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Progressive dopaminergic alterations and mitochondrial abnormalities in LRRK2 G2019S knock-in mice
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Multiple studies point to a role for LRRK2 at the presynaptic terminal where it plays a role in release of dopamine from striato-nigral neurons, and glutamate from corticostriatal neurons.
“Multiple studies point to a role for LRRK2 at the presynaptic terminal where it plays a role in release of dopamine from striato-nigral neurons, and glutamate from corticostriatal neurons [5, 6, 11, 50, 86, 92, 95].”
From Cellular and subcellular localization of Rab10 and phospho-T73 Rab10 in the mouse and human brain (2023) · cites this paper as [95]
The Discussion (page unavailable) reports reduced striatal dopamine release in G2019S mice and proposes impaired vesicular exocytosis; it also reports increased glutamate release in cortical cultures. It does not establish glutamate release specifically from corticostriatal neurons, and it describes the dopamine projections as nigro-striatal rather than striato-nigral. (LLM, conf=0.86)
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Cooper, O., Seo, H., Andrabi, S., Guardia-Laguarta, C., Graziotto, J., Sundberg, M., McLean, J. R., Carrillo-Reid, L., Xie, Z., Osborn, T., et al. (2012) · Science Translational Medicine · doi:10.1126/scitranslmed.3003985 · Cited by 508
Ramonet, D., Daher, J. P. L., Lin, B. M., Stafa, K., Kim, J., Banerjee, R., Westerlund, M., Pletnikova, O., Glauser, L., Yang, L., et al. (2011) · PLoS ONE · doi:10.1371/journal.pone.0018568 · Cited by 405
Friedman, L. G., Lachenmayer, M. L., Wang, J., He, L., Poulose, S. M., Komatsu, M., Holstein, G. R., & Yue, Z. (2012) · The Journal of Neuroscience · doi:10.1523/jneurosci.5809-11.2012 · Cited by 303
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Research works printed but not linked: 111
- Angeles, 2011, Mutations in LRRK2 increase phosphorylation of peroxiredoxin 3 exacerbating oxidative stress-induced neuronal death, Hum. Mutat., 32, 1390, 10.1002/humu.21582 · DOI
- Arbuthnott, 1990, Dopamine release and metabolism in the rat striatum: an analysis by ‘in vivo’ brain microdialysis, Pharmacol. Ther., 48, 281, 10.1016/0163-7258(90)90050-C · DOI
- Bailey, 2013, LRRK2 phosphorylates novel tau epitopes and promotes tauopathy, Acta Neuropathol., 126, 809, 10.1007/s00401-013-1188-4 · DOI
- Bannon, 1983, Pharmacology of mesocortical dopamine neurons, Pharmacol. Rev., 35, 53, 10.1016/S0031-6997(25)06572-X · DOI
- Baptista, 2013, Loss of leucine-rich repeat kinase 2 (LRRK2) in rats leads to progressive abnormal phenotypes in peripheral organs, PLoS One, 8, e80705, 10.1371/journal.pone.0080705 · DOI
- Beccano-Kelly, 2014, Synaptic function is modulated by LRRK2 and glutamate release is increased in cortical neurons of G2019S LRRK2 knock-in mice, Front. Cell. Neurosci., 8, 301, 10.3389/fncel.2014.00301 · DOI · Paper page
- Beccano-Kelly, 2014, LRRK2 overexpression alters glutamatergic presynaptic plasticity, striatal dopamine tone, postsynaptic signal transduction, motor activity and memory, Hum. Mol. Genet., 24, 1336, 10.1093/hmg/ddu543 · DOI · Paper page
