GSK‐3 in Neurodegenerative Diseases

Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B

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Amyloid plaque core protein in Alzheimer disease and Down syndrome.

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β-Secretase Cleavage of Alzheimer's Amyloid Precursor Protein by the Transmembrane Aspartic Protease BACE

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Abnormal phosphorylation of the microtubule-associated protein tau (tau) in Alzheimer cytoskeletal pathology.

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Alzheimer’s disease

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A protein factor essential for microtubule assembly

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Neurodegenerative Tauopathies

Lee, V. M.-Y., Goedert, M., & Trojanowski, J. Q. (2001) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.24.1.1121 · Cited by 2,480 · see citing works

A molecular mechanism for the effect of lithium on development.

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Amyloid β-peptide is produced by cultured cells during normal metabolism

Haass, C., Schlossmacher, M. G., Hung, A. Y., Vigo-Pelfrey, C., Mellon, A., Ostaszewski, B. L., Lieberburg, I., Koo, E. H., Schenk, D., Teplow, D. B., et al. (1992) · Nature · doi:10.1038/359322a0 · Cited by 1,921 · see citing works

Genome-wide association study reveals genetic risk underlying Parkinson's disease

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Two transmembrane aspartates in presenilin-1 required for presenilin endoproteolysis and γ-secretase activity

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Reducing Endogenous Tau Ameliorates Amyloid ß-Induced Deficits in an Alzheimer's Disease Mouse Model

Roberson, E. D., Scearce-Levie, K., Palop, J. J., Yan, F., Cheng, I. H., Wu, T., Gerstein, H., Yu, G.-Q., & Mucke, L. (2007) · Science · doi:10.1126/science.1141736 · Cited by 1,892 · see citing works

Dendritic Function of Tau Mediates Amyloid-β Toxicity in Alzheimer's Disease Mouse Models

Ittner, L. M., Ke, Y. D., Delerue, F., Bi, M., Gladbach, A., van Eersel, J., Wölfing, H., Chieng, B. C., Christie, M. J., Napier, I. A., et al. (2010) · Cell · doi:10.1016/j.cell.2010.06.036 · Cited by 1,821 · see citing works

Microtubule-associated protein tau. A component of Alzheimer paired helical filaments.

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Progress in Clinical and Biological Research

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Formation of Neurofibrillary Tangles in P301L Tau Transgenic Mice Induced by Aβ42 Fibrils

Götz, J., Chen, F., van Dorpe, J., & Nitsch, R. M. (2001) · Science · doi:10.1126/science.1062097 · Cited by 1,526 · see citing works

Microtubule-associated protein tau (tau) is a major antigenic component of paired helical filaments in Alzheimer disease.

Kosik, K. S., Joachim, C. L., & Selkoe, D. J. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.11.4044 · Cited by 1,462 · see citing works

LITHIUM SALTS IN THE TREATMENT OF PSYCHOTIC EXCITEMENT

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GSK3 takes centre stage more than 20 years after its discovery

FRAME, S., & COHEN, P. (2001) · Biochemical Journal · doi:10.1042/0264-6021:3590001 · Cited by 1,433 · see citing works

Molecular cloning and expression of glycogen synthase kinase‐3/factor A.

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GSK-3α regulates production of Alzheimer's disease amyloid-β peptides

Phiel, C. J., Wilson, C., Lee, V. M. ‐., & Klein, P. S. (2003) · Nature · doi:10.1038/nature01640 · Cited by 1,200 · see citing works

Lithium salts in the treatment of psychotic excitement

Cade, J. F. (1999) · Australian & New Zealand Journal of Psychiatry · doi:10.1080/j.1440-1614.1999.06241.x · Cited by 1,146 · see citing works

Glycogen synthase kinase-3 from rabbit skeletal muscle. Separation from cyclic-AMP-dependent protein kinase and phosphorylase kinase.

