Davies, P.1    Hinkle, K.M.2    Sukar, N.N.3    Sepulveda, B.4    Mesias, R.5    Serrano, G.6
  • 31
    • 79952263859 scopus 로고    scopus 로고
    • Plk5, a polo box domain-only protein with specific roles in neuron differentiationandglioblastomasuppression
    • doi: 10.1128/MCB.00607-10
    • de Carcer, G., Escobar, B., Higuero, A. M., Garcia, L., Anson, A., Perez, G., et al. (2011a). Plk5, a polo box domain-only protein with specific roles in neuron differentiationandglioblastomasuppression. Mol. Cell. Biol. 31,1225-1239. doi: 10.1128/MCB.00607-10
    • (2011) Mol. Cell. Biol , vol.31 , pp. 1225-1239
    • de Carcer, G.1    Escobar, B.2    Higuero, A.M.3    Garcia, L.4    Anson, A.5    Perez, G.6
  • 32
    • 79960446938 scopus 로고    scopus 로고
    • From Plk1 to Plk5: Functional evolution of polo-like kinases
    • doi: 10.4161/cc.10.14.16494
    • de Carcer, G., Manning, G., and Malumbres, M. (2011b). From Plk1 to Plk5: functional evolution of polo-like kinases. Cell Cycle 10, 2255-2262. doi: 10.4161/cc.10.14.16494
    • (2011) Cell Cycle , vol.10 , pp. 2255-2262
    • de Carcer, G.1    Manning, G.2    Malumbres, M.3
  • 33
    • 77956855813 scopus 로고    scopus 로고
    • Pathogenic lysosomal depletion in Parkinson's disease
    • doi: 10.1523/JNEUROSCI.1920-10.2010
    • Dehay, B., Bove, J., Rodriguez-Muela, N., Perier, C., Recasens, A., Boya, P., et al. (2010). Pathogenic lysosomal depletion in Parkinson's disease. J. Neurosci. 30, 12535-12544. doi: 10.1523/JNEUROSCI.1920-10.2010
    • (2010) J. Neurosci , vol.30 , pp. 12535-12544
    • Dehay, B.1    Bove, J.2    Rodriguez-Muela, N.3    Perier, C.4    Recasens, A.5    Boya, P.6
  • 34
    • 77956767794 scopus 로고    scopus 로고
    • Kinase regulation of Na+-K+-2Cl- cotransport in primary afferent neurons
    • doi: 10.1113/jphysiol.2010.190769
    • Delpire, E., and Austin, T. M. (2010). Kinase regulation of Na+-K+-2Cl- cotransport in primary afferent neurons. J. Physiol. 588, 3365-3373. doi: 10.1113/jphysiol.2010.190769
    • (2010) J. Physiol , vol.588 , pp. 3365-3373
    • Delpire, E.1    Austin, T.M.2
  • 35
    • 84869830250 scopus 로고    scopus 로고
    • Leucine-rich repeat kinase 2 inhibitors: A patent review (2006-2011)
    • doi: 10.1517/13543776.2012.729041
    • Deng, X., Choi, H. G., Buhrlage, S. J., and Gray, N. S. (2012). Leucine-rich repeat kinase 2 inhibitors: a patent review (2006-2011). Expert Opin. Ther. Pat. 22, 1415-1426. doi: 10.1517/13543776.2012.729041
    • (2012) Expert Opin. Ther. Pat , vol.22 , pp. 1415-1426
    • Deng, X.1    Choi, H.G.2    Buhrlage, S.J.3    Gray, N.S.4
  • 36
    • 84890263516 scopus 로고    scopus 로고
    • The protective role of AMP-activated protein kinase in alpha-synuclein neurotoxicity in vitro
    • doi: 10.1016/j.nbd.2013.11.002
    • Dulovic, M., Jovanovic, M., Xilouri, M., Stefanis, L., Harhaji-Trajkovic, L., Kravic-Stevovic, T., et al. (2014). The protective role of AMP-activated protein kinase in alpha-synuclein neurotoxicity in vitro. Neurobiol. Dis. 63, 1-11. doi: 10.1016/j.nbd.2013.11.002
    • (2014) Neurobiol. Dis , vol.63 , pp. 1-11
    • Dulovic, M.1    Jovanovic, M.2    Xilouri, M.3    Stefanis, L.4    Harhaji-Trajkovic, L.5    Kravic-Stevovic, T.6
  • 37
    • 79953088908 scopus 로고    scopus 로고
    • Cyclin-G-associated kinase modifies alpha-synuclein expression levels and toxicity in Parkinson's disease: Results from the GenePD Study
    • doi: 10.1093/hmg/ddr026
    • Dumitriu, A., Pacheco, C. D., Wilk, J. B., Strathearn, K. E., Latourelle, J. C., Goldwurm, S., et al. (2011). Cyclin-G-associated kinase modifies alpha-synuclein expression levels and toxicity in Parkinson's disease: results from the GenePD Study. Hum. Mol. Genet. 20, 1478-1487. doi: 10.1093/hmg/ddr026
    • (2011) Hum. Mol. Genet , vol.20 , pp. 1478-1487
    • Dumitriu, A.1    Pacheco, C.D.2    Wilk, J.B.3    Strathearn, K.E.4    Latourelle, J.C.5    Goldwurm, S.6
  • 38
    • 77956655427 scopus 로고    scopus 로고
    • Inhibition of LRRK2 kinase activity leads to dephosphorylation ofSer(910)/Ser(935), disruption of14-3-3 binding and altered cytoplasmic localization
    • doi: 10.1042/BJ20100784
    • Dzamko, N., Deak, M., Hentati, F., Reith, A. D., Prescott, A. R., Alessi, D. R., et al. (2010). Inhibition of LRRK2 kinase activity leads to dephosphorylation ofSer(910)/Ser(935), disruption of14-3-3 binding and altered cytoplasmic localization. Biochem. J. 430, 405-413. doi: 10.1042/BJ20100784
    • (2010) Biochem. J , vol.430 , pp. 405-413
    • Dzamko, N.1    Deak, M.2    Hentati, F.3    Reith, A.D.4    Prescott, A.R.5    Alessi, D.R.6
  • 39
    • 84877302161 scopus 로고    scopus 로고
    • Unlocking the secrets of LRRK2 function with selective kinase inhibitors
    • doi: 10.2217/fnl.13.9
    • Dzamko, N., and Halliday, G. M. (2013). Unlocking the secrets of LRRK2 function with selective kinase inhibitors. Future Neurol. 8, 347-357. doi: 10.2217/fnl.13.9
    • (2013) Future Neurol , vol.8 , pp. 347-357
    • Dzamko, N.1    Halliday, G.M.2
  • 40
    • 34249058118 scopus 로고    scopus 로고
    • Multiple roles of auxilin and hsc70 in clathrin-mediated endocytosis
    • doi: 10.1111/j.1600-0854.2007.00568.x
    • Eisenberg, E., and Greene, L. E. (2007). Multiple roles of auxilin and hsc70 in clathrin-mediated endocytosis. Traffic 8, 640-646. doi: 10.1111/j.1600-0854.2007.00568.x
    • (2007) Traffic , vol.8 , pp. 640-646
    • Eisenberg, E.1    Greene, L.E.2
  • 41
    • 84893921726 scopus 로고    scopus 로고
    • Transgenic mice expressing S129 phosphorylation mutations in alpha-synuclein
    • doi: 10.1016/j.neulet.2014.01.033
    • Escobar, V. D., Kuo, Y. M., Orrison, B. M., Giasson, B. I., and Nussbaum, R. L. (2014). Transgenic mice expressing S129 phosphorylation mutations in alpha-synuclein. Neurosci. Lett. 563, 96-100. doi: 10.1016/j.neulet.2014.01.033
    • (2014) Neurosci. Lett , vol.563 , pp. 96-100
    • Escobar, V.D.1    Kuo, Y.M.2    Orrison, B.M.3    Giasson, B.I.4    Nussbaum, R.L.5
  • 42
    • 84877352565 scopus 로고    scopus 로고
    • Ser129D mutant alpha-synuclein induces earlier motor dysfunction while S129A results in distinctive pathology in a rat model of Parkinson's disease
    • doi: 10.1016/j.nbd.2013.03.014
    • Febbraro, F., Sahin, G., Farran, A., Soares, S., Jensen, P. H., Kirik, D., et al. (2013). Ser129D mutant alpha-synuclein induces earlier motor dysfunction while S129A results in distinctive pathology in a rat model of Parkinson's disease. Neurobiol. Dis. 56, 47-58. doi: 10.1016/j.nbd.2013.03.014
    • (2013) Neurobiol. Dis , vol.56 , pp. 47-58
    • Febbraro, F.1    Sahin, G.2    Farran, A.3    Soares, S.4    Jensen, P.H.5    Kirik, D.6
  • 43
    • 0035668350 scopus 로고    scopus 로고
    • Active, phosphorylation-dependent mitogen-activated protein kinase (MAPK/ERK), stress-activated protein kinase/c-Jun N-terminal kinase (SAPK/JNK), and p38 kinase expression in Parkinson's disease and dementia with Lewy bodies
    • doi: 10.1007/ s007020100015
    • Ferrer, I., Blanco, R., Carmona, M., Puig, B., Barrachina, M., Gomez, C., et al. (2001). Active, phosphorylation-dependent mitogen-activated protein kinase (MAPK/ERK), stress-activated protein kinase/c-Jun N-terminal kinase (SAPK/JNK), and p38 kinase expression in Parkinson's disease and dementia with Lewy bodies. J. Neural. Transm. 108, 1383-1396. doi: 10.1007/ s007020100015
    • (2001) J. Neural. Transm , vol.108 , pp. 1383-1396
    • Ferrer, I.1    Blanco, R.2    Carmona, M.3    Puig, B.4    Barrachina, M.5    Gomez, C.6
  • 44
    • 0029036113 scopus 로고
    • Isolation and characterization of human casein kinase I epsilon (CKI), a novel member of the CKI gene family
    • doi: 10.1074/jbc.270.25.14875
    • Fish, K. J., Cegielska, A., Getman, M. E., Landes, G. M., and Virshup, D. M. (1995). Isolation and characterization of human casein kinase I epsilon (CKI), a novel member of the CKI gene family. J. Biol. Chem. 270, 14875-14883. doi: 10.1074/jbc.270.25.14875
    • (1995) J. Biol. Chem , vol.270 , pp. 14875-14883
    • Fish, K.J.1    Cegielska, A.2    Getman, M.E.3    Landes, G.M.4    Virshup, D.M.5
  • 45
    • 84875623628 scopus 로고    scopus 로고
    • Pharmacological inhibition of polo like kinase 2 (PLK2) does not cause chromosomal damage or result in the formation of micronuclei
    • doi: 10.1016/j.taap.2013.02.012
    • Fitzgerald, K., Bergeron, M., Willits, C., Bowers, S., Aubele, D. L., Goldbach, E., et al. (2013). Pharmacological inhibition of polo like kinase 2 (PLK2) does not cause chromosomal damage or result in the formation of micronuclei. Toxicol. Appl. Pharmacol. 269,1-7. doi: 10.1016/j.taap.2013.02.012
    • (2013) Toxicol. Appl. Pharmacol , vol.269 , pp. 1-7
    • Fitzgerald, K.1    Bergeron, M.2    Willits, C.3    Bowers, S.4    Aubele, D.L.5    Goldbach, E.6
  • 46
    • 0037067666 scopus 로고    scopus 로고
    • The anti-diabetic drugs rosiglitazone and metformin stimulate AMP-activated protein kinase through distinct signaling pathways
    • doi: 10.1074/jbc.M202489200
    • Fryer, L. G., Parbu-Patel, A., and Carling, D. (2002). The anti-diabetic drugs rosiglitazone and metformin stimulate AMP-activated protein kinase through distinct signaling pathways. J. Biol. Chem. 277, 25226-25232. doi: 10.1074/jbc.M202489200
    • (2002) J. Biol. Chem , vol.277 , pp. 25226-25232
    • Fryer, L.G.1    Parbu-Patel, A.2    Carling, D.3
  • 47
  • 48
    • 33745087689 scopus 로고    scopus 로고
    • PINK1 protein in normal human brain and Parkinson's disease
    • doi: 10.1093/brain/awl114
    • Gandhi, S., Muqit, M. M., Stanyer, L., Healy, D. G., Abou-Sleiman, P.M., Hargreaves, et al. (2006). PINK1 protein in normal human brain and Parkinson's disease. Brain 129, 1720-1731. doi: 10.1093/brain/awl114
    • (2006) Brain , vol.129 , pp. 1720-1731
    • Gandhi, S.1    Muqit, M.M.2    Stanyer, L.3    Healy, D.G.4    Abou-Sleiman, P.M.5
  • 49
    • 84882643371 scopus 로고    scopus 로고
    • Rotenone directly induces BV2 cell activation via the p38 MAPK pathway
    • doi: 10.1371/journal.pone.0072046
    • Gao, F., Chen, D., Hu, Q., and Wang, G. (2013). Rotenone directly induces BV2 cell activation via the p38 MAPK pathway. PLoS ONE 8:e72046. doi: 10.1371/journal.pone.0072046
    • (2013) PLoS ONE , vol.8
    • Gao, F.1    Chen, D.2    Hu, Q.3    Wang, G.4
  • 50
    • 78149473340 scopus 로고    scopus 로고
    • LRRK2 is involved in the IFN-gamma response and host response to pathogens
    • doi: 10.4049/jimmunol.1000548
    • Gardet, A., Benita, Y., Li, C., Sands, B. E., Ballester, I., Stevens, C., et al. (2010). LRRK2 is involved in the IFN-gamma response and host response to pathogens. J. Immunol. 185, 5577-5585. doi: 10.4049/jimmunol.1000548
    • (2010) J. Immunol , vol.185 , pp. 5577-5585
    • Gardet, A.1    Benita, Y.2    Li, C.3    Sands, B.E.4    Ballester, I.5    Stevens, C.6
  • 51
    • 69149089036 scopus 로고    scopus 로고
    • Molecular pathogenesis ofParkinson disease: Insights from genetic studies
    • doi: 10.1017/S1462399409001148
    • Gasser, T. (2009). Molecular pathogenesis ofParkinson disease: insights from genetic studies. Expert Rev Mol. Med. 11:e22. doi: 10.1017/S1462399409001148
    • (2009) Expert Rev Mol. Med , vol.11
    • Gasser, T.1
  • 53
    • 79851508036 scopus 로고    scopus 로고
    • SPAK andWNK kinases: Anewtarget for blood pressure treatment?
