메뉴 건너뛰기




Volumn 78, Issue , 2015, Pages 172-195

Progressive dopaminergic alterations and mitochondrial abnormalities in LRRK2 G2019S knock-in mice

Author keywords

Dopamine; Gene targeted mouse model; Microdialysis; Mitochondria; Parkinson's disease

Indexed keywords

DOPAMINE; LEUCINE RICH REPEAT KINASE 2; LRRK2 PROTEIN, MOUSE; MAPT PROTEIN, MOUSE; PROTEIN SERINE THREONINE KINASE; TAU PROTEIN;

EID: 84928594767     PISSN: 09699961     EISSN: 1095953X     Source Type: Journal    
DOI: 10.1016/j.nbd.2015.02.031     Document Type: Article
Times cited : (191)

References (115)
  • 1
    • 81255208412 scopus 로고    scopus 로고
    • Mutations in LRRK2 increase phosphorylation of peroxiredoxin 3 exacerbating oxidative stress-induced neuronal death
    • Angeles D.C., et al. Mutations in LRRK2 increase phosphorylation of peroxiredoxin 3 exacerbating oxidative stress-induced neuronal death. Hum. Mutat. 2011, 32:1390-1397.
    • (2011) Hum. Mutat. , vol.32 , pp. 1390-1397
    • Angeles, D.C.1
  • 2
    • 0025610514 scopus 로고
    • Dopamine release and metabolism in the rat striatum: an analysis by 'in vivo' brain microdialysis
    • Arbuthnott G.W., et al. Dopamine release and metabolism in the rat striatum: an analysis by 'in vivo' brain microdialysis. Pharmacol. Ther. 1990, 48:281-293.
    • (1990) Pharmacol. Ther. , vol.48 , pp. 281-293
    • Arbuthnott, G.W.1
  • 3
    • 84892588907 scopus 로고    scopus 로고
    • LRRK2 phosphorylates novel tau epitopes and promotes tauopathy
    • Bailey R.M., et al. LRRK2 phosphorylates novel tau epitopes and promotes tauopathy. Acta Neuropathol. 2013, 126(6):809-827. 10.1007/s00401-013-1188-4.
    • (2013) Acta Neuropathol. , vol.126 , Issue.6 , pp. 809-827
    • Bailey, R.M.1
  • 4
    • 0020956260 scopus 로고
    • Pharmacology of mesocortical dopamine neurons
    • Bannon M.J., Roth R.H. Pharmacology of mesocortical dopamine neurons. Pharmacol. Rev. 1983, 35:53-68.
    • (1983) Pharmacol. Rev. , vol.35 , pp. 53-68
    • Bannon, M.J.1    Roth, R.H.2
  • 5
    • 84893527711 scopus 로고    scopus 로고
    • Loss of leucine-rich repeat kinase 2 (LRRK2) in rats leads to progressive abnormal phenotypes in peripheral organs
    • Baptista M.A., et al. Loss of leucine-rich repeat kinase 2 (LRRK2) in rats leads to progressive abnormal phenotypes in peripheral organs. PLoS One 2013, 8:e80705.
    • (2013) PLoS One , vol.8 , pp. e80705
    • Baptista, M.A.1
  • 6
    • 84907573660 scopus 로고    scopus 로고
    • Synaptic function is modulated by LRRK2 and glutamate release is increased in cortical neurons of G2019S LRRK2 knock-in mice
    • Beccano-Kelly D.A., et al. Synaptic function is modulated by LRRK2 and glutamate release is increased in cortical neurons of G2019S LRRK2 knock-in mice. Front. Cell. Neurosci. 2014, 8:301.
    • (2014) Front. Cell. Neurosci. , vol.8 , pp. 301
    • Beccano-Kelly, D.A.1
  • 7
    • 84924455094 scopus 로고    scopus 로고
    • LRRK2 overexpression alters glutamatergic presynaptic plasticity, striatal dopamine tone, postsynaptic signal transduction, motor activity and memory
    • Beccano-Kelly D.A., et al. LRRK2 overexpression alters glutamatergic presynaptic plasticity, striatal dopamine tone, postsynaptic signal transduction, motor activity and memory. Hum. Mol. Genet. 2014, 24(5):1336-1349. 10.1093/hmg/ddu543.
    • (2014) Hum. Mol. Genet. , vol.24 , Issue.5 , pp. 1336-1349
    • Beccano-Kelly, D.A.1
  • 8
    • 84866721819 scopus 로고    scopus 로고
    • Presynaptic dysfunction in Parkinson's disease: a focus on LRRK2
    • Belluzzi E., et al. Presynaptic dysfunction in Parkinson's disease: a focus on LRRK2. Biochem. Soc. Trans. 2012, 40:1111-1116.
    • (2012) Biochem. Soc. Trans. , vol.40 , pp. 1111-1116
    • Belluzzi, E.1
  • 9
    • 77954197844 scopus 로고    scopus 로고
    • Membrane localization of LRRK2 is associated with increased formation of the highly active LRRK2 dimer and changes in its phosphorylation
    • Berger Z., et al. Membrane localization of LRRK2 is associated with increased formation of the highly active LRRK2 dimer and changes in its phosphorylation. Biochemistry 2010, 49:5511-5523.
    • (2010) Biochemistry , vol.49 , pp. 5511-5523
    • Berger, Z.1
  • 10
    • 84868156773 scopus 로고    scopus 로고
    • LRRK2 functions as a Wnt signaling scaffold, bridging cytosolic proteins and membrane-localized LRP6
    • Berwick D.C., Harvey K. LRRK2 functions as a Wnt signaling scaffold, bridging cytosolic proteins and membrane-localized LRP6. Hum. Mol. Genet. 2012, 21:4966-4979.
    • (2012) Hum. Mol. Genet. , vol.21 , pp. 4966-4979
    • Berwick, D.C.1    Harvey, K.2
  • 11
    • 84872691988 scopus 로고    scopus 로고
    • Mutant LRRK2 elicits calcium imbalance and depletion of dendritic mitochondria in neurons
    • Cherra S.J., et al. Mutant LRRK2 elicits calcium imbalance and depletion of dendritic mitochondria in neurons. Am. J. Pathol. 2013, 182:474-484.
    • (2013) Am. J. Pathol. , vol.182 , pp. 474-484
    • Cherra, S.J.1
  • 12
    • 84901669528 scopus 로고    scopus 로고
    • LRRK2 kinase activity regulates synaptic vesicle trafficking and neurotransmitter release through modulation of LRRK2 macro-molecular complex
    • Cirnaru M.D., et al. LRRK2 kinase activity regulates synaptic vesicle trafficking and neurotransmitter release through modulation of LRRK2 macro-molecular complex. Front. Mol. Neurosci. 2014, 7:49.