- Belluzzi, 2012, Presynaptic dysfunction in Parkinson's disease: a focus on LRRK2, Biochem. Soc. Trans., 40, 1111, 10.1042/BST20120124 · DOI
- Berger, 2010, Membrane localization of LRRK2 is associated with increased formation of the highly active LRRK2 dimer and changes in its phosphorylation, Biochemistry, 49, 5511, 10.1021/bi100157u · DOI
- Berwick, 2012, LRRK2 functions as a Wnt signaling scaffold, bridging cytosolic proteins and membrane-localized LRP6, Hum. Mol. Genet., 21, 4966, 10.1093/hmg/dds342 · DOI
- Cherra, 2013, Mutant LRRK2 elicits calcium imbalance and depletion of dendritic mitochondria in neurons, Am. J. Pathol., 182, 474, 10.1016/j.ajpath.2012.10.027 · DOI
- Cirnaru, 2014, LRRK2 kinase activity regulates synaptic vesicle trafficking and neurotransmitter release through modulation of LRRK2 macro-molecular complex, Front. Mol. Neurosci., 7, 49, 10.3389/fnmol.2014.00049 · DOI · Paper page
- Daberkow, 2013, Amphetamine paradoxically augments exocytotic dopamine release and phasic dopamine signals, J. Neurosci., 33, 452, 10.1523/JNEUROSCI.2136-12.2013 · DOI
- Darvesh, 2011, In vivo brain microdialysis: advances in neuropsychopharmacology and drug discovery, Expert Opin. Drug Discov., 6, 109, 10.1517/17460441.2011.547189 · DOI
- Davies, 2013, Comprehensive characterization and optimization of anti-LRRK2 (leucine-rich repeat kinase 2) monoclonal antibodies, Biochem. J., 453, 101, 10.1042/BJ20121742 · DOI
- Deng, 2008, 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., 105, 1499, 10.1073/pnas.0709098105 · DOI
- Di Fonzo, 2006, A common missense variant in the LRRK2 gene, Gly2385Arg, associated with Parkinson's disease risk in Taiwan, Neurogenetics, 7, 133, 10.1007/s10048-006-0041-5 · DOI
- Du, 2010, Early deficits in synaptic mitochondria in an Alzheimer's disease mouse model, Proc. Natl. Acad. Sci. U. S. A., 107, 18670, 10.1073/pnas.1006586107 · DOI · Paper page
- Dusonchet, 2011, A rat model of progressive nigral neurodegeneration induced by the Parkinson's disease-associated G2019S mutation in LRRK2, J. Neurosci., 31, 907, 10.1523/JNEUROSCI.5092-10.2011 · DOI
- Farrer, 2007, Lrrk2 G2385R is an ancestral risk factor for Parkinson's disease in Asia, Parkinsonism Relat. Disord., 13, 89, 10.1016/j.parkreldis.2006.12.001 · DOI
- Ferree, 2012, Regulation of physiologic actions of LRRK2: focus on autophagy, Neurodegener. Dis., 10, 238, 10.1159/000332599 · DOI
- Galter, 2006, LRRK2 expression linked to dopamine-innervated areas, Ann. Neurol., 59, 714, 10.1002/ana.20808 · DOI
- Galter, 2010, MitoPark mice mirror the slow progression of key symptoms and L-DOPA response in Parkinson's disease, Genes Brain Behav., 9, 173, 10.1111/j.1601-183X.2009.00542.x · DOI
- Giesert, 2013, Expression analysis of Lrrk1, Lrrk2 and Lrrk2 splice variants in mice, PLoS One, 8, e63778, 10.1371/journal.pone.0063778 · DOI
- Gomez-Suaga, 2014, LRRK2 delays degradative receptor trafficking by impeding late endosomal budding through decreasing Rab7 activity, Hum. Mol. Genet., 23, 6779, 10.1093/hmg/ddu395 · DOI · Paper page
