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Volumn 2015, Issue , 2015, Pages

The role of α-synuclein and LRRK2 in tau phosphorylation

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA SYNUCLEIN; HEAT SHOCK PROTEIN; LEUCINE RICH REPEAT KINASE 2; TAU PROTEIN;

EID: 84929353300     PISSN: None     EISSN: 20420080     Source Type: Journal    
DOI: 10.1155/2015/734746     Document Type: Review
Times cited : (17)

References (93)
  • 3
    • 33750705653 scopus 로고    scopus 로고
    • A century of Alzheimer's disease
    • M. Goedert and M. G. Spillantini, "A century of Alzheimer's disease, " Science, vol. 314, no. 5800, pp. 777-781, 2006.
    • (2006) Science , vol.314 , Issue.5800 , pp. 777-781
    • Goedert, M.1    Spillantini, M.G.2
  • 4
    • 0022365608 scopus 로고
    • The distribution of tau in the mammalian central nervous system
    • L. I. Binder, A. Frankfurter, and L. I. Rebhun, "The distribution of tau in the mammalian central nervous system, " The Journal of Cell Biology, vol. 101, no. 4, pp. 1371-1378, 1985.
    • (1985) The Journal of Cell Biology , vol.101 , Issue.4 , pp. 1371-1378
    • Binder, L.I.1    Frankfurter, A.2    Rebhun, L.I.3
  • 5
    • 0022827447 scopus 로고
    • Identification of cDNA clones for the human microtubuleassociated protein tau and chromosomal localization of the genes for tau and microtubule-associated protein 2
    • R. L. Neve, P. Harris, K. S. Kosik, D. M. Kurnit, andT. A. Donlon, "Identification of cDNA clones for the human microtubuleassociated protein tau and chromosomal localization of the genes for tau and microtubule-associated protein 2, " Brain Research, vol. 387, no. 3, pp. 271-280, 1986.
    • (1986) Brain Research , vol.387 , Issue.3 , pp. 271-280
    • Neve, R.L.1    Harris, P.2    Kosik, K.S.3    Kurnit, D.M.4    Donlon, T.A.5
  • 6
    • 0024745894 scopus 로고
    • Multiple isoforms of humanmicrotubule-associated protein tau: Sequences and localization in neurofibrillary tangles of Alzheimer's disease
    • M. Goedert, M. G. Spillantini, R. Jakes, D. Rutherford, andR. A. Crowther, "Multiple isoforms of humanmicrotubule-associated protein tau: sequences and localization in neurofibrillary tangles of Alzheimer's disease, " Neuron, vol. 3, no. 4, pp. 519-526, 1989.
    • (1989) Neuron , vol.3 , Issue.4 , pp. 519-526
    • Goedert, M.1    Spillantini, M.G.2    Jakes, R.3    Rutherford, D.4    Crowther, R.A.5
  • 7
    • 0026488111 scopus 로고
    • Structure and novel exons of the human tau gene
    • A. Andreadis, W. M. Brown, and K. S. Kosik, "Structure and novel exons of the human tau gene, " Biochemistry, vol. 31, no. 43, pp. 10626-10633, 1992.
    • (1992) Biochemistry , vol.31 , Issue.43 , pp. 10626-10633
    • Andreadis, A.1    Brown, W.M.2    Kosik, K.S.3
  • 8
    • 0025600995 scopus 로고
    • Expression of separate isoforms of human tau protein: Correlation with the tau pattern in brain and effects on tubulin polymerization
    • M. Goedert and R. Jakes, "Expression of separate isoforms of human tau protein: correlation with the tau pattern in brain and effects on tubulin polymerization, " The EMBO Journal, vol. 9, no. 13, pp. 4225-4230, 1990.
    • (1990) The EMBO Journal , vol.9 , Issue.13 , pp. 4225-4230
    • Goedert, M.1    Jakes, R.2
  • 9
    • 0024641959 scopus 로고
    • Developmentally regulated expression of specific tau sequences
    • K. S. Kosik, L. D. Orecchio, S. Bakalis, and R. L. Neve, "Developmentally regulated expression of specific tau sequences, " Neuron, vol. 2, no. 4, pp. 1389-1397, 1989.
    • (1989) Neuron , vol.2 , Issue.4 , pp. 1389-1397
    • Kosik, K.S.1    Orecchio, L.D.2    Bakalis, S.3    Neve, R.L.4
  • 10
    • 0024675418 scopus 로고
    • The microtubule binding domain of tau protein
    • G. Lee, R. L. Neve, and K. S. Kosik, "The microtubule binding domain of tau protein, " Neuron, vol. 2, no. 6, pp. 1615-1624, 1989.
    • (1989) Neuron , vol.2 , Issue.6 , pp. 1615-1624
    • Lee, G.1    Neve, R.L.2    Kosik, K.S.3
  • 11
    • 0024094998 scopus 로고
    • Tau proteins: The molecular structure and mode of binding on microtubules
    • N. Hirokawa, Y. Shiomura, and S. Okabe, "Tau proteins: the molecular structure and mode of binding on microtubules, " Journal of Cell Biology, vol. 107, no. 4, pp. 1449-1459, 1988.
    • (1988) Journal of Cell Biology , vol.107 , Issue.4 , pp. 1449-1459
    • Hirokawa, N.1    Shiomura, Y.2    Okabe, S.3
  • 12
    • 0344505849 scopus 로고    scopus 로고
    • Tau interacts with src-family non-receptor tyrosine kinases
    • G. Lee, S. T. Newman, D. L. Gard, H. Band, and G. Panchamoorthy, "Tau interacts with src-family non-receptor tyrosine kinases, " Journal of Cell Science, vol. 111, no. 21, pp. 3167-3177, 1998.
    • (1998) Journal of Cell Science , vol.111 , Issue.21 , pp. 3167-3177
    • Lee, G.1    Newman, S.T.2    Gard, D.L.3    Band, H.4    Panchamoorthy, G.5
  • 13
    • 1642289188 scopus 로고    scopus 로고
    • Role of tau protein in both physiological and pathological conditions
    • J. Avila, J. J. Lucas, M. Pérez, and F. Hernández, "Role of tau protein in both physiological and pathological conditions, " Physiological Reviews, vol. 84, no. 2, pp. 361-384, 2004.