    • (2014) Front. Mol. Neurosci. , vol.7 , pp. 49
    • Cirnaru, M.D.1
  • 13
    • 84863584524 scopus 로고    scopus 로고
    • Pharmacological rescue of mitochondrial deficits in iPSC-derived neural cells from patients with familial Parkinson's disease
    • Cooper O., et al. Pharmacological rescue of mitochondrial deficits in iPSC-derived neural cells from patients with familial Parkinson's disease. Sci. Transl. Med. 2012, 4:141ra90.
    • (2012) Sci. Transl. Med. , vol.4 , pp. 141-190
    • Cooper, O.1
  • 14
    • 84872079731 scopus 로고    scopus 로고
    • Amphetamine paradoxically augments exocytotic dopamine release and phasic dopamine signals
    • Daberkow D.P., et al. Amphetamine paradoxically augments exocytotic dopamine release and phasic dopamine signals. J. Neurosci. 2013, 33:452-463.
    • (2013) J. Neurosci. , vol.33 , pp. 452-463
    • Daberkow, D.P.1
  • 15
    • 79251517788 scopus 로고    scopus 로고
    • In vivo brain microdialysis: advances in neuropsychopharmacology and drug discovery
    • Darvesh A.S., et al. In vivo brain microdialysis: advances in neuropsychopharmacology and drug discovery. Expert Opin. Drug Discov. 2011, 6:109-127.
    • (2011) Expert Opin. Drug Discov. , vol.6 , pp. 109-127
    • Darvesh, A.S.1
  • 16
    • 84879024830 scopus 로고    scopus 로고
    • Comprehensive characterization and optimization of anti-LRRK2 (leucine-rich repeat kinase 2) monoclonal antibodies
    • Davies P., et al. Comprehensive characterization and optimization of anti-LRRK2 (leucine-rich repeat kinase 2) monoclonal antibodies. Biochem. J. 2013, 453:101-113.
    • (2013) Biochem. J. , vol.453 , pp. 101-113
    • Davies, P.1
  • 17
    • 40349101849 scopus 로고    scopus 로고
    • Structure of the ROC domain from the Parkinson's disease-associated leucine-rich repeat kinase 2 reveals a dimeric GTPase
    • Deng J., et al. Structure of the ROC domain from the Parkinson's disease-associated leucine-rich repeat kinase 2 reveals a dimeric GTPase. Proc. Natl. Acad. Sci. U. S. A. 2008, 105:1499-1504.
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 1499-1504
    • Deng, J.1
  • 18
    • 33746079596 scopus 로고    scopus 로고
    • A common missense variant in the LRRK2 gene, Gly2385Arg, associated with Parkinson's disease risk in Taiwan
    • Di Fonzo A., et al. A common missense variant in the LRRK2 gene, Gly2385Arg, associated with Parkinson's disease risk in Taiwan. Neurogenetics 2006, 7:133-138.
    • (2006) Neurogenetics , vol.7 , pp. 133-138
    • Di Fonzo, A.1
  • 19
    • 78649815388 scopus 로고    scopus 로고
    • Early deficits in synaptic mitochondria in an Alzheimer's disease mouse model
    • Du H., et al. Early deficits in synaptic mitochondria in an Alzheimer's disease mouse model. Proc. Natl. Acad. Sci. U. S. A. 2010, 107:18670-18675.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 18670-18675
    • Du, H.1
  • 20
    • 78751522558 scopus 로고    scopus 로고
    • A rat model of progressive nigral neurodegeneration induced by the Parkinson's disease-associated G2019S mutation in LRRK2
    • Dusonchet J., et al. A rat model of progressive nigral neurodegeneration induced by the Parkinson's disease-associated G2019S mutation in LRRK2. J. Neurosci. 2011, 31:907-912.
    • (2011) J. Neurosci. , vol.31 , pp. 907-912
    • Dusonchet, J.1
  • 21
    • 33847267765 scopus 로고    scopus 로고
    • Lrrk2 G2385R is an ancestral risk factor for Parkinson's disease in Asia
    • Farrer M.J., et al. Lrrk2 G2385R is an ancestral risk factor for Parkinson's disease in Asia. Parkinsonism Relat. Disord. 2007, 13:89-92.
    • (2007) Parkinsonism Relat. Disord. , vol.13 , pp. 89-92
    • Farrer, M.J.1
  • 22
    • 84860222537 scopus 로고    scopus 로고
    • Regulation of physiologic actions of LRRK2: focus on autophagy
    • Ferree A., et al. Regulation of physiologic actions of LRRK2: focus on autophagy. Neurodegener. Dis. 2012, 10:238-241.
    • (2012) Neurodegener. Dis. , vol.10 , pp. 238-241
    • Ferree, A.1
  • 23
    • 84861595545 scopus 로고    scopus 로고
    • Disrupted autophagy leads to dopaminergic axon and dendrite degeneration and promotes presynaptic accumulation of alpha-synuclein and LRRK2 in the brain
    • Friedman L.G., et al. Disrupted autophagy leads to dopaminergic axon and dendrite degeneration and promotes presynaptic accumulation of alpha-synuclein and LRRK2 in the brain. J. Neurosci. 2012, 32:7585-7593.
    • (2012) J. Neurosci. , vol.32 , pp. 7585-7593
    • Friedman, L.G.1
  • 24
    • 33645790701 scopus 로고    scopus 로고
    • LRRK2 expression linked to dopamine-innervated areas
    • Galter D., et al. LRRK2 expression linked to dopamine-innervated areas. Ann. Neurol. 2006, 59:714-719.
    • (2006) Ann. Neurol. , vol.59 , pp. 714-719
    • Galter, D.1
  • 25
    • 77949342539 scopus 로고    scopus 로고
    • MitoPark mice mirror the slow progression of key symptoms and L-DOPA response in Parkinson's disease
    • Galter D., et al. MitoPark mice mirror the slow progression of key symptoms and L-DOPA response in Parkinson's disease. Genes Brain Behav. 2010, 9:173-181.
    • (2010) Genes Brain Behav. , vol.9 , pp. 173-181
    • Galter, D.1
  • 26
    • 84877636702 scopus 로고    scopus 로고
    • Expression analysis of Lrrk1, Lrrk2 and Lrrk2 splice variants in mice
    • Giesert F., et al. Expression analysis of Lrrk1, Lrrk2 and Lrrk2 splice variants in mice. PLoS One 2013, 8:e63778.
    • (2013) PLoS One , vol.8 , pp. e63778
    • Giesert, F.1
  • 27
    • 84910004657 scopus 로고    scopus 로고
    • LRRK2 delays degradative receptor trafficking by impeding late endosomal budding through decreasing Rab7 activity
    • Gomez-Suaga P., et al. LRRK2 delays degradative receptor trafficking by impeding late endosomal budding through decreasing Rab7 activity. Hum. Mol. Genet. 2014, 23:6779-6796.