- Greggio, 2008, The Parkinson disease-associated leucine-rich repeat kinase 2 (LRRK2) is a dimer that undergoes intramolecular autophosphorylation, J. Biol. Chem., 283, 16906, 10.1074/jbc.M708718200 · DOI
- Greggio, 2009, The Parkinson's disease kinase LRRK2 autophosphorylates its GTPase domain at multiple sites, Biochem. Biophys. Res. Commun., 389, 449, 10.1016/j.bbrc.2009.08.163 · DOI
- Healy, 2008, Phenotype, genotype, and worldwide genetic penetrance of LRRK2-associated Parkinson's disease: a case–control study, Lancet Neurol., 7, 583, 10.1016/S1474-4422(08)70117-0 · DOI · Paper page
- Hernandez, 2012, Regulation of presynaptic neurotransmission by macroautophagy, Neuron, 74, 277, 10.1016/j.neuron.2012.02.020 · DOI
- Herzig, 2011, LRRK2 protein levels are determined by kinase function and are crucial for kidney and lung homeostasis in mice, Hum. Mol. Genet., 20, 4209, 10.1093/hmg/ddr348 · DOI
- Herzig, 2012, High LRRK2 levels fail to induce or exacerbate neuronal alpha-synucleinopathy in mouse brain, PLoS One, 7, e36581, 10.1371/journal.pone.0036581 · DOI
- Higashi, 2007, Localization of Parkinson's disease-associated LRRK2 in normal and pathological human brain, Brain Res., 1155, 208, 10.1016/j.brainres.2007.04.034 · DOI
- Higashi, 2007, Expression and localization of Parkinson's disease-associated leucine-rich repeat kinase 2 in the mouse brain, J. Neurochem., 100, 368, 10.1111/j.1471-4159.2006.04246.x · DOI
- Hindle, 2013, Dopaminergic expression of the Parkinsonian gene LRRK2-G2019S leads to non-autonomous visual neurodegeneration, accelerated by increased neural demands for energy, Hum. Mol. Genet., 22, 2129, 10.1093/hmg/ddt061 · DOI
- Hinkle, 2012, LRRK2 knockout mice have an intact dopaminergic system but display alterations in exploratory and motor co-ordination behaviors, Mol. Neurodegener., 7, 25, 10.1186/1750-1326-7-25 · DOI
- Hinkle, 2012, LRRK2 knockout mice have an intact dopaminergic system but display alterations in exploratory and motor co-ordination behaviors, Mol. Neurodegener., 7, 25, 10.1186/1750-1326-7-25 · DOI
- Hulihan, 2008, LRRK2 Gly2019Ser penetrance in Arab-Berber patients from Tunisia: a case–control genetic study, Lancet Neurol., 7, 591, 10.1016/S1474-4422(08)70116-9 · DOI
- Ishihara, 2006, Clinical features of Parkinson disease patients with homozygous leucine-rich repeat kinase 2 G2019S mutations, Arch. Neurol., 63, 1250, 10.1001/archneur.63.9.1250 · DOI
- Ishihara, 2007, Screening for Lrrk2 G2019S and clinical comparison of Tunisian and North American Caucasian Parkinson's disease families, Mov. Disord., 22, 55, 10.1002/mds.21180 · DOI
- Kachergus, 2005, Identification of a novel LRRK2 mutation linked to autosomal dominant parkinsonism: evidence of a common founder across European populations, Am. J. Hum. Genet., 76, 672, 10.1086/429256 · DOI
- Kay, 2005, Escaping Parkinson's disease: a neurologically healthy octogenarian with the LRRK2 G2019S mutation, Mov. Disord., 20, 1077, 10.1002/mds.20618 · DOI
- Keating, 2008, Mitochondrial dysfunction, oxidative stress, regulation of exocytosis and their relevance to neurodegenerative diseases, J. Neurochem., 104, 298, 10.1111/j.1471-4159.2007.04997.x · DOI