    • doi: 10.1097/MNH.0b013e32834132bc
    • Glover, M., and O'shaughnessy, K. M. (2011). SPAK andWNK kinases: anewtarget for blood pressure treatment? Curr. Opin. Nephrol. Hypertens. 20, 16-22. doi: 10.1097/MNH.0b013e32834132bc
    • (2011) Curr. Opin. Nephrol. Hypertens , vol.20 , pp. 16-22
    • Glover, M.1    O'Shaughnessy, K.M.2
  • 54
    • 0037052633 scopus 로고    scopus 로고
    • MPP+ increases alpha-synuclein expression and ERK/MAP-kinase phosphorylation in human neuroblastoma SH-SY5Y cells
    • doi: 10.1016/S0006-8993(02)02422-8
    • Gomez-Santos, C., Ferrer, I., Reiriz, J., Vinals, F., Barrachina, M., and Ambrosio, S. (2002). MPP+ increases alpha-synuclein expression and ERK/MAP-kinase phosphorylation in human neuroblastoma SH-SY5Y cells. Brain Res. 935, 32-39. doi: 10.1016/S0006-8993(02)02422-8
    • (2002) Brain Res , vol.935 , pp. 32-39
    • Gomez-Santos, C.1    Ferrer, I.2    Reiriz, J.3    Vinals, F.4    Barrachina, M.5    Ambrosio, S.6
  • 55
    • 85027943896 scopus 로고    scopus 로고
    • Akt as a victim, villain and potential hero in Parkinson's disease pathophysiology and treatment
    • doi: 10.1007/s10571-011-9671-9678
    • Greene, L. A., Levy, O., and Malagelada, C. (2011). Akt as a victim, villain and potential hero in Parkinson's disease pathophysiology and treatment. Cell Mol. Neurobiol. 31, 969-978. doi: 10.1007/s10571-011-9671-9678
    • (2011) Cell Mol. Neurobiol , vol.31 , pp. 969-978
    • Greene, L.A.1    Levy, O.2    Malagelada, C.3
  • 56
    • 84883492814 scopus 로고    scopus 로고
    • Parkin- and PINK1-dependent mitophagyinneurons: Will the real pathwayplease standup?
    • doi: 10.3389/fneur.2013.00100
    • Grenier, K., Mclelland, G. L., and Fon, E. A. (2013). Parkin- and PINK1-dependent mitophagyinneurons: will the real pathwayplease standup? Front. Neurol. 4:100. doi: 10.3389/fneur.2013.00100
    • (2013) Front. Neurol , vol.4 , pp. 100
    • Grenier, K.1    McLelland, G.L.2    Fon, E.A.3
  • 57
    • 19944428747 scopus 로고    scopus 로고
    • Gene expression profiling of parkinsonian substantia nigra pars compacta; alterations in ubiquitin-proteasome, heat shock protein, iron and oxidative stress regulated proteins, cell adhesion/cellular matrix and vesicle trafficking genes
    • doi: 10.1007/s00702-004-0212-1
    • Grunblatt, E., Mandel, S., Jacob-Hirsch, J., Zeligson, S., Amariglo, N., Rechavi, G., et al. (2004). Gene expression profiling of parkinsonian substantia nigra pars compacta; alterations in ubiquitin-proteasome, heat shock protein, iron and oxidative stress regulated proteins, cell adhesion/cellular matrix and vesicle trafficking genes. J. Neural. Transm. 111, 1543-1573. doi: 10.1007/s00702-004-0212-1
    • (2004) J. Neural. Transm , vol.111 , pp. 1543-1573
    • Grunblatt, E.1    Mandel, S.2    Jacob-Hirsch, J.3    Zeligson, S.4    Amariglo, N.5    Rechavi, G.6
  • 58
    • 84879602725 scopus 로고    scopus 로고
    • LRRK2 interactions with alpha-synuclein in Parkinson's disease brains and in cell models
    • doi: 10.1007/s00109-012- 0984-y
    • Guerreiro, P. S., Huang, Y., Gysbers, A., Cheng, D., Gai, W. P., Outeiro, T. F., et al. (2013). LRRK2 interactions with alpha-synuclein in Parkinson's disease brains and in cell models. J. Mol. Med. (Berl.) 91, 513-522. doi: 10.1007/s00109-012- 0984-y
    • (2013) J. Mol. Med. (Berl.) , vol.91 , pp. 513-522
    • Guerreiro, P.S.1    Huang, Y.2    Gysbers, A.3    Cheng, D.4    Gai, W.P.5    Outeiro, T.F.6
  • 59
    • 83555168220 scopus 로고    scopus 로고
    • G protein-coupled receptor kinases: More than just kinases and not only for GPCRs
    • doi: 10.1016/j.pharmthera.2011.08.001
    • Gurevich, E. V., Tesmer, J. J., Mushegian, A., and Gurevich, V. V. (2012). G protein-coupled receptor kinases: more than just kinases and not only for GPCRs. Pharmacol. Ther. 133, 40-69. doi: 10.1016/j.pharmthera.2011.08.001
    • (2012) Pharmacol. Ther , vol.133 , pp. 40-69
    • Gurevich, E.V.1    Tesmer, J.J.2    Mushegian, A.3    Gurevich, V.V.4
  • 60
    • 41149177434 scopus 로고    scopus 로고
    • The progression of pathology in longitudinally followed patients with Parkinson's disease
    • doi: 10.1007/s00401-008-0344-8
    • Halliday, G., Hely, M., Reid, W., and Morris, J. (2008). The progression of pathology in longitudinally followed patients with Parkinson's disease. Acta Neuropathol. 115,409-415. doi: 10.1007/s00401-008-0344-8
    • (2008) Acta Neuropathol , vol.115 , pp. 409-415
    • Halliday, G.1    Hely, M.2    Reid, W.3    Morris, J.4
  • 61
    • 0000056069 scopus 로고
    • ZurPathologie derparalysis agitans unddespost-enzephalitschen Parkinsonismus
    • Hassler, R. (1938).ZurPathologie derparalysis agitans unddespost-enzephalitschen Parkinsonismus. J. Psychol. Neurol. 48, 387-476.
    • (1938) J. Psychol. Neurol , vol.48 , pp. 387-476
    • Hassler, R.1
  • 62
    • 50049104725 scopus 로고    scopus 로고
    • Phenotype, genotype, andworldwide genetic penetrance ofLRRK2- associated Parkinson's disease: A case-control study
    • doi: 10.1016/S1474-4422(08)70117-0
    • Healy, D. G., Falchi, M., O'sullivan, S. S., Bonifati, V., Durr, A., Bressman, S., et al. (2008). Phenotype, genotype, andworldwide genetic penetrance ofLRRK2- associated Parkinson's disease: a case-control study. Lancet Neurol. 7, 583-590. doi: 10.1016/S1474-4422(08)70117-0
    • (2008) Lancet Neurol , vol.7 , pp. 583-590
    • Healy, D.G.1    Falchi, M.2    O'Sullivan, S.S.3    Bonifati, V.4    Durr, A.5    Bressman, S.6
  • 63
    • 2942605831 scopus 로고    scopus 로고
    • Role of extracellular signal regulated kinases 1 and2in neuronal survival
    • doi: 10.1111/j.1432-1033.2004.04133.x
    • Hetman, M., and Gozdz, A. (2004). Role of extracellular signal regulated kinases 1 and2in neuronal survival. Eur. J. Biochem. 271, 2050-2055.doi: 10.1111/j.1432-1033.2004.04133.x
    • (2004) Eur. J. Biochem , vol.271 , pp. 2050-2055
    • Hetman, M.1    Gozdz, A.2
  • 64
    • 34250199013 scopus 로고    scopus 로고
    • Localization of Parkinson's disease-associated LRRK2 in normal and pathological human brain
    • doi: 10.1016/j.brainres.2007.04.034
    • Higashi, S., Biskup, S., West, A. B., Trinkaus, D., Dawson, V. L., Faull, R. L., et al. (2007). Localization of Parkinson's disease-associated LRRK2 in normal and pathological human brain. Brain Res. 1155, 208-219. doi: 10.1016/j.brainres.2007.04.034
    • (2007) Brain Res , vol.1155 , pp. 208-219
    • Higashi, S.1    Biskup, S.2    West, A.B.3    Trinkaus, D.4    Dawson, V.L.5    Faull, R.L.6
  • 65
    • 84866343400 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3beta activation mediates rotenone-induced cytotoxicity with the involvement of microtubule destabilization
    • doi: 10.1016/j.bbrc.2012.08.042
    • Hongo, H., Kihara, T., Kume, T., Izumi, Y., Niidome, T., Sugimoto, H., et al. (2012). Glycogen synthase kinase-3beta activation mediates rotenone-induced cytotoxicity with the involvement of microtubule destabilization. Biochem. Biophys. Res. Commun. 426, 94-99. doi: 10.1016/j.bbrc.2012.08.042
    • (2012) Biochem. Biophys. Res. Commun , vol.426 , pp. 94-99
    • Hongo, H.1    Kihara, T.2    Kume, T.3    Izumi, Y.4    Niidome, T.5    Sugimoto, H.6
  • 67
    • 0346374790 scopus 로고    scopus 로고
    • JNK-mediatedinduction of cyclooxygenase 2 is requiredfor neurodegeneration inamouse model ofParkinson's disease
    • doi: 10.1073/pnas.0307453101
    • Hunot, S., Vila, M., Teismann, P., Davis, R. J., Hirsch, E. C., Przedborski, S., et al. (2014). JNK-mediatedinduction of cyclooxygenase 2 is requiredfor neurodegeneration inamouse model ofParkinson's disease. Proc. Natl. Acad. Sci. U.S.A. 101, 665-670. doi: 10.1073/pnas.0307453101
    • (2014) Proc. Natl. Acad. Sci. U.S.A , vol.101 , pp. 665-670
    • Hunot, S.1    Vila, M.2    Teismann, P.3    Davis, R.J.4    Hirsch, E.C.5    Przedborski, S.6
  • 68
    • 59149090357 scopus 로고    scopus 로고
    • Polo-like kinase 2 (PLK2) phosphorylates alpha-synuclein at serine 129 in central nervous system
    • doi: 10.1074/jbc.C800206200
    • Inglis, K. J., Chereau, D., Brigham, E. F., Chiou, S. S., Schobel, S., Frigon, N. L., et al. (2009). Polo-like kinase 2 (PLK2) phosphorylates alpha-synuclein at serine 129 in central nervous system. J. Biol. Chem. 284, 2598-2602. doi: 10.1074/jbc.C800206200
    • (2009) J. Biol. Chem , vol.284 , pp. 2598-2602
    • Inglis, K.J.1    Chereau, D.2    Brigham, E.F.3    Chiou, S.S.4    Schobel, S.5    Frigon, N.L.6
  • 69
    • 35148882113 scopus 로고    scopus 로고
    • Mixed lineage kinase inhibitor CEP-1347 fails to delay disability in early Parkinson disease
    • doi: 10.1212/01.wnl.0000277648.63931.c0
    • Investigators P. S. G. P. (2007). Mixed lineage kinase inhibitor CEP-1347 fails to delay disability in early Parkinson disease. Neurology 69, 1480-1490. doi: 10.1212/01.wnl.0000277648.63931.c0
    • (2007) Neurology , vol.69 , pp. 1480-1490
    • Investigators, P.S.G.P.1
  • 70
    • 34548702649 scopus 로고    scopus 로고
    • Casein kinase 2 is the major enzyme in brain that phosphorylates Ser129 ofhuman alpha- synuclein: Implication for alpha-synucleinopathies
    • doi: 10.1016/j.febslet.2007.08.067