Embi, N., Rylatt, D. B., & Cohen, P. (1980) · PubMed · Cited by 911 · see citing works

Decreased nuclear β‐catenin, tau hyperphosphorylation and neurodegeneration in GSK‐3β conditional transgenic mice

Lucas, J. J., Hernández, F., Gómez‐Ramos, P., Morán, M. A., Hen, R., & Avila, J. (2001) · The EMBO Journal · doi:10.1093/emboj/20.1.27 · Cited by 903 · see citing works

Abnormal tau phosphorylation at Ser396 in Alzheimer's disease recapitulates development and contributes to reduced microtubule binding

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Glycogen Synthase Kinase‐3 from Rabbit Skeletal Muscle

Noor, E. M. B. I., RYLATT, D. B., & Cohen, P. (1980) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1980.tb06059.x · Cited by 837 · see citing works

Altered microtubule organization in small-calibre axons of mice lacking tau protein

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Glycogen synthase kinase-3 induces Alzheimer's disease-like phosphorylation of tau: Generation of paired helical filament epitopes and neuronal localisation of the kinase

Hanger, D. P., Hughes, K., Woodgett, J. R., Brion, J.-P., & Anderton, B. H. (1992) · Neuroscience Letters · doi:10.1016/0304-3940(92)90774-2 · Cited by 737 · see citing works

Indirubins Inhibit Glycogen Synthase Kinase-3β and CDK5/P25, Two Protein Kinases Involved in Abnormal Tau Phosphorylation in Alzheimer's Disease

Leclerc, S., Garnier, M., Hoessel, R., Marko, D., Bibb, J. A., Snyder, G. L., Greengard, P., Biernat, J., Wu, Y., Mandelkow, E., et al. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m002466200 · Cited by 730 · see citing works

Inhibition of glycogen synthase kinase-3 by lithium correlates with reduced tauopathy and degeneration <i>in vivo</i>

Noble, W., Planel, E., Zehr, C., Olm, V., Meyerson, J., Suleman, F., Gaynor, K., Wang, L., LaFrancois, J., Feinstein, B., et al. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0500466102 · Cited by 709 · see citing works

LTP Inhibits LTD in the Hippocampus via Regulation of GSK3β

Peineau, S., Taghibiglou, C., Bradley, C. A., Wong, T. P., Liu, L., Lu, J., Lo, E., Wu, D., Saule, E., Bouschet, T., et al. (2007) · Neuron · doi:10.1016/j.neuron.2007.01.029 · Cited by 690 · see citing works

Crystal Structure of Glycogen Synthase Kinase 3β

Dajani, R., Fraser, E., Roe, S. M., Young, N., Good, V. M., Dale, T. C., & Pearl, L. H. (2001) · Cell · doi:10.1016/s0092-8674(01)00374-9 · Cited by 678 · see citing works

THE BIOCHEMISTRY OF PARKINSON'S DISEASE

Cookson, M. (2005) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.74.082803.133400 · Cited by 659 · see citing works

Activation of the Wnt Signaling Pathway: A Molecular Mechanism for Lithium Action

Hedgepeth, C. M., Conrad, L. J., Zhang, J., Huang, H., Lee, V. M.-Y., & Klein, P. S. (1997) · Developmental Biology · doi:10.1006/dbio.1997.8552 · Cited by 637 · see citing works

Lithium delays progression of amyotrophic lateral sclerosis

Fornai, F., Longone, P., Cafaro, L., Kastsiuchenka, O., Ferrucci, M., Manca, M. L., Lazzeri, G., Spalloni, A., Bellio, N., Lenzi, P., et al. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0708022105 · Cited by 550 · see citing works

Lithium activates the serine/threonine kinase Akt-1 and suppresses glutamate-induced inhibition of Akt-1 activity in neurons

Chalecka-Franaszek, E., & Chuang, D. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.15.8745 · Cited by 544 · see citing works

Glycogen synthase kinase‐3 and the Alzheimer‐like state of microtubule‐associated protein tau

Mandelkow, E.-M., Drewes, G., Biernat, J., Gustke, N., Van Lint, J., Vandenheede, J. R., & Mandelkow, E. (1992) · FEBS Letters · doi:10.1016/0014-5793(92)81496-9 · Cited by 515 · see citing works