    • (2004) Physiological Reviews , vol.84 , Issue.2 , pp. 361-384
    • Avila, J.1    Lucas, J.J.2    Pérez, M.3    Hernández, F.4
  • 14
    • 79952105548 scopus 로고    scopus 로고
    • Post-translational modifications of tau protein: Implications for Alzheimer's disease
    • L. Martin, X. Latypova, and F. Terro, "Post-translational modifications of tau protein: implications for Alzheimer's disease, " Neurochemistry International, vol. 58, no. 4, pp. 458-471, 2011.
    • (2011) Neurochemistry International , vol.58 , Issue.4 , pp. 458-471
    • Martin, L.1    Latypova, X.2    Terro, F.3
  • 16
    • 0032987650 scopus 로고    scopus 로고
    • Phosphorylation of tau protein by recombinant GSK-3: Pronounced phosphorylation at select Ser/Thr-Pro motifs but no phosphorylation at Ser262 in the repeat domain
    • R. Godemann, J. Biernat, E. Mandelkow, and E.-M. Mandelkow, "Phosphorylation of tau protein by recombinant GSK-3: pronounced phosphorylation at select Ser/Thr-Pro motifs but no phosphorylation at Ser262 in the repeat domain, " FEBS Letters, vol. 454, no. 1-2, pp. 157-164, 1999.
    • (1999) FEBS Letters , vol.454 , Issue.1-2 , pp. 157-164
    • Godemann, R.1    Biernat, J.2    Mandelkow, E.3    Mandelkow, E.-M.4
  • 17
    • 0040141570 scopus 로고    scopus 로고
    • Interaction of tau with the neural membrane cortex is regulated by phosphorylation at sites that are modified in paired helical filaments
    • T. Maas, J. Eidenmüller, and R. Brandt, "Interaction of tau with the neural membrane cortex is regulated by phosphorylation at sites that are modified in paired helical filaments, " The Journal of Biological Chemistry, vol. 275, no. 21, pp. 15733-15740, 2000.
    • (2000) The Journal of Biological Chemistry , vol.275 , Issue.21 , pp. 15733-15740
    • Maas, T.1    Eidenmüller, J.2    Brandt, R.3
  • 18
    • 0029998294 scopus 로고    scopus 로고
    • Cellular phosphorylation of tau by GSK-3 influences tau binding to microtubules and microtubule organisation
    • U. Wagner, M. Utton, J.-M. Gallo, and C. C. J. Miller, "Cellular phosphorylation of tau by GSK-3 influences tau binding to microtubules and microtubule organisation, " Journal of Cell Science, vol. 109, no. 6, pp. 1537-1543, 1996.
    • (1996) Journal of Cell Science , vol.109 , Issue.6 , pp. 1537-1543
    • Wagner, U.1    Utton, M.2    Gallo, J.-M.3    Miller, C.C.J.4
  • 19
    • 84891832231 scopus 로고    scopus 로고
    • Leucine-rich repeat kinase 2 regulates tau phosphorylation through direct activation of glycogen synthase kinase-3
    • F. Kawakami, N. Shimada, E. Ohta et al. , "Leucine-rich repeat kinase 2 regulates tau phosphorylation through direct activation of glycogen synthase kinase-3, " FEBS Journal, vol. 281, no. 1, pp. 3-13, 2014.
    • (2014) FEBS Journal , vol.281 , Issue.1 , pp. 3-13
    • Kawakami, F.1    Shimada, N.2    Ohta, E.3
  • 20
    • 84856404449 scopus 로고    scopus 로고
    • LRRK2 phosphorylates tubulin-associated tau but not the free molecule: LRRK2-mediated regulation of the tau-tubulin association and neurite outgrowth
    • F. Kawakami, T. Yabata, E. Ohta et al. , "LRRK2 phosphorylates tubulin-associated tau but not the free molecule: LRRK2-mediated regulation of the tau-tubulin association and neurite outgrowth, " PLoS ONE, vol. 7, no. 1, Article ID e30834, 2012.
    • (2012) PLoS ONE , vol.7 , Issue.1
    • Kawakami, F.1    Yabata, T.2    Ohta, E.3
  • 21
    • 82755177802 scopus 로고    scopus 로고
    • Stimulatory effect of-synuclein on the tau-phosphorylation by GSK-3
    • F. Kawakami, M. Suzuki, N. Shimada et al. , "Stimulatory effect of-synuclein on the tau-phosphorylation by GSK-3, " The FEBS Journal, vol. 278, no. 24, pp. 4895-4904, 2011.
    • (2011) The FEBS Journal , vol.278 , Issue.24 , pp. 4895-4904
    • Kawakami, F.1    Suzuki, M.2    Shimada, N.3
  • 22
    • 0031763264 scopus 로고    scopus 로고
    • The synuclein family
    • C. Lavedan, "The synuclein family, " Genome Research, vol. 8, no. 9, pp. 871-880, 1998.
    • (1998) Genome Research , vol.8 , Issue.9 , pp. 871-880
    • Lavedan, C.1
  • 23
    • 80555155665 scopus 로고    scopus 로고
    • Therole of alpha-synuclein in neurotransmission and synaptic plasticity
    • F. Cheng, G. Vivacqua, and S. Yu, "Therole of alpha-synuclein in neurotransmission and synaptic plasticity, " Journal of Chemical Neuroanatomy, vol. 42, no. 4, pp. 242-248, 2011.
    • (2011) Journal of Chemical Neuroanatomy , vol.42 , Issue.4 , pp. 242-248
    • Cheng, F.1    Vivacqua, G.2    Yu, S.3
  • 24
    • 0028985267 scopus 로고
    • The precursor protein of non-A component of Alzheimer's disease amyloid is a presynaptic protein of the central nervous system
    • A. Iwai, E. Masliah, M. Yoshimoto et al. , "The precursor protein of non-A component of Alzheimer's disease amyloid is a presynaptic protein of the central nervous system, " Neuron, vol. 14, no. 2, pp. 467-475, 1995.