- Kontgen, 1993, Simple screening procedure to detect gene targeting events in embryonic stem cells, Methods Enzymol., 225, 878, 10.1016/0076-6879(93)25055-7 · DOI
- Lee, 2010, Inhibitors of leucine-rich repeat kinase-2 protect against models of Parkinson's disease, Nat. Med., 16, 998, 10.1038/nm.2199 · DOI · Paper page
- Lee, 2015, Behavioral, neurochemical, and pathologic alterations in bacterial artificial chromosome transgenic G2019S leucine-rich repeated kinase 2 rats, Neurobiol. Aging, 36, 505, 10.1016/j.neurobiolaging.2014.07.011 · DOI
- Lewis, 2012, LRRK2 and human disease: a complicated question or a question of complexes?, Sci. Signal., 5, pe2, 10.1126/scisignal.2002680 · DOI
- Li, 2007, Leucine-rich repeat kinase 2 (LRRK2)/PARK8 possesses GTPase activity that is altered in familial Parkinson's disease R1441C/G mutants, J. Neurochem., 103, 238, 10.1111/j.1471-4159.2007.04743.x · DOI
- Li, 2009, Mutant LRRK2(R1441G) BAC transgenic mice recapitulate cardinal features of Parkinson's disease, Nat. Neurosci., 12, 826, 10.1038/nn.2349 · DOI
- Li, 2010, Enhanced striatal dopamine transmission and motor performance with LRRK2 overexpression in mice is eliminated by familial Parkinson's disease mutation G2019S, J. Neurosci., 30, 1788, 10.1523/JNEUROSCI.5604-09.2010 · DOI
- Liao, 2014, Parkinson disease-associated mutation R1441H in LRRK2 prolongs the “active state” of its GTPase domain, Proc. Natl. Acad. Sci. U. S. A., 111, 4055, 10.1073/pnas.1323285111 · DOI
- Lin, 2009, Leucine-rich repeat kinase 2 regulates the progression of neuropathology induced by Parkinson's-disease-related mutant alpha-synuclein, Neuron, 64, 807, 10.1016/j.neuron.2009.11.006 · DOI
- Liu, 2014, LRRK2 R1441G mice are more liable to dopamine depletion and locomotor inactivity, Ann. Clin. Transl. Neurol., 1, 199, 10.1002/acn3.45 · DOI
- Longo, 2014, Genetic and pharmacological evidence that G2019S LRRK2 confers a hyperkinetic phenotype, resistant to motor decline associated with aging, Neurobiol. Dis., 71, 62, 10.1016/j.nbd.2014.07.013 · DOI
- MacLeod, 2006, The familial Parkinsonism gene LRRK2 regulates neurite process morphology, Neuron, 52, 587, 10.1016/j.neuron.2006.10.008 · DOI
- Mandemakers, 2012, LRRK2 expression is enriched in the striosomal compartment of mouse striatum, Neurobiol. Dis., 48, 582, 10.1016/j.nbd.2012.07.017 · DOI
- Manzoni, 2013, Inhibition of LRRK2 kinase activity stimulates macroautophagy, Biochim. Biophys. Acta, 1833, 2900, 10.1016/j.bbamcr.2013.07.020 · DOI
- Matta, 2012, LRRK2 controls an EndoA phosphorylation cycle in synaptic endocytosis, Neuron, 75, 1008, 10.1016/j.neuron.2012.08.022 · DOI · Paper page
- Melrose, 2006, Anatomical localization of leucine-rich repeat kinase 2 in mouse brain, Neuroscience, 139, 791, 10.1016/j.neuroscience.2006.01.017 · DOI
- Melrose, 2007, A comparative analysis of leucine-rich repeat kinase 2 (Lrrk2) expression in mouse brain and Lewy body disease, Neuroscience, 147, 1047, 10.1016/j.neuroscience.2007.05.027 · DOI
- Melrose, 2010, Impaired dopaminergic neurotransmission and microtubule-associated protein tau alterations in human LRRK2 transgenic mice, Neurobiol. Dis., 40, 503, 10.1016/j.nbd.2010.07.010 · DOI