Molecular Targets of Lithium Action

Phiel, C. J., & Klein, P. S. (2001) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.41.1.789 · Cited by 513 · see citing works

Genome-wide association study confirms SNPs in SNCA and the MAPT region as common risk factors for Parkinson disease

Edwards, T. L., Scott, W. K., Almonte, C., Burt, A., Powell, E., Beecham, G., Wang, L.-Y., Züchner, S., Konidari, I., Wang, G., et al. (2010) · Annals of Human Genetics · doi:10.1111/j.1469-1809.2009.00560.x · Cited by 512 · see citing works

Lithium Inhibits Glycogen Synthase Kinase-3 by Competition for Magnesium

Ryves, W. J., & Harwood, A. J. (2001) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2000.4169 · Cited by 495 · see citing works

Spherical aggregates of β-amyloid (amylospheroid) show high neurotoxicity and activate tau protein kinase I/glycogen synthase kinase-3β

Hoshi, M. M., Sato, M., Matsumoto, S., Noguchi, A., Yasutake, K., Yoshida, N., & Sato, K. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1237107100 · Cited by 494 · see citing works

Phosphorylation by p38 MAPK as an Alternative Pathway for GSK3β Inactivation

Thornton, T. M., Pedraza-Alva, G., Deng, B., Wood, C. D., Aronshtam, A., Clements, J. L., Sabio, G., Davis, R. J., Matthews, D. E., Doble, B., et al. (2008) · Science · doi:10.1126/science.1156037 · Cited by 484 · see citing works

Lithium Reduces Tau Phosphorylation by Inhibition of Glycogen Synthase Kinase-3

Hong, M., Chen, D. C. R., Klein, P. S., & Lee, V. M. ‐. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.40.25326 · Cited by 470 · see citing works

Alzheimer's disease-like phosphorylation of the microtubule-associated protein tau by glycogen synthase kinase-3 in transfected mammalian cells

Lovestone, S., Reynolds, C. H., Latimer, D. A., Davis, D. R., Anderton, B. H., Gallo, J., Hanger, D. P., Mulot, S., Marquardt, B., Stabel, S., et al. (1994) · Current Biology · doi:10.1016/s0960-9822(00)00246-3 · Cited by 470 · see citing works

Regulation of Akt and glycogen synthase kinase-3β phosphorylation by sodium valproate and lithium

Sarno, P. D., Li, X., & Jope, R. S. (2002) · Neuropharmacology · doi:10.1016/s0028-3908(02)00215-0 · Cited by 433 · see citing works

Glycogen Synthase Kinase-3β Haploinsufficiency Mimics the Behavioral and Molecular Effects of Lithium

O'Brien, W. T., Harper, A. D., Jove, F. A., Woodgett, J. R., Maretto, S., Piccolo, S., & Klein, P. S. (2004) · Journal of Neuroscience · doi:10.1523/jneurosci.4753-03.2004 · Cited by 415 · see citing works

Abnormal phosphorylation of the microtubule-associated protein? (tau) in Alzheimer cytoskeletal pathology

Grundke, I., Iqbal, K., Tung, Y.-C., Quinlan, M., Wisniewski, H., & Binder, L. (1987) · Alzheimer Disease & Associated Disorders · doi:10.1097/00002093-198701030-00020 · Cited by 410 · see citing works

Tau protein kinase I is essential for amyloid beta-protein-induced neurotoxicity.

