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Volumn 6, Issue 6, 2006, Pages 579-595

Tau therapeutic strategies for the treatment of Alzheimer's disease

Author keywords

Alzheimer's disease; Cdk; GSK; Kinase; MAPT; MARK; Microtubule; Tau

Indexed keywords

ALOISINE A; ALSTERPAULLONE; AMYLOID BETA PROTEIN; CASEIN KINASE; CYCLIC AMP DEPENDENT PROTEIN KINASE INHIBITOR; CYCLIN DEPENDENT KINASE 5; CYCLIN DEPENDENT KINASE INHIBITOR; FLAVOPIRIDOL; GLYCOGEN SYNTHASE KINASE 3 INHIBITOR; HYMENIALDESINE; INDIRUBIN; MALEIMIDE DERIVATIVE; MICROTUBULE ASSOCIATED PROTEIN; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 3; MITOGEN ACTIVATED PROTEIN KINASE INHIBITOR; MITOGEN ACTIVATED PROTEIN KINASE KINASE; OLIGOMER; OLOMOUCINE; PHOSPHOPROTEIN PHOSPHATASE; PHOSPHOTRANSFERASE INHIBITOR; PROTEIN KINASE; PROTEIN KINASE (CALCIUM,CALMODULIN) II; PROTEIN KINASE INHIBITOR; PYRIDAZINE DERIVATIVE; ROSCOVITINE; STAUROSPORINE; STRESS ACTIVATED PROTEIN KINASE INHIBITOR; TAU PROTEIN; UNCLASSIFIED DRUG; UNINDEXED DRUG;

EID: 33646198145     PISSN: 15680266     EISSN: None     Source Type: Journal    
DOI: 10.2174/156802606776743057     Document Type: Review
Times cited : (126)

References (177)
  • 2
    • 0022365608 scopus 로고
    • The distribution of tau in the mammalian central nervous system
    • Binder, L. I.; Frankfurter, A.; Rebhun, L. I. The distribution of tau in the mammalian central nervous system. J. Cell Biol. 1985, 101, 1371-1378.
    • (1985) J. Cell Biol. , vol.101 , pp. 1371-1378
    • Binder, L.I.1    Frankfurter, A.2    Rebhun, L.I.3
  • 3
    • 0024442369 scopus 로고
    • Tau in situ hybridization in normal and Alzheimer brain: Localization in the somatodendritic compartment
    • Kosik, K. S.; Crandall, J. E.; Mufson, E. J.; Neve, R. L. Tau in situ hybridization in normal and Alzheimer brain: localization in the somatodendritic compartment. Ann. Neurol. 1989, 26, 352-361.
    • (1989) Ann. Neurol. , vol.26 , pp. 352-361
    • Kosik, K.S.1    Crandall, J.E.2    Mufson, E.J.3    Neve, R.L.4
  • 4
    • 0029040690 scopus 로고
    • I Presence of tau in isolated nuclei from human brain
    • Brady, R. M.; Zinkowski, R. P.; Binder, L., I Presence of tau in isolated nuclei from human brain. Neurobiol. Aging 1995, 16, 479-486.
    • (1995) Neurobiol. Aging , vol.16 , pp. 479-486
    • Brady, R.M.1    Zinkowski, R.P.2    Binder, L.3
  • 5
    • 0028853922 scopus 로고
    • Functional implications for the microtubule-associated protein tau: Localization in oligodendrocytes
    • LoPresti, P.; Szuchet, S.; Papasozomenos, S. C.; Zinkowski, R. P.; Binder, L. I. Functional implications for the microtubule-associated protein tau: localization in oligodendrocytes. Proc. Natl. Acad. Sci. USA 1995, 92, 10369-10373.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 10369-10373
    • LoPresti, P.1    Szuchet, S.2    Papasozomenos, S.C.3    Zinkowski, R.P.4    Binder, L.I.5
  • 8
    • 0028852644 scopus 로고
    • Guanosine triphosphate binding to beta-subunit of tubulin in Alzheimer's disease brain: Role of microtubule-associated protein tau
    • Khatoon, S.; Grundke-Iqbal, I.; Iqbal, K. Guanosine triphosphate binding to beta-subunit of tubulin in Alzheimer's disease brain: role of microtubule-associated protein tau. J. Neurochem. 1995, 64, 777-787.
    • (1995) J. Neurochem. , vol.64 , pp. 777-787
    • Khatoon, S.1    Grundke-Iqbal, I.2    Iqbal, K.3
  • 10
    • 0001169160 scopus 로고    scopus 로고
    • Activation of phospholipase C-gamma by the concerted action of tau proteins and arachidonic acid
    • Hwang, S. C.; Jhon, D. Y.; Bae, Y. S.; Kim, J. H.; Rhee, S. G. Activation of phospholipase C-gamma by the concerted action of tau proteins and arachidonic acid. J. Biol. Chem. 1996, 271, 18342-18349.
    • (1996) J. Biol. Chem. , vol.271 , pp. 18342-18349
    • Hwang, S.C.1    Jhon, D.Y.2    Bae, Y.S.3    Kim, J.H.4    Rhee, S.G.5
  • 11
    • 0025335664 scopus 로고
    • The tubulin-binding sequence of brain microtubule-associated proteins, tau and MAP-2, is also involved in actin binding
    • Correas, I.; Padilla, R.; Avila, J. The tubulin-binding sequence of brain microtubule-associated proteins, tau and MAP-2, is also involved in actin binding. Biochem. J. 1990, 269, 61-64.
    • (1990) Biochem. J. , vol.269 , pp. 61-64
    • Correas, I.1    Padilla, R.2    Avila, J.3
  • 12
    • 10944227282 scopus 로고    scopus 로고
    • Tau phosphorylation: Physiological and pathological consequences
    • Stoothoff, W. H.; Johnson, G. V. W. Tau phosphorylation: physiological and pathological consequences. Biochim. Biophys. Acta 2005, 1739, 280-297.
    • (2005) Biochim. Biophys. Acta , vol.1739 , pp. 280-297
    • Stoothoff, W.H.1    Johnson, G.V.W.2
  • 13
    • 0036403702 scopus 로고    scopus 로고
    • Deciphering the genetic basis of Alzheimer's disease
    • Selkoe, D. J.; Podlisny, M. B. Deciphering the genetic basis of Alzheimer's disease. Ann. Rev. Genom. Hum. Genet. 2002, 3, 67-99.
    • (2002) Ann. Rev. Genom. Hum. Genet. , vol.3 , pp. 67-99
    • Selkoe, D.J.1    Podlisny, M.B.2
  • 14
    • 0033624414 scopus 로고    scopus 로고
    • Genetics of Alzheimer's disease - Routes to the pathophysiology
    • (Advances in Dementia Research)
    • Lannfelt, L.; Nordstedt, C. Genetics of Alzheimer's disease - routes to the pathophysiology. J. Neural Transmission, Suppl. 2000, 59, (Advances in Dementia Research), 155-161.
    • (2000) J. Neural Transmission , vol.59 , Issue.SUPPL. , pp. 155-161
    • Lannfelt, L.1    Nordstedt, C.2
  • 15
    • 0032150877 scopus 로고    scopus 로고
    • Genetic dissection of Alzheimer's disease and related dementias: Amyloid and its relationship to tau
    • Hardy, J.; Duff, K.; Hardy, K. G.; Perez-Tur, J.; Hutton, M. Genetic dissection of Alzheimer's disease and related dementias: amyloid and its relationship to tau. Nat. Neurosci. 1998, 1, 355-358.