    • (2014) Hum. Mol. Genet. , vol.23 , pp. 6779-6796
    • Gomez-Suaga, P.1
  • 28
    • 47749114984 scopus 로고    scopus 로고
    • The Parkinson disease-associated leucine-rich repeat kinase 2 (LRRK2) is a dimer that undergoes intramolecular autophosphorylation
    • Greggio E., et al. The Parkinson disease-associated leucine-rich repeat kinase 2 (LRRK2) is a dimer that undergoes intramolecular autophosphorylation. J. Biol. Chem. 2008, 283:16906-16914.
    • (2008) J. Biol. Chem. , vol.283 , pp. 16906-16914
    • Greggio, E.1
  • 29
    • 70449732284 scopus 로고    scopus 로고
    • The Parkinson's disease kinase LRRK2 autophosphorylates its GTPase domain at multiple sites
    • Greggio E., et al. The Parkinson's disease kinase LRRK2 autophosphorylates its GTPase domain at multiple sites. Biochem. Biophys. Res. Commun. 2009, 389:449-454.
    • (2009) Biochem. Biophys. Res. Commun. , vol.389 , pp. 449-454
    • Greggio, E.1
  • 30
    • 50049104725 scopus 로고    scopus 로고
    • Phenotype, genotype, and worldwide genetic penetrance of LRRK2-associated Parkinson's disease: a case-control study
    • Healy D.G., et al. Phenotype, genotype, and worldwide genetic penetrance of LRRK2-associated Parkinson's disease: a case-control study. Lancet Neurol. 2008, 7:583-590.
    • (2008) Lancet Neurol. , vol.7 , pp. 583-590
    • Healy, D.G.1
  • 31
    • 84860310590 scopus 로고    scopus 로고
    • Regulation of presynaptic neurotransmission by macroautophagy
    • Hernandez D., et al. Regulation of presynaptic neurotransmission by macroautophagy. Neuron 2012, 74:277-284.
    • (2012) Neuron , vol.74 , pp. 277-284
    • Hernandez, D.1
  • 32
    • 80053968304 scopus 로고    scopus 로고
    • LRRK2 protein levels are determined by kinase function and are crucial for kidney and lung homeostasis in mice
    • Herzig M.C., et al. LRRK2 protein levels are determined by kinase function and are crucial for kidney and lung homeostasis in mice. Hum. Mol. Genet. 2011, 20:4209-4223.
    • (2011) Hum. Mol. Genet. , vol.20 , pp. 4209-4223
    • Herzig, M.C.1
  • 33
    • 84866145895 scopus 로고    scopus 로고
    • High LRRK2 levels fail to induce or exacerbate neuronal alpha-synucleinopathy in mouse brain
    • Herzig M.C., et al. High LRRK2 levels fail to induce or exacerbate neuronal alpha-synucleinopathy in mouse brain. PLoS One 2012, 7:e36581.
    • (2012) PLoS One , vol.7 , pp. e36581
    • Herzig, M.C.1
  • 34
    • 34250199013 scopus 로고    scopus 로고
    • Localization of Parkinson's disease-associated LRRK2 in normal and pathological human brain
    • Higashi S., et al. Localization of Parkinson's disease-associated LRRK2 in normal and pathological human brain. Brain Res. 2007, 1155:208-219.
    • (2007) Brain Res. , vol.1155 , pp. 208-219
    • Higashi, S.1
  • 35
    • 33845796537 scopus 로고    scopus 로고
    • Expression and localization of Parkinson's disease-associated leucine-rich repeat kinase 2 in the mouse brain
    • Higashi S., et al. Expression and localization of Parkinson's disease-associated leucine-rich repeat kinase 2 in the mouse brain. J. Neurochem. 2007, 100:368-381.
    • (2007) J. Neurochem. , vol.100 , pp. 368-381
    • Higashi, S.1
  • 36
    • 84877891666 scopus 로고    scopus 로고
    • Dopaminergic expression of the Parkinsonian gene LRRK2-G2019S leads to non-autonomous visual neurodegeneration, accelerated by increased neural demands for energy
    • Hindle S., et al. Dopaminergic expression of the Parkinsonian gene LRRK2-G2019S leads to non-autonomous visual neurodegeneration, accelerated by increased neural demands for energy. Hum. Mol. Genet. 2013, 22:2129-2140.
    • (2013) Hum. Mol. Genet. , vol.22 , pp. 2129-2140
    • Hindle, S.1
  • 37
    • 84861552733 scopus 로고    scopus 로고
    • LRRK2 knockout mice have an intact dopaminergic system but display alterations in exploratory and motor co-ordination behaviors
    • Hinkle K.M., et al. LRRK2 knockout mice have an intact dopaminergic system but display alterations in exploratory and motor co-ordination behaviors. Mol. Neurodegener. 2012, 7:25.
    • (2012) Mol. Neurodegener. , vol.7 , pp. 25
    • Hinkle, K.M.1
  • 38
    • 84861552733 scopus 로고    scopus 로고
    • LRRK2 knockout mice have an intact dopaminergic system but display alterations in exploratory and motor co-ordination behaviors
    • Hinkle K.M., et al. LRRK2 knockout mice have an intact dopaminergic system but display alterations in exploratory and motor co-ordination behaviors. Mol. Neurodegener. 2012, 7:25.
    • (2012) Mol. Neurodegener. , vol.7 , pp. 25
    • Hinkle, K.M.1
  • 39
    • 48849092336 scopus 로고    scopus 로고
    • LRRK2 Gly2019Ser penetrance in Arab-Berber patients from Tunisia: a case-control genetic study
    • Hulihan M.M., et al. LRRK2 Gly2019Ser penetrance in Arab-Berber patients from Tunisia: a case-control genetic study. Lancet Neurol. 2008, 7:591-594.
    • (2008) Lancet Neurol. , vol.7 , pp. 591-594
    • Hulihan, M.M.1
  • 40
    • 33748621731 scopus 로고    scopus 로고
    • Clinical features of Parkinson disease patients with homozygous leucine-rich repeat kinase 2 G2019S mutations
    • Ishihara L., et al. Clinical features of Parkinson disease patients with homozygous leucine-rich repeat kinase 2 G2019S mutations. Arch. Neurol. 2006, 63:1250-1254.
    • (2006) Arch. Neurol. , vol.63 , pp. 1250-1254
    • Ishihara, L.1
  • 41
    • 33847751421 scopus 로고    scopus 로고
    • Screening for Lrrk2 G2019S and clinical comparison of Tunisian and North American Caucasian Parkinson's disease families
    • Ishihara L., et al. Screening for Lrrk2 G2019S and clinical comparison of Tunisian and North American Caucasian Parkinson's disease families. Mov. Disord. 2007, 22:55-61.
    • (2007) Mov. Disord. , vol.22 , pp. 55-61
    • Ishihara, L.1
  • 42
    • 20144387207 scopus 로고    scopus 로고
    • Identification of a novel LRRK2 mutation linked to autosomal dominant parkinsonism: evidence of a common founder across European populations
    • Kachergus J., et al. Identification of a novel LRRK2 mutation linked to autosomal dominant parkinsonism: evidence of a common founder across European populations. Am. J. Hum. Genet. 2005, 76:672-680.