- Migheli, 2013, LRRK2 affects vesicle trafficking, neurotransmitter extracellular level and membrane receptor localization, PLoS One, 8, e77198, 10.1371/journal.pone.0077198 · DOI
- Miklavc, 2014, Surfactant secretion in LRRK2 knock-out rats: changes in lamellar body morphology and rate of exocytosis, PLoS One, 9, e84926, 10.1371/journal.pone.0084926 · DOI
- Miyajima, 2015, 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., 588, 142, 10.1016/j.neulet.2015.01.003 · DOI
- Mortiboys, 2010, Mitochondrial impairment in patients with Parkinson disease with the G2019S mutation in LRRK2, Neurology, 75, 2017, 10.1212/WNL.0b013e3181ff9685 · DOI
- Ness, 2013, Leucine-rich repeat kinase 2 (LRRK2)-deficient rats exhibit renal tubule injury and perturbations in metabolic and immunological homeostasis, PLoS One, 8, e66164, 10.1371/journal.pone.0066164 · DOI
- Ng, 2009, Parkin protects against LRRK2 G2019S mutant-induced dopaminergic neurodegeneration in Drosophila, J. Neurosci., 29, 11257, 10.1523/JNEUROSCI.2375-09.2009 · DOI
- Nichols, 2009, Substrate specificity and inhibitors of LRRK2, a protein kinase mutated in Parkinson's disease, Biochem. J., 424, 47, 10.1042/BJ20091035 · DOI
- Niu, 2012, Leucine-rich repeat kinase 2 disturbs mitochondrial dynamics via Dynamin-like protein, J. Neurochem., 122, 650, 10.1111/j.1471-4159.2012.07809.x · DOI
- Ohta, 2013, Dominant-negative effects of LRRK2 heterodimers: a possible mechanism of neurodegeneration in Parkinson's disease caused by LRRK2 I2020T mutation, Biochem. Biophys. Res. Commun., 430, 560, 10.1016/j.bbrc.2012.11.113 · DOI
- Orenstein, 2013, Interplay of LRRK2 with chaperone-mediated autophagy, Nat. Neurosci., 16, 394, 10.1038/nn.3350 · DOI · Paper page
- Ozelius, 2006, LRRK2 G2019S as a cause of Parkinson's disease in Ashkenazi Jews, N. Engl. J. Med., 354, 424, 10.1056/NEJMc055509 · DOI
- Papkovskaia, 2012, G2019S leucine-rich repeat kinase 2 causes uncoupling protein-mediated mitochondrial depolarization, Hum. Mol. Genet., 21, 4201, 10.1093/hmg/dds244 · DOI
- Parisiadou, 2014, LRRK2 regulates synaptogenesis and dopamine receptor activation through modulation of PKA activity, Nat. Neurosci., 17, 367, 10.1038/nn.3636 · DOI
- Piccoli, 2011, LRRK2 controls synaptic vesicle storage and mobilization within the recycling pool, J. Neurosci., 31, 2225, 10.1523/JNEUROSCI.3730-10.2011 · DOI
- Ross, 2008, Analysis of Lrrk2 R1628P as a risk factor for Parkinson's disease, Ann. Neurol., 64, 88, 10.1002/ana.21405 · DOI
- Ross, 2011, Association of LRRK2 exonic variants with susceptibility to Parkinson's disease: a case-control study, Lancet Neurol., 10, 898, 10.1016/S1474-4422(11)70175-2 · DOI
- Saez-Atienzar, 2014, 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., 5, e1368, 10.1038/cddis.2014.320 · DOI
- Saha, 2009, LRRK2 modulates vulnerability to mitochondrial dysfunction in Caenorhabditis elegans, J. Neurosci., 29, 9210, 10.1523/JNEUROSCI.2281-09.2009 · DOI