    • (1998) Nat. Neurosci. , vol.1 , pp. 355-358
    • Hardy, J.1    Duff, K.2    Hardy, K.G.3    Perez-Tur, J.4    Hutton, M.5
  • 16
    • 0026597063 scopus 로고
    • Alzheimer's disease: The amyloid cascade hypothesis
    • Hardy, J. A.; Higgins, G. A. Alzheimer's disease: the amyloid cascade hypothesis. Science 1992, 256, 184-185.
    • (1992) Science , vol.256 , pp. 184-185
    • Hardy, J.A.1    Higgins, G.A.2
  • 17
    • 0023585273 scopus 로고
    • Brain amyloid in normal aging and cerebral amyloid angiopathy is antigenically related to Alzheimer's disease beta-protein
    • Coria, F.; Castano, E. M.; Frangione, B. Brain amyloid in normal aging and cerebral amyloid angiopathy is antigenically related to Alzheimer's disease beta-protein. Am. J. Pathol. 1987, 129, 422-428.
    • (1987) Am. J. Pathol. , vol.129 , pp. 422-428
    • Coria, F.1    Castano, E.M.2    Frangione, B.3
  • 19
    • 0033545946 scopus 로고    scopus 로고
    • Missense and silent tau gene mutations cause frontotemporal dementia with parkinsonism-chromosome 17 type, by affecting multiple alternative RNA splicing regulatory elements
    • D'Souza, I.; Poorkaj, P.; Hong, M.; Nochlin, D.; Lee, V. M. Y.; Bird, T. D.; Schellenberg, G. D. Missense and silent tau gene mutations cause frontotemporal dementia with parkinsonism-chromosome 17 type, by affecting multiple alternative RNA splicing regulatory elements. Proc. Natl. Acad. Sci. USA 1999, 96, 5598-5603.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 5598-5603
    • D'Souza, I.1    Poorkaj, P.2    Hong, M.3    Nochlin, D.4    Lee, V.M.Y.5    Bird, T.D.6    Schellenberg, G.D.7
  • 23
    • 10944256690 scopus 로고    scopus 로고
    • Inability of tau to properly regulate neuronal microtubule dynamics: A loss-of-function mechanism by which tau might mediate neuronal cell death
    • Feinstein, S. C.; Wilson, L. Inability of tau to properly regulate neuronal microtubule dynamics: a loss-of-function mechanism by which tau might mediate neuronal cell death. Biochim. Biophys. Acta 2005, 1739, 268-279.
    • (2005) Biochim. Biophys. Acta , vol.1739 , pp. 268-279
    • Feinstein, S.C.1    Wilson, L.2
  • 24
    • 26844433190 scopus 로고    scopus 로고
    • Axonal gegeneration induced by targeted expression of mutant human tau on oligodendrocytes of transgenic mice that model glial tauopathies
    • Higuchi, M.; Zhang, B.; Forman, M. S.; Yoshiyama, Y.; Trojanowski, J. Q.; Lee, V. M. Y. Axonal gegeneration induced by targeted expression of mutant human tau on oligodendrocytes of transgenic mice that model glial tauopathies. J. Neurosci. 2005, 25, 9434-9443.
    • (2005) J. Neurosci. , vol.25 , pp. 9434-9443
    • Higuchi, M.1    Zhang, B.2    Forman, M.S.3    Yoshiyama, Y.4    Trojanowski, J.Q.5    Lee, V.M.Y.6
  • 25
    • 20044370830 scopus 로고    scopus 로고
    • The generation of a 17 kDa neurotoxic fragment: An alternative mechanism by which tau mediates beta-amyloid-induced neurodegeneration
    • Park, S. Y.; Ferreira, A. The generation of a 17 kDa neurotoxic fragment: An alternative mechanism by which tau mediates beta-amyloid-induced neurodegeneration. J. Neurosci. 2005, 25, 5365-5375.
    • (2005) J. Neurosci. , vol.25 , pp. 5365-5375
    • Park, S.Y.1    Ferreira, A.2
  • 26
    • 0036904519 scopus 로고    scopus 로고
    • Assembly of tau in transgenic animals expressing P301L tau: Alteration of phosphorylation and solubility
    • Sahara, N.; Lewis, J.; DeTure, M.; McGowan, E.; Dickson, D. W.; Hutton, M.; Yen, S. H. Assembly of tau in transgenic animals expressing P301L tau: alteration of phosphorylation and solubility. J. Neurochem. 2002, 83, 1498-1508.
    • (2002) J. Neurochem. , vol.83 , pp. 1498-1508
    • Sahara, N.1    Lewis, J.2    DeTure, M.3    McGowan, E.4    Dickson, D.W.5    Hutton, M.6    Yen, S.H.7
  • 28
    • 0035943436 scopus 로고    scopus 로고
    • Formation of neurofibrillary tangles in P301L tau transgenic mice induced by Abeta 42 fibrils
    • Gotz, J.; Chen, F.; Van Dorpe, J.; Nitsch, R. M. Formation of neurofibrillary tangles in P301L tau transgenic mice induced by Abeta 42 fibrils. Science 2001, 293, 1491-1495.
    • (2001) Science , vol.293 , pp. 1491-1495
    • Gotz, J.1    Chen, F.2    Van Dorpe, J.3    Nitsch, R.M.4
  • 29
    • 0033230886 scopus 로고    scopus 로고
    • Age-dependent emergence and progression of a tauopathy in transgenic mice overexpressing the shortest human tau isoform
    • Ishihara, T.; Hong, M.; Zhang, B.; Nakagawa, Y.; Lee, M. K.; Trojanowski, J. Q.; Lee, V. M. Y. Age-dependent emergence and progression of a tauopathy in transgenic mice overexpressing the shortest human tau isoform. Neuron 1999, 24, 751-762.
    • (1999) Neuron , vol.24 , pp. 751-762
    • Ishihara, T.1    Hong, M.2    Zhang, B.3    Nakagawa, Y.4    Lee, M.K.5    Trojanowski, J.Q.6    Lee, V.M.Y.7
  • 30
    • 0035134081 scopus 로고    scopus 로고
    • Age-dependent induction of congophilic neurofibrillary tau inclusions in tau transgenic mice
    • Ishihara, T.; Zhang, B.; Higuchi, M.; Yoshiyama, Y.; Trojanowski, J. Q.; Lee, V. M. Y. Age-dependent induction of congophilic neurofibrillary tau inclusions in tau transgenic mice. Am. J. Pathol. 2001, 158, 555-562.
    • (2001) Am. J. Pathol. , vol.158 , pp. 555-562
    • Ishihara, T.1    Zhang, B.2    Higuchi, M.3    Yoshiyama, Y.4    Trojanowski, J.Q.5    Lee, V.M.Y.6
  • 31
    • 0345580607 scopus 로고    scopus 로고
    • Transgenic expression of the shortest human tau affects its compartmentalization and its phosphorylation as in the pretangle stage of Alzheimer's disease
    • Brion, J. P.; Tremp, G.; Octave, J. N. Transgenic expression of the shortest human tau affects its compartmentalization and its phosphorylation as in the pretangle stage of Alzheimer's disease. Am. J. Pathol. 1999, 154, 255-270.
    • (1999) Am. J. Pathol. , vol.154 , pp. 255-270
    • Brion, J.P.1    Tremp, G.2    Octave, J.N.3
  • 35
  • 37
    • 0344845132 scopus 로고    scopus 로고
    • Amyloid deposition precedes tangle formation in a triple transgenic model of Alzheimer's disease
    • Oddo, S.; Caccamo, A.; Kitazawa, M.; Tseng, B. P.; LaFerla, F. M. Amyloid deposition precedes tangle formation in a triple transgenic model of Alzheimer's disease. Neurobiol. Aging 2003, 24, 1063-1070.