    • (1995) Neuron , vol.14 , Issue.2 , pp. 467-475
    • Iwai, A.1    Masliah, E.2    Yoshimoto, M.3
  • 25
    • 0035964758 scopus 로고    scopus 로고
    • Altered expression of the synuclein family mRNA in Lewy body and Alzheimer's disease
    • E. Rockenstein, L. A. Hansen, M. Mallory, J. Q. Trojanowski, D. Galasko, and E. Masliah, "Altered expression of the synuclein family mRNA in Lewy body and Alzheimer's disease, " Brain Research, vol. 914, no. 1-2, pp. 48-56, 2001.
    • (2001) Brain Research , vol.914 , Issue.1-2 , pp. 48-56
    • Rockenstein, E.1    Hansen, L.A.2    Mallory, M.3    Trojanowski, J.Q.4    Galasko, D.5    Masliah, E.6
  • 26
    • 44049099669 scopus 로고    scopus 로고
    • Mitochondrial import and accumulation of-synuclein impair complex i in human dopaminergic neuronal cultures and Parkinson disease brain
    • L. Devi, V. Raghavendran, B. M. Prabhu, N. G. Avadhani, and H. K. Anandatheerthavarada, "Mitochondrial import and accumulation of-synuclein impair complex I in human dopaminergic neuronal cultures and Parkinson disease brain, " The Journal of Biological Chemistry, vol. 283, no. 14, pp. 9089-9100, 2008.
    • (2008) The Journal of Biological Chemistry , vol.283 , Issue.14 , pp. 9089-9100
    • Devi, L.1    Raghavendran, V.2    Prabhu, B.M.3    Avadhani, N.G.4    Anandatheerthavarada, H.K.5
  • 27
    • 84915746157 scopus 로고    scopus 로고
    • Alpha-synuclein binds to the inner membrane of mitochondria in an-helical conformation
    • M. Robotta, H. R. Gerding, A. Vogel et al. , "Alpha-synuclein binds to the inner membrane of mitochondria in an-helical conformation, " ChemBioChem, vol. 15, no. 17, pp. 2499-2502, 2014.
    • (2014) ChemBioChem , vol.15 , Issue.17 , pp. 2499-2502
    • Robotta, M.1    Gerding, H.R.2    Vogel, A.3
  • 28
    • 0032540327 scopus 로고    scopus 로고
    • Stabilization of-synuclein secondary structure upon binding to synthetic membranes
    • W. S. Davidson, A. Jonas, D. F. Clayton, and J. M. George, "Stabilization of-synuclein secondary structure upon binding to synthetic membranes, " The Journal of Biological Chemistry, vol. 273, no. 16, pp. 9443-9449, 1998.
    • (1998) The Journal of Biological Chemistry , vol.273 , Issue.16 , pp. 9443-9449
    • Davidson, W.S.1    Jonas, A.2    Clayton, D.F.3    George, J.M.4
  • 29
    • 0043157875 scopus 로고    scopus 로고
    • Synuclein expression localizes to the Golgi apparatus in bovine adrenal medullary chromaffin cells
    • M. M. Tompkins, W. P. Gai, S. Douglas, and S. J. Bunn, "-synuclein expression localizes to the Golgi apparatus in bovine adrenal medullary chromaffin cells, " Brain Research, vol. 984, no. 1-2, pp. 233-236, 2003.
    • (2003) Brain Research , vol.984 , Issue.1-2 , pp. 233-236
    • Tompkins, M.M.1    Gai, W.P.2    Douglas, S.3    Bunn, S.J.4
  • 30
    • 77957347060 scopus 로고    scopus 로고
    • Synuclein promotes SNARE-complex assembly in vivo and in vitro
    • J. Burré, M. Sharma, T. Tsetsenis, V. Buchman, M. R. Etherton, and T. C. Südhof, "-Synuclein promotes SNARE-complex assembly in vivo and in vitro, " Science, vol. 329, no. 5999, pp. 1663-1667, 2010.
    • (2010) Science , vol.329 , Issue.5999 , pp. 1663-1667
    • Burré, J.1    Sharma, M.2    Tsetsenis, T.3    Buchman, V.4    Etherton, M.R.5    Südhof, T.C.6
  • 33
    • 32544442518 scopus 로고    scopus 로고
    • Gastric-synuclein immunoreactive inclusions in Meissner's and Auerbach's plexuses in cases staged for Parkinson's diseaserelated brain pathology
    • H. Braak, R. A. I. de Vos, J. Bohl, and K. Del Tredici, "Gastric-synuclein immunoreactive inclusions in Meissner's and Auerbach's plexuses in cases staged for Parkinson's diseaserelated brain pathology, " Neuroscience Letters, vol. 396, no. 1, pp. 67-72, 2006.
    • (2006) Neuroscience Letters , vol.396 , Issue.1 , pp. 67-72
    • Braak, H.1    De Vos, R.A.I.2    Bohl, J.3    Del Tredici, K.4
  • 34
    • 0035409575 scopus 로고    scopus 로고
    • Alpha-synuclein and neurodegenerative diseases
    • M. Goedert, "Alpha-synuclein and neurodegenerative diseases, " Nature Reviews Neuroscience, vol. 2, no. 7, pp. 492-501, 2001.
    • (2001) Nature Reviews Neuroscience , vol.2 , Issue.7 , pp. 492-501
    • Goedert, M.1
  • 35
    • 77951185469 scopus 로고    scopus 로고
    • Genome-Wide association study confirms SNPs in SNCA and the MAPT region as common risk factors for parkinson disease
    • T. L. Edwards, W. K. Scott, C. Almonte et al. , "Genome-Wide association study confirms SNPs in SNCA and the MAPT region as common risk factors for parkinson disease, " Annals of Human Genetics, vol. 74, no. 2, pp. 97-109, 2010.
    • (2010) Annals of Human Genetics , vol.74 , Issue.2 , pp. 97-109
    • Edwards, T.L.1    Scott, W.K.2    Almonte, C.3
  • 36
    • 70549088602 scopus 로고    scopus 로고
    • Genome-wide association study reveals genetic risk underlying Parkinson's disease
    • J. Simón-Sánchez, C. Schulte, J. M. Bras et al. , "Genome-wide association study reveals genetic risk underlying Parkinson's disease, " Nature Genetics, vol. 41, no. 12, pp. 1308-1312, 2009.