    • Ishii, A., Nonaka, T., Taniguchi, S., Saito, T., Arai, T., Mann, D., et al. (2007). Casein kinase 2 is the major enzyme in brain that phosphorylates Ser129 ofhuman alpha- synuclein: Implication for alpha-synucleinopathies. FEBS Lett. 581, 4711-4717. doi: 10.1016/j.febslet.2007.08.067
    • (2007) FEBS Lett , vol.581 , pp. 4711-4717
    • Ishii, A.1    Nonaka, T.2    Taniguchi, S.3    Saito, T.4    Arai, T.5    Mann, D.6
  • 71
    • 34447118788 scopus 로고    scopus 로고
    • LRRK2 phosphorylates moesin at threonine-558: Characterization ofhow Parkinson's disease mutants affect kinase activity
    • doi: 10.1042/BJ20070209
    • Jaleel, M., Nichols, R. J., Deak, M., Campbell, D. G., Gillardon, F., Knebel, A., et al. (2007). LRRK2 phosphorylates moesin at threonine-558: characterization ofhow Parkinson's disease mutants affect kinase activity. Biochem. J. 405, 307-317. doi: 10.1042/BJ20070209
    • (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
  • 72
    • 84869037113 scopus 로고    scopus 로고
    • G protein-coupled receptor kinases in cardiovascular disease: Why"where" matters
    • doi: 10.1016/j.tcm.2012.07.023
    • Kamal, F. A., Travers, J. G., and Blaxall, B. C. (2012). G protein-coupled receptor kinases in cardiovascular disease: why"where" matters. Trends Cardiovasc. Med. 22,213-219. doi: 10.1016/j.tcm.2012.07.023
    • (2012) Trends Cardiovasc. Med , vol.22 , pp. 213-219
    • Kamal, F.A.1    Travers, J.G.2    Blaxall, B.C.3
  • 73
    • 0031023433 scopus 로고    scopus 로고
    • GAK: A cyclin G associated kinase contains a tensin/auxilin-like domain
    • doi: 10.1016/S0014-5793(96)01484-6
    • Kanaoka, Y., Kimura, S. H., Okazaki, I., Ikeda, M., and Nojima, H. (1997). GAK: a cyclin G associated kinase contains a tensin/auxilin-like domain. FEBS Lett. 402, 73-80. doi: 10.1016/S0014-5793(96)01484-6
    • (1997) FEBS Lett , vol.402 , pp. 73-80
    • Kanaoka, Y.1    Kimura, S.H.2    Okazaki, I.3    Ikeda, M.4    Nojima, H.5
  • 74
    • 80053353078 scopus 로고    scopus 로고
    • Genetic mutations and functions of PINK1
    • doi: 10.1016/j.tips.2011.06.001
    • Kawajiri, S., Saiki, S., Sato, S., and Hattori, N. (2011). Genetic mutations and functions of PINK1. Trends Pharmacol. Sci. 32, 573-580. doi: 10.1016/j.tips.2011.06.001
    • (2011) Trends Pharmacol. Sci , vol.32 , pp. 573-580
    • Kawajiri, S.1    Saiki, S.2    Sato, S.3    Hattori, N.4
  • 75
    • 84886642469 scopus 로고    scopus 로고
    • Leucine-rich repeat kinase 2 for beginners: Six key questions
    • doi: 10.1101/cshperspect.a009407
    • Kett, L. R., and Dauer, W. T. (2012). Leucine-rich repeat kinase 2 for beginners: six key questions. Cold Spring Harb. Perspect. Med. 2, a009407. doi: 10.1101/cshperspect.a009407
    • (2012) Cold Spring Harb. Perspect. Med , vol.2
    • Kett, L.R.1    Dauer, W.T.2
  • 76
    • 84883638818 scopus 로고    scopus 로고
    • PINK1 deficiency enhances inflammatory cytokine release from acutely prepared brain slices
    • doi: 10.5607/en.2013.22.1.38
    • Kim, J., Byun, J. W., Choi, I., Kim, B., Jeong, H. K., Jou, I., et al. (2013). PINK1 deficiency enhances inflammatory cytokine release from acutely prepared brain slices. Exp. Neurobiol. 22, 38-44. doi: 10.5607/en.2013.22.1.38
    • (2013) Exp. Neurobiol , vol.22 , pp. 38-44
    • Kim, J.1    Byun, J.W.2    Choi, I.3    Kim, B.4    Jeong, H.K.5    Jou, I.6
  • 77
    • 13844294211 scopus 로고    scopus 로고
    • The casein kinase 1 family: Participation in multiple cellular processes in eukaryotes
    • doi: 10.1016/j.cellsig.2004.12.011
    • Knippschild, U., Gocht, A., Wolff, S., Huber, N., Lohler, J., and Stoter, M. (2005). The casein kinase 1 family: participation in multiple cellular processes in eukaryotes. Cell. Signal. 17, 675-689. doi: 10.1016/j.cellsig.2004.12.011
    • (2005) Cell. Signal , vol.17 , pp. 675-689
    • Knippschild, U.1    Gocht, A.2    Wolff, S.3    Huber, N.4    Lohler, J.5    Stoter, M.6
  • 78
    • 84864267876 scopus 로고    scopus 로고
    • PINK1 is activated bymitochondrial membrane potential depolarization and stimulates Parkin E3 ligase activity by phosphorylating Serine 65
    • doi: 10.1098/rsob.120080
    • Kondapalli, C., Kazlauskaite, A., Zhang, N., Woodroof, H. I., Campbell, D. G., Gourlay, R., et al. (2012). PINK1 is activated bymitochondrial membrane potential depolarization and stimulates Parkin E3 ligase activity by phosphorylating Serine 65. Open Biol. 2, 120080. doi: 10.1098/rsob.120080.
    • (2012) Open Biol , vol.2 , pp. 120080
    • Kondapalli, C.1    Kazlauskaite, A.2    Zhang, N.3    Woodroof, H.I.4    Campbell, D.G.5    Gourlay, R.6
  • 79
    • 33646483645 scopus 로고    scopus 로고
    • Highly potent and specific GSK-3beta inhibitors that block tau phosphorylation and decrease alpha-synuclein protein expression in a cellular model of Parkinson's disease
    • doi: 10.1002/cmdc.200500039
    • Kozikowski, A. P., Gaisina, I. N., Petukhov, P. A., Sridhar, J., King, L. T., Blond, S. Y., et al. (2006). Highly potent and specific GSK-3beta inhibitors that block tau phosphorylation and decrease alpha-synuclein protein expression in a cellular model of Parkinson's disease. Chem. Med. Chem. 1, 256-266. doi: 10.1002/cmdc.200500039
    • (2006) Chem. Med. Chem , vol.1 , pp. 256-266
    • Kozikowski, A.P.1    Gaisina, I.N.2    Petukhov, P.A.3    Sridhar, J.4    King, L.T.5    Blond, S.Y.6
  • 80
    • 0035018119 scopus 로고    scopus 로고
    • Sustained extracellular signal-regulated kinase activation by 6-hydroxydopamine: Implications for Parkinson's disease
    • doi: 10.1046/j.1471-4159.2001.00304.x
    • Kulich, S. M., and Chu, C. T. (2001). Sustained extracellular signal-regulated kinase activation by 6-hydroxydopamine: implications for Parkinson's disease. J. Neurochem. 77,1058-1066. doi: 10.1046/j.1471-4159.2001.00304.x
    • (2001) J. Neurochem , vol.77 , pp. 1058-1066
    • Kulich, S.M.1    Chu, C.T.2
  • 81
    • 84860165740 scopus 로고    scopus 로고
    • Mammalian MAPK signal transduction pathways activated by stress and inflammation: A 10-year update
    • doi: 10.1152/physrev.00028.2011
    • Kyriakis, J. M., andAvruch, J. (2012). Mammalian MAPK signal transduction pathways activated by stress and inflammation: a 10-year update. Physiol. Rev. 92, 689-737. doi: 10.1152/physrev.00028.2011
    • (2012) Physiol. Rev , vol.92 , pp. 689-737
    • Kyriakis, J.M.1    Andavruch, J.2
  • 82
    • 84859778293 scopus 로고    scopus 로고
    • mTOR signaling in growth control and disease
    • doi: 10.1016/j.cell.2012.03.017
    • Laplante, M., and Sabatini, D. M. (2012). mTOR signaling in growth control and disease. Cell 149, 274-293. doi: 10.1016/j.cell.2012.03.017
    • (2012) Cell , vol.149 , pp. 274-293
    • Laplante, M.1    Sabatini, D.M.2
  • 83
    • 51349084970 scopus 로고    scopus 로고
    • Essential role of cyclin-G-associated kinase (Auxilin-2) in developing and mature mice
    • doi: 10.1091/mbc.E07-11-1115
    • Lee, D. W., Zhao, X., Yim, Y. I., Eisenberg, E., and Greene, L. E. (2008). Essential role of cyclin-G-associated kinase (Auxilin-2) in developing and mature mice. Mol. Biol. Cell 19,2766-2776. doi: 10.1091/mbc.E07-11-1115
    • (2008) Mol. Biol. Cell , vol.19 , pp. 2766-2776
    • Lee, D.W.1    Zhao, X.2    Yim, Y.I.3    Eisenberg, E.4    Greene, L.E.5
  • 84
    • 84870980411 scopus 로고    scopus 로고
    • PINK1 positively regulates IL-1beta-mediated signaling through Tollip and IRAK1 modulation
    • doi: 10.1186/1742-2094-9-271
    • Lee, H. J., and Chung, K. C. (2012). PINK1 positively regulates IL-1beta-mediated signaling through Tollip and IRAK1 modulation. J. Neuroinflammation 9, 271. doi: 10.1186/1742-2094-9-271
    • (2012) J. Neuroinflammation , vol.9 , pp. 271
    • Lee, H.J.1    Chung, K.C.2
  • 85
    • 84873157042 scopus 로고    scopus 로고
    • Neuroprotectiveandanti-inflammatorypropertiesofacoffeecomponent in the MPTP model of Parkinson's disease
    • doi: 10.1007/s13311-012-0165-2
    • Lee, K. W., Im, J. Y., Woo, J. M., Grosso, H., Kim, Y. S., Cristovao, A. C., et al. (2013).Neuroprotectiveandanti-inflammatorypropertiesofacoffeecomponent in the MPTP model of Parkinson's disease. Neurotherapeutics 10, 143-153. doi: 10.1007/s13311-012-0165-2
    • (2013) Neurotherapeutics , vol.10 , pp. 143-153
    • Lee, K.W.1    Im, J.Y.2    Woo, J.M.3    Grosso, H.4    Kim, Y.S.5    Cristovao, A.C.6
  • 86
    • 84897986995 scopus 로고    scopus 로고
    • Adiponectin offers protection against L166P mutant DJ-1-induced neuronal cytotoxicity mediated by APPL1-dependent AMPK activation
    • doi: 10.3109/00207454.2013.846340
    • Li, X., Geng, J., and Liu, J. (2014). Adiponectin offers protection against L166P mutant DJ-1-induced neuronal cytotoxicity mediated by APPL1-dependent AMPK activation. Int. J. Neurosci. 124, 350-361. doi: 10.3109/00207454.2013.846340
    • (2014) Int. J. Neurosci , vol.124 , pp. 350-361
    • Li, X.1    Geng, J.2    Liu, J.3
  • 87
    • 84896522656 scopus 로고    scopus 로고
    • Parkinson disease-associated mutation R1441H in LRRK2 prolongs the "active state" of its GTPase domain
    • doi: 10.1073/pnas.1323285111
    • Liao, J., Wu, C.X., Burlak, C., Zhang, S., Sahm, H., Wang, M., et al. (2014). Parkinson disease-associated mutation R1441H in LRRK2 prolongs the "active state" of its GTPase domain. Proc. Natl. Acad. Sci U.S.A. doi: 10.1073/pnas.1323285111.