    • (2003) Neurobiol. Aging , vol.24 , pp. 1063-1070
    • Oddo, S.1    Caccamo, A.2    Kitazawa, M.3    Tseng, B.P.4    LaFerla, F.M.5
  • 39
    • 0031741247 scopus 로고    scopus 로고
    • New phosphorylation sites identified in hyperphosphorylated tau (paired helical filament-tau) from Alzheimer's disease brain using nanoelectrospray mass spectrometry
    • Hanger, D. P.; Betts, J. C.; Loviny, T. L. F.; Blackstock, W. P.; Anderton, B. H. New phosphorylation sites identified in hyperphosphorylated tau (paired helical filament-tau) from Alzheimer's disease brain using nanoelectrospray mass spectrometry. J. Neurochem. 1998, 71, 2465-2476.
    • (1998) J. Neurochem. , vol.71 , pp. 2465-2476
    • Hanger, D.P.1    Betts, J.C.2    Loviny, T.L.F.3    Blackstock, W.P.4    Anderton, B.H.5
  • 40
    • 25844458239 scopus 로고    scopus 로고
    • Current advances on different kinases involved in Tau phosphorylation, and implications in Alzheimer's disease and tauopathies
    • Ferrer, I.; Gomez-Isla, T.; Puig, B.; Freixes, M.; Ribe, E.; Dalfo, E.; Avila, J. Current advances on different kinases involved in Tau phosphorylation, and implications in Alzheimer's disease and tauopathies. Curr. Alzheimer Res. 2005, 2, 3-18.
    • (2005) Curr. Alzheimer Res. , vol.2 , pp. 3-18
    • Ferrer, I.1    Gomez-Isla, T.2    Puig, B.3    Freixes, M.4    Ribe, E.5    Dalfo, E.6    Avila, J.7
  • 42
    • 4444262625 scopus 로고    scopus 로고
    • Cdk5 deregulation in the pathogenesis of Alzheimer's disease
    • Cruz, J. C.; Tsai, L. H. Cdk5 deregulation in the pathogenesis of Alzheimer's disease. Trends Mol. Med. 2004, 10, 452-458.
    • (2004) Trends Mol. Med. , vol.10 , pp. 452-458
    • Cruz, J.C.1    Tsai, L.H.2
  • 43
    • 1542328910 scopus 로고    scopus 로고
    • Cdk5, a therapeutic target for Alzheimer's disease?
    • Tsai, L. H.; Lee, M. S.; Cruz, J. Cdk5, a therapeutic target for Alzheimer's disease? Biochim. Biophys. Acta 2004, 1697, 137-142.
    • (2004) Biochim. Biophys. Acta , vol.1697 , pp. 137-142
    • Tsai, L.H.1    Lee, M.S.2    Cruz, J.3
  • 44
    • 0036169172 scopus 로고    scopus 로고
    • Cdk5 behind the wheel: A role in trafficking and transport?
    • Smith, D. S.; Tsai, L. H. Cdk5 behind the wheel: a role in trafficking and transport? Trends Cell Biol. 2002, 12, 28-36.
    • (2002) Trends Cell Biol. , vol.12 , pp. 28-36
    • Smith, D.S.1    Tsai, L.H.2
  • 47
    • 0345405447 scopus 로고    scopus 로고
    • Aberrant Cdk5 activation by p25 triggers pathological events leading to neurodegeneration and neurofibrillary tangles
    • Cruz, J. C.; Tseng, H. C.; Goldman, J. A.; Shih, H.; Tsai, L. H. Aberrant Cdk5 activation by p25 triggers pathological events leading to neurodegeneration and neurofibrillary tangles. Neuron 2003, 40, 471-483.
    • (2003) Neuron , vol.40 , pp. 471-483
    • Cruz, J.C.1    Tseng, H.C.2    Goldman, J.A.3    Shih, H.4    Tsai, L.H.5
  • 49
    • 0037277244 scopus 로고    scopus 로고
    • Cyclin-dependent kinase inhibitors: Cancer killers to neuronal guardians
    • Monaco, E. A., III.; Vallano, M. L. Cyclin-dependent kinase inhibitors: Cancer killers to neuronal guardians. Curr. Med. Chem. 2003, 10, 367-379.
    • (2003) Curr. Med. Chem. , vol.10 , pp. 367-379
    • Monaco III, E.A.1    Vallano, M.L.2
  • 50
    • 0036710767 scopus 로고    scopus 로고
    • Pharmacological inhibitors of cyclin-dependent kinases
    • Knockaert, M.; Greengard, P.; Meijer, L. Pharmacological inhibitors of cyclin-dependent kinases. Trends Pharmacol. Sci. 2002, 23, 417-425.
    • (2002) Trends Pharmacol. Sci. , vol.23 , pp. 417-425
    • Knockaert, M.1    Greengard, P.2    Meijer, L.3
  • 51
    • 0031037714 scopus 로고    scopus 로고
    • Biochemical and cellular effects of roscovitine, a potent and selective inhibitor of the cyclin-dependent kinases cdc2, cdk2, and cdk5
    • Meijer, L.; Borgne, A.; Mulner, O.; Chong, J. P. J.; Blow, J. J.; Inagaki, N.; Inagaki, M.; Delcros, J. G.; Moulinoux, J. P. Biochemical and cellular effects of roscovitine, a potent and selective inhibitor of the cyclin-dependent kinases cdc2, cdk2, and cdk5. Eur. J. Biochem. 1997, 243, 527-536.
    • (1997) Eur. J. Biochem. , vol.243 , pp. 527-536
    • Meijer, L.1    Borgne, A.2    Mulner, O.3    Chong, J.P.J.4    Blow, J.J.5    Inagaki, N.6    Inagaki, M.7    Delcros, J.G.8    Moulinoux, J.P.9
  • 52
    • 0031028163 scopus 로고    scopus 로고
    • Inhibition of cyclin-dependent kinases by purine analogs. Crystal structure of human cdk2 complexed with roscovitine
    • De Azevedo, W. F.; Leclerc, S.; Meijer, L.; Havlicek, L.; Strnad, M.; Kim, S. H. Inhibition of cyclin-dependent kinases by purine analogs. Crystal structure of human cdk2 complexed with roscovitine. Eur. J. Biochem. 1997, 243, 518-526.
    • (1997) Eur. J. Biochem. , vol.243 , pp. 518-526
    • De Azevedo, W.F.1    Leclerc, S.2    Meijer, L.3    Havlicek, L.4    Strnad, M.5    Kim, S.H.6
  • 55
    • 4344637728 scopus 로고    scopus 로고
    • Cyclin-dependent kinase inhibitors attenuate protein hyperphosphorylation, cytoskeletal lesion formation, and motor defects in Niemann-Pick type C mice
    • Zhang, M.; Li, J.; Chakrabarty, P.; Bu, B.; Vincent, I. Cyclin-dependent kinase inhibitors attenuate protein hyperphosphorylation, cytoskeletal lesion formation, and motor defects in Niemann-Pick type C mice. Am. J. Pathol. 2004, 165, 843-853.
    • (2004) Am. J. Pathol. , vol.165 , pp. 843-853
    • Zhang, M.1    Li, J.2    Chakrabarty, P.3    Bu, B.4    Vincent, I.5
  • 56
    • 33646191321 scopus 로고    scopus 로고
    • Presented at "Alzheimer's Disease: From Molecular Mechanisms to Drug Discovery", Cancun 13 December 56
    • Tsai, Li Huei. Presented at "Alzheimer's Disease: From Molecular Mechanisms to Drug Discovery", Cancun 13 December 2004.
    • (2004)
    • Tsai, L.H.1
  • 63
    • 0035808457 scopus 로고    scopus 로고
    • Indirubins inhibit glycogen synthase kinase-3beta and CDK5/p25, two protein kinases involved in abnormal tau phosphorylation in Alzheimer's disease. A property common to most cyclin-dependent kinase inhibitors?