    • (2009) Nature Genetics , vol.41 , Issue.12 , pp. 1308-1312
    • Simón-Sánchez, J.1    Schulte, C.2    Bras, J.M.3
  • 37
    • 0033945604 scopus 로고    scopus 로고
    • NACP/-synuclein and tau constitute two distinctive subsets of filaments in the same neuronal inclusions in brains from a family of parkinsonism and dementia with Lewy bodies: Double-immunolabeling fluorescence and electron microscopic studies
    • K. Arima, T. Mizutani, M. A. Alim et al. , "NACP/-synuclein and tau constitute two distinctive subsets of filaments in the same neuronal inclusions in brains from a family of parkinsonism and dementia with Lewy bodies: double-immunolabeling fluorescence and electron microscopic studies, " Acta Neuropathologica, vol. 100, no. 2, pp. 115-121, 2000.
    • (2000) Acta Neuropathologica , vol.100 , Issue.2 , pp. 115-121
    • Arima, K.1    Mizutani, T.2    Alim, M.A.3
  • 38
    • 33947537591 scopus 로고    scopus 로고
    • Proteomic identification of novel proteins in cortical Lewy bodies
    • J. B. Leverenz, I. Umar, Q. Wang et al. , "Proteomic identification of novel proteins in cortical Lewy bodies, " Brain Pathology, vol. 17, no. 2, pp. 139-145, 2007.
    • (2007) Brain Pathology , vol.17 , Issue.2 , pp. 139-145
    • Leverenz, J.B.1    Umar, I.2    Wang, Q.3
  • 39
    • 34248595601 scopus 로고    scopus 로고
    • Synuclein and its disease-related mutants interact differentially with the microtubule protein tau and associate with the actin cytoskeleton
    • A. Esposito, C. P. Dohm, P. Kermer, M. Bähr, and F. S. Wouters, "-synuclein and its disease-related mutants interact differentially with the microtubule protein tau and associate with the actin cytoskeleton, " Neurobiology of Disease, vol. 26, no. 3, pp. 521-531, 2007.
    • (2007) Neurobiology of Disease , vol.26 , Issue.3 , pp. 521-531
    • Esposito, A.1    Dohm, C.P.2    Kermer, P.3    Bähr, M.4    Wouters, F.S.5
  • 40
    • 33845643466 scopus 로고    scopus 로고
    • Alpha-synuclein induces hyperphosphorylation of Tau in the MPTP model of Parkinsonism
    • T. Duka, M. Rusnak, R. E. Drolet et al. , "Alpha-synuclein induces hyperphosphorylation of Tau in the MPTP model of Parkinsonism, " The FASEB Journal, vol. 20, no. 13, pp. 2302-2312, 2006.
    • (2006) The FASEB Journal , vol.20 , Issue.13 , pp. 2302-2312
    • Duka, T.1    Rusnak, M.2    Drolet, R.E.3
  • 41
    • 0033520474 scopus 로고    scopus 로고
    • Synuclein binds to tau and stimulates the protein kinase A-catalyzed tau phosphorylation of serine residues 262 and 356
    • P. H. Jensen, H. Hager, M. S. Nielsen, P. Højrup, J. Gliemann, and R. Jakes, "-synuclein binds to tau and stimulates the protein kinase A-catalyzed tau phosphorylation of serine residues 262 and 356, "The Journal of Biological Chemistry, vol. 274, no. 36, pp. 25481-25489, 1999.
    • (1999) The Journal of Biological Chemistry , vol.274 , Issue.36 , pp. 25481-25489
    • Jensen, P.H.1    Hager, H.2    Nielsen, M.S.3    Højrup, P.4    Gliemann, J.5    Jakes, R.6
  • 42
    • 70349331692 scopus 로고    scopus 로고
    • Synuclein contributes to GSK-3-catalyzed Tau phosphorylation in Parkinson's disease models
    • T. Duka, V. Duka, J. N. Joyce, and A. Sidhu, "-synuclein contributes to GSK-3-catalyzed Tau phosphorylation in Parkinson's disease models, " The FASEB Journal, vol. 23, no. 9, pp. 2820-2830, 2009.
    • (2009) The FASEB Journal , vol.23 , Issue.9 , pp. 2820-2830
    • Duka, T.1    Duka, V.2    Joyce, J.N.3    Sidhu, A.4
  • 43
    • 3042558276 scopus 로고    scopus 로고
    • Glycogen synthase kinase 3:adrug target forCNS therapies
    • R. V. Bhat, S. L. B. Haeberlein, and J. Avila, "Glycogen synthase kinase 3:adrug target forCNS therapies, " Journal ofNeurochemistry, vol. 89, no. 6, pp. 1313-1317, 2004.
    • (2004) Journal OfNeurochemistry , vol.89 , Issue.6 , pp. 1313-1317
    • Bhat, R.V.1    Haeberlein, S.L.B.2    Avila, J.3
  • 44
    • 7244243876 scopus 로고    scopus 로고
    • Stabilization of-synuclein protein with aging and familial Parkinson's disease-linked A53T mutation
    • W. Li, C. Lesuisse, Y. Xu, J. C. Troncoso, D. L. Price, and M. K. Lee, "Stabilization of-synuclein protein with aging and familial Parkinson's disease-linked A53T mutation, " Journal of Neuroscience, vol. 24, no. 33, pp. 7400-7409, 2004.
    • (2004) Journal of Neuroscience , vol.24 , Issue.33 , pp. 7400-7409
    • Li, W.1    Lesuisse, C.2    Xu, Y.3    Troncoso, J.C.4    Price, D.L.5    Lee, M.K.6
  • 45
    • 79951936156 scopus 로고    scopus 로고
    • The decrease of-synuclein in cortical brain areas defines a molecular subgroup of dementia with Lewy bodies
    • K. Beyer, M. Domingo-Sàbat, C. Santos, E. Tolosa, I. Ferrer, and A. Ariza, "The decrease of-synuclein in cortical brain areas defines a molecular subgroup of dementia with Lewy bodies, " Brain, vol. 133, no. 12, pp. 3724-3733, 2010.