Takashima, A., Noguchi, K., Sato, K., Hoshino, T., & Imahori, K. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.16.7789 · Cited by 381 · see citing works

Lithium and risk for Alzheimer's disease in elderly patients with bipolar disorder

Nunes, P. V., Forlenza, O. V., & Gattaz, W. F. (2007) · The British Journal of Psychiatry · doi:10.1192/bjp.bp.106.029868 · Cited by 369 · see citing works

A novel GSK-3β inhibitor reduces Alzheimer's pathology and rescues neuronal loss in vivo

Serenó, L., Coma, M., Rodríguez, M., Sánchez-Ferrer, P., Sánchez, M. B., Gich, I., Agulló, J. M., Pérez, M., Avila, J., Guardia-Laguarta, C., et al. (2009) · Neurobiology of Disease · doi:10.1016/j.nbd.2009.05.025 · Cited by 368 · see citing works

Mitochondrial Oxidative Stress Causes Hyperphosphorylation of Tau

Melov, S., Adlard, P. A., Morten, K., Johnson, F., Golden, T. R., Hinerfeld, D., Schilling, B., Mavros, C., Masters, C. L., Volitakis, I., et al. (2007) · PLoS ONE · doi:10.1371/journal.pone.0000536 · Cited by 363 · see citing works

Detection of Phosphorylated Ser262 in Fetal Tau, Adult Tau, and Paired Helical Filament Tau

Seubert, P., Mawal-Dewan, M., Barbour, R., Jakes, R., Goedert, M., Johnson, G. V. W., Litersky, J. M., Schenk, D., Lieberburg, I., Trojanowski, J. Q., et al. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.32.18917 · Cited by 345 · see citing works

Transgenic Mice Overexpressing Glycogen Synthase Kinase 3β: A Putative Model of Hyperactivity and Mania

Prickaerts, J., Moechars, D., Cryns, K., Lenaerts, I., van Craenendonck, H., Goris, I., Daneels, G., Bouwknecht, J. A., & Steckler, T. (2006) · The Journal of Neuroscience · doi:10.1523/jneurosci.5216-05.2006 · Cited by 341 · see citing works

Further evidence that the tyrosine phosphorylation of glycogen synthase kinase-3 (GSK3) in mammalian cells is an autophosphorylation event

Cole, A. R., Frame, S., & Cohen, P. (2004) · Biochemical Journal · doi:10.1042/bj20031259 · Cited by 324 · see citing works

Lithium inhibits Alzheimer's disease‐like tau protein phosphorylation in neurons

Muñoz-Montaño, J. R., Moreno, F. J., Ávila, J., & Díaz‐Nido, J. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)00688-1 · Cited by 322 · see citing works

Glycogen Synthase Kinase-3β Phosphorylates Protein Tau and Rescues the Axonopathy in the Central Nervous System of Human Four-repeat Tau Transgenic Mice

Spittaels, K., den Haute, C. V., Dorpe, J. V., Geerts, H., Mercken, M. H., Bruynseels, K., Lasrado, R., Vandezande, K., Laenen, I., Boon, T., et al. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m006219200 · Cited by 317 · see citing works

Lithium trial in Alzheimer's disease: a randomized, single-blind, placebo-controlled, multicenter 10-week study.

Hampel, H. J., Ewers, M., Bürger, K., Annas, P., Mörtberg, A., Bogstedt, A., Frölich, L., Schröder, J., Schönknecht, P., Riepe, M. W., et al. (2009) · PubMed · Cited by 305 · see citing works

Amyloid Activates GSK-3β to Aggravate Neuronal Tauopathy in Bigenic Mice

Terwel, D., Muyllaert, D., Dewachter, I., Borghgraef, P., Croes, S., Devijver, H., & Van Leuven, F. (2008) · The American Journal of Pathology · doi:10.2353/ajpath.2008.070904 · Cited by 300 · see citing works

Lithium Trial in Alzheimer's Disease

Hampel, H. J., Ewers, M., Bürger, K., Annas, P., Mörtberg, A., Bogstedt, A., Frölich, L., Schröder, J., Schönknecht, P., Riepe, M. W., et al. (2009) · The Journal of Clinical Psychiatry · doi:10.4088/jcp.08m04606 · Cited by 297 · see citing works

Lithium, a Common Drug for Bipolar Disorder Treatment, Regulates Amyloid-β Precursor Protein Processing