    • Leclerc, S.; Garnier, M.; Hoessel, R.; Marko, D.; Bibb, J. A.; Snyder, G. L.; Greengard, P.; Biernat, J.; Wu, Y. Z.; Mandelkow, E. M.; Eisenbrand, G.; Meijer, L. Indirubins inhibit glycogen synthase kinase-3beta and CDK5/p25, two protein kinases involved in abnormal tau phosphorylation in Alzheimer's disease. A property common to most cyclin-dependent kinase inhibitors? J. Biol. Chem. 2001, 276, 251-260.
    • (2001) J. Biol. Chem. , vol.276 , pp. 251-260
    • Leclerc, S.1    Garnier, M.2    Hoessel, R.3    Marko, D.4    Bibb, J.A.5    Snyder, G.L.6    Greengard, P.7    Biernat, J.8    Wu, Y.Z.9    Mandelkow, E.M.10    Eisenbrand, G.11    Meijer, L.12
  • 65
    • 0037468466 scopus 로고    scopus 로고
    • Evaluation of the First Cytostatically Active 1-Aza-9-oxafluorenes as Novel Selective CDK1 Inhibitors with P-Glycoprotein Modulating Properties
    • Brachwitz, K.; Voigt B.; Meijer, L.; Lozach, O.; Schaechtele, C.; Molnar, J.; Hilgeroth, A. Evaluation of the First Cytostatically Active 1-Aza-9-oxafluorenes as Novel Selective CDK1 Inhibitors with P-Glycoprotein Modulating Properties. J. Med. Chem. 2003, 46, 876-879.
    • (2003) J. Med. Chem. , vol.46 , pp. 876-879
    • Brachwitz, K.1    Voigt, B.2    Meijer, L.3    Lozach, O.4    Schaechtele, C.5    Molnar, J.6    Hilgeroth, A.7
  • 73
    • 0041969008 scopus 로고    scopus 로고
    • Calpain and its involvement in the pathophysiology of CNS injuries and diseases: Therapeutic potential of calpain inhibitors for prevention of neurodegeneration
    • Ray, S. K.; Banik, N. L. Calpain and its involvement in the pathophysiology of CNS injuries and diseases: Therapeutic potential of calpain inhibitors for prevention of neurodegeneration. Curr. Drug Targets: CNS Neurol. Disord. 2003, 2, 173-189.
    • (2003) Curr. Drug Targets: CNS Neurol. Disord. , vol.2 , pp. 173-189
    • Ray, S.K.1    Banik, N.L.2
  • 74
    • 0141783985 scopus 로고    scopus 로고
    • Calpain inhibitors - A review of the recent patent literature
    • DePetrillo, P. B. Calpain inhibitors - a review of the recent patent literature. IDrugs 2002, 5, 568-576.
    • (2002) IDrugs , vol.5 , pp. 568-576
    • DePetrillo, P.B.1
  • 75
    • 0037966577 scopus 로고    scopus 로고
    • Regulation of amyloid precursor protein (APP) phosphorylation and processing by p35/Cdk5 and p25/Cdk5
    • Liu, F.; Su, Y.; Li, B.; Zhou, Y.; Ryder, J.; Gonzalez-DeWhitt, P.; May, P. C.; Ni, B. Regulation of amyloid precursor protein (APP) phosphorylation and processing by p35/Cdk5 and p25/Cdk5. FEBS Lett. 2003, 547, 193-196.
    • (2003) FEBS Lett. , vol.547 , pp. 193-196
    • Liu, F.1    Su, Y.2    Li, B.3    Zhou, Y.4    Ryder, J.5    Gonzalez-DeWhitt, P.6    May, P.C.7    Ni, B.8
  • 77
    • 3042558276 scopus 로고    scopus 로고
    • Glycogen synthase kinase 3: A drug target for CNS therapies
    • Bhat, R. V.; Haeberlein, S. L. B.; Avila, J. Glycogen synthase kinase 3: A drug target for CNS therapies. J. Neurochem. 2004, 89, 1313-1317.
    • (2004) J. Neurochem. , vol.89 , pp. 1313-1317
    • Bhat, R.V.1    Haeberlein, S.L.B.2    Avila, J.3
  • 78
    • 4344619713 scopus 로고    scopus 로고
    • Pharmacological inhibitors of glycogen synthase kinase 3
    • Meijer, L.; Flajolet, M.; Greengard, P. Pharmacological inhibitors of glycogen synthase kinase 3. Trends Pharmacol. Sci. 2004, 25, 471-480.
    • (2004) Trends Pharmacol. Sci. , vol.25 , pp. 471-480
    • Meijer, L.1    Flajolet, M.2    Greengard, P.3
  • 80
    • 0037118247 scopus 로고    scopus 로고
    • Human wild-type tau interacts with wingless pathway components and produces neurofibrillary pathology in Drosophila
    • Jackson, G. R.; Wiedau-Pazos, M.; Sang, T. K.; Wagle, N.; Brown, C. A.; Massachi, S.; Geschwind, D. H. Human wild-type tau interacts with wingless pathway components and produces neurofibrillary pathology in Drosophila. Neuron 2002, 34, 509-519.
    • (2002) Neuron , vol.34 , pp. 509-519
    • Jackson, G.R.1    Wiedau-Pazos, M.2    Sang, T.K.3    Wagle, N.4    Brown, C.A.5    Massachi, S.6    Geschwind, D.H.7
  • 81
    • 0035863188 scopus 로고    scopus 로고
    • Decreased nuclear beta-catenin, tau hyperphos-phorylation and neurodegeneration in GSK-3beta conditional transgenic mice
    • Lucas, J. J.; Hernandez, F.; Gomez-Ramos, P.; Moran, M. A.; Hen, R.; Avila, J. Decreased nuclear beta-catenin, tau hyperphos-phorylation and neurodegeneration in GSK-3beta conditional transgenic mice. EMBO J. 2001, 20, 27-39.
    • (2001) EMBO J. , vol.20 , pp. 27-39
    • Lucas, J.J.1    Hernandez, F.2    Gomez-Ramos, P.3    Moran, M.A.4    Hen, R.5    Avila, J.6
  • 82
    • 0034718421 scopus 로고    scopus 로고
    • Regulation and localization of tyrosine216 phosphorylation of glycogen synthase kinase-3beta in cellular and animal models of neuronal degeneration
    • Bhat, R. V.; Shanley, J.; Correll, M. P.; Fieles, W. E.; Keith, R. A.; Scott, C. W.; Lee, C. M. Regulation and localization of tyrosine216 phosphorylation of glycogen synthase kinase-3beta in cellular and animal models of neuronal degeneration. Proc. Natl. Acad Sci. USA 2000, 97, 11074-11079.
    • (2000) Proc. Natl. Acad Sci. USA , vol.97 , pp. 11074-11079
    • Bhat, R.V.1    Shanley, J.2    Correll, M.P.3    Fieles, W.E.4    Keith, R.A.5    Scott, C.W.6    Lee, C.M.7
  • 83
    • 0034175688 scopus 로고    scopus 로고
    • Role of glycogen synthase kinase-3beta in neuronal apoptosis induced by trophic withdrawal
    • Hetman, M.; Cavanaugh, J. E.; Kimelman, D.; Xia, Z. Role of glycogen synthase kinase-3beta in neuronal apoptosis induced by trophic withdrawal. J. Neurosci. 2000, 20, 2567-2574.