    • (2014) Proc. Natl. Acad. Sci U.S.A
    • Liao, J.1    Wu, C.X.2    Burlak, C.3    Zhang, S.4    Sahm, H.5    Wang, M.6
  • 88
    • 84859339977 scopus 로고    scopus 로고
    • Comprehensive research synopsis and systematic meta-analyses in Parkinson's disease genetics: The PDGene database
    • doi: 10.1371/journal.pgen.1002548
    • Lill, C. M., Roehr, J. T., Mcqueen, M. B., Kavvoura, F. K., Bagade, S., Schjeide, B. M., et al. (2012). Comprehensive research synopsis and systematic meta-analyses in Parkinson's disease genetics: the PDGene database. PLoS Genet. 8:e1002548. doi: 10.1371/journal.pgen.1002548
    • (2012) PLoS Genet , vol.8
    • Lill, C.M.1    Roehr, J.T.2    McQueen, M.B.3    Kavvoura, F.K.4    Bagade, S.5    Schjeide, B.M.6
  • 89
    • 84871606902 scopus 로고    scopus 로고
    • Therapeutic effects of rapamycin on MPTP-induced Parkinsonism in mice
    • doi: 10.1007/s11064-012-0909-8
    • Liu, K., Shi, N., Sun, Y., Zhang, T., and Sun, X. (2013). Therapeutic effects of rapamycin on MPTP-induced Parkinsonism in mice. Neurochem. Res. 38, 201207. doi: 10.1007/s11064-012-0909-8
    • (2013) Neurochem. Res , vol.38 , pp. 201207
    • Liu, K.1    Shi, N.2    Sun, Y.3    Zhang, T.4    Sun, X.5
  • 90
    • 70949099222 scopus 로고    scopus 로고
    • G protein-coupled receptor kinase 5, overexpressed in the alpha-synuclein up-regulation model of Parkinson's disease, regulates bcl-2 expression
    • doi: 10.1016/j.brainres.2009.10.036
    • Liu, P., Wang, X., Gao, N., Zhu, H., Dai, X., Xu, Y., et al. (2010). G protein-coupled receptor kinase 5, overexpressed in the alpha-synuclein up-regulation model of Parkinson's disease, regulates bcl-2 expression. Brain Res. 1307, 134-141. doi: 10.1016/j.brainres.2009.10.036
    • (2010) Brain Res , pp. 134-141
    • Liu, P.1    Wang, X.2    Gao, N.3    Zhu, H.4    Dai, X.5    Xu, Y.6
  • 91
    • 79960981876 scopus 로고    scopus 로고
    • Genome-wide association study identifies candidate genes for Parkinson's disease in an Ashkenazi Jewish population
    • doi: 10.1186/1471-2350-12-104
    • Liu, X., Cheng, R., Verbitsky, M., Kisselev, S., Browne, A., Mejia-Sanatana, H., et al. (2011). Genome-wide association study identifies candidate genes for Parkinson's disease in an Ashkenazi Jewish population. BMC Med. Genet. 12:104. doi: 10.1186/1471-2350-12-104
    • (2011) BMC Med. Genet , vol.12 , pp. 104
    • Liu, X.1    Cheng, R.2    Verbitsky, M.3    Kisselev, S.4    Browne, A.5    Mejia-Sanatana, H.6
  • 92
    • 84867581207 scopus 로고    scopus 로고
    • Biochemical increase in phosphorylated alpha-synuclein precedes histopathology of Lewy-type synucleinopathies
    • doi: 10.1111/j.1750- 3639.2012.00585.x
    • Lue, L. F., Walker, D. G., Adler, C. H., Shill, H., Tran, H., Akiyama, H., et al. (2012). Biochemical increase in phosphorylated alpha-synuclein precedes histopathology of Lewy-type synucleinopathies. Brain Pathol. 22, 745-756. doi: 10.1111/j.1750- 3639.2012.00585.x
    • (2012) Brain Pathol , vol.22 , pp. 745-756
    • Lue, L.F.1    Walker, D.G.2    Adler, C.H.3    Shill, H.4    Tran, H.5    Akiyama, H.6
  • 94
    • 58149395816 scopus 로고    scopus 로고
    • RTP801 is inducedinParkinson's disease and mediates neuron death by inhibiting Akt phosphorylation/activation
    • doi: 10.1523/JNEUROSCI.3928-08.2008
    • Malagelada, C., Jin, Z.H., and Greene, L.A. (2008). RTP801 is inducedinParkinson's disease and mediates neuron death by inhibiting Akt phosphorylation/activation. J. Neurosci. 28, 14363-14371. doi: 10.1523/JNEUROSCI.3928-08.2008
    • (2008) J. Neurosci , vol.28 , pp. 14363-14371
    • Malagelada, C.1    Jin, Z.H.2    Greene, L.A.3
  • 95
    • 34548721105 scopus 로고    scopus 로고
    • Rasagiline promotes regeneration of substantia nigra dopaminergic neurons in post-MPTP-induced Parkinsonism via activation of tyrosine kinase receptor signaling pathway
    • doi: 10.1007/s11064-007-9351-8
    • Mandel, S. A., Sagi, Y., and Amit, T. (2007). Rasagiline promotes regeneration of substantia nigra dopaminergic neurons in post-MPTP-induced Parkinsonism via activation of tyrosine kinase receptor signaling pathway. Neurochem. Res. 32, 1694-1699. doi: 10.1007/s11064-007-9351-8
    • (2007) Neurochem. Res , vol.32 , pp. 1694-1699
    • Mandel, S.A.1    Sagi, Y.2    Amit, T.3
  • 96
    • 77951181836 scopus 로고    scopus 로고
    • PINK1 stabilized by mitochondrial depolarization recruits Parkin to damaged mitochondriaandactivateslatentParkinformitophagy
    • doi: 10.1083/jcb.200910140
    • Matsuda, N., Sato, S., Shiba, K., Okatsu, K., Saisho, K., Gautier, C. A., et al. (2010). PINK1 stabilized by mitochondrial depolarization recruits Parkin to damaged mitochondriaandactivateslatentParkinformitophagy. J. CellBiol. 189,211-221. doi: 10.1083/jcb.200910140
    • (2010) J. CellBiol , vol.189 , pp. 211-221
    • Matsuda, N.1    Sato, S.2    Shiba, K.3    Okatsu, K.4    Saisho, K.5    Gautier, C.A.6
  • 97
    • 77449113371 scopus 로고    scopus 로고
    • Phosphorylation of synucleins by members of the Polo-like kinase family
    • doi: 10.1074/jbc.M109.081950
    • Mbefo, M. K., Paleologou, K. E., Boucharaba, A., Oueslati, A., Schell, H., Fournier, M., et al. (2010). Phosphorylation of synucleins by members of the Polo-like kinase family. J. Biol. Chem. 285,2807-2822. doi: 10.1074/jbc.M109.081950
    • (2010) J. Biol. Chem , vol.285 , pp. 2807-2822
    • Mbefo, M.K.1    Paleologou, K.E.2    Boucharaba, A.3    Oueslati, A.4    Schell, H.5    Fournier, M.6
  • 98
    • 70149118325 scopus 로고    scopus 로고
    • Alpha-synuclein S129 phosphorylation mutants do not alter nigrostriatal toxicity in a rat model of Parkinson disease
    • doi: 10.1097/NEN.0b013e3181a24b53
    • McFarland, N. R., Fan, Z., Xu, K., Schwarzschild, M. A., Feany, M. B., Hyman, T., et al. (2009). Alpha-synuclein S129 phosphorylation mutants do not alter nigrostriatal toxicity in a rat model of Parkinson disease. J. Neuropathol. Exp. Neurol. 68, 515-524. doi: 10.1097/NEN.0b013e3181a24b53
    • (2009) J. Neuropathol. Exp. Neurol , vol.68 , pp. 515-524
    • McFarland, N.R.1    Fan, Z.2    Xu, K.3    Schwarzschild, M.A.4    Feany, M.B.5    Hyman, T.6
  • 99
    • 0037334895 scopus 로고    scopus 로고
    • One-thousand-and-one substrates of protein kinase CK2?
    • doi: 10.1096/fj.02-0473rev
    • Meggio, F., and Pinna, L. A. (2003). One-thousand-and-one substrates of protein kinase CK2? FASEB J. 17, 349-368. doi: 10.1096/fj.02-0473rev
    • (2003) FASEB J , vol.17 , pp. 349-368
    • Meggio, F.1    Pinna, L.A.2
  • 100
    • 34547107314 scopus 로고    scopus 로고
    • A comparative analysis of leucine-rich repeat kinase 2 (Lrrk2) expression in mouse brain and Lewy body disease
    • doi: 10.1016/j.neuroscience.2007.05.027
    • Melrose, H. L., Kent, C. B., Taylor, J. P., Dachsel, J. C., Hinkle, K. M., Lincoln, S. J., et al. (2007). A comparative analysis of leucine-rich repeat kinase 2 (Lrrk2) expression in mouse brain and Lewy body disease. Neuroscience 147, 1047-1058. doi: 10.1016/j.neuroscience.2007.05.027
    • (2007) Neuroscience , vol.147 , pp. 1047-1058
    • Melrose, H.L.1    Kent, C.B.2    Taylor, J.P.3    Dachsel, J.C.4    Hinkle, K.M.5    Lincoln, S.J.6
  • 101
    • 33749463769 scopus 로고    scopus 로고
    • LRRK2 expression in normal and pathologic human brain and in human cell lines
    • doi: 10.1097/01.jnen.0000235121.98052.54
    • Miklossy, J., Arai, T., Guo, J. P., Klegeris, A., Yu, S., Mcgeer, E. G., et al. (2006). LRRK2 expression in normal and pathologic human brain and in human cell lines. J. Neu- ropathol. Exp. Neurol. 65, 953-963. doi: 10.1097/01.jnen.0000235121.98052.54
    • (2006) J. Neu- Ropathol. Exp. Neurol , vol.65 , pp. 953-963
    • Miklossy, J.1    Arai, T.2    Guo, J.P.3    Klegeris, A.4    Yu, S.5    McGeer, E.G.6
  • 102
    • 84856632181 scopus 로고    scopus 로고
    • LRRK2 inhibition attenuates microglial inflammatory responses
    • doi: 10.1523/JNEUROSCI.5601-11.2012
    • Moehle, M. S., Webber, P. J., Tse, T., Sukar, N., Standaert, D. G., Desilva, T. M., et al. (2012). LRRK2 inhibition attenuates microglial inflammatory responses. J. Neurosci. 32, 1602-1611. doi: 10.1523/JNEUROSCI.5601-11.2012
    • (2012) J. Neurosci , vol.32 , pp. 1602-1611
    • Moehle, M.S.1    Webber, P.J.2    Tse, T.3    Sukar, N.4    Standaert, D.G.5    Desilva, T.M.6
  • 103
    • 84874086124 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3 inhibitors as potent therapeutic agents for the treatment of Parkinson disease
    • doi: 10.1021/cn300182g
    • Morales-Garcia, J. A., Susin, C., Alonso-Gil, S., Perez, D. I., Palomo, V., Perez, C., et al. (2013). Glycogen synthase kinase-3 inhibitors as potent therapeutic agents for the treatment of Parkinson disease. ACS Chem. Neurosci. 4, 350-360. doi: 10.1021/cn300182g
    • (2013) ACS Chem. Neurosci , vol.4 , pp. 350-360
    • Morales-Garcia, J.A.1    Susin, C.2    Alonso-Gil, S.3    Perez, D.I.4    Palomo, V.5    Perez, C.6
  • 104
    • 84885463900 scopus 로고    scopus 로고
    • Oral treatment targeting the unfolded protein response prevents neurodegeneration and clinical disease in prion-infected mice
    • doi: 10.1126/scitranslmed.3006767
    • Moreno, J.A., Halliday, M., Molloy, C., Radford, H., Verity, N., Axten, J.M., et al. (2013). Oral treatment targeting the unfolded protein response prevents neurodegeneration and clinical disease in prion-infected mice. Sci. Transl. Med. 5, 206ra138. doi: 10.1126/scitranslmed.3006767
    • (2013) Sci. Transl. Med , vol.5
    • Moreno, J.A.1    Halliday, M.2    Molloy, C.3    Radford, H.4    Verity, N.5    Axten, J.M.6
  • 105
    • 56949087160 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3beta is associated with Parkinson's disease
    • doi: 10.1016/j.neulet.2008.10.104
    • Nagao, M., and Hayashi, H. (2009). Glycogen synthase kinase-3beta is associated with Parkinson's disease. Neurosci. Lett. 449, 103-107. doi: 10.1016/j.neulet.2008.10.104
    • (2009) Neurosci. Lett , vol.449 , pp. 103-107
    • Nagao, M.1    Hayashi, H.2
  • 106
    • 0030749732 scopus 로고    scopus 로고
    • p35nck5a and cyclin-dependent kinase 5 colocalize in Lewybodies ofbrains with Parkinson's disease
    • doi: 10.1007/s004010050687
    • Nakamura, S., Kawamoto, Y., Nakano, S., Akiguchi, I., and Kimura, J. (1997). p35nck5a and cyclin-dependent kinase 5 colocalize in Lewybodies ofbrains with Parkinson's disease. Acta Neuropathol. 94,153-157. doi: 10.1007/s004010050687
    • (1997) Acta Neuropathol , vol.94 , pp. 153-157
    • Nakamura, S.1    Kawamoto, Y.2    Nakano, S.3    Akiguchi, I.4    Kimura, J.5
  • 107
    • 79951811351 scopus 로고    scopus 로고
    • Imputation of sequence variants for identification of genetic risks for Parkinson's disease: A meta-analysis of genome-wide association studies
    • doi: 10.1016/S0140-6736(10)62345-8
    • Nalls, M. A., Plagnol, V., Hernandez, D. G., Sharma, M., Sheerin, U. M., Saad, M., et al. (2011). Imputation of sequence variants for identification of genetic risks for Parkinson's disease: a meta-analysis of genome-wide association studies. Lancet 377, 641-649. doi: 10.1016/S0140-6736(10)62345-8.
    • (2011) Lancet , vol.377 , pp. 641-649
    • Nalls, M.A.1    Plagnol, V.2    Hernandez, D.G.3    Sharma, M.4    Sheerin, U.M.5    Saad, M.6
  • 108
    • 75749156257 scopus 로고    scopus 로고
    • PINK1 is selectively stabilized on impaired mitochondria to activate Parkin
    • doi: 10.1371/journal.pbio.1000298
    • Narendra, D. P., Jin, S. M., Tanaka, A., Suen, D. F., Gautier, C.A., Shen, J., et al. (2010). PINK1 is selectively stabilized on impaired mitochondria to activate Parkin. PLoS Biol. 8:e1000298. doi: 10.1371/journal.pbio.1000298
    • (2010) PLoS Biol , vol.8
    • Narendra, D.P.1    Jin, S.M.2    Tanaka, A.3    Suen, D.F.4    Gautier, C.A.5    Shen, J.6
  • 109
    • 2442671608 scopus 로고    scopus 로고
    • Rotenone-induced apoptosis is mediated by p38 and JNK MAP kinases in human dopaminergic SH-SY5Y cells
    • doi: 10.1093/toxsci/kfh089
    • Newhouse, K., Hsuan, S. L., Chang, S. H., Cai, B., Wang, Y., and Xia, Z. (2004). Rotenone-induced apoptosis is mediated by p38 and JNK MAP kinases in human dopaminergic SH-SY5Y cells. Toxicol. Sci. 79, 137-146. doi: 10.1093/toxsci/kfh089
    • (2004) Toxicol. Sci , vol.79 , pp. 137-146
    • Newhouse, K.1    Hsuan, S.L.2    Chang, S.H.3    Cai, B.4    Wang, Y.5    Xia, Z.6
  • 110
    • 0034614415 scopus 로고    scopus 로고
    • Constitutive phosphorylation of the Parkinson's disease associated alpha-synuclein
    • doi: 10.1074/jbc.275.1.390
    • Okochi, M., Walter, J., Koyama, A., Nakajo, S., Baba, M., Iwatsubo, T., et al. (2000). Constitutive phosphorylation of the Parkinson's disease associated alpha-synuclein. J. Biol. Chem. 275, 390-397. doi: 10.1074/jbc.275.1.390
    • (2000) J. Biol. Chem , vol.275 , pp. 390-397
    • Okochi, M.1    Walter, J.2    Koyama, A.3    Nakajo, S.4    Baba, M.5    Iwatsubo, T.6
  • 111
    • 84873458538 scopus 로고    scopus 로고
    • Parkinson's disease and alpha synu- clein: Is Parkinson's disease a prion-like disorder?