- Sanders, 2014, LRRK2 mutations cause mitochondrial DNA damage in iPSC-derived neural cells from Parkinson's disease patients: reversal by gene correction, Neurobiol. Dis., 62, 381, 10.1016/j.nbd.2013.10.013 · DOI
- Schapansky, 2014, Membrane recruitment of endogenous LRRK2 precedes its potent regulation of autophagy, Hum. Mol. Genet., 23, 4201, 10.1093/hmg/ddu138 · DOI · Paper page
- Sen, 2009, Dependence of leucine-rich repeat kinase 2 (LRRK2) kinase activity on dimerization, J. Biol. Chem., 284, 36346, 10.1074/jbc.M109.025437 · DOI
- Sharp, 1986, An in vivo study of dopamine release and metabolism in rat brain regions using intracerebral dialysis, J. Neurochem., 47, 113, 10.1111/j.1471-4159.1986.tb02838.x · DOI
- Skibinski, 2014, Mutant LRRK2 toxicity in neurons depends on LRRK2 levels and synuclein but not kinase activity or inclusion bodies, J. Neurosci., 34, 418, 10.1523/JNEUROSCI.2712-13.2014 · DOI
- Sossi, 2002, 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., 22, 232, 10.1097/00004647-200202000-00011 · DOI
- Sossi, 2004, 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., 24, 869, 10.1097/01.WCB.0000126563.85360.75 · DOI
- Sossi, 2010, Dopamine turnover increases in asymptomatic LRRK2 mutations carriers, Mov. Disord., 25, 2717, 10.1002/mds.23356 · DOI
- Stafa, 2014, Functional interaction of Parkinson's disease-associated LRRK2 with members of the dynamin GTPase superfamily, Hum. Mol. Genet., 23, 2055, 10.1093/hmg/ddt600 · DOI
- Sterky, 2012, Altered dopamine metabolism and increased vulnerability to MPTP in mice with partial deficiency of mitochondrial complex I in dopamine neurons, Hum. Mol. Genet., 21, 1078, 10.1093/hmg/ddr537 · DOI
- Su, 2013, Inhibition of excessive mitochondrial fission reduced aberrant autophagy and neuronal damage caused by LRRK2 G2019S mutation, Hum. Mol. Genet., 22, 4545, 10.1093/hmg/ddt301 · DOI
- Sulzer, 2005, Mechanisms of neurotransmitter release by amphetamines: a review, Prog. Neurobiol., 75, 406, 10.1016/j.pneurobio.2005.04.003 · DOI
- Tan, 2006, Identification of a common genetic risk variant (LRRK2 Gly2385Arg) in Parkinson's disease, Ann. Acad. Med. Singapore, 35, 840, 10.47102/annals-acadmedsg.V35N11p840 · DOI
- Taymans, 2006, Distribution of PINK1 and LRRK2 in rat and mouse brain, J. Neurochem., 98, 951, 10.1111/j.1471-4159.2006.03919.x · DOI
- Tong, 2009, R1441C mutation in LRRK2 impairs dopaminergic neurotransmission in mice, Proc. Natl. Acad. Sci. U. S. A., 106, 14622, 10.1073/pnas.0906334106 · DOI
- Tong, 2010, 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., 107, 9879, 10.1073/pnas.1004676107 · DOI
- Tong, 2012, Loss of leucine-rich repeat kinase 2 causes age-dependent bi-phasic alterations of the autophagy pathway, Mol. Neurodegener., 7, 2, 10.1186/1750-1326-7-2 · DOI
- Trushina, 2012, Defects in mitochondrial dynamics and metabolomic signatures of evolving energetic stress in mouse models of familial Alzheimer's disease, PLoS One, 7, e32737, 10.1371/journal.pone.0032737 · DOI
- Tsika, 2014, Conditional expression of Parkinson's disease-related R1441C LRRK2 in midbrain dopaminergic neurons of mice causes nuclear abnormalities without neurodegeneration, Neurobiol. Dis., 71, 345, 10.1016/j.nbd.2014.08.027 · DOI