    • (2000) J. Neurosci. , vol.20 , pp. 2567-2574
    • Hetman, M.1    Cavanaugh, J.E.2    Kimelman, D.3    Xia, Z.4
  • 84
    • 0029998294 scopus 로고    scopus 로고
    • Cellular phosphorylation of tau by GSK-3beta influences tau binding to microtubules and microtubule organization
    • Wagner, U.; Utton, M.; Gallo, J. M.; Miner, C. C. J. Cellular phosphorylation of tau by GSK-3beta influences tau binding to microtubules and microtubule organization. J. Cell Sci. 1996, 109, 1537-1543.
    • (1996) J. Cell Sci. , vol.109 , pp. 1537-1543
    • Wagner, U.1    Utton, M.2    Gallo, J.M.3    Miner, C.C.J.4
  • 85
    • 0346457015 scopus 로고    scopus 로고
    • Primed phosphorylation of tau at Thr231 by glycogen synthase kinase 3beta (GSK3beta) plays a critical role in regulating tau's ability to bind and stabilize microtubules
    • Cho, J. H.; Johnson, G. V. W. Primed phosphorylation of tau at Thr231 by glycogen synthase kinase 3beta (GSK3beta) plays a critical role in regulating tau's ability to bind and stabilize microtubules. J. Neurochem. 2004, 88, 349-358.
    • (2004) J. Neurochem. , vol.88 , pp. 349-358
    • Cho, J.H.1    Johnson, G.V.W.2
  • 87
    • 3042635178 scopus 로고    scopus 로고
    • GSK3 inhibitors: Development and therapeutic potential
    • Cohen, P.; Goedert, M. GSK3 inhibitors: development and therapeutic potential. Nat. Rev. Drug Discov. 2004, 3, 479-487.
    • (2004) Nat. Rev. Drug Discov. , vol.3 , pp. 479-487
    • Cohen, P.1    Goedert, M.2
  • 88
    • 0036273020 scopus 로고    scopus 로고
    • Glycogen synthase kinase 3 (GSK-3) inhibitors as new promising drugs for diabetes, neurodegeneration, cancer, and inflammation
    • Martinez, A.; Castro, A.; Dorronsoro, I.; Alonso, M. Glycogen synthase kinase 3 (GSK-3) inhibitors as new promising drugs for diabetes, neurodegeneration, cancer, and inflammation. Med. Res. Rev. 2002, 22, 373-384.
    • (2002) Med. Res. Rev. , vol.22 , pp. 373-384
    • Martinez, A.1    Castro, A.2    Dorronsoro, I.3    Alonso, M.4
  • 89
    • 1842588303 scopus 로고    scopus 로고
    • Discovery and development of GSK3 inhibitors for the treatment of type 2 diabetes
    • Wagman, A. S.; Johnson, K. W.; Bussiere, D. E. Discovery and development of GSK3 inhibitors for the treatment of type 2 diabetes. Curr. Pharmaceut. Des. 2004, 10, 1105-1137.
    • (2004) Curr. Pharmaceut. Des. , vol.10 , pp. 1105-1137
    • Wagman, A.S.1    Johnson, K.W.2    Bussiere, D.E.3
  • 90
    • 27744574179 scopus 로고    scopus 로고
    • GSK-3 inhibitors and their potential in the treatment of Alzheimer's disease
    • Kypta, R. M. GSK-3 inhibitors and their potential in the treatment of Alzheimer's disease. Exp. Opin. Therapeut. Patents 2005, 15, 1315-1331.
    • (2005) Exp. Opin. Therapeut. Patents , vol.15 , pp. 1315-1331
    • Kypta, R.M.1
  • 95
    • 2542434120 scopus 로고    scopus 로고
    • Design, synthesis, and biological evaluation of novel 7-azaindolyl-heteroaryl-maleimides as potent and selective glycogen synthase kinase-3beta (GSK-3beta) inhibitors
    • O'Neill, D. J.; Shen, L.; Prouty, C.; Conway, B. R.; Westover, L.; Xu, J. Z.; Zhang, H. C.; Maryanoff, B. E.; Murray, W. V.; Demarest, K. T.; Kuo, G. H. Design, synthesis, and biological evaluation of novel 7-azaindolyl-heteroaryl-maleimides as potent and selective glycogen synthase kinase-3beta (GSK-3beta) inhibitors. Bioorg. Med. Chem. 2004, 12, 3167-3185.
    • (2004) Bioorg. Med. Chem. , vol.12 , pp. 3167-3185
    • O'Neill, D.J.1    Shen, L.2    Prouty, C.3    Conway, B.R.4    Westover, L.5    Xu, J.Z.6    Zhang, H.C.7    Maryanoff, B.E.8    Murray, W.V.9    Demarest, K.T.10    Kuo, G.H.11
  • 104
    • 4444288154 scopus 로고    scopus 로고
    • N-Phenyl4-pyrazolo[1,5-b]pyridazin-3-ylpyrimidin-2-amines as Potent and Selective Inhibitors of Glycogen Synthase Kinase 3 with Good Cellular Efficacy
    • Tavares, F. X.; Boucheron, J. A.; Dickerson, S. H.; Griffin, R. J.; Preugschat, F.; Thomson, S. A.; Wang, T. Y.; Zhou, H. Q. N-Phenyl4-pyrazolo[1,5-b]pyridazin-3-ylpyrimidin-2-amines as Potent and Selective Inhibitors of Glycogen Synthase Kinase 3 with Good Cellular Efficacy. J. Med. Chem. 2004, 47, 4716-4730.
    • (2004) J. Med. Chem. , vol.47 , pp. 4716-4730
    • Tavares, F.X.1    Boucheron, J.A.2    Dickerson, S.H.3    Griffin, R.J.4    Preugschat, F.5    Thomson, S.A.6    Wang, T.Y.7    Zhou, H.Q.8
  • 106
    • 13944252481 scopus 로고    scopus 로고
    • CHO., and CH...N Hydrogen Bonds in Ligand Design: A Novel Quinazolin-4-ylthiazol-2-ylamine Protein Kinase Inhibitor
    • Pierce, A. C.; ter Haar, E.; Binch, H. M.; Kay, D. P.; Patel, S. R.; Li, P. CH., O and CH...N Hydrogen Bonds in Ligand Design: A Novel Quinazolin-4-ylthiazol-2-ylamine Protein Kinase Inhibitor. J. Med. Chem. 2005, 48, 1278-1281.
    • (2005) J. Med. Chem. , vol.48 , pp. 1278-1281
    • Pierce, A.C.1    ter Haar, E.2    Binch, H.M.3    Kay, D.P.4    Patel, S.R.5    Li, P.6
  • 109
    • 0038187674 scopus 로고    scopus 로고
    • GSK-3alpha regulates production of Alzheimer's disease amyloid-beta peptides
    • Phiel, C. J.; Wilson, C. A.; Lee, V. M. Y.; Klein, P. S. GSK-3alpha regulates production of Alzheimer's disease amyloid-beta peptides. Nature 2003, 423, 435-439.
    • (2003) Nature , vol.423 , pp. 435-439
    • Phiel, C.J.1    Wilson, C.A.2    Lee, V.M.Y.3    Klein, P.S.4
  • 110
    • 2642552331 scopus 로고    scopus 로고
    • Lithium, a common drug for bipolar disorder treatment, regulates amyloid-beta precursor protein processing
    • Su, Y.; Ryder, J.; Li, B.; Wu, X.; Fox, N.; Solenberg, P.; Brune, K.; Paul, S.; Zhou, Y.; Liu, F.; Ni, B. Lithium, a common drug for bipolar disorder treatment, regulates amyloid-beta precursor protein processing. Biochemistry 2004, 43, 6899-6908.