    • doi: 10.1002/mds.25373
    • Olanow, C. W., and Brundin, P. (2013). Parkinson's disease and alpha synu- clein: is Parkinson's disease a prion-like disorder? Mov. Disord. 28, 31-40. doi: 10.1002/mds.25373
    • (2013) Mov. Disord , vol.28 , pp. 31-40
    • Olanow, C.W.1    Brundin, P.2
  • 112
    • 77955366745 scopus 로고    scopus 로고
    • Role of post-translational modifications in modulating the structure, function and toxicity of alpha- synuclein: Implications for Parkinson's disease pathogenesis and therapies
    • doi: 10.1016/S0079-6123(10)83007-9
    • Oueslati, A., Fournier, M., and Lashuel, H. A. (2010). Role of post-translational modifications in modulating the structure, function and toxicity of alpha- synuclein: implications for Parkinson's disease pathogenesis and therapies. Prog. BrainRes. 183, 115-145. doi: 10.1016/S0079-6123(10)83007-9
    • (2010) Prog. BrainRes , vol.183 , pp. 115-145
    • Oueslati, A.1    Fournier, M.2    Lashuel, H.A.3
  • 113
    • 84885363886 scopus 로고    scopus 로고
    • Polo-like kinase 2 regulates selective autophagic alpha-synuclein clearance and suppresses its toxicity in vivo
    • doi: 10.1073/pnas.1309991110
    • Oueslati, A., Schneider, B. L., Aebischer, P., and Lashuel, H. A. (2013). Polo-like kinase 2 regulates selective autophagic alpha-synuclein clearance and suppresses its toxicity in vivo. Proc. Natl. Acad. Sci. U.S.A. 110, E3945-E3954. doi: 10.1073/pnas.1309991110
    • (2013) Proc. Natl. Acad. Sci. U.S.A , vol.110
    • Oueslati, A.1    Schneider, B.L.2    Aebischer, P.3    Lashuel, H.A.4
  • 114
    • 67749118059 scopus 로고    scopus 로고
    • LRRK2 gene variation and its contribution to Parkinson disease
    • doi: 10.1002/humu.21038
    • Paisan-Ruiz, C. (2009). LRRK2 gene variation and its contribution to Parkinson disease. Hum. Mutat. 30, 1153-1160. doi: 10.1002/humu.21038
    • (2009) Hum. Mutat , vol.30 , pp. 1153-1160
    • Paisan-Ruiz, C.1
  • 115
    • 8844266996 scopus 로고    scopus 로고
    • Cloning of the gene containing mutations that cause PARK8- linked Parkinson's disease
    • doi: 10.1016/j.neuron.2004.10.023
    • Paisan-Ruiz, C., Jain, S., Evans, E. W., Gilks, W. P., Simon, J., Van Der Brug, M., et al. (2004). Cloning of the gene containing mutations that cause PARK8- linked Parkinson's disease. Neuron 44, 595-600. doi: 10.1016/j.neuron.2004.10.023
    • (2004) Neuron , vol.44 , pp. 595-600
    • Paisan-Ruiz, C.1    Jain, S.2    Evans, E.W.3    Gilks, W.P.4    Simon, J.5    van der Brug, M.6
  • 116
    • 70349750492 scopus 로고    scopus 로고
    • Rapamycin protects against rotenone-induced apoptosis through autophagy induction
    • doi: 10.1016/j.neuroscience.2009.08.014
    • Pan, T., Rawal, P., Wu, Y., Xie, W., Jankovic, J., and Le, W. (2009). Rapamycin protects against rotenone-induced apoptosis through autophagy induction. Neuroscience 164, 541-551. doi: 10.1016/j.neuroscience.2009.08.014
    • (2009) Neuroscience , vol.164 , pp. 541-551
    • Pan, T.1    Rawal, P.2    Wu, Y.3    Xie, W.4    Jankovic, J.5    Le, W.6
  • 117
    • 58149100151 scopus 로고    scopus 로고
    • Genomewide association study for susceptibility genes contributing to familial Parkinson disease
    • doi: 10.1007/s00439- 008-0582-9
    • Pankratz, N., Wilk, J. B., Latourelle, J. C., Destefano, A. L., Halter, C., Pugh, E. W., et al. (2009). Genomewide association study for susceptibility genes contributing to familial Parkinson disease. Hum. Genet. 124, 593-605. doi: 10.1007/s00439- 008-0582-9
    • (2009) Hum. Genet , vol.124 , pp. 593-605
    • Pankratz, N.1    Wilk, J.B.2    Latourelle, J.C.3    Destefano, A.L.4    Halter, C.5    Pugh, E.W.6
  • 118
    • 80053941298 scopus 로고    scopus 로고
    • Protein kinases CK1 and CK2 as new targets for neurodegenerative diseases
    • doi: 10.1002/med.20207
    • Perez, D. I., Gil, C., and Martinez, A. (2011). Protein kinases CK1 and CK2 as new targets for neurodegenerative diseases. Med. Res. Rev. 31, 924-954. doi: 10.1002/med.20207
    • (2011) Med. Res. Rev , vol.31 , pp. 924-954
    • Perez, D.I.1    Gil, C.2    Martinez, A.3
  • 119
    • 79951623073 scopus 로고    scopus 로고
    • A genome-wide association study-derived candidate gene seeks replication: STK39
    • doi: 10.1097/HJH.0b013e328344b6b3
    • Persu, A., and Vikkula, M. (2011). A genome-wide association study-derived candidate gene seeks replication: STK39. J. Hypertens. 29, 434-436. doi: 10.1097/HJH.0b013e328344b6b3
    • (2011) J. Hypertens , vol.29 , pp. 434-436
    • Persu, A.1    Vikkula, M.2
  • 120
    • 0033598401 scopus 로고    scopus 로고
    • Casein kinase I transduces Wnt signals
    • doi: 10.1038/43830
    • Peters, J. M., Mckay, R. M., Mckay, J. P., and Graff, J. M. (1999). Casein kinase I transduces Wnt signals. Nature 401, 345-350. doi: 10.1038/43830
    • (1999) Nature , vol.401 , pp. 345-350
    • Peters, J.M.1    McKay, R.M.2    McKay, J.P.3    Graff, J.M.4
  • 121
    • 84855262350 scopus 로고    scopus 로고
    • Genetic variability in SNCA and Parkinson's disease
    • doi: 10.1007/s10048-011-0292-7
    • Pihlstrom, L., and Toft, M. (2011). Genetic variability in SNCA and Parkinson's disease. Neurogenetics 12, 283-293. doi: 10.1007/s10048-011-0292-7
    • (2011) Neurogenetics , vol.12 , pp. 283-293
    • Pihlstrom, L.1    Toft, M.2
  • 122
    • 0030744876 scopus 로고    scopus 로고
    • Mutation in the alpha-synuclein gene identified in families with Parkinson's disease
    • doi: 10.1126/science.276.5321.2045
    • Polymeropoulos, M. H., Lavedan, C., Leroy, E., Ide, S. E., Dehejia, A., Dutra, A., et al. (1997). Mutation in the alpha-synuclein gene identified in families with Parkinson's disease. Science 276, 2045-2047. doi: 10.1126/science.276.5321.2045
    • (1997) Science , vol.276 , pp. 2045-2047
    • Polymeropoulos, M.H.1    Lavedan, C.2    Leroy, E.3    Ide, S.E.4    Dehejia, A.5    Dutra, A.6
  • 123
    • 0034714204 scopus 로고    scopus 로고
    • Synucleins are a novel class of substrates for G protein-coupled receptor kinases
    • doi: 10.1074/jbc.M003542200
    • Pronin, A. N., Morris, A. J., Surguchov, A., and Benovic, J. L. (2000). Synucleins are a novel class of substrates for G protein-coupled receptor kinases. J. Biol. Chem. 275, 26515-26522. doi: 10.1074/jbc.M003542200
    • (2000) J. Biol. Chem , vol.275 , pp. 26515-26522
    • Pronin, A.N.1    Morris, A.J.2    Surguchov, A.3    Benovic, J.L.4
  • 124
    • 70450246992 scopus 로고    scopus 로고
    • Lrrk2 interaction with alpha-synuclein in diffuse Lewy body disease
    • doi: 10.1016/j.bbrc.2009.10.126
    • Qing, H., Zhang, Y., Deng, Y., Mcgeer, E. G., and Mcgeer, P. L. (2009). Lrrk2 interaction with alpha-synuclein in diffuse Lewy body disease. Biochem. Biophys. Res. Commun. 390, 1229-1234. doi: 10.1016/j.bbrc.2009.10.126
    • (2009) Biochem. Biophys. Res. Commun , vol.390 , pp. 1229-1234
    • Qing, H.1    Zhang, Y.2    Deng, Y.3    McGeer, E.G.4    McGeer, P.L.5
  • 125
    • 34250897267 scopus 로고    scopus 로고
    • Role of Cdk5-mediated phosphorylation of Prx2 in MPTP toxicity and Parkinson's disease
    • doi: 10.1016/j.neuron.2007.05.033
    • Qu, D., Rashidian, J., Mount, M. P., Aleyasin, H., Parsanejad, M., Lira, A., et al. (2007). Role of Cdk5-mediated phosphorylation of Prx2 in MPTP toxicity and Parkinson's disease. Neuron 55, 37-52. doi: 10.1016/j.neuron.2007.05.033
    • (2007) Neuron , vol.55 , pp. 37-52
    • Qu, D.1    Rashidian, J.2    Mount, M.P.3    Aleyasin, H.4    Parsanejad, M.5    Lira, A.6
  • 126
    • 84897977607 scopus 로고    scopus 로고
    • Lewybodyextracts from Parkinson disease brains trigger alpha- synuclein pathologyand neurodegeneration in mice and monkeys
    • doi: 10.1002/ana.24066
    • Recasens, A., Dehay, B., Bove, J., Carballo-Carbajal, I., Dovero, S., Perez-Villalba, A., et al. (2014). Lewybodyextracts from Parkinson disease brains trigger alpha- synuclein pathologyand neurodegeneration in mice and monkeys. Ann. Neurol. 75, 351-362. doi: 10.1002/ana.24066
    • (2014) Ann. Neurol , vol.75 , pp. 351-362
    • Recasens, A.1    Dehay, B.2    Bove, J.3    Carballo-Carbajal, I.4    Dovero, S.5    Perez-Villalba, A.6
  • 127
    • 79851497835 scopus 로고    scopus 로고
    • Replication of GWAS associations for GAK and MAPT in Parkinson's disease
    • doi: 10.1111/j.1469-1809.2010.00616.x
    • Rhodes, S. L., Sinsheimer, J. S., Bordelon, Y., Bronstein, J. M., and Ritz, B. (2011). Replication of GWAS associations for GAK and MAPT in Parkinson's disease. Ann. Hum. Genet. 75, 195-200. doi: 10.1111/j.1469-1809.2010.00616.x
    • (2011) Ann. Hum. Genet , vol.75 , pp. 195-200
    • Rhodes, S.L.1    Sinsheimer, J.S.2    Bordelon, Y.3    Bronstein, J.M.4    Ritz, B.5
  • 128
    • 56349151939 scopus 로고    scopus 로고
    • The regulation of salt transport and blood pressure bytheWNK-SPAK/OSR1 signalling pathway
    • doi: 10.1242/jcs.029223
    • Richardson, C., and Alessi, D. R. (2008). The regulation of salt transport and blood pressure bytheWNK-SPAK/OSR1 signalling pathway. J. CellSci. 121, 3293-3304. doi: 10.1242/jcs.029223
    • (2008) J. CellSci , vol.121 , pp. 3293-3304
    • Richardson, C.1    Alessi, D.R.2
  • 129
    • 33845507061 scopus 로고    scopus 로고
    • Oncoprotein Akt/PKB induces trophic effects in murine models of Parkinson's disease
    • doi: 10.1073/pnas.0606401103
    • Ries, V., Henchcliffe, C., Kareva, T., Rzhetskaya, M., Bland, R., During, M. J., et al. (2006). Oncoprotein Akt/PKB induces trophic effects in murine models of Parkinson's disease. Proc. Natl. Acad. Sci. U.S.A. 103, 18757-18762. doi: 10.1073/pnas.0606401103
    • (2006) Proc. Natl. Acad. Sci. U.S.A , vol.103 , pp. 18757-18762
    • Ries, V.1    Henchcliffe, C.2    Kareva, T.3    Rzhetskaya, M.4    Bland, R.5    During, M.J.6
  • 131
    • 84856227695 scopus 로고    scopus 로고
    • Identification and functional characterization of polo-like kinase 2 autoregulatory sites
    • doi: 10.1016/j.neuroscience.2011.11.003
    • Rozeboom, A. M., and Pak, D. T. (2012). Identification and functional characterization of polo-like kinase 2 autoregulatory sites. Neuroscience 202, 147-157. doi: 10.1016/j.neuroscience.2011.11.003
    • (2012) Neuroscience , vol.202 , pp. 147-157
    • Rozeboom, A.M.1    Pak, D.T.2
  • 132
    • 84857285604 scopus 로고    scopus 로고
    • Is inhibition of kinase activity the only therapeutic strategy for LRRK2-associated Parkinson's disease?