Yuan, S., Ryder, J. W., Li, B., Wu, X., Fox, N. W., Solenberg, P., Brune, K. A., Paul, S. M., Zhou, Y., Liu, F., et al. (2004) · Biochemistry · doi:10.1021/bi035627j · Cited by 295 · see citing works

Activation of Wnt signaling by lithium and rosiglitazone reduced spatial memory impairment and neurodegeneration in brains of an APPswe/PSEN1ΔE9 mouse model of Alzheimer's disease

Toledo, E. M., & Inestrosa, N. C. (2009) · Molecular Psychiatry · doi:10.1038/mp.2009.72 · Cited by 290 · see citing works

Activation of tau protein kinase I/glycogen synthase kinase-3β by amyloid β peptide (25–35) enhances phosphorylation of tau in hippocampal neurons

Takashima, A., Honda, T., Yasutake, K., Michel, G., Murayama, O., Murayama, M., Ishiguro, K., & Yamaguchi, H. (1998) · Neuroscience Research · doi:10.1016/s0168-0102(98)00061-3 · Cited by 287 · see citing works

Neuroprotective Effects of Regulators of the Glycogen Synthase Kinase-3β Signaling Pathway in a Transgenic Model of Alzheimer's Disease Are Associated with Reduced Amyloid Precursor Protein Phosphorylation

Rockenstein, E. M., Torrance, M., Adame, A., Mante, M., Bar‐On, P., Rose, J. B., Crews, L. A., & Masliah, E. (2007) · Journal of Neuroscience · doi:10.1523/jneurosci.4321-06.2007 · Cited by 286 · see citing works

Glycogen synthase from rabbit skeletal muscle. Amino acid sequence at the sites phosphorylated by glycogen synthase kinase-3, and extension of the N-terminal sequence containing the site phosphorylated by phosphorylase kinase.

Rylatt, D. B., Aitken, A., Bilham, T., Condon, G. D., Embi, N., & Cohen, P. (1980) · PubMed · Cited by 285 · see citing works

Glycogen Synthase Kinase-3 - An Overview of An Over-Achieving Protein Kinase

Kockeritz, L. K., Doble, B. W., Patel, S., & Woodgett, J. R. (2006) · Current Drug Targets · doi:10.2174/1389450110607011377 · Cited by 285 · see citing works

Microtubule-Associated Protein Tau

Yen, S.-H. C., Nacharaju, P., Ko, L., Kenessey, Á., & Liu, W.-K. (1998) · Elsevier eBooks · doi:10.1016/b978-012734610-6/50012-9 · Cited by 284 · see citing works

Increasing Cu bioavailability inhibits Aβ oligomers and tau phosphorylation

Crouch, P. J., Hung, L. W., Adlard, P. A., Cortés, M., Lal, V., Filiz, G., Perez, K. A., Nurjono, M., Caragounis, A., Du, T., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0809057106 · Cited by 280 · see citing works

α‐Synuclein contributes to GSK‐3β‐catalyzed Tau phosphorylation in Parkinson's disease models

Duka, T., Duka, V., Joyce, J. N., & Sidhu, A. (2009) · The FASEB Journal · doi:10.1096/fj.08-120410 · Cited by 276 · see citing works

Glycogen Synthase Kinase 3β Phosphorylates Tau at Both Primed and Unprimed Sites

Cho, J.-H., & Johnson, G. V. W. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m206236200 · Cited by 266 · see citing works

Full Reversal of Alzheimer's Disease-Like Phenotype in a Mouse Model with Conditional Overexpression of Glycogen Synthase Kinase-3

Engel, T., Hernández, F., Ávila, J., & Lucas, J. J. (2006) · Journal of Neuroscience · doi:10.1523/jneurosci.0604-06.2006 · Cited by 261 · see citing works

Exposure of rat hippocampal neurons to amyloid β peptide (25–35) induces the inactivation of phosphatidyl inositol-3 kinase and the activation of tau protein kinase I/glycogen synthase kinase-3β