    • (2004) Biochemistry , vol.43 , pp. 6899-6908
    • Su, Y.1    Ryder, J.2    Li, B.3    Wu, X.4    Fox, N.5    Solenberg, P.6    Brune, K.7    Paul, S.8    Zhou, Y.9    Liu, F.10    Ni, B.11
  • 111
    • 12244279939 scopus 로고    scopus 로고
    • Up-regulation of mitogen-activated protein kinases ERK1/2 and MEK1/2 is associated with the progression of neurofibrillary degeneration in Alzheimer's disease
    • Pei, J. J.; Braak, H.; An, W. L.; Winblad, B.; Cowburn, R. F.; Iqbal, K.; Grundke-Iqbal, I. Up-regulation of mitogen-activated protein kinases ERK1/2 and MEK1/2 is associated with the progression of neurofibrillary degeneration in Alzheimer's disease. Mol. Brain Res. 2002, 109, 45-55.
    • (2002) Mol. Brain Res. , vol.109 , pp. 45-55
    • Pei, J.J.1    Braak, H.2    An, W.L.3    Winblad, B.4    Cowburn, R.F.5    Iqbal, K.6    Grundke-Iqbal, I.7
  • 112
    • 0034797352 scopus 로고    scopus 로고
    • Differential activation of neuronal ERK, JNK/SAPK and p38 in Alzheimer disease: The 'two hit' hypothesis
    • Zhu, X.; Castellani, R. J.; Takeda, A.; Nunomura, A.; Atwood, C. S.; Perry, G.; Smith, M. A. Differential activation of neuronal ERK, JNK/ SAPK and p38 in Alzheimer disease: the 'two hit' hypothesis. Mech. Ageing Develop. 2001, 123, 39-46.
    • (2001) Mech. Ageing Develop. , vol.123 , pp. 39-46
    • Zhu, X.1    Castellani, R.J.2    Takeda, A.3    Nunomura, A.4    Atwood, C.S.5    Perry, G.6    Smith, M.A.7
  • 113
    • 0042679509 scopus 로고    scopus 로고
    • Okadaic-acid-induced inhibition of protein phosphatase 2A produces activation of mitogen-activated protein kinases ERK1/2, MEK1/2, and p70 S6, similar to that in Alzheimer's disease
    • Pei, J. J.; Gong, C. X.; An, W. L.; Winblad, B.; Cowburn, R. F.; Grundke-Iqbal, I.; Iqbal, K. Okadaic-acid-induced inhibition of protein phosphatase 2A produces activation of mitogen-activated protein kinases ERK1/2, MEK1/2, and p70 S6, similar to that in Alzheimer's disease. Am. J. Pathol. 2003, 163, 845-858.
    • (2003) Am. J. Pathol. , vol.163 , pp. 845-858
    • Pei, J.J.1    Gong, C.X.2    An, W.L.3    Winblad, B.4    Cowburn, R.F.5    Grundke-Iqbal, I.6    Iqbal, K.7
  • 114
    • 0033957692 scopus 로고    scopus 로고
    • PD98059 prevents neurite degeneration induced by fibrillar beta-amyloid in mature hippocampal neurons
    • Rapoport, M.; Ferreira, A. PD98059 prevents neurite degeneration induced by fibrillar beta-amyloid in mature hippocampal neurons. J. Neurochem. 2000, 74, 125-133.
    • (2000) J. Neurochem. , vol.74 , pp. 125-133
    • Rapoport, M.1    Ferreira, A.2
  • 115
    • 0037336701 scopus 로고    scopus 로고
    • Interleukin-1 mediates pathological effects of microglia on tau phosphorylation and on synaptophysin synthesis in cortical neurons through a p38-MAPK pathway
    • Li, Y.; Liu, L.; Barger, S. W.; Griffin, W. S. T. Interleukin-1 mediates pathological effects of microglia on tau phosphorylation and on synaptophysin synthesis in cortical neurons through a p38-MAPK pathway. J. Neurosci. 2003, 23, 1605-1611.
    • (2003) J. Neurosci. , vol.23 , pp. 1605-1611
    • Li, Y.1    Liu, L.2    Barger, S.W.3    Griffin, W.S.T.4
  • 116
    • 1842610852 scopus 로고    scopus 로고
    • Block of long-term potentiation by naturally secreted and synthetic amyloid b-peptide in hippocampal slices is mediated via activation of the kinases c-Jun N-terminal kinase, cyclin-dependent kinase 5, and p38 mitogen-activated protein kinase as well as metabotropic glutamate receptor type 5
    • Wang, Q.; Walsh, D. M.; Rowan, M. J.; Selkoe, D. J.; Anwyl, R. Block of long-term potentiation by naturally secreted and synthetic amyloid b-peptide in hippocampal slices is mediated via activation of the kinases c-Jun N-terminal kinase, cyclin-dependent kinase 5, and p38 mitogen-activated protein kinase as well as metabotropic glutamate receptor type 5. J. Neurosci. 2004, 24, 3370-3378.
    • (2004) J. Neurosci. , vol.24 , pp. 3370-3378
    • Wang, Q.1    Walsh, D.M.2    Rowan, M.J.3    Selkoe, D.J.4    Anwyl, R.5
  • 117
    • 11144249896 scopus 로고    scopus 로고
    • Increased tau phosphorylation on mitogen-activated protein kinase consensus sites and cognitive decline in transgenic models for Alzheimer's disease and FTDP-17: Evidence for distinct molecular processes underlying tau abnormalities
    • Lambourne, S. L.; Sellers, L. A.; Bush, T. G.; Choudhury, S. K.; Emson, P. C.; Suh, Y. H.; Wilkinson, L. S. Increased tau phosphorylation on mitogen-activated protein kinase consensus sites and cognitive decline in transgenic models for Alzheimer's disease and FTDP-17: Evidence for distinct molecular processes underlying tau abnormalities. Mol. Cell. Biol. 2005, 25, 278-293.
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 278-293
    • Lambourne, S.L.1    Sellers, L.A.2    Bush, T.G.3    Choudhury, S.K.4    Emson, P.C.5    Suh, Y.H.6    Wilkinson, L.S.7
  • 118
    • 0036580703 scopus 로고    scopus 로고
    • Activation of c-Jun N-terminal kinase and p38 in an Alzheimer's disease model is associated with amyloid deposition
    • Savage, M. J.; Lin, Y. G.; Ciallella, J. R.; Flood, D. G.; Scott, R. W. Activation of c-Jun N-terminal kinase and p38 in an Alzheimer's disease model is associated with amyloid deposition. J. Neurosci. 2002, 22, 3376-3385.
    • (2002) J. Neurosci. , vol.22 , pp. 3376-3385
    • Savage, M.J.1    Lin, Y.G.2    Ciallella, J.R.3    Flood, D.G.4    Scott, R.W.5
  • 119
    • 7244253060 scopus 로고    scopus 로고
    • Increased tau Phosphorylation in Apolipoprotein E4 Transgenic Mice Is Associated with Activation of Extracellular Signal-regulated Kinase: Modulation by Zinc
    • Harris, F. M.; Brecht, W. J.; Xu, Q.; Mahley, R. W.; Huang, Y. Increased tau Phosphorylation in Apolipoprotein E4 Transgenic Mice Is Associated with Activation of Extracellular Signal-regulated Kinase: Modulation by Zinc. J. Biol. Chem. 2004, 279, 44795-44801.
    • (2004) J. Biol. Chem. , vol.279 , pp. 44795-44801
    • Harris, F.M.1    Brecht, W.J.2    Xu, Q.3    Mahley, R.W.4    Huang, Y.5
  • 120
    • 0034685703 scopus 로고    scopus 로고
    • Casein kinase 1 delta mRNA is upregulated in Alzheimer disease brain
    • Yasojima, K.; Kuret, J.; DeMaggio, A. J.; McGeer, E.; McGeer, P. L. Casein kinase 1 delta mRNA is upregulated in Alzheimer disease brain. Brain Res. 2000, 865, 116-120.