    • doi: 10.1186/1741-7015-10-20
    • Rudenko, I. N., Chia, R., and Cookson, M. R. (2012a). Is inhibition of kinase activity the only therapeutic strategy for LRRK2-associated Parkinson's disease? BMCMed. 10:20.doi: 10.1186/1741-7015-10-20
    • (2012) BMCMed , vol.10 , pp. 20
    • Rudenko, I.N.1    Chia, R.2    Cookson, M.R.3
  • 133
    • 84864743687 scopus 로고    scopus 로고
    • The G2385Rvariant ofleucine-rich repeat kinase 2 associatedwith Parkinson's disease isapartialloss-of-functionmutation
    • doi: 10.1042/BJ20120637
    • Rudenko, I. N., Kaganovich, A., Hauser, D. N., Beylina, A., Chia, R., Ding, J., et al. (2012b). The G2385Rvariant ofleucine-rich repeat kinase 2 associatedwith Parkinson's disease isapartialloss-of-functionmutation. Biochem. J. 446,99-111. doi: 10.1042/BJ20120637
    • (2012) Biochem. J , vol.446 , pp. 99-111
    • Rudenko, I.N.1    Kaganovich, A.2    Hauser, D.N.3    Beylina, A.4    Chia, R.5    Ding, J.6
  • 134
    • 38749131954 scopus 로고    scopus 로고
    • Localization of CKII beta subunits in Lewy bodies of Parkinson's disease
    • doi: 10.1016/j.jns.2007.08.027
    • Ryu, M. Y., Kim, D. W., Arima, K., Mouradian, M. M., Kim, S. U., and Lee, G. (2008). Localization of CKII beta subunits in Lewy bodies of Parkinson's disease. J. Neurol. Sci. 266, 9-12. doi: 10.1016/j.jns.2007.08.027
    • (2008) J. Neurol. Sci , vol.266 , pp. 9-12
    • Ryu, M.Y.1    Kim, D.W.2    Arima, K.3    Mouradian, M.M.4    Kim, S.U.5    Lee, G.6
  • 135
    • 33751078859 scopus 로고    scopus 로고
    • Activation of tyrosine kinase receptor signaling pathway by rasagiline facilitates neurorescue and restoration of nigrostriatal dopamine neurons in post-MPTP-induced parkinsonism
    • doi: 10.1016/j.nbd.2006.07.020
    • Sagi, Y., Mandel, S., Amit, T., andYoudim, M. B. (2007).Activation of tyrosine kinase receptor signaling pathway by rasagiline facilitates neurorescue and restoration of nigrostriatal dopamine neurons in post-MPTP-induced parkinsonism. Neurobiol. Dis. 25, 35-44. doi: 10.1016/j.nbd.2006.07.020
    • (2007) Neurobiol. Dis , vol.25 , pp. 35-44
    • Sagi, Y.1    Mandel, S.2    Amit, T.3    Andyoudim, M.B.4
  • 136
    • 65649116247 scopus 로고    scopus 로고
    • Contribution of endogenous G-protein-coupled receptor kinases to Ser129 phosphorylation of alpha-synuclein in HEK293 cells
    • doi: 10.1016/j.bbrc.2009.04.130
    • Sakamoto, M., Arawaka, S., Hara, S., Sato, H., Cui, C., Machiya, Y., et al. (2009). Contribution of endogenous G-protein-coupled receptor kinases to Ser129 phosphorylation of alpha-synuclein in HEK293 cells. Biochem. Biophys. Res. Commun. 384, 378-382. doi: 10.1016/j.bbrc.2009.04.130
    • (2009) Biochem. Biophys. Res. Commun , vol.384 , pp. 378-382
    • Sakamoto, M.1    Arawaka, S.2    Hara, S.3    Sato, H.4    Cui, C.5    Machiya, Y.6
  • 137
    • 84867668373 scopus 로고    scopus 로고
    • Investigation on PLK2 and PLK3 substrate recognition
    • doi: 10.1016/j.bbapap.2012.07.003
    • Salvi, M., Trashi, E., Cozza, G., Franchin, C., Arrigoni, G., and Pinna, L. A. (2012). Investigation on PLK2 and PLK3 substrate recognition. Biochim. Biophys. Acta 1824, 1366-1373. doi: 10.1016/j.bbapap.2012.07.003
    • (2012) Biochim. Biophys. Acta , vol.1824 , pp. 1366-1373
    • Salvi, M.1    Trashi, E.2    Cozza, G.3    Franchin, C.4    Arrigoni, G.5    Pinna, L.A.6
  • 138
    • 77950855127 scopus 로고    scopus 로고
    • PINK1-linked parkinsonism is associated with Lewy body pathology
    • doi: 10.1093/brain/awq051
    • Samaranch, L., Lorenzo-Betancor, O., Arbelo, J. M., Ferrer, I., Lorenzo, E., Irigoyen, J., et al. (2010). PINK1-linked parkinsonism is associated with Lewy body pathology. Brain 133, 1128-1142. doi: 10.1093/brain/awq051
    • (2010) Brain , vol.133 , pp. 1128-1142
    • Samaranch, L.1    Lorenzo-Betancor, O.2    Arbelo, J.M.3    Ferrer, I.4    Lorenzo, E.5    Irigoyen, J.6
  • 139
    • 0033029823 scopus 로고    scopus 로고
    • CEP-1347/KT- 7515, an inhibitor of c-jun N-terminal kinase activation, attenuates the 1- methyl-4-phenyl tetrahydropyridine-mediated loss of nigrostriatal dopaminergic neurons in vivo
    • Saporito, M. S., Brown, E. M., Miller, M. S., and Carswell, S. (1999). CEP-1347/KT- 7515, an inhibitor of c-jun N-terminal kinase activation, attenuates the 1- methyl-4-phenyl tetrahydropyridine-mediated loss of nigrostriatal dopaminergic neurons in vivo. J. Pharmacol. Exp. Ther. 288, 421-427.
    • (1999) J. Pharmacol. Exp. Ther , vol.288 , pp. 421-427
    • Saporito, M.S.1    Brown, E.M.2    Miller, M.S.3    Carswell, S.4
  • 140
    • 0033840581 scopus 로고    scopus 로고
    • MPTP activates c-Jun NH(2)-terminal kinase (JNK) and its upstream regulatory kinase MKK4 in nigrostriatal neurons in vivo
    • doi: 10.1046/j.1471- 4159.2000.0751200.x
    • Saporito, M. S., Thomas, B. A., and Scott, R. W. (2000). MPTP activates c-Jun NH(2)-terminal kinase (JNK) and its upstream regulatory kinase MKK4 in nigrostriatal neurons in vivo. J. Neurochem. 75, 1200-1208. doi: 10.1046/j.1471- 4159.2000.0751200.x
    • (2000) J. Neurochem , vol.75 , pp. 1200-1208
    • Saporito, M.S.1    Thomas, B.A.2    Scott, R.W.3
  • 141
    • 70549084415 scopus 로고    scopus 로고
    • Genome-wide association study identifies common variants at four loci as genetic risk factors for Parkinson's disease
    • doi: 10.1038/ng.485
    • Satake, W., Nakabayashi, Y., Mizuta, I., Hirota, Y., Ito, C., Kubo, M., et al. (2009). Genome-wide association study identifies common variants at four loci as genetic risk factors for Parkinson's disease. Nat. Genet. 41, 1303-1307. doi: 10.1038/ng.485
    • (2009) Nat. Genet , vol.41 , pp. 1303-1307
    • Satake, W.1    Nakabayashi, Y.2    Mizuta, I.3    Hirota, Y.4    Ito, C.5    Kubo, M.6
  • 142
    • 84878000169 scopus 로고    scopus 로고
    • The role of Ser129 phosphorylation of alpha-synuclein in neurodegeneration of Parkinson's disease: A review of in vivo models
    • doi: 10.1515/revneuro-2012-0071
    • Sato, H., Kato, T., and Arawaka, S. (2013). The role of Ser129 phosphorylation of alpha-synuclein in neurodegeneration of Parkinson's disease: a review of in vivo models. Rev. Neurosci. 24, 115-123. doi: 10.1515/revneuro-2012-0071
    • (2013) Rev. Neurosci , vol.24 , pp. 115-123
    • Sato, H.1    Kato, T.2    Arawaka, S.3
  • 143
    • 0034622242 scopus 로고    scopus 로고
    • Casein kinase 1 delta is associated with pathological accumulation of tau in several neurodegenerative diseases
    • doi: 10.1016/S0197-4580(00)00110-X
    • Schwab, C., Demaggio, A. J., Ghoshal, N., Binder, L. I., Kuret, J., and Mcgeer, P. L. (2000). Casein kinase 1 delta is associated with pathological accumulation of tau in several neurodegenerative diseases. Neurobiol. Aging 21, 503-510. doi: 10.1016/S0197-4580(00)00110-X
    • (2000) Neurobiol. Aging , vol.21 , pp. 503-510
    • Schwab, C.1    Demaggio, A.J.2    Ghoshal, N.3    Binder, L.I.4    Kuret, J.5    McGeer, P.L.6
  • 144
    • 13244249573 scopus 로고    scopus 로고
    • Polo-like kinases in the nervous system
    • doi: 10.1038/sj.onc.1208277
    • Seeburg, D. P., Pak, D., and Sheng, M. (2005). Polo-like kinases in the nervous system. Oncogene 24, 292-298. doi: 10.1038/sj.onc.1208277
    • (2005) Oncogene , vol.24 , pp. 292-298
    • Seeburg, D.P.1    Pak, D.2    Sheng, M.3
  • 145
    • 84865196862 scopus 로고    scopus 로고
    • Large-scale replication and heterogeneity in Parkinson disease genetic loci
    • doi: 10.1212/WNL.0b013e318264e353
    • Sharma, M., Ioannidis, J. P., Aasly, J. O., Annesi, G., Brice, A., Van Broeckhoven, C., et al. (2012). Large-scale replication and heterogeneity in Parkinson disease genetic loci. Neurology 79, 659-667. doi: 10.1212/WNL.0b013e318264e353
    • (2012) Neurology , vol.79 , pp. 659-667
    • Sharma, M.1    Ioannidis, J.P.2    Aasly, J.O.3    Annesi, G.4    Brice, A.5    van Broeckhoven, C.6
  • 146
    • 79960661378 scopus 로고    scopus 로고
    • LRRK2 expression in idiopathic and G2019S positive Parkinson's disease subjects: Amorphological and quantitative study
    • doi: 10.1111/j.1365-2990.2011.01187.x
    • Sharma, S., Bandopadhyay, R., Lashley, T., Renton, A. E., Kingsbury, A. E., Kumaran, R., et al. (2011). LRRK2 expression in idiopathic and G2019S positive Parkinson's disease subjects: amorphological and quantitative study. Neuropathol. Appl. Neurobiol. 37, 777-790. doi: 10.1111/j.1365-2990.2011.01187.x
    • (2011) Neuropathol. Appl. Neurobiol , vol.37 , pp. 777-790
    • Sharma, S.1    Bandopadhyay, R.2    Lashley, T.3    Renton, A.E.4    Kingsbury, A.E.5    Kumaran, R.6
  • 147
    • 84874720265 scopus 로고    scopus 로고
    • Ser1292 autophosphorylation is an indicator of LRRK2 kinase activity and contributes to the cellular effects of PD mutations
    • doi: 10.1126/scitranslmed.3004485
    • Sheng, Z., Zhang, S., Bustos, D., Kleinheinz, T., Le Pichon, C. E., Dominguez, S. L., et al. (2012). Ser1292 autophosphorylation is an indicator of LRRK2 kinase activity and contributes to the cellular effects of PD mutations. Sci. Transl. Med. 4, 164ra161. doi: 10.1126/scitranslmed.3004485
    • (2012) Sci. Transl. Med , vol.4
    • Sheng, Z.1    Zhang, S.2    Bustos, D.3    Kleinheinz, T.4    Le Pichon, C.E.5    Dominguez, S.L.6
  • 148
    • 70549088602 scopus 로고    scopus 로고
    • Genome-wide association study reveals genetic risk underlying Parkinson's disease
    • doi: 10.1038/ng.487
    • Simon-Sanchez, J., Schulte, C., Bras, J. M., Sharma, M., Gibbs, J. R., Berg, D., et al. (2009). Genome-wide association study reveals genetic risk underlying Parkinson's disease. Nat. Genet. 41, 1308-1312. doi: 10.1038/ng.487
    • (2009) Nat. Genet , vol.41 , pp. 1308-1312
    • Simon-Sanchez, J.1    Schulte, C.2    Bras, J.M.3    Sharma, M.4    Gibbs, J.R.5    Berg, D.6
  • 149
    • 0344823864 scopus 로고    scopus 로고
    • Cyclin-dependent kinase 5 is a mediator of dopaminergic neuron loss in a mouse model ofParkinson's disease
    • doi: 10.1073/pnas.2232515100
    • Smith, P. D., Crocker, S. J., Jackson-Lewis, V., Jordan-Sciutto, K. L., Hayley, S., Mount, M. P., et al. (2003). Cyclin-dependent kinase 5 is a mediator of dopaminergic neuron loss in a mouse model ofParkinson's disease. Proc. Natl. Acad. Sci. U.S.A. 100, 13650-13655. doi: 10.1073/pnas.2232515100