- Walker, 2014, Behavioral deficits and striatal DA signaling in LRRK2 p.G2019S transgenic rats: a multimodal investigation including PET neuroimaging, J. Parkinsons Dis., 4, 483, 10.3233/JPD-140344 · DOI
- Wang, 2011, DLP1-dependent mitochondrial fragmentation mediates 1-methyl-4-phenylpyridinium toxicity in neurons: implications for Parkinson's disease, Aging Cell, 10, 807, 10.1111/j.1474-9726.2011.00721.x · DOI
- Wang, 2012, LRRK2 regulates mitochondrial dynamics and function through direct interaction with DLP1, Hum. Mol. Genet., 21, 1931, 10.1093/hmg/dds003 · DOI
- Webber, 2011, Autophosphorylation in the leucine-rich repeat kinase 2 (LRRK2) GTPase domain modifies kinase and GTP-binding activities, J. Mol. Biol., 412, 94, 10.1016/j.jmb.2011.07.033 · DOI
- West, 2014, Differential LRRK2 expression in the cortex, striatum, and substantia nigra in transgenic and nontransgenic rodents, J. Comp. Neurol., 522, 2465, 10.1002/cne.23583 · DOI · Paper page
- Westerink, 1985, Sequence and significance of dopamine metabolism in the rat brain, Neurochem. Int., 7, 221, 10.1016/0197-0186(85)90108-1 · DOI
- Westerlund, 2008, 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, 152, 429, 10.1016/j.neuroscience.2007.10.062 · DOI
- Westerlund, 2008, Lrrk2 and alpha-synuclein are co-regulated in rodent striatum, Mol. Cell. Neurosci., 39, 586, 10.1016/j.mcn.2008.08.001 · DOI
- Yakhine-Diop, 2014, G2019S LRRK2 mutant fibroblasts from Parkinson's disease patients show increased sensitivity to neurotoxin 1-methyl-4-phenylpyridinium dependent of autophagy, Toxicology, 324, 1, 10.1016/j.tox.2014.07.001 · DOI
- Zetterstrom, 1986, 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., 334, 117, 10.1007/BF00505810 · DOI
- Zetterstrom, 1988, 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., 148, 327, 10.1016/0014-2999(88)90110-0 · DOI
- Zhou, 2011, Temporal expression of mutant LRRK2 in adult rats impairs dopamine reuptake, Int. J. Biol. Sci., 7, 753, 10.7150/ijbs.7.753 · DOI
- Zigmond, 2002, Increased dopamine turnover after partial loss of dopaminergic neurons: compensation or toxicity?, Parkinsonism Relat. Disord., 8, 389, 10.1016/S1353-8020(02)00019-6 · DOI
- Zimprich, 2004, Mutations in LRRK2 cause autosomal-dominant parkinsonism with pleomorphic pathology, Neuron, 44, 601, 10.1016/j.neuron.2004.11.005 · DOI
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Metadata
- Authors
- Yue, M., Hinkle, K. M., Davies, P., Trushina, E., Fiesel, F. C., Christenson, T. A., Schroeder, A. S., Zhang, L., Bowles, E., Behrouz, B., Lincoln, S. J., Beevers, J. E., Milnerwood, A. J., Kurti, A., McLean, P. J., Fryer, J. D., Springer, W., Dickson, D. W., Farrer, M. J., & Melrose, H. L.
- Venue
- Neurobiology of Disease
- Publisher
- Elsevier BV
- Published
- 2015-06
- Volume
- 78
- Pages
- 172-195
- ISSN
- 0969-9961
- PMC
- PMC4526103
- Cited by
- 281
- References
- 3
- Language
- en
- Funders
- Mayo Clinic
- NIH (NS065860, NS40256, NS072187, ES020715, NS073740)
- Alzheimer's Association
- Michael J. Fox Foundation
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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