    • (2000) Brain Res. , vol.865 , pp. 116-120
    • Yasojima, K.1    Kuret, J.2    DeMaggio, A.J.3    McGeer, E.4    McGeer, P.L.5
  • 121
    • 0030723127 scopus 로고    scopus 로고
    • Casein kinase 1 is tightly associated with paired-helical filaments isolated from Alzheimer's disease brain
    • Kuret, J.; Johnson, G. S.; Cha, D.; Christenson, E. R.; DeMaggio, A. J.; Hoekstra, M. F. Casein kinase 1 is tightly associated with paired-helical filaments isolated from Alzheimer's disease brain. J. Neurochem. 1997, 69, 2506-2515.
    • (1997) J. Neurochem. , vol.69 , pp. 2506-2515
    • Kuret, J.1    Johnson, G.S.2    Cha, D.3    Christenson, E.R.4    DeMaggio, A.J.5    Hoekstra, M.F.6
  • 122
    • 0034622242 scopus 로고    scopus 로고
    • Casein kinase 1 delta is associated with pathological accumulation of tau in several neurodegenerative diseases
    • Schwab, C.; DeMaggio, A. J.; Ghoshal, N.; Binder, L. I.; Kuret, J.; McGeer, P. L. Casein kinase 1 delta is associated with pathological accumulation of tau in several neurodegenerative diseases. Neurobiol. Aging 2000, 21, 503-510.
    • (2000) Neurobiol. Aging , vol.21 , pp. 503-510
    • Schwab, C.1    DeMaggio, A.J.2    Ghoshal, N.3    Binder, L.I.4    Kuret, J.5    McGeer, P.L.6
  • 123
    • 0028871109 scopus 로고
    • Phosphorylation of tau protein by casein kinase-1 converts it to an abnormal Alzheimer-like state
    • Singh, T.; Grundke-Iqbal, I.; Iqbal, K. Phosphorylation of tau protein by casein kinase-1 converts it to an abnormal Alzheimer-like state. J. Neurochem. 1995, 64, 1420-1423.
    • (1995) J. Neurochem. , vol.64 , pp. 1420-1423
    • Singh, T.1    Grundke-Iqbal, I.2    Iqbal, K.3
  • 124
    • 1942469505 scopus 로고    scopus 로고
    • Casein Kinase 1 Delta Phosphorylates Tau and Disrupts Its Binding to Microtubules
    • Li, G.; Yin, H.; Kuret, J. Casein Kinase 1 Delta Phosphorylates Tau and Disrupts Its Binding to Microtubules. J. Biol. Chem. 2004, 279, 15938-15945.
    • (2004) J. Biol. Chem. , vol.279 , pp. 15938-15945
    • Li, G.1    Yin, H.2    Kuret, J.3
  • 127
    • 0029899091 scopus 로고    scopus 로고
    • Tau protein is phosphorylated by cyclic AMP-dependent protein kinase and calcium/calmodulin-dependent protein kinase II within its microtubule-binding domains at Ser-262 and Ser-356
    • Litersky, J. M.; Johnson, G. V. W.; Jakes, R.; Goedert, M.; Lee, M.; Seubert, P. Tau protein is phosphorylated by cyclic AMP-dependent protein kinase and calcium/calmodulin-dependent protein kinase II within its microtubule-binding domains at Ser-262 and Ser-356. Biochem. J. 1996, 316 (Pt 2), 655-660.
    • (1996) Biochem. J. , vol.316 , Issue.PART 2 , pp. 655-660
    • Litersky, J.M.1    Johnson, G.V.W.2    Jakes, R.3    Goedert, M.4    Lee, M.5    Seubert, P.6
  • 128
    • 0031046463 scopus 로고    scopus 로고
    • Protein kinase C and calcium/calmodulin-dependent protein kinase II phosphorylate three-repeat and four-repeat tau isoforms at different rates
    • Singh, T. J.; Grundke-Iqbal, I.; Wu, W. Q.; Chauhan, V.; Novak, M.; Kontzekova, E.; Iqbal, K. Protein kinase C and calcium/ calmodulin-dependent protein kinase II phosphorylate three-repeat and four-repeat tau isoforms at different rates. Mol. Cell. Biochem. 1997, 168, 141-148.
    • (1997) Mol. Cell. Biochem. , vol.168 , pp. 141-148
    • Singh, T.J.1    Grundke-Iqbal, I.2    Wu, W.Q.3    Chauhan, V.4    Novak, M.5    Kontzekova, E.6    Iqbal, K.7
  • 129
    • 0029888525 scopus 로고    scopus 로고
    • Calcium/calmodulin-dependent protein kinase II phosphorylates tau at Ser-262 but only partially inhibits its binding to microtubules
    • Singh, T. J.; Wang, J. Z.; Novak, M.; Kontzekova, E.; Grundke-Iqbal, I.; Iqbal, K. Calcium/calmodulin-dependent protein kinase II phosphorylates tau at Ser-262 but only partially inhibits its binding to microtubules. FEBS Lett. 1996, 387, 145-148.
    • (1996) FEBS Lett. , vol.387 , pp. 145-148
    • Singh, T.J.1    Wang, J.Z.2    Novak, M.3    Kontzekova, E.4    Grundke-Iqbal, I.5    Iqbal, K.6
  • 130
    • 0026787130 scopus 로고
    • Protein sequence and mass spectrometric analyses of tau in the Alzheimer's disease brain
    • Hasegawa, M.; Morishima-Kawashima, M.; Takio, K.; Suzuki, M.; Titani, K.; Ihara, Y. Protein sequence and mass spectrometric analyses of tau in the Alzheimer's disease brain. J. Biol. Chem. 1992, 267, 17047-17054.
    • (1992) J. Biol. Chem. , vol.267 , pp. 17047-17054
    • Hasegawa, M.1    Morishima-Kawashima, M.2    Takio, K.3    Suzuki, M.4    Titani, K.5    Ihara, Y.6
  • 131
    • 0027338266 scopus 로고
    • Phosphorylation of Ser262 strongly reduces binding of Tau to microtubules: Distinction between PHF-like immunoreactivity and microtubule binding
    • Biernat, J.; Gustke, N.; Drewes, G.; Mandelkow, E. M.; Mandelkow, E. Phosphorylation of Ser262 strongly reduces binding of Tau to microtubules: Distinction between PHF-like immunoreactivity and microtubule binding. Neuron 1993, 11, 153-163.
    • (1993) Neuron , vol.11 , pp. 153-163
    • Biernat, J.1    Gustke, N.2    Drewes, G.3    Mandelkow, E.M.4    Mandelkow, E.5
  • 132
    • 1542358895 scopus 로고    scopus 로고
    • PAR-1 kinase plays an initiator role in a temporally ordered phosphorylation process that confers tau toxicity in Drosophila
    • Nishimura, I.; Yang, Y.; Lu, B. PAR-1 kinase plays an initiator role in a temporally ordered phosphorylation process that confers tau toxicity in Drosophila. Cell 2004, 116, 671-682.
    • (2004) Cell , vol.116 , pp. 671-682
    • Nishimura, I.1    Yang, Y.2    Lu, B.3
  • 133
    • 0031727983 scopus 로고    scopus 로고
    • Ser-262 in human recombinant tau protein is a markedly more favorable site for phosphorylation by CaMKII than PKA or PhK
    • Sironi, J. J.; Yen, S. H.; Gondal, J. A.; Wu, Q.; Grundke-Iqbal, I.; Iqbal, K. Ser-262 in human recombinant tau protein is a markedly more favorable site for phosphorylation by CaMKII than PKA or PhK. FEBS Lett. 1998, 436, 471-475.