    • (2005) Am. J. Hum. Genet. , vol.76 , pp. 672-680
    • Kachergus, J.1
  • 43
    • 26444613397 scopus 로고    scopus 로고
    • Escaping Parkinson's disease: a neurologically healthy octogenarian with the LRRK2 G2019S mutation
    • Kay D.M., et al. Escaping Parkinson's disease: a neurologically healthy octogenarian with the LRRK2 G2019S mutation. Mov. Disord. 2005, 20:1077-1078.
    • (2005) Mov. Disord. , vol.20 , pp. 1077-1078
    • Kay, D.M.1
  • 44
    • 37349034239 scopus 로고    scopus 로고
    • Mitochondrial dysfunction, oxidative stress, regulation of exocytosis and their relevance to neurodegenerative diseases
    • Keating D.J. Mitochondrial dysfunction, oxidative stress, regulation of exocytosis and their relevance to neurodegenerative diseases. J. Neurochem. 2008, 104:298-305.
    • (2008) J. Neurochem. , vol.104 , pp. 298-305
    • Keating, D.J.1
  • 45
    • 0027385938 scopus 로고
    • Simple screening procedure to detect gene targeting events in embryonic stem cells
    • Kontgen F., Stewart C.L. Simple screening procedure to detect gene targeting events in embryonic stem cells. Methods Enzymol. 1993, 225:878-890.
    • (1993) Methods Enzymol. , vol.225 , pp. 878-890
    • Kontgen, F.1    Stewart, C.L.2
  • 46
    • 77956441086 scopus 로고    scopus 로고
    • Inhibitors of leucine-rich repeat kinase-2 protect against models of Parkinson's disease
    • Lee B.D., et al. Inhibitors of leucine-rich repeat kinase-2 protect against models of Parkinson's disease. Nat. Med. 2010, 16:998-1000.
    • (2010) Nat. Med. , vol.16 , pp. 998-1000
    • Lee, B.D.1
  • 47
    • 84920406808 scopus 로고    scopus 로고
    • Behavioral, neurochemical, and pathologic alterations in bacterial artificial chromosome transgenic G2019S leucine-rich repeated kinase 2 rats
    • Lee J.W., et al. Behavioral, neurochemical, and pathologic alterations in bacterial artificial chromosome transgenic G2019S leucine-rich repeated kinase 2 rats. Neurobiol. Aging 2015, 36:505-518.
    • (2015) Neurobiol. Aging , vol.36 , pp. 505-518
    • Lee, J.W.1
  • 48
    • 84856070973 scopus 로고    scopus 로고
    • LRRK2 and human disease: a complicated question or a question of complexes?
    • Lewis P.A., Manzoni C. LRRK2 and human disease: a complicated question or a question of complexes?. Sci. Signal. 2012, 5:pe2.
    • (2012) Sci. Signal. , vol.5 , pp. pe2
    • Lewis, P.A.1    Manzoni, C.2
  • 49
    • 34548621385 scopus 로고    scopus 로고
    • Leucine-rich repeat kinase 2 (LRRK2)/PARK8 possesses GTPase activity that is altered in familial Parkinson's disease R1441C/G mutants
    • Li X., et al. Leucine-rich repeat kinase 2 (LRRK2)/PARK8 possesses GTPase activity that is altered in familial Parkinson's disease R1441C/G mutants. J. Neurochem. 2007, 103:238-247.
    • (2007) J. Neurochem. , vol.103 , pp. 238-247
    • Li, X.1
  • 50
    • 67649813448 scopus 로고    scopus 로고
    • Mutant LRRK2(R1441G) BAC transgenic mice recapitulate cardinal features of Parkinson's disease
    • Li Y., et al. Mutant LRRK2(R1441G) BAC transgenic mice recapitulate cardinal features of Parkinson's disease. Nat. Neurosci. 2009, 12:826-828.
    • (2009) Nat. Neurosci. , vol.12 , pp. 826-828
    • Li, Y.1
  • 51
    • 76149134717 scopus 로고    scopus 로고
    • Enhanced striatal dopamine transmission and motor performance with LRRK2 overexpression in mice is eliminated by familial Parkinson's disease mutation G2019S
    • Li X., et al. Enhanced striatal dopamine transmission and motor performance with LRRK2 overexpression in mice is eliminated by familial Parkinson's disease mutation G2019S. J. Neurosci. 2010, 30:1788-1797.
    • (2010) J. Neurosci. , vol.30 , pp. 1788-1797
    • Li, X.1
  • 52
    • 84896522656 scopus 로고    scopus 로고
    • Parkinson disease-associated mutation R1441H in LRRK2 prolongs the "active state" of its GTPase domain
    • Liao J., et al. Parkinson disease-associated mutation R1441H in LRRK2 prolongs the "active state" of its GTPase domain. Proc. Natl. Acad. Sci. U. S. A. 2014, 111:4055-4060.
    • (2014) Proc. Natl. Acad. Sci. U. S. A. , vol.111 , pp. 4055-4060
    • Liao, J.1
  • 53
    • 72149087091 scopus 로고    scopus 로고
    • Leucine-rich repeat kinase 2 regulates the progression of neuropathology induced by Parkinson's-disease-related mutant alpha-synuclein
    • Lin X., et al. Leucine-rich repeat kinase 2 regulates the progression of neuropathology induced by Parkinson's-disease-related mutant alpha-synuclein. Neuron 2009, 64:807-827.
    • (2009) Neuron , vol.64 , pp. 807-827
    • Lin, X.1
  • 54
    • 84928634712 scopus 로고    scopus 로고
    • LRRK2 R1441G mice are more liable to dopamine depletion and locomotor inactivity
    • Liu H.F., et al. LRRK2 R1441G mice are more liable to dopamine depletion and locomotor inactivity. Ann. Clin. Transl. Neurol. 2014, 1:199-208.
    • (2014) Ann. Clin. Transl. Neurol. , vol.1 , pp. 199-208
    • Liu, H.F.1
  • 55
    • 84906572600 scopus 로고    scopus 로고
    • Genetic and pharmacological evidence that G2019S LRRK2 confers a hyperkinetic phenotype, resistant to motor decline associated with aging
    • Longo F., et al. Genetic and pharmacological evidence that G2019S LRRK2 confers a hyperkinetic phenotype, resistant to motor decline associated with aging. Neurobiol. Dis. 2014, 71:62-73.
    • (2014) Neurobiol. Dis. , vol.71 , pp. 62-73
    • Longo, F.1
  • 56
    • 33751256567 scopus 로고    scopus 로고
    • The familial Parkinsonism gene LRRK2 regulates neurite process morphology
    • MacLeod D., et al. The familial Parkinsonism gene LRRK2 regulates neurite process morphology. Neuron 2006, 52:587-593.
    • (2006) Neuron , vol.52 , pp. 587-593
    • MacLeod, D.1
  • 57
    • 84865560576 scopus 로고    scopus 로고
    • LRRK2 expression is enriched in the striosomal compartment of mouse striatum
    • Mandemakers W., et al. LRRK2 expression is enriched in the striosomal compartment of mouse striatum. Neurobiol. Dis. 2012, 48:582-593.