    • (2003) Proc. Natl. Acad. Sci. U.S.A , vol.100 , pp. 13650-13655
    • Smith, P.D.1    Crocker, S.J.2    Jackson-Lewis, V.3    Jordan-Sciutto, K.L.4    Hayley, S.5    Mount, M.P.6
  • 150
    • 70350550208 scopus 로고    scopus 로고
    • Beclin 1 gene transfer activates autophagy and ameliorates the neurodegenerative pathology in alpha-synuclein models of Parkinson's and Lewy body diseases
    • doi: 10.1523/JNEUROSCI.4390-09.2009
    • Spencer, B., Potkar, R., Trejo, M., Rockenstein, E., Patrick, C., Gindi, R., et al. (2009). Beclin 1 gene transfer activates autophagy and ameliorates the neurodegenerative pathology in alpha-synuclein models of Parkinson's and Lewy body diseases. J. Neurosci. 29, 13578-13588. doi: 10.1523/JNEUROSCI.4390-09.2009
    • (2009) J. Neurosci , vol.29 , pp. 13578-13588
    • Spencer, B.1    Potkar, R.2    Trejo, M.3    Rockenstein, E.4    Patrick, C.5    Gindi, R.6
  • 152
    • 80053997817 scopus 로고    scopus 로고
    • Neonatal lethality in knockout mice expressing the kinase-dead form of the gefitinib target GAK is caused by pulmonary dysfunction
    • doi: 10.1371/journal.pone.0026034
    • Tabara, H., Naito, Y., Ito, A., Katsuma, A., Sakurai, M. A., Ohno, S., et al. (2011). Neonatal lethality in knockout mice expressing the kinase-dead form of the gefitinib target GAK is caused by pulmonary dysfunction. PLoS ONE 6:e26034. doi: 10.1371/journal.pone.0026034
    • (2011) PLoS ONE , vol.6
    • Tabara, H.1    Naito, Y.2    Ito, A.3    Katsuma, A.4    Sakurai, M.A.5    Ohno, S.6
  • 153
    • 33845372239 scopus 로고    scopus 로고
    • Identification of G-protein coupled receptor kinase 2 in paired helical filaments and neurofibrillary tangles
    • doi: 10.1097/01.jnen.0000248542.82681.12
    • Takahashi, M., Uchikado, H., Caprotti, D., Weidenheim, K. M., Dickson, D. W., Ksiezak-Reding, H., et al. (2006). Identification of G-protein coupled receptor kinase 2 in paired helical filaments and neurofibrillary tangles. J. Neuropathol. Exp. Neurol. 65, 1157-1169. doi: 10.1097/01.jnen.0000248542.82681.12
    • (2006) J. Neuropathol. Exp. Neurol , vol.65 , pp. 1157-1169
    • Takahashi, M.1    Uchikado, H.2    Caprotti, D.3    Weidenheim, K.M.4    Dickson, D.W.5    Ksiezak-Reding, H.6
  • 154
    • 84866652723 scopus 로고    scopus 로고
    • The GTPase function of LRRK2
    • doi: 10.1042/BST20120133
    • Taymans, J. M. (2012). The GTPase function of LRRK2. Biochem. Soc. Trans. 40, 1063-1069. doi: 10.1042/BST20120133
    • (2012) Biochem. Soc. Trans , vol.40 , pp. 1063-1069
    • Taymans, J.M.1
  • 155
    • 33745917404 scopus 로고    scopus 로고
    • Distribution of PINK1 and LRRK2 in rat and mouse brain
    • doi: 10.1111/j.1471-4159.2006.03919.x
    • Taymans, J. M., Van Den Haute, C., and Baekelandt, V. (2006). Distribution of PINK1 and LRRK2 in rat and mouse brain. J. Neurochem. 98, 951-961. doi: 10.1111/j.1471-4159.2006.03919.x
    • (2006) J. Neurochem , vol.98 , pp. 951-961
    • Taymans, J.M.1    Van Den Haute, C.2    Baekelandt, V.3
  • 156
    • 80051611506 scopus 로고    scopus 로고
    • LRRK2 kinase activity is dependent on LRRK2 GTP binding capacity but independent of LRRK2 GTP binding
    • doi: 10.1371/journal.pone.0023207
    • Taymans, J. M., Vancraenenbroeck, R., Ollikainen, P., Beilina, A., Lobbestael, E., De Maeyer, M., et al. (2011). LRRK2 kinase activity is dependent on LRRK2 GTP binding capacity but independent of LRRK2 GTP binding. PLoS ONE 6:e23207. doi: 10.1371/journal.pone.0023207
    • (2011) PLoS ONE , vol.6
    • Taymans, J.M.1    Vancraenenbroeck, R.2    Ollikainen, P.3    Beilina, A.4    Lobbestael, E.5    de Maeyer, M.6
  • 157
    • 43549083894 scopus 로고    scopus 로고
    • MAPKAP kinase 2-deficiency prevents neurons from cell death by reducing neuroinflammation-relevance in a mouse model of Parkinson's disease
    • doi: 10.1111/j.1471-4159.2008. 05310.x
    • Thomas, T., Timmer, M., Cesnulevicius, K., Hitti, E., Kotlyarov, A., and Gaestel, M. (2008). MAPKAP kinase 2-deficiency prevents neurons from cell death by reducing neuroinflammation-relevance in a mouse model of Parkinson's disease. J. Neurochem. 105, 2039-2052. doi: 10.1111/j.1471-4159.2008. 05310.x
    • (2008) J. Neurochem , vol.105 , pp. 2039-2052
    • Thomas, T.1    Timmer, M.2    Cesnulevicius, K.3    Hitti, E.4    Kotlyarov, A.5    Gaestel, M.6
  • 158
    • 70350347175 scopus 로고    scopus 로고
    • Akt signal transduction dysfunction in Parkinson's disease
    • doi: 10.1016/j.neulet.2009.09.055
    • Timmons, S., Coakley, M. F., Moloney, A. M., and O' Neill, C. (2009). Akt signal transduction dysfunction in Parkinson's disease. Neurosci. Lett. 467, 30-35. doi: 10.1016/j.neulet.2009.09.055
    • (2009) Neurosci. Lett , vol.467 , pp. 30-35
    • Timmons, S.1    Coakley, M.F.2    Moloney, A.M.3    O'Neill, C.4
  • 159
    • 0038054032 scopus 로고    scopus 로고
    • Effects of GDNF on 6-OHDA-induced death in a dopaminergic cell line: Modulation by inhibitors of PI3 kinase and MEK
    • doi: 10.1002/jnr.10632
    • Ugarte, S. D., Lin, E., Klann, E., Zigmond, M. J., and Perez, R. G. (2003). Effects of GDNF on 6-OHDA-induced death in a dopaminergic cell line: modulation by inhibitors of PI3 kinase and MEK. J. Neurosci. Res. 73, 105-112. doi: 10.1002/jnr.10632
    • (2003) J. Neurosci. Res , vol.73 , pp. 105-112
    • Ugarte, S.D.1    Lin, E.2    Klann, E.3    Zigmond, M.J.4    Perez, R.G.5
  • 160
    • 0032528534 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a novel Ste20-related protein kinase enriched in neurons and transporting epithelia
    • doi: 10.1006/abbi.1998.0736
    • Ushiro, H., Tsutsumi, T., Suzuki, K., Kayahara, T., and Nakano, K. (1998). Molecular cloning and characterization of a novel Ste20-related protein kinase enriched in neurons and transporting epithelia. Arch. Biochem. Biophys. 355, 233-240. doi: 10.1006/abbi.1998.0736
    • (1998) Arch. Biochem. Biophys , vol.355 , pp. 233-240
    • Ushiro, H.1    Tsutsumi, T.2    Suzuki, K.3    Kayahara, T.4    Nakano, K.5
  • 161
    • 2442668926 scopus 로고    scopus 로고
    • Hereditary early-onset Parkinson's disease caused by mutations in PINK1
    • doi: 10.1126/science.1096284
    • Valente, E. M., Abou-Sleiman, P. M., Caputo, V., Muqit, M. M., Harvey, K., Gispert, S., et al. (2004). Hereditary early-onset Parkinson's disease caused by mutations in PINK1. Science 304, 1158-1160. doi: 10.1126/science.1096284
    • (2004) Science , vol.304 , pp. 1158-1160
    • Valente, E.M.1    Abou-Sleiman, P.M.2    Caputo, V.3    Muqit, M.M.4    Harvey, K.5    Gispert, S.6
  • 162
    • 84871489685 scopus 로고    scopus 로고
    • Changes in properties of serine 129 phosphorylatedalpha-synuclein with progression ofLewy-type histopathologyin human brains
    • doi: 10.1016/j.expneurol.2012.11.020
    • Walker, D. G., Lue, L. F., Adler, C. H., Shill, H. A., Caviness, J. N., Sabbagh, M. N., et al. (2013). Changes in properties of serine 129 phosphorylatedalpha-synuclein with progression ofLewy-type histopathologyin human brains. Exp. Neurol. 240, 190-204. doi: 10.1016/j.expneurol.2012.11.020
    • (2013) Exp. Neurol , vol.240 , pp. 190-204
    • Walker, D.G.1    Lue, L.F.2    Adler, C.H.3    Shill, H.A.4    Caviness, J.N.5    Sabbagh, M.N.6
  • 163
    • 9144220172 scopus 로고    scopus 로고
    • SP600125, a new JNK inhibitor, protects dopaminergic neurons in the MPTP model of Parkinson's disease
    • doi: 10.1016/j.neures.2003.10.012
    • Wang, W., Shi, L., Xie, Y., Ma, C., Li, W., Su, X., et al. (2004). SP600125, a new JNK inhibitor, protects dopaminergic neurons in the MPTP model of Parkinson's disease. Neurosci. Res. 48, 195-202. doi: 10.1016/j.neures.2003.10.012
    • (2004) Neurosci. Res , vol.48 , pp. 195-202
    • Wang, W.1    Shi, L.2    Xie, Y.3    Ma, C.4    Li, W.5    Su, X.6
  • 164
    • 34249689633 scopus 로고    scopus 로고
    • Inhibition of glycogen synthase kinase-3beta protects dopaminergic neurons from MPTP toxicity
    • doi: 10.1016/j.neuropharm.2007.03.017
    • Wang, W., Yang, Y., Ying, C., Li, W., Ruan, H., Zhu, X., et al. (2007). Inhibition of glycogen synthase kinase-3beta protects dopaminergic neurons from MPTP toxicity. Neuropharmacology 52, 1678-1684. doi: 10.1016/j.neuropharm.2007.03.017
    • (2007) Neuropharmacology , vol.52 , pp. 1678-1684
    • Wang, W.1    Yang, Y.2    Ying, C.3    Li, W.4    Ruan, H.5    Zhu, X.6
  • 165
    • 58549108489 scopus 로고    scopus 로고
    • From the Cover: Whole-genome association studyidentifies STK39 as a hypertension susceptibility gene
    • doi: 10.1073/pnas.0808358106
    • Wang, Y., O'connell, J. R., Mcardle, P. F., Wade, J. B., Dorff, S. E., Shah, S. J., et al. (2009a). From the Cover: Whole-genome association studyidentifies STK39 as a hypertension susceptibility gene. Proc. Natl. Acad. Sci. U.S.A. 106, 226-231. doi: 10.1073/pnas.0808358106
    • (2009) Proc. Natl. Acad. Sci. U.S.A , vol.106 , pp. 226-231
    • Wang, Y.1    O'Connell, J.R.2    McArdle, P.F.3    Wade, J.B.4    Dorff, S.E.5    Shah, S.J.6
  • 166
    • 69549127950 scopus 로고    scopus 로고
    • JNK inhibitor protects dopaminergic neurons by reducing COX-2 expression in the MPTP mouse model of subacute Parkinson's disease
    • doi: 10.1016/j.jns.2009.06.034
    • Wang, Y., Zhang, Y., Wei, Z., Li, H., Zhou, H., Zhang, Z., et al. (2009b). JNK inhibitor protects dopaminergic neurons by reducing COX-2 expression in the MPTP mouse model of subacute Parkinson's disease. J. Neurol. Sci. 285,172-177. doi: 10.1016/j.jns.2009.06.034
    • (2009) J. Neurol. Sci , vol.285 , pp. 172-177
    • Wang, Y.1    Zhang, Y.2    Wei, Z.3    Li, H.4    Zhou, H.5    Zhang, Z.6
  • 167
    • 68249153855 scopus 로고    scopus 로고
    • Leucine-rich repeat kinase 2 expression leads to aggresome formation that is not associated with alpha-synuclein inclusions
    • doi: 10.1097/NEN.0b013e3181aaf4fd
    • Waxman, E. A., Covy, J. P., Bukh, I., Li, X., Dawson, T. M., and Giasson, B. I. (2009). Leucine-rich repeat kinase 2 expression leads to aggresome formation that is not associated with alpha-synuclein inclusions. J. Neuropathol. Exp. Neurol. 68, 785-796. doi: 10.1097/NEN.0b013e3181aaf4fd