    • (2010) Brain , vol.133 , Issue.12 , pp. 3724-3733
    • Beyer, K.1    Domingo-Sàbat, M.2    Santos, C.3    Tolosa, E.4    Ferrer, I.5    Ariza, A.6
  • 46
    • 0034602176 scopus 로고    scopus 로고
    • Parkinson's diseaseassociated-synuclein is more fibrillogenic than-and-synuclein and cannot cross-seed its homologs
    • A. L. Biere, S. J. Wood, J. Wypych et al. , "Parkinson's diseaseassociated-synuclein is more fibrillogenic than-and-synuclein and cannot cross-seed its homologs, " The Journal of Biological Chemistry, vol. 275, no. 44, pp. 34574-34579, 2000.
    • (2000) The Journal of Biological Chemistry , vol.275 , Issue.44 , pp. 34574-34579
    • Biere, A.L.1    Wood, S.J.2    Wypych, J.3
  • 48
    • 0026046950 scopus 로고
    • Tau protein binds to microtubules through a flexible array of distributed weak sites
    • K. A. Butner and M. W. Kirschner, "Tau protein binds to microtubules through a flexible array of distributed weak sites, " The Journal of Cell Biology, vol. 115, no. 3, pp. 717-730, 1991.
    • (1991) The Journal of Cell Biology , vol.115 , Issue.3 , pp. 717-730
    • Butner, K.A.1    Kirschner, M.W.2
  • 49
    • 0026694783 scopus 로고
    • Brain levels of microtubule-associated protein tau are elevated in Alzheimer's disease: A radioimmuno-slot-blot assay for nanograms of the protein
    • S. Khatoon, I. Grundke-Iqbal, and K. Iqbal, "Brain levels of microtubule-associated protein tau are elevated in Alzheimer's disease: a radioimmuno-slot-blot assay for nanograms of the protein, " Journal of Neurochemistry, vol. 59, no. 2, pp. 750-753, 1992.
    • (1992) Journal of Neurochemistry , vol.59 , Issue.2 , pp. 750-753
    • Khatoon, S.1    Grundke-Iqbal, I.2    Iqbal, K.3
  • 50
    • 8844266996 scopus 로고    scopus 로고
    • Cloning of the gene containing mutations that cause PARK8-linked Parkinson's disease
    • C. Paisán-Rúz, S. Jain, E. W. Evans et al. , "Cloning of the gene containing mutations that cause PARK8-linked Parkinson's disease, " Neuron, vol. 44, no. 4, pp. 595-600, 2004.
    • (2004) Neuron , vol.44 , Issue.4 , pp. 595-600
    • Paisán-Rúz, C.1
  • 51
    • 8844233579 scopus 로고    scopus 로고
    • Mutations in LRRK2 cause autosomal-dominant parkinsonism with pleomorphic pathology
    • A. Zimprich, S. Biskup, P. Leitner et al. , "Mutations in LRRK2 cause autosomal-dominant parkinsonism with pleomorphic pathology, " Neuron, vol. 44, no. 4, pp. 601-607, 2004.
    • (2004) Neuron , vol.44 , Issue.4 , pp. 601-607
    • Zimprich, A.1    Biskup, S.2    Leitner, P.3
  • 52
    • 63149090431 scopus 로고    scopus 로고
    • Parkinson's disease: From monogenic forms to genetic susceptibility factors
    • S. Lesage and A. Brice, "Parkinson's disease: from monogenic forms to genetic susceptibility factors, " Human Molecular Genetics, vol. 18, no. 1, pp. R48-R59, 2009.
    • (2009) Human Molecular Genetics , vol.18 , Issue.1 , pp. R48-R59
    • Lesage, S.1    Brice, A.2
  • 53
    • 44949138796 scopus 로고    scopus 로고
    • A review of Parkinson's disease
    • C. A. Davie, "A review of Parkinson's disease, " British Medical Bulletin, vol. 86, no. 1, pp. 109-127, 2008.
    • (2008) British Medical Bulletin , vol.86 , Issue.1 , pp. 109-127
    • Davie, C.A.1
  • 54
    • 33646151866 scopus 로고    scopus 로고
    • LRRK2 in Parkinson's disease: Protein domains and functional insights
    • I. F. Mata, W. J. Wedemeyer, M. J. Farrer, J. P. Taylor, and K. A. Gallo, "LRRK2 in Parkinson's disease: protein domains and functional insights, " Trends in Neurosciences, vol. 29, no. 5, pp. 286-293, 2006.
    • (2006) Trends in Neurosciences , vol.29 , Issue.5 , pp. 286-293
    • Mata, I.F.1    Wedemeyer, W.J.2    Farrer, M.J.3    Taylor, J.P.4    Gallo, K.A.5
  • 55
    • 28544434193 scopus 로고    scopus 로고
    • PET in LRRK2 mutations: Comparison to sporadic Parkinson's disease and evidence for presymptomatic compensation
    • J. R. Adams, H. Van Netten, M. Schulzer et al. , "PET in LRRK2 mutations: comparison to sporadic Parkinson's disease and evidence for presymptomatic compensation, " Brain, vol. 128, no. 12, pp. 2777-2785, 2005.
    • (2005) Brain , vol.128 , Issue.12 , pp. 2777-2785
    • Adams, J.R.1    Van Netten, H.2    Schulzer, M.3
  • 56
    • 84921033215 scopus 로고    scopus 로고
    • Clinical correlations with lewy body pathology in LRRK2-related Parkinson disease
    • L. V. Kalia, A. E. Lang, L. N. Hazrati et al. , "Clinical correlations with lewy body pathology in LRRK2-related Parkinson disease, " JAMA Neurology, vol. 72, no. 1, pp. 100-105, 2015.
    • (2015) JAMA Neurology , vol.72 , Issue.1 , pp. 100-105
    • Kalia, L.V.1    Lang, A.E.2    Hazrati, L.N.3
  • 57
    • 84896111174 scopus 로고    scopus 로고
    • Prediction of the repeat domain structures and impact of Parkinsonism-associated variations on structure and function of all functional domains of leucine-rich repeat kinase 2 (LRRK2)
    • R. D. Mills, T. D. Mulhern, F. Liu, J. G. Culvenor, and H. C. Cheng, "Prediction of the repeat domain structures and impact of Parkinsonism-associated variations on structure and function of all functional domains of leucine-rich repeat kinase 2 (LRRK2), " Human Mutation, vol. 35, no. 4, pp. 395-412, 2014.