    • (2012) Neurobiol. Dis. , vol.48 , pp. 582-593
    • Mandemakers, W.1
  • 58
    • 84882754673 scopus 로고    scopus 로고
    • Inhibition of LRRK2 kinase activity stimulates macroautophagy
    • Manzoni C., et al. Inhibition of LRRK2 kinase activity stimulates macroautophagy. Biochim. Biophys. Acta 2013, 1833:2900-2910.
    • (2013) Biochim. Biophys. Acta , vol.1833 , pp. 2900-2910
    • Manzoni, C.1
  • 59
    • 84866510734 scopus 로고    scopus 로고
    • LRRK2 controls an EndoA phosphorylation cycle in synaptic endocytosis
    • Matta S., et al. LRRK2 controls an EndoA phosphorylation cycle in synaptic endocytosis. Neuron 2012, 75:1008-1021.
    • (2012) Neuron , vol.75 , pp. 1008-1021
    • Matta, S.1
  • 60
    • 33646146878 scopus 로고    scopus 로고
    • Anatomical localization of leucine-rich repeat kinase 2 in mouse brain
    • Melrose H., et al. Anatomical localization of leucine-rich repeat kinase 2 in mouse brain. Neuroscience 2006, 139:791-794.
    • (2006) Neuroscience , vol.139 , pp. 791-794
    • Melrose, H.1
  • 61
    • 34547107314 scopus 로고    scopus 로고
    • A comparative analysis of leucine-rich repeat kinase 2 (Lrrk2) expression in mouse brain and Lewy body disease
    • Melrose H.L., et al. A comparative analysis of leucine-rich repeat kinase 2 (Lrrk2) expression in mouse brain and Lewy body disease. Neuroscience 2007, 147:1047-1058.
    • (2007) Neuroscience , vol.147 , pp. 1047-1058
    • Melrose, H.L.1
  • 62
    • 77957794336 scopus 로고    scopus 로고
    • Impaired dopaminergic neurotransmission and microtubule-associated protein tau alterations in human LRRK2 transgenic mice
    • Melrose H.L., et al. Impaired dopaminergic neurotransmission and microtubule-associated protein tau alterations in human LRRK2 transgenic mice. Neurobiol. Dis. 2010, 40:503-517.
    • (2010) Neurobiol. Dis. , vol.40 , pp. 503-517
    • Melrose, H.L.1
  • 63
    • 84885989906 scopus 로고    scopus 로고
    • LRRK2 affects vesicle trafficking, neurotransmitter extracellular level and membrane receptor localization
    • Migheli R., et al. LRRK2 affects vesicle trafficking, neurotransmitter extracellular level and membrane receptor localization. PLoS One 2013, 8:e77198.
    • (2013) PLoS One , vol.8 , pp. e77198
    • Migheli, R.1
  • 64
    • 84898639480 scopus 로고    scopus 로고
    • Surfactant secretion in LRRK2 knock-out rats: changes in lamellar body morphology and rate of exocytosis
    • Miklavc P., et al. Surfactant secretion in LRRK2 knock-out rats: changes in lamellar body morphology and rate of exocytosis. PLoS One 2014, 9:e84926.
    • (2014) PLoS One , vol.9 , pp. e84926
    • Miklavc, P.1
  • 65
    • 84923035922 scopus 로고    scopus 로고
    • The mouse/human cross-species heterodimer of leucine-rich repeat kinase 2: Possible significance in the transgenic model mouse of Parkinson's disease
    • Miyajima T., et al. The mouse/human cross-species heterodimer of leucine-rich repeat kinase 2: Possible significance in the transgenic model mouse of Parkinson's disease. Neurosci. Lett. 2015, 588:142-146.
    • (2015) Neurosci. Lett. , vol.588 , pp. 142-146
    • Miyajima, T.1
  • 66
    • 78650025189 scopus 로고    scopus 로고
    • Mitochondrial impairment in patients with Parkinson disease with the G2019S mutation in LRRK2
    • Mortiboys H., et al. Mitochondrial impairment in patients with Parkinson disease with the G2019S mutation in LRRK2. Neurology 2010, 75:2017-2020.
    • (2010) Neurology , vol.75 , pp. 2017-2020
    • Mortiboys, H.1
  • 67
    • 84879129926 scopus 로고    scopus 로고
    • Leucine-rich repeat kinase 2 (LRRK2)-deficient rats exhibit renal tubule injury and perturbations in metabolic and immunological homeostasis
    • Ness D., et al. Leucine-rich repeat kinase 2 (LRRK2)-deficient rats exhibit renal tubule injury and perturbations in metabolic and immunological homeostasis. PLoS One 2013, 8:e66164.
    • (2013) PLoS One , vol.8 , pp. e66164
    • Ness, D.1
  • 68
    • 70349103837 scopus 로고    scopus 로고
    • Parkin protects against LRRK2 G2019S mutant-induced dopaminergic neurodegeneration in Drosophila
    • Ng C.H., et al. Parkin protects against LRRK2 G2019S mutant-induced dopaminergic neurodegeneration in Drosophila. J. Neurosci. 2009, 29:11257-11262.
    • (2009) J. Neurosci. , vol.29 , pp. 11257-11262
    • Ng, C.H.1
  • 69
    • 70350653779 scopus 로고    scopus 로고
    • Substrate specificity and inhibitors of LRRK2, a protein kinase mutated in Parkinson's disease
    • Nichols R.J., et al. Substrate specificity and inhibitors of LRRK2, a protein kinase mutated in Parkinson's disease. Biochem. J. 2009, 424:47-60.
    • (2009) Biochem. J. , vol.424 , pp. 47-60
    • Nichols, R.J.1
  • 70
    • 84863728713 scopus 로고    scopus 로고
    • Leucine-rich repeat kinase 2 disturbs mitochondrial dynamics via Dynamin-like protein
    • Niu J., et al. Leucine-rich repeat kinase 2 disturbs mitochondrial dynamics via Dynamin-like protein. J. Neurochem. 2012, 122:650-658.
    • (2012) J. Neurochem. , vol.122 , pp. 650-658
    • Niu, J.1
  • 71
    • 84872320159 scopus 로고    scopus 로고
    • Dominant-negative effects of LRRK2 heterodimers: a possible mechanism of neurodegeneration in Parkinson's disease caused by LRRK2 I2020T mutation
    • Ohta E., et al. Dominant-negative effects of LRRK2 heterodimers: a possible mechanism of neurodegeneration in Parkinson's disease caused by LRRK2 I2020T mutation. Biochem. Biophys. Res. Commun. 2013, 430:560-566.