    • (2009) J. Neuropathol. Exp. Neurol , vol.68 , pp. 785-796
    • Waxman, E.A.1    Covy, J.P.2    Bukh, I.3    Li, X.4    Dawson, T.M.5    Giasson, B.I.6
  • 168
    • 43249108653 scopus 로고    scopus 로고
    • Specificity and regulation of casein kinase- mediated phosphorylation of alpha-synuclein
    • doi: 10.1097/NEN.0b013e31816fc995
    • Waxman, E. A., and Giasson, B. I. (2008). Specificity and regulation of casein kinase- mediated phosphorylation of alpha-synuclein. J. Neuropathol. Exp. Neurol. 67, 402-416. doi: 10.1097/NEN.0b013e31816fc995
    • (2008) J. Neuropathol. Exp. Neurol , vol.67 , pp. 402-416
    • Waxman, E.A.1    Giasson, B.I.2
  • 169
    • 78650203006 scopus 로고    scopus 로고
    • Characterization of kinases involved in the phosphorylation of aggregatedalpha-synuclein
    • doi: 10.1002/jnr.22537
    • Waxman, E. A., and Giasson, B. I. (2011). Characterization of kinases involved in the phosphorylation of aggregatedalpha-synuclein. J. Neurosci. Res. 89,231-247. doi: 10.1002/jnr.22537
    • (2011) J. Neurosci. Res , vol.89 , pp. 231-247
    • Waxman, E.A.1    Giasson, B.I.2
  • 170
    • 84901648685 scopus 로고    scopus 로고
    • Differential LRRK2 expression in the cortex, striatum, and substantia nigra in transgenic and nontransgenic rodents
    • Spc1. doi: 10.1002/cne.23583
    • West, A. B., Cowell, R. M., Daher, J. P., Moehle, M. S., Hinkle, K. M., Melrose, H. L., et al. (2014). Differential LRRK2 expression in the cortex, striatum, and substantia nigra in transgenic and nontransgenic rodents. J. Comp. Neurol. 522, Spc1. doi: 10.1002/cne.23583
    • (2014) J. Comp. Neurol , vol.522
    • West, A.B.1    Cowell, R.M.2    Daher, J.P.3    Moehle, M.S.4    Hinkle, K.M.5    Melrose, H.L.6
  • 171
    • 28044460070 scopus 로고    scopus 로고
    • Parkinson's disease-associated mutations in leucine-rich repeat kinase 2 augment kinase activity
    • doi: 10.1073/pnas.0507360102
    • West, A. B., Moore, D. J., Biskup, S., Bugayenko, A., Smith, W. W., Ross, C. A., et al. (2005). Parkinson's disease-associated mutations in leucine-rich repeat kinase 2 augment kinase activity. Proc. Natl. Acad. Sci. U.S.A. 102, 16842-16847. doi: 10.1073/pnas.0507360102
    • (2005) Proc. Natl. Acad. Sci. U.S.A , vol.102 , pp. 16842-16847
    • West, A.B.1    Moore, D.J.2    Biskup, S.3    Bugayenko, A.4    Smith, W.W.5    Ross, C.A.6
  • 172
    • 77955664249 scopus 로고    scopus 로고
    • Elevated tauopathy and alpha-synuclein pathology in postmortem Parkinson's disease brains with and without dementia
    • doi: 10.1016/j.expneurol.2010.06.017
    • Wills, J., Jones, J., Haggerty, T., Duka, V., Joyce, J. N., and Sidhu, A. (2010). Elevated tauopathy and alpha-synuclein pathology in postmortem Parkinson's disease brains with and without dementia. Exp. Neurol. 225, 210-218. doi: 10.1016/j.expneurol.2010.06.017
    • (2010) Exp. Neurol , vol.225 , pp. 210-218
    • Wills, J.1    Jones, J.2    Haggerty, T.3    Duka, V.4    Joyce, J.N.5    Sidhu, A.6
  • 173
    • 13244253709 scopus 로고    scopus 로고
    • Differential regulation of polo-like kinase 1, 2, 3,and4geneexpressioninmammaliancellsandtissues
    • doi: 10.1038/sj.onc.1208219
    • Winkles, J.A., andAlberts, G. F. (2005). Differential regulation of polo-like kinase 1, 2, 3,and4geneexpressioninmammaliancellsandtissues. Oncogene 24,260-266. doi: 10.1038/sj.onc.1208219
    • (2005) Oncogene , vol.24 , pp. 260-266
    • Winkles, J.A.1    Andalberts, G.F.2
  • 174
    • 84864197915 scopus 로고    scopus 로고
    • Discovery of catalytically active orthologues of the Parkinson's disease kinase PINK1: Analysis of substrate specificity and impact of mutations
    • doi: 10.1098/rsob.110012
    • Woodroof, H. I., Pogson, J. H., Begley, M., Cantley, L. C., Deak, M., Campbell, D. G., et al. (2011). Discovery of catalytically active orthologues of the Parkinson's disease kinase PINK1: analysis of substrate specificity and impact of mutations. Open Biol. 1, 110012. doi: 10.1098/rsob.110012
    • (2011) Open Biol , vol.1 , pp. 110012
    • Woodroof, H.I.1    Pogson, J.H.2    Begley, M.3    Cantley, L.C.4    Deak, M.5    Campbell, D.G.6
  • 175
    • 80052359850 scopus 로고    scopus 로고
    • Resveratrol-activated AMPK/SIRT1/autophagy in cellular models of Parkinson's disease
    • doi: 10.1159/000328516
    • Wu, Y., Li, X., Zhu, J. X., Xie, W., Le, W., Fan, Z., et al. (2011). Resveratrol-activated AMPK/SIRT1/autophagy in cellular models of Parkinson's disease. Neurosignals 19, 163-174. doi: 10.1159/000328516
    • (2011) Neurosignals , vol.19 , pp. 163-174
    • Wu, Y.1    Li, X.2    Zhu, J.X.3    Xie, W.4    Le, W.5    Fan, Z.6
  • 176
    • 36749097843 scopus 로고    scopus 로고
    • Neuroprotection with pioglitazone against LPS insult on dopaminergic neurons may be associated with its inhibition of NF- kappaB and JNK activation and suppression of COX-2 activity
    • doi: 10.1016/j.jneuroim.2007.09.029
    • Xing, B., Liu, M., and Bing, G. (2007). Neuroprotection with pioglitazone against LPS insult on dopaminergic neurons may be associated with its inhibition of NF- kappaB and JNK activation and suppression of COX-2 activity. J. Neuroimmunol. 192, 89-98. doi: 10.1016/j.jneuroim.2007.09.029
    • (2007) J. Neuroimmunol , vol.192 , pp. 89-98
    • Xing, B.1    Liu, M.2    Bing, G.3
  • 177
    • 83055186447 scopus 로고    scopus 로고
    • Potential autophagy enhancers attenuate rotenone-induced toxicity in SH-SY5Y
    • doi: 10.1016/j.neuroscience.2011.10.031
    • Xiong, N., Jia, M., Chen, C., Xiong, J., Zhang, Z., Huang, J., et al. (2011). Potential autophagy enhancers attenuate rotenone-induced toxicity in SH-SY5Y. Neuroscience 199,292-302. doi: 10.1016/j.neuroscience.2011.10.031
    • (2011) Neuroscience , vol.199 , pp. 292-302
    • Xiong, N.1    Jia, M.2    Chen, C.3    Xiong, J.4    Zhang, Z.5    Huang, J.6
  • 178
    • 33847374563 scopus 로고    scopus 로고
    • Cloning and characterization of a new intestinal inflammation-associated colonic epithelial Ste20-related protein kinase isoform
    • doi: 10.1016/j.bbaexp.2007.01.003
    • Yan, Y., Nguyen, H., Dalmasso, G., Sitaraman, S. V., and Merlin, D. (2007). Cloning and characterization of a new intestinal inflammation-associated colonic epithelial Ste20-related protein kinase isoform. Biochim. Biophys. Acta 1769, 106-116. doi: 10.1016/j.bbaexp.2007.01.003
    • (2007) Biochim. Biophys. Acta , vol.1769 , pp. 106-116
    • Yan, Y.1    Nguyen, H.2    Dalmasso, G.3    Sitaraman, S.V.4    Merlin, D.5
  • 179
    • 57749173844 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3 regulates microglial migration, inflammation, and inflammation-induced neurotoxicity
    • doi: 10.1016/j.cellsig.2008.10.014
    • Yuskaitis, C. J., and Jope, R. S. (2009). Glycogen synthase kinase-3 regulates microglial migration, inflammation, and inflammation-induced neurotoxicity. Cell. Signal. 21, 264-273. doi: 10.1016/j.cellsig.2008.10.014
    • (2009) Cell. Signal , vol.21 , pp. 264-273
    • Yuskaitis, C.J.1    Jope, R.S.2
  • 180
    • 84878302230 scopus 로고    scopus 로고
    • Secalonic acidAprotects dopaminergic neurons from 1-methyl-4-phenylpyridinium (MPP(+))-induced cell deathviathe mitochondrialapoptoticpathway
    • doi: 10.1016/j.ejphar.2013.04.029
    • Zhai, A., Zhu, X., Wang, X., Chen, R., and Wang, H. (2013). Secalonic acidAprotects dopaminergic neurons from 1-methyl-4-phenylpyridinium (MPP(+))-induced cell deathviathe mitochondrialapoptoticpathway. Eur. J. Pharmacol. 713, 58-67. doi: 10.1016/j.ejphar.2013.04.029
    • (2013) Eur. J. Pharmacol , vol.713 , pp. 58-67
    • Zhai, A.1    Zhu, X.2    Wang, X.3    Chen, R.4    Wang, H.5
  • 181
    • 79958169700 scopus 로고    scopus 로고
    • Changes in the solubilityand phosphorylation of alpha-synuclein over the course ofParkinson's disease
    • doi: 10.1007/s00401-011- 0815-1
    • Zhou, J., Broe, M., Huang, Y., Anderson, J. P., Gai, W. P., Milward, E. A., et al. (2011). Changes in the solubilityand phosphorylation of alpha-synuclein over the course ofParkinson's disease. Acta Neuropathol. 121, 695-704. doi: 10.1007/s00401-011- 0815-1
    • (2011) Acta Neuropathol , vol.121 , pp. 695-704
    • Zhou, J.1    Broe, M.2    Huang, Y.3    Anderson, J.P.4    Gai, W.P.5    Milward, E.A.6
  • 182
    • 0242499488 scopus 로고    scopus 로고
    • Localization of phosphorylated ERK/MAP kinases to mitochondria and autophagosomes in Lewy body diseases
    • doi: 10.1111/j.1750-3639.2003.tb 00478.x
    • Zhu, J. H., Guo, F., Shelburne, J., Watkins, S., and Chu, C. T. (2003). Localization of phosphorylated ERK/MAP kinases to mitochondria and autophagosomes in Lewy body diseases. Brain Pathol. 13, 473-481 doi: 10.1111/j.1750-3639.2003.tb 00478.x
    • (2003) Brain Pathol , vol.13 , pp. 473-481
    • Zhu, J.H.1    Guo, F.2    Shelburne, J.3    Watkins, S.4    Chu, C.T.5
  • 183
    • 0036899278 scopus 로고    scopus 로고
    • Cytoplasmic aggregates of phosphorylated extracellular signal-regulated protein kinases in Lewy body diseases
    • doi: 10.1016/S0002-9440(10) 64487-2
    • Zhu, J. H., Kulich, S. M., Oury, T. D., and Chu, C. T. (2002). Cytoplasmic aggregates of phosphorylated extracellular signal-regulated protein kinases in Lewy body diseases. Am. J. Pathol. 161, 2087-2098. doi: 10.1016/S0002-9440(10) 64487-2
    • (2002) Am. J. Pathol , vol.161 , pp. 2087-2098
    • Zhu, J.H.1    Kulich, S.M.2    Oury, T.D.3    Chu, C.T.4
  • 184
    • 8844233579 scopus 로고    scopus 로고
    • Mutations in LRRK2 cause autosomal-dominant parkinsonismwith pleomorphic pathology
    • doi: 10.1016/j.neuron.2004.11.005
    • Zimprich, A., Biskup, S., Leitner, P., Lichtner, P., Farrer, M., Lincoln, S., et al. (2004). Mutations in LRRK2 cause autosomal-dominant parkinsonismwith pleomorphic pathology. Neuron 44, 601-607. doi: 10.1016/j.neuron.2004.11.005
    • (2004) Neuron , vol.44 , pp. 601-607
    • Zimprich, A.1    Biskup, S.2    Leitner, P.3    Lichtner, P.4    Farrer, M.5    Lincoln, S.6


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