    • (2014) Human Mutation , vol.35 , Issue.4 , pp. 395-412
    • Mills, R.D.1    Mulhern, T.D.2    Liu, F.3    Culvenor, J.G.4    Cheng, H.C.5
  • 59
    • 33846818834 scopus 로고    scopus 로고
    • GTP binding is essential to the protein kinase activity of LRRK2, a causative gene product for familial Parkinson's disease
    • G. Ito, T. Okai, G. Fujino et al. , "GTP binding is essential to the protein kinase activity of LRRK2, a causative gene product for familial Parkinson's disease, " Biochemistry, vol. 46, no. 5, pp. 1380-1388, 2007.
    • (2007) Biochemistry , vol.46 , Issue.5 , pp. 1380-1388
    • Ito, G.1    Okai, T.2    Fujino, G.3
  • 60
    • 80051611506 scopus 로고    scopus 로고
    • LRRK2 kinase activity is dependent on LRRK2 GTP binding capacity but independent of LRRK2 GTP binding
    • J.-M. Taymans, R. Vancraenenbroeck, P. Ollikainen et al. , "LRRK2 kinase activity is dependent on LRRK2 GTP binding capacity but independent of LRRK2 GTP binding, " PLoS ONE, vol. 6, no. 8, Article ID e23207, 2011.
    • (2011) PLoS ONE , vol.6 , Issue.8
    • Taymans, J.-M.1    Vancraenenbroeck, R.2    Ollikainen, P.3
  • 61
    • 47749114984 scopus 로고    scopus 로고
    • The Parkinson disease-associated leucine-rich repeat kinase 2 (LRRK2) is a dimer that undergoes intramolecular autophosphorylation
    • E. Greggio, I. Zambrano, A. Kaganovich et al. , "The Parkinson disease-associated leucine-rich repeat kinase 2 (LRRK2) is a dimer that undergoes intramolecular autophosphorylation, " The Journal of Biological Chemistry, vol. 283, no. 24, pp. 16906-16914, 2008.
    • (2008) The Journal of Biological Chemistry , vol.283 , Issue.24 , pp. 16906-16914
    • Greggio, E.1    Zambrano, I.2    Kaganovich, A.3
  • 62
    • 73649120624 scopus 로고    scopus 로고
    • Leucine-rich repeat kinase 2 (LRRK2) kinase activity: Dependence on dimerization
    • S. Sen, P. J. Webber, and A. B. West, "Leucine-rich repeat kinase 2 (LRRK2) kinase activity: dependence on dimerization, " The Journal of Biological Chemistry, vol. 284, no. 52, pp. 36346-36356, 2009.
    • (2009) The Journal of Biological Chemistry , vol.284 , Issue.52 , pp. 36346-36356
    • Sen, S.1    Webber, P.J.2    West, A.B.3
  • 63
    • 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
    • Z. Berger, K. A. Smith, andM. J. Lavoie, "Membrane localization of LRRK2 is associated with increased formation of the highly active LRRK2 dimer and changes in its phosphorylation, " Biochemistry, vol. 49, no. 26, pp. 5511-5523, 2010.
    • (2010) Biochemistry , vol.49 , Issue.26 , pp. 5511-5523
    • Berger, Z.1    Smith, K.A.2    Lavoie, M.J.3
  • 65
    • 78649389313 scopus 로고    scopus 로고
    • The role of leucine-rich repeat kinase 2 (LRRK2) in Parkinson's disease
    • M. R. Cookson, "The role of leucine-rich repeat kinase 2 (LRRK2) in Parkinson's disease, " Nature Reviews Neuroscience, vol. 11, no. 12, pp. 791-797, 2010.
    • (2010) Nature Reviews Neuroscience , vol.11 , Issue.12 , pp. 791-797
    • Cookson, M.R.1
  • 67
    • 84891776413 scopus 로고    scopus 로고
    • Mutant LRRK2 toxicity in neurons depends on LRRK2 levels and synuclein but not kinase activity or inclusion bodies
    • G. Skibinski, K. Nakamura, M. R. Cookson, and S. Finkbeiner, "Mutant LRRK2 toxicity in neurons depends on LRRK2 levels and synuclein but not kinase activity or inclusion bodies, " Journal of Neuroscience, vol. 34, no. 2, pp. 418-433, 2014.
    • (2014) Journal of Neuroscience , vol.34 , Issue.2 , pp. 418-433
    • Skibinski, G.1    Nakamura, K.2    Cookson, M.R.3    Finkbeiner, S.4
  • 68
    • 84865341866 scopus 로고    scopus 로고
    • LRRK2 I2020T mutation is associated with tau pathology
    • S. Ujiie, T. Hatano, S.-I. Kubo et al. , "LRRK2 I2020T mutation is associated with tau pathology, " Parkinsonism & Related Disorders, vol. 18, no. 7, pp. 819-823, 2012.
    • (2012) Parkinsonism & Related Disorders , vol.18 , Issue.7 , pp. 819-823
    • Ujiie, S.1    Hatano, T.2    Kubo, S.-I.3
  • 69
    • 84892588907 scopus 로고    scopus 로고
    • LRRK2 phosphorylates novel tau epitopes and promotes tauopathy
    • R. M. Bailey, J. P. Covy, H. L. Melrose et al. , "LRRK2 phosphorylates novel tau epitopes and promotes tauopathy, " Acta Neuropathologica, vol. 126, no. 6, pp. 809-827, 2013.
    • (2013) Acta Neuropathologica , vol.126 , Issue.6 , pp. 809-827
    • Bailey, R.M.1    Covy, J.P.2    Melrose, H.L.3
  • 70
    • 77957794336 scopus 로고    scopus 로고
    • Impaired dopaminergic neurotransmission and microtubule-associated protein tau alterations in human LRRK2 transgenic mice
    • H. L. Melrose, J. C. Dächsel, B. Behrouz et al. , "Impaired dopaminergic neurotransmission and microtubule-associated protein tau alterations in human LRRK2 transgenic mice, " Neurobiology of Disease, vol. 40, no. 3, pp. 503-517, 2010.