    • (2013) Biochem. Biophys. Res. Commun. , vol.430 , pp. 560-566
    • Ohta, E.1
  • 72
    • 84875640261 scopus 로고    scopus 로고
    • Interplay of LRRK2 with chaperone-mediated autophagy
    • Orenstein S.J., et al. Interplay of LRRK2 with chaperone-mediated autophagy. Nat. Neurosci. 2013, 16:394-406.
    • (2013) Nat. Neurosci. , vol.16 , pp. 394-406
    • Orenstein, S.J.1
  • 73
    • 31344439221 scopus 로고    scopus 로고
    • LRRK2 G2019S as a cause of Parkinson's disease in Ashkenazi Jews
    • Ozelius L.J., et al. LRRK2 G2019S as a cause of Parkinson's disease in Ashkenazi Jews. N. Engl. J. Med. 2006, 354:424-425.
    • (2006) N. Engl. J. Med. , vol.354 , pp. 424-425
    • Ozelius, L.J.1
  • 74
    • 84866384715 scopus 로고    scopus 로고
    • G2019S leucine-rich repeat kinase 2 causes uncoupling protein-mediated mitochondrial depolarization
    • Papkovskaia T.D., et al. G2019S leucine-rich repeat kinase 2 causes uncoupling protein-mediated mitochondrial depolarization. Hum. Mol. Genet. 2012, 21:4201-4213.
    • (2012) Hum. Mol. Genet. , vol.21 , pp. 4201-4213
    • Papkovskaia, T.D.1
  • 75
    • 84896736721 scopus 로고    scopus 로고
    • LRRK2 regulates synaptogenesis and dopamine receptor activation through modulation of PKA activity
    • Parisiadou L., et al. LRRK2 regulates synaptogenesis and dopamine receptor activation through modulation of PKA activity. Nat. Neurosci. 2014, 17:367-376.
    • (2014) Nat. Neurosci. , vol.17 , pp. 367-376
    • Parisiadou, L.1
  • 77
    • 79951534656 scopus 로고    scopus 로고
    • LRRK2 controls synaptic vesicle storage and mobilization within the recycling pool
    • Piccoli G., et al. LRRK2 controls synaptic vesicle storage and mobilization within the recycling pool. J. Neurosci. 2011, 31:2225-2237.
    • (2011) J. Neurosci. , vol.31 , pp. 2225-2237
    • Piccoli, G.1
  • 78
    • 79953758383 scopus 로고    scopus 로고
    • Dopaminergic neuronal loss, reduced neurite complexity and autophagic abnormalities in transgenic mice expressing G2019S mutant LRRK2
    • Ramonet D., et al. Dopaminergic neuronal loss, reduced neurite complexity and autophagic abnormalities in transgenic mice expressing G2019S mutant LRRK2. PLoS One 2011, 6:e18568.
    • (2011) PLoS One , vol.6 , pp. e18568
    • Ramonet, D.1
  • 79
    • 48949092066 scopus 로고    scopus 로고
    • Analysis of Lrrk2 R1628P as a risk factor for Parkinson's disease
    • Ross O.A., et al. Analysis of Lrrk2 R1628P as a risk factor for Parkinson's disease. Ann. Neurol. 2008, 64:88-92.
    • (2008) Ann. Neurol. , vol.64 , pp. 88-92
    • Ross, O.A.1
  • 80
    • 80052967403 scopus 로고    scopus 로고
    • Association of LRRK2 exonic variants with susceptibility to Parkinson's disease: a case-control study
    • Ross O.A., et al. Association of LRRK2 exonic variants with susceptibility to Parkinson's disease: a case-control study. Lancet Neurol. 2011, 10:898-908.
    • (2011) Lancet Neurol. , vol.10 , pp. 898-908
    • Ross, O.A.1
  • 81
    • 84906850990 scopus 로고    scopus 로고
    • The LRRK2 inhibitor GSK2578215A induces protective autophagy in SH-SY5Y cells: involvement of Drp-1-mediated mitochondrial fission and mitochondrial-derived ROS signaling
    • Saez-Atienzar S., et al. The LRRK2 inhibitor GSK2578215A induces protective autophagy in SH-SY5Y cells: involvement of Drp-1-mediated mitochondrial fission and mitochondrial-derived ROS signaling. Cell Death Dis. 2014, 5:e1368.
    • (2014) Cell Death Dis. , vol.5 , pp. e1368
    • Saez-Atienzar, S.1
  • 82
    • 67651171368 scopus 로고    scopus 로고
    • LRRK2 modulates vulnerability to mitochondrial dysfunction in Caenorhabditis elegans
    • Saha S., et al. LRRK2 modulates vulnerability to mitochondrial dysfunction in Caenorhabditis elegans. J. Neurosci. 2009, 29:9210-9218.
    • (2009) J. Neurosci. , vol.29 , pp. 9210-9218
    • Saha, S.1
  • 83
    • 84887506882 scopus 로고    scopus 로고
    • LRRK2 mutations cause mitochondrial DNA damage in iPSC-derived neural cells from Parkinson's disease patients: reversal by gene correction
    • Sanders L.H., et al. LRRK2 mutations cause mitochondrial DNA damage in iPSC-derived neural cells from Parkinson's disease patients: reversal by gene correction. Neurobiol. Dis. 2014, 62:381-386.
    • (2014) Neurobiol. Dis. , vol.62 , pp. 381-386
    • Sanders, L.H.1
  • 84
    • 84902163498 scopus 로고    scopus 로고
    • Membrane recruitment of endogenous LRRK2 precedes its potent regulation of autophagy
    • Schapansky J., et al. Membrane recruitment of endogenous LRRK2 precedes its potent regulation of autophagy. Hum. Mol. Genet. 2014, 23:4201-4214.
    • (2014) Hum. Mol. Genet. , vol.23 , pp. 4201-4214
    • Schapansky, J.1
  • 85
    • 73649120624 scopus 로고    scopus 로고
    • Dependence of leucine-rich repeat kinase 2 (LRRK2) kinase activity on dimerization
    • Sen S., et al. Dependence of leucine-rich repeat kinase 2 (LRRK2) kinase activity on dimerization. J. Biol. Chem. 2009, 284:36346-36356.
    • (2009) J. Biol. Chem. , vol.284 , pp. 36346-36356
    • Sen, S.1
  • 86
    • 0022521066 scopus 로고
    • An in vivo study of dopamine release and metabolism in rat brain regions using intracerebral dialysis
    • Sharp T., et al. An in vivo study of dopamine release and metabolism in rat brain regions using intracerebral dialysis. J. Neurochem. 1986, 47:113-122.
    • (1986) J. Neurochem. , vol.47 , pp. 113-122
    • Sharp, T.1
  • 87
    • 84891776413 scopus 로고    scopus 로고
    • Mutant LRRK2 toxicity in neurons depends on LRRK2 levels and synuclein but not kinase activity or inclusion bodies
    • Skibinski G., et al. Mutant LRRK2 toxicity in neurons depends on LRRK2 levels and synuclein but not kinase activity or inclusion bodies. J. Neurosci. 2014, 34:418-433.