Takashima, A., Noguchi, K., Michel, G., Mercken, M., Hoshi, M., Ishiguro, K., & Imahori, K. (1996) · Neuroscience Letters · doi:10.1016/0304-3940(95)12257-5 · Cited by 260 · see citing works

Preferential labeling of Alzheimer neurofibrillary tangles with antisera for tau protein kinase (TPK) I/glycogen synthase kinase-3β and cyclin-dependent kinase 5, a component of TPK II

Yamaguchi, H., Ishiguro, K., Uchida, T., Takashima, A., Lemere, C. A., & Imahori, K. (1996) · Acta Neuropathologica · doi:10.1007/s004010050513 · Cited by 253 · see citing works

Alzheimer's disease-like pathological features in transgenic mice expressing the APP intracellular domain

Ghosal, K., Vogt, D. L., Liang, M., Shen, Y., Lamb, B. T., & Pimplikar, S. W. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0907652106 · Cited by 245 · see citing works

Insulin Transiently Increases Tau Phosphorylation

Lesort, M. J., Jope, R. S., & Johnson, G. V. W. (1999) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1999.0720576.x · Cited by 240 · see citing works

Inactivation of Glycogen Synthase Kinase 3 Promotes Axonal Growth and Recovery in the CNS

Dill, J., Wang, H., Zhou, F., & Li, S. (2008) · Journal of Neuroscience · doi:10.1523/jneurosci.1178-08.2008 · Cited by 229 · see citing works

Combined lithium and valproate treatment delays disease onset, reduces neurological deficits and prolongs survival in an amyotrophic lateral sclerosis mouse model

Feng, H., Leng, Y., Ma, C., Zhang, J., Ren, M., & Chuang, D. M. (2008) · Neuroscience · doi:10.1016/j.neuroscience.2008.06.040 · Cited by 228 · see citing works

Overactivation of glycogen synthase kinase‐3 by inhibition of phosphoinositol‐3 kinase and protein kinase C leads to hyperphosphorylation of tau and impairment of spatial memory

Liu, S. J., Zhang, A. H., Li, H. L., Wang, Q., Deng, H. M., Netzer, W. J., Xu, H., & Wang, J. Z. (2003) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2003.02070.x · Cited by 225 · see citing works

Chronic lithium administration to FTDP‐17 tau and GSK‐3β overexpressing mice prevents tau hyperphosphorylation and neurofibrillary tangle formation, but pre‐formed neurofibrillary tangles do not revert

Engel, T., Goñi‐Oliver, P., Lucas, J. J., Avila, J., & Hernández, F. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.04139.x · Cited by 223 · see citing works

Lithium Reduces Tau Phosphorylation but Not Aβ or Working Memory Deficits in a Transgenic Model with Both Plaques and Tangles

Caccamo, A., Oddo, S., Tran, L. X., & LaFerla, F. M. (2007) · American Journal Of Pathology · doi:10.2353/ajpath.2007.061178 · Cited by 218 · see citing works

Amyloid- Peptide Oligomers Disrupt Axonal Transport through an NMDA Receptor-Dependent Mechanism That Is Mediated by Glycogen Synthase Kinase 3 in Primary Cultured Hippocampal Neurons

Decker, H., Lo, K. Y., Unger, S. M., Ferreira, S. T., & Silverman, M. A. (2010) · Journal of Neuroscience · doi:10.1523/jneurosci.1074-10.2010 · Cited by 216 · see citing works

Does lithium protect against dementia?

Kessing, L. V., Forman, J. L., & Andersen, P. K. (2010) · Bipolar Disorders · doi:10.1111/j.1399-5618.2009.00788.x · Cited by 215 · see citing works

Glycogen Synthase from Rabbit Skeletal Muscle

Rylatt, D. B., Aitken, A., Bilham, T., Condon, G. D., Embi, N., & Cohen, P. (1980) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1980.tb06060.x · Cited by 212 · see citing works

Elevated tauopathy and alpha-synuclein pathology in postmortem Parkinson's disease brains with and without dementia

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<i>GSK3B</i> polymorphisms alter transcription and splicing in Parkinson's disease

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