    • (2010) Neurobiology of Disease , vol.40 , Issue.3 , pp. 503-517
    • Melrose, H.L.1    Dächsel, J.C.2    Behrouz, B.3
  • 71
    • 84860901516 scopus 로고    scopus 로고
    • Atypical tauopathy in a patient with LRRK2-G2019S mutation and tremordominant Parkinsonism
    • C. Ruffmann, G. Giaccone, M. Canesi et al. , "Atypical tauopathy in a patient with LRRK2-G2019S mutation and tremordominant Parkinsonism, " Neuropathology and Applied Neurobiology, vol. 38, no. 4, pp. 382-386, 2012.
    • (2012) Neuropathology and Applied Neurobiology , vol.38 , Issue.4 , pp. 382-386
    • Ruffmann, C.1    Giaccone, G.2    Canesi, M.3
  • 72
    • 67649813448 scopus 로고    scopus 로고
    • Mutant LRRK2 (R1441G) BAC transgenic mice recapitulate cardinal features of Parkinson's disease
    • Y. Li, W. Liu, T. F. Oo et al. , "Mutant LRRK2 (R1441G) BAC transgenic mice recapitulate cardinal features of Parkinson's disease, " Nature Neuroscience, vol. 12, no. 7, pp. 826-828, 2009.
    • (2009) Nature Neuroscience , vol.12 , Issue.7 , pp. 826-828
    • Li, Y.1    Liu, W.2    Oo, T.F.3
  • 73
    • 33750308194 scopus 로고    scopus 로고
    • Parkinsonism, Lrrk2 G2019S, and tau neuropathology
    • A. Rajput, D. W. Dickson, C. A. Robinson et al. , "Parkinsonism, Lrrk2 G2019S, and tau neuropathology, " Neurology, vol. 67, no. 8, pp. 1506-1508, 2006.
    • (2006) Neurology , vol.67 , Issue.8 , pp. 1506-1508
    • Rajput, A.1    Dickson, D.W.2    Robinson, C.A.3
  • 74
    • 68949218403 scopus 로고    scopus 로고
    • Leucine-rich repeat kinase 2 phosphorylates brain tubulin-beta isoforms and modulates microtubule stability -A point of convergence in Parkinsonian neurodegeneration
    • F. Gillardon, "Leucine-rich repeat kinase 2 phosphorylates brain tubulin-beta isoforms and modulates microtubule stability-a point of convergence in Parkinsonian neurodegeneration" Journal of Neurochemistry, vol. 110, no. 5, pp. 1514-1522, 2009.
    • (2009) Journal of Neurochemistry , vol.110 , Issue.5 , pp. 1514-1522
    • Gillardon, F.1
  • 75
    • 77957377567 scopus 로고    scopus 로고
    • LRRK2 G2019S mutation induces dendrite degeneration through mislocalization and phosphorylation of tau by recruiting autoactivated GSK3
    • C.-H. Lin, P.-I. Tsai, R.-M. Wu, and C.-T. Chien, "LRRK2 G2019S mutation induces dendrite degeneration through mislocalization and phosphorylation of tau by recruiting autoactivated GSK3, " The Journal of Neuroscience, vol. 30, no. 39, pp. 13138-13149, 2010.
    • (2010) The Journal of Neuroscience , vol.30 , Issue.39 , pp. 13138-13149
    • Lin, C.-H.1    Tsai, P.-I.2    Wu, R.-M.3    Chien, C.-T.4
  • 76
    • 79960346073 scopus 로고    scopus 로고
    • LRRK2 directly phosphorylates Akt1 as a possible physiological substrate: Impairment of the kinase activity by Parkinson's diseaseassociated mutations
    • E. Ohta, F. Kawakami, M. Kubo, and F. Obata, "LRRK2 directly phosphorylates Akt1 as a possible physiological substrate: impairment of the kinase activity by Parkinson's diseaseassociated mutations, " FEBS Letters, vol. 585, no. 14, pp. 2165-2170, 2011.
    • (2011) FEBS Letters , vol.585 , Issue.14 , pp. 2165-2170
    • Ohta, E.1    Kawakami, F.2    Kubo, M.3    Obata, F.4
  • 77
    • 33746079596 scopus 로고    scopus 로고
    • A common missense variant in the LRRK2 gene, Gly2385Arg, associated with Parkinson's disease risk in Taiwan
    • A. Di Fonzo, Y.-H. Wu-Chou, C.-S. Lu et al. , "A common missense variant in the LRRK2 gene, Gly2385Arg, associated with Parkinson's disease risk in Taiwan, " Neurogenetics, vol. 7, no. 3, pp. 133-138, 2006.
    • (2006) Neurogenetics , vol.7 , Issue.3 , pp. 133-138
    • Di Fonzo, A.1    Wu-Chou, Y.-H.2    Lu, C.-S.3
  • 78
    • 33847226901 scopus 로고    scopus 로고
    • Leucine-Rich Repeat kinase 2 G2385R variant is a risk factor for Parkinson disease in Asian population
    • M. Funayama, Y. Li, H. Tomiyama et al. , "Leucine-Rich Repeat kinase 2 G2385R variant is a risk factor for Parkinson disease in Asian population, " NeuroReport, vol. 18, no. 3, pp. 273-275, 2007.
    • (2007) NeuroReport , vol.18 , Issue.3 , pp. 273-275
    • Funayama, M.1    Li, Y.2    Tomiyama, H.3
  • 79
    • 39149133173 scopus 로고    scopus 로고
    • LRRK2 Gly2385Arg variant is a risk factor of Parkinson's disease among Han-Chinese from mainland China
    • X.-K. An, R. Peng, T. Li et al. , "LRRK2 Gly2385Arg variant is a risk factor of Parkinson's disease among Han-Chinese from mainland China, " European Journal of Neurology, vol. 15, no. 3, pp. 301-305, 2008.
    • (2008) European Journal of Neurology , vol.15 , Issue.3 , pp. 301-305
    • An, X.-K.1    Peng, R.2    Li, T.3
  • 80
    • 75949122054 scopus 로고    scopus 로고
    • The LRRK2G2385Rvariant is a risk factor for sporadic Parkinson's disease in the Korean population
    • J.-M. Kim, J.-Y. Lee, H. J. Kim et al. , "The LRRK2G2385Rvariant is a risk factor for sporadic Parkinson's disease in the Korean population, " Parkinsonism and Related Disorders, vol. 16, no. 2, pp. 85-88, 2010.