    • (2014) J. Neurosci. , vol.34 , pp. 418-433
    • Skibinski, G.1
  • 88
    • 0036167679 scopus 로고    scopus 로고
    • Increase in dopamine turnover occurs early in Parkinson's disease: evidence from a new modeling approach to PET 18F-fluorodopa data
    • Sossi V., et al. Increase in dopamine turnover occurs early in Parkinson's disease: evidence from a new modeling approach to PET 18F-fluorodopa data. J. Cereb. Blood Flow Metab. 2002, 22:232-239.
    • (2002) J. Cereb. Blood Flow Metab. , vol.22 , pp. 232-239
    • Sossi, V.1
  • 89
    • 3843057052 scopus 로고    scopus 로고
    • Changes of dopamine turnover in the progression of Parkinson's disease as measured by positron emission tomography: their relation to disease-compensatory mechanisms
    • Sossi V., et al. Changes of dopamine turnover in the progression of Parkinson's disease as measured by positron emission tomography: their relation to disease-compensatory mechanisms. J. Cereb. Blood Flow Metab. 2004, 24:869-876.
    • (2004) J. Cereb. Blood Flow Metab. , vol.24 , pp. 869-876
    • Sossi, V.1
  • 90
    • 78650209340 scopus 로고    scopus 로고
    • Dopamine turnover increases in asymptomatic LRRK2 mutations carriers
    • Sossi V., et al. Dopamine turnover increases in asymptomatic LRRK2 mutations carriers. Mov. Disord. 2010, 25:2717-2723.
    • (2010) Mov. Disord. , vol.25 , pp. 2717-2723
    • Sossi, V.1
  • 91
    • 84897586124 scopus 로고    scopus 로고
    • Functional interaction of Parkinson's disease-associated LRRK2 with members of the dynamin GTPase superfamily
    • Stafa K., et al. Functional interaction of Parkinson's disease-associated LRRK2 with members of the dynamin GTPase superfamily. Hum. Mol. Genet. 2014, 23:2055-2077.
    • (2014) Hum. Mol. Genet. , vol.23 , pp. 2055-2077
    • Stafa, K.1
  • 92
    • 84856976662 scopus 로고    scopus 로고
    • Altered dopamine metabolism and increased vulnerability to MPTP in mice with partial deficiency of mitochondrial complex I in dopamine neurons
    • Sterky F.H., et al. Altered dopamine metabolism and increased vulnerability to MPTP in mice with partial deficiency of mitochondrial complex I in dopamine neurons. Hum. Mol. Genet. 2012, 21:1078-1089.
    • (2012) Hum. Mol. Genet. , vol.21 , pp. 1078-1089
    • Sterky, F.H.1
  • 93
    • 84887004639 scopus 로고    scopus 로고
    • Inhibition of excessive mitochondrial fission reduced aberrant autophagy and neuronal damage caused by LRRK2 G2019S mutation
    • Su Y.C., Qi X. Inhibition of excessive mitochondrial fission reduced aberrant autophagy and neuronal damage caused by LRRK2 G2019S mutation. Hum. Mol. Genet. 2013, 22(22):4545-4561. 10.1093/hmg/ddt301.
    • (2013) Hum. Mol. Genet. , vol.22 , Issue.22 , pp. 4545-4561
    • Su, Y.C.1    Qi, X.2
  • 94
    • 20644441994 scopus 로고    scopus 로고
    • Mechanisms of neurotransmitter release by amphetamines: a review
    • Sulzer D., et al. Mechanisms of neurotransmitter release by amphetamines: a review. Prog. Neurobiol. 2005, 75:406-433.
    • (2005) Prog. Neurobiol. , vol.75 , pp. 406-433
    • Sulzer, D.1
  • 95
    • 33846000636 scopus 로고    scopus 로고
    • Identification of a common genetic risk variant (LRRK2 Gly2385Arg) in Parkinson's disease
    • Tan E.K. Identification of a common genetic risk variant (LRRK2 Gly2385Arg) in Parkinson's disease. Ann. Acad. Med. Singapore 2006, 35:840-842.
    • (2006) Ann. Acad. Med. Singapore , vol.35 , pp. 840-842
    • Tan, E.K.1
  • 96
    • 33745917404 scopus 로고    scopus 로고
    • Distribution of PINK1 and LRRK2 in rat and mouse brain
    • Taymans J.M., et al. Distribution of PINK1 and LRRK2 in rat and mouse brain. J. Neurochem. 2006, 98:951-961.
    • (2006) J. Neurochem. , vol.98 , pp. 951-961
    • Taymans, J.M.1
  • 97
    • 70149124508 scopus 로고    scopus 로고
    • R1441C mutation in LRRK2 impairs dopaminergic neurotransmission in mice
    • Tong Y., et al. R1441C mutation in LRRK2 impairs dopaminergic neurotransmission in mice. Proc. Natl. Acad. Sci. U. S. A. 2009, 106:14622-14627.
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 14622-14627
    • Tong, Y.1
  • 98
    • 77953090478 scopus 로고    scopus 로고
    • Loss of leucine-rich repeat kinase 2 causes impairment of protein degradation pathways, accumulation of alpha-synuclein, and apoptotic cell death in aged mice
    • Tong Y., et al. Loss of leucine-rich repeat kinase 2 causes impairment of protein degradation pathways, accumulation of alpha-synuclein, and apoptotic cell death in aged mice. Proc. Natl. Acad. Sci. U. S. A. 2010, 107:9879-9884.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 9879-9884
    • Tong, Y.1
  • 99
    • 84863294414 scopus 로고    scopus 로고
    • Loss of leucine-rich repeat kinase 2 causes age-dependent bi-phasic alterations of the autophagy pathway
    • Tong Y., et al. Loss of leucine-rich repeat kinase 2 causes age-dependent bi-phasic alterations of the autophagy pathway. Mol. Neurodegener. 2012, 7:2.
    • (2012) Mol. Neurodegener. , vol.7 , pp. 2
    • Tong, Y.1
  • 100
    • 84863245760 scopus 로고    scopus 로고
    • Defects in mitochondrial dynamics and metabolomic signatures of evolving energetic stress in mouse models of familial Alzheimer's disease
    • Trushina E., et al. Defects in mitochondrial dynamics and metabolomic signatures of evolving energetic stress in mouse models of familial Alzheimer's disease. PLoS One 2012, 7:e32737.
    • (2012) PLoS One , vol.7 , pp. e32737
    • Trushina, E.1
  • 101
    • 84949117317 scopus 로고    scopus 로고
    • Conditional expression of Parkinson's disease-related R1441C LRRK2 in midbrain dopaminergic neurons of mice causes nuclear abnormalities without neurodegeneration
    • Tsika E., et al. Conditional expression of Parkinson's disease-related R1441C LRRK2 in midbrain dopaminergic neurons of mice causes nuclear abnormalities without neurodegeneration. Neurobiol. Dis. 2014, 71:345-358.
    • (2014) Neurobiol. Dis. , vol.71 , pp. 345-358
    • Tsika, E.1
  • 102
    • 84928611110 scopus 로고    scopus 로고
    • Behavioral deficits and striatal DA signaling in LRRK2 p.G2019S transgenic rats: a multimodal investigation including PET neuroimaging
    • Walker M.D., et al. Behavioral deficits and striatal DA signaling in LRRK2 p.G2019S transgenic rats: a multimodal investigation including PET neuroimaging. J. Parkinsons Dis. 2014, 4:483-498.
    • (2014) J. Parkinsons Dis. , vol.4 , pp. 483-498
    • Walker, M.D.1
  • 103
    • 80052794422 scopus 로고    scopus 로고
    • DLP1-dependent mitochondrial fragmentation mediates 1-methyl-4-phenylpyridinium toxicity in neurons: implications for Parkinson's disease
    • Wang X., et al. DLP1-dependent mitochondrial fragmentation mediates 1-methyl-4-phenylpyridinium toxicity in neurons: implications for Parkinson's disease. Aging Cell 2011, 10:807-823.
    • (2011) Aging Cell , vol.10 , pp. 807-823
    • Wang, X.1
  • 104
    • 84859259002 scopus 로고    scopus 로고
    • LRRK2 regulates mitochondrial dynamics and function through direct interaction with DLP1
    • Wang X., et al. LRRK2 regulates mitochondrial dynamics and function through direct interaction with DLP1. Hum. Mol. Genet. 2012, 21:1931-1944.
    • (2012) Hum. Mol. Genet. , vol.21 , pp. 1931-1944
    • Wang, X.1
  • 105
    • 84860389765 scopus 로고    scopus 로고
    • Autophosphorylation in the leucine-rich repeat kinase 2 (LRRK2) GTPase domain modifies kinase and GTP-binding activities
    • Webber P.J., et al. Autophosphorylation in the leucine-rich repeat kinase 2 (LRRK2) GTPase domain modifies kinase and GTP-binding activities. J. Mol. Biol. 2011, 412:94-110.
    • (2011) J. Mol. Biol. , vol.412 , pp. 94-110
    • Webber, P.J.1
  • 106
    • 84901648685 scopus 로고    scopus 로고
    • Differential LRRK2 expression in the cortex, striatum, and substantia nigra in transgenic and nontransgenic rodents
    • West A.B., et al. Differential LRRK2 expression in the cortex, striatum, and substantia nigra in transgenic and nontransgenic rodents. J. Comp. Neurol. 2014, 522:2465-2480.
    • (2014) J. Comp. Neurol. , vol.522 , pp. 2465-2480
    • West, A.B.1
  • 107
    • 0021963877 scopus 로고
    • Sequence and significance of dopamine metabolism in the rat brain
    • Westerink B.H. Sequence and significance of dopamine metabolism in the rat brain. Neurochem. Int. 1985, 7:221-227.
    • (1985) Neurochem. Int. , vol.7 , pp. 221-227
    • Westerink, B.H.1
  • 108
    • 40949145205 scopus 로고    scopus 로고
    • Developmental regulation of leucine-rich repeat kinase 1 and 2 expression in the brain and other rodent and human organs: implications for Parkinson's disease
    • Westerlund M., et al. Developmental regulation of leucine-rich repeat kinase 1 and 2 expression in the brain and other rodent and human organs: implications for Parkinson's disease. Neuroscience 2008, 152:429-436.
    • (2008) Neuroscience , vol.152 , pp. 429-436
    • Westerlund, M.1
  • 109
    • 56249144183 scopus 로고    scopus 로고
    • Lrrk2 and alpha-synuclein are co-regulated in rodent striatum
    • Westerlund M., et al. Lrrk2 and alpha-synuclein are co-regulated in rodent striatum. Mol. Cell. Neurosci. 2008, 39:586-591.
    • (2008) Mol. Cell. Neurosci. , vol.39 , pp. 586-591
    • Westerlund, M.1
  • 110
    • 84904400238 scopus 로고    scopus 로고
    • G2019S LRRK2 mutant fibroblasts from Parkinson's disease patients show increased sensitivity to neurotoxin 1-methyl-4-phenylpyridinium dependent of autophagy
    • Yakhine-Diop S.M., et al. G2019S LRRK2 mutant fibroblasts from Parkinson's disease patients show increased sensitivity to neurotoxin 1-methyl-4-phenylpyridinium dependent of autophagy. Toxicology 2014, 324:1-9.
    • (2014) Toxicology , vol.324 , pp. 1-9
    • Yakhine-Diop, S.M.1
  • 111
    • 0022441119 scopus 로고
    • Effect of dopamine D-1 and D-2 receptor selective drugs on dopamine release and metabolism in rat striatum in vivo
    • Zetterstrom T., et al. Effect of dopamine D-1 and D-2 receptor selective drugs on dopamine release and metabolism in rat striatum in vivo. Naunyn Schmiedeberg's Arch. Pharmacol. 1986, 334:117-124.
    • (1986) Naunyn Schmiedeberg's Arch. Pharmacol. , vol.334 , pp. 117-124
    • Zetterstrom, T.1
  • 112
    • 0023898407 scopus 로고
    • In vivo measurement of extracellular dopamine and DOPAC in rat striatum after various dopamine-releasing drugs; implications for the origin of extracellular DOPAC
    • Zetterstrom T., et al. In vivo measurement of extracellular dopamine and DOPAC in rat striatum after various dopamine-releasing drugs; implications for the origin of extracellular DOPAC. Eur. J. Pharmacol. 1988, 148:327-334.
    • (1988) Eur. J. Pharmacol. , vol.148 , pp. 327-334
    • Zetterstrom, T.1
  • 113
    • 79960972765 scopus 로고    scopus 로고
    • Temporal expression of mutant LRRK2 in adult rats impairs dopamine reuptake
    • Zhou H., et al. Temporal expression of mutant LRRK2 in adult rats impairs dopamine reuptake. Int. J. Biol. Sci. 2011, 7:753-761.
    • (2011) Int. J. Biol. Sci. , vol.7 , pp. 753-761
    • Zhou, H.1
  • 114
    • 0036767723 scopus 로고    scopus 로고
    • Increased dopamine turnover after partial loss of dopaminergic neurons: compensation or toxicity?
    • Zigmond M.J., et al. Increased dopamine turnover after partial loss of dopaminergic neurons: compensation or toxicity?. Parkinsonism Relat. Disord. 2002, 8:389-393.
    • (2002) Parkinsonism Relat. Disord. , vol.8 , pp. 389-393
    • Zigmond, M.J.1
  • 115
    • 8844233579 scopus 로고    scopus 로고
    • Mutations in LRRK2 cause autosomal-dominant parkinsonism with pleomorphic pathology
    • Zimprich A., et al. Mutations in LRRK2 cause autosomal-dominant parkinsonism with pleomorphic pathology. Neuron 2004, 44:601-607.
    • (2004) Neuron , vol.44 , pp. 601-607
    • Zimprich, A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.