    • (2010) Parkinsonism and Related Disorders , vol.16 , Issue.2 , pp. 85-88
    • Kim, J.-M.1    Lee, J.-Y.2    Kim, H.J.3
  • 81
    • 78049288601 scopus 로고    scopus 로고
    • Signal transduction protein array analysis links LRRK2 to Ste20 kinases and PKC zeta that modulate neuronal plasticity
    • S. Zach, S. Felk, and F. Gillardon, "Signal transduction protein array analysis links LRRK2 to Ste20 kinases and PKC zeta that modulate neuronal plasticity, " PLoS ONE, vol. 5, no. 10, Article ID e13191, 2010.
    • (2010) PLoS ONE , vol.5 , Issue.10
    • Zach, S.1    Felk, S.2    Gillardon, F.3
  • 82
    • 17044387386 scopus 로고    scopus 로고
    • Hsp70 chaperones: Cellular functions and molecular mechanism
    • M. P. Mayer and B. Bukau, "Hsp70 chaperones: cellular functions and molecular mechanism, " Cellular and Molecular Life Sciences, vol. 62, no. 6, pp. 670-684, 2005.
    • (2005) Cellular and Molecular Life Sciences , vol.62 , Issue.6 , pp. 670-684
    • Mayer, M.P.1    Bukau, B.2
  • 83
    • 80052324528 scopus 로고    scopus 로고
    • The Parkinson's disease protein LRRK2 impairs proteasome substrate clearance without affecting proteasome catalytic activity
    • M. Lichtenberg, A. Mansilla, V. R. Zecchini, A. Fleming, and D. C. Rubinsztein, "The Parkinson's disease protein LRRK2 impairs proteasome substrate clearance without affecting proteasome catalytic activity, " Cell Death & Disease, vol. 2, no. 8, article e196, 2011.
    • (2011) Cell Death & Disease , vol.2 , Issue.8
    • Lichtenberg, M.1    Mansilla, A.2    Zecchini, V.R.3    Fleming, A.4    Rubinsztein, D.C.5
  • 84
    • 11144356089 scopus 로고    scopus 로고
    • CHIP andHsp70 regulate tau ubiquitination, degradation and aggregation
    • L. Petrucelli, D. Dickson, K. Kehoe et al. , "CHIP andHsp70 regulate tau ubiquitination, degradation and aggregation, " Human Molecular Genetics, vol. 13, no. 7, pp. 703-714, 2004.
    • (2004) Human Molecular Genetics , vol.13 , Issue.7 , pp. 703-714
    • Petrucelli, L.1    Dickson, D.2    Kehoe, K.3
  • 85
    • 31144443248 scopus 로고    scopus 로고
    • The Parkinson disease causing LRRK2 mutation I2020T is associated with increased kinase activity
    • C. J. Gloeckner, N. Kinkl, A. Schumacher et al. , "The Parkinson disease causing LRRK2 mutation I2020T is associated with increased kinase activity, " Human Molecular Genetics, vol. 15, no. 2, pp. 223-232, 2006.
    • (2006) Human Molecular Genetics , vol.15 , Issue.2 , pp. 223-232
    • Gloeckner, C.J.1    Kinkl, N.2    Schumacher, A.3
  • 86
    • 41549144503 scopus 로고    scopus 로고
    • The chaperone activity of heat shock protein 90 is critical for maintaining the stability of leucine-rich repeat kinase 2
    • L. Wang, C. Xie, E. Greggio et al. , "The chaperone activity of heat shock protein 90 is critical for maintaining the stability of leucine-rich repeat kinase 2, " Journal of Neuroscience, vol. 28, no. 13, pp. 3384-3391, 2008.
    • (2008) Journal of Neuroscience , vol.28 , Issue.13 , pp. 3384-3391
    • Wang, L.1    Xie, C.2    Greggio, E.3
  • 87
    • 21044449225 scopus 로고    scopus 로고
    • Inhibition of glycogen synthase kinase-3 by lithium correlates with reduced tauopathy and degeneration in vivo
    • W. Noble, E. Planel, C. Zehr et al. , "Inhibition of glycogen synthase kinase-3 by lithium correlates with reduced tauopathy and degeneration in vivo, " Proceedings of the National Academy of Sciences of the United States of America, vol. 102, no. 19, pp. 6990-6995, 2005.
    • (2005) Proceedings of the National Academy of Sciences of the United States of America , vol.102 , Issue.19 , pp. 6990-6995
    • Noble, W.1    Planel, E.2    Zehr, C.3
  • 89
    • 0035413614 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3: Properties, functions, and regulation
    • A. Ali, K. P. Hoeflich, and J. R. Woodgett, "Glycogen synthase kinase-3: properties, functions, and regulation, " Chemical Reviews, vol. 101, no. 8, pp. 2527-2540, 2001.
    • (2001) Chemical Reviews , vol.101 , Issue.8 , pp. 2527-2540
    • Ali, A.1    Hoeflich, K.P.2    Woodgett, J.R.3
  • 90
    • 17644383748 scopus 로고    scopus 로고
    • Heat shock protein 70 inhibits-synuclein fibril formation via preferential binding to prefibrillar species
    • M. M. Dedmon, J. Christodoulou, M. R. Wilson, and C. M. Dobson, "Heat shock protein 70 inhibits-synuclein fibril formation via preferential binding to prefibrillar species, " Journal of Biological Chemistry, vol. 280, no. 15, pp. 14733-14740, 2005.
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.15 , pp. 14733-14740
    • Dedmon, M.M.1    Christodoulou, J.2    Wilson, M.R.3    Dobson, C.M.4
  • 93
    • 34548034011 scopus 로고    scopus 로고
    • Characterizing the role of Hsp90 in production of heat shock proteins in motor neurons reveals a suppressive effect of wildtypeHsf1
    • D. M. Taylor, M. L. Tradewell, S. Minotti, and H. D. Durham, "Characterizing the role of Hsp90 in production of heat shock proteins in motor neurons reveals a suppressive effect of wildtypeHsf1, " Cell Stress Chaperones, vol. 12, no. 2, pp. 151-162, 2007.
    • (2007) Cell Stress Chaperones , vol.12 , Issue.2 , pp. 151-162
    • Taylor, D.M.1    Tradewell, M.L.2    Minotti, S.3    Durham, H.D.4


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