    • (1998) FEBS Lett. , vol.436 , pp. 471-475
    • Sironi, J.J.1    Yen, S.H.2    Gondal, J.A.3    Wu, Q.4    Grundke-Iqbal, I.5    Iqbal, K.6
  • 134
    • 0035830740 scopus 로고    scopus 로고
    • Inhibition of PP-2A upregulates CaMKII in rat forebrain and induces hyperphosphorylation of tau at Ser 262/356
    • Bennecib, M.; Gong, C. X; Grundke-Iqbal, I.; Iqbal, K. Inhibition of PP-2A upregulates CaMKII in rat forebrain and induces hyperphosphorylation of tau at Ser 262/356. FEBS Lett. 2001, 490, 15-22.
    • (2001) FEBS Lett. , vol.490 , pp. 15-22
    • Bennecib, M.1    Gong, C.X.2    Grundke-Iqbal, I.3    Iqbal, K.4
  • 135
    • 24144497098 scopus 로고    scopus 로고
    • Phosphorylation of tau at serine 416 by Ca2+/calmodulin-dependent protein kinase II in neuronal soma in brain
    • Yamamoto, H.; Hiragami, Y.; Murayama, M.; Ishizuka, K.; Kawahara, M.; Takashima, A. Phosphorylation of tau at serine 416 by Ca2+/ calmodulin-dependent protein kinase II in neuronal soma in brain. J. Neurochem. 2005, 94, 1438-1447.
    • (2005) J. Neurochem. , vol.94 , pp. 1438-1447
    • Yamamoto, H.1    Hiragami, Y.2    Murayama, M.3    Ishizuka, K.4    Kawahara, M.5    Takashima, A.6
  • 136
    • 15944418222 scopus 로고    scopus 로고
    • Induction of long-term potentiation in single nociceptive dorsal horn neurons is blocked by the CaMKII inhibitor AIP
    • Pedersen, L. M.; Lien, G. F.; Bollerud, I.; Gjerstad, J. Induction of long-term potentiation in single nociceptive dorsal horn neurons is blocked by the CaMKII inhibitor AIP. Brain Res. 2005, 1041, 66-71.
    • (2005) Brain Res. , vol.1041 , pp. 66-71
    • Pedersen, L.M.1    Lien, G.F.2    Bollerud, I.3    Gjerstad, J.4
  • 137
    • 0036006169 scopus 로고    scopus 로고
    • A fresh look at the role of CaMKII in hippocampal synaptic plasticity and memory
    • Rongo, C. A fresh look at the role of CaMKII in hippocampal synaptic plasticity and memory. BioEssays 2002, 24, 223-233.
    • (2002) BioEssays , vol.24 , pp. 223-233
    • Rongo, C.1
  • 138
    • 0036513485 scopus 로고    scopus 로고
    • The molecular basis of CaMKII function in synaptic and behavioral memory
    • Lisman, J.; Schulman, H.; Cline, H. The molecular basis of CaMKII function in synaptic and behavioral memory. Nat. Rev. Neurosci. 2002, 3, 175-190.
    • (2002) Nat. Rev. Neurosci. , vol.3 , pp. 175-190
    • Lisman, J.1    Schulman, H.2    Cline, H.3
  • 139
    • 4644360412 scopus 로고    scopus 로고
    • Marking tau for tangles and toxicity
    • Drewes, G. Marking tau for tangles and toxicity. Trends Biochem. Sci. 2004, 29, 548-555.
    • (2004) Trends Biochem. Sci. , vol.29 , pp. 548-555
    • Drewes, G.1
  • 140
    • 1842816667 scopus 로고    scopus 로고
    • An overview of the KIN1/PAR-1/MARK kinase family
    • Tassan, J. P.; Le Goff, X. An overview of the KIN1/PAR-1/MARK kinase family. Biol. Cell. 2004, 96, 193-199.
    • (2004) Biol. Cell. , vol.96 , pp. 193-199
    • Tassan, J.P.1    Le Goff, X.2
  • 141
    • 0028937631 scopus 로고
    • Microtubule-associated protein/microtubule affinity-regulating kinase (p110mark). A novel protein kinase that regulates tau-microtubule interactions and dynamic instability by phosphorylation at the Alzheimer-specific site serine 262
    • Drewes, G.; Trinczek, B.; Illenberger, S.; Biernat, J.; Schmitt-Ulms, G.; Meyer, H. E.; Mandelkow, E. M.; Mandelkow, E. Microtubule-associated protein/microtubule affinity-regulating kinase (p110mark). A novel protein kinase that regulates tau-microtubule interactions and dynamic instability by phosphorylation at the Alzheimer-specific site serine 262. J. Biol. Chem. 1995, 270, 7679-7688.
    • (1995) J. Biol. Chem. , vol.270 , pp. 7679-7688
    • Drewes, G.1    Trinczek, B.2    Illenberger, S.3    Biernat, J.4    Schmitt-Ulms, G.5    Meyer, H.E.6    Mandelkow, E.M.7    Mandelkow, E.8
  • 142
    • 0034071269 scopus 로고    scopus 로고
    • Microtabule/MAP-affinity regulating kinase (MARK) is activated by phenylarsine oxide in situ and phosphorylates tau within its microtubule-binding domain
    • Jenkins, S. M.; Johnson, G. V. W. Microtabule/MAP-affinity regulating kinase (MARK) is activated by phenylarsine oxide in situ and phosphorylates tau within its microtubule-binding domain. J. Neurochem. 2000, 74, 1463-1468.
    • (2000) J. Neurochem. , vol.74 , pp. 1463-1468
    • Jenkins, S.M.1    Johnson, G.V.W.2
  • 143
    • 0030969575 scopus 로고    scopus 로고
    • MARK, a novel family of protein kinases that phosphorylate microtubule-associated proteins and trigger microtubule disruption
    • Drewes, G.; Ebneth, A.; Preuss, U.; Mandelkow, E. M.; Mandelkow, E. MARK, a novel family of protein kinases that phosphorylate microtubule-associated proteins and trigger microtubule disruption. Cell 1997, 89, 297-308.
    • (1997) Cell , vol.89 , pp. 297-308
    • Drewes, G.1    Ebneth, A.2    Preuss, U.3    Mandelkow, E.M.4    Mandelkow, E.5
  • 144
    • 0033758105 scopus 로고    scopus 로고
    • Microtubule-affinity regulating kinase (MARK) is tightly associated with neurofibrillary tangles in Alzheimer brain: A fluorescence resonance energy transfer study
    • Chin, J. Y.; Knowles, R. B.; Schneider, A.; Drewes, G.; Mandelkow, E. M.; Hyman, B. T. Microtubule-affinity regulating kinase (MARK) is tightly associated with neurofibrillary tangles in Alzheimer brain: A fluorescence resonance energy transfer study. J. Neuropath. Exp. Neurol. 2000, 59, 966-971.
    • (2000) J. Neuropath. Exp. Neurol. , vol.59 , pp. 966-971
    • Chin, J.Y.1    Knowles, R.B.2    Schneider, A.3    Drewes, G.4    Mandelkow, E.M.5    Hyman, B.T.6
  • 145
    • 0032731434 scopus 로고    scopus 로고
    • Phosphorylation of MAP2c and MAP4 by MARK kinases leads to the destabilization of microtubules in cells
    • Ebneth, A.; Drewes, G.; Mandelkow, E. M.; Mandelkow, E. Phosphorylation of MAP2c and MAP4 by MARK kinases leads to the destabilization of microtubules in cells. Cell Motility and the Cytoskeleton 1999, 44, 209-224.
    • (1999) Cell Motility and the Cytoskeleton , vol.44 , pp. 209-224
    • Ebneth, A.1    Drewes, G.2    Mandelkow, E.M.3    Mandelkow, E.4
  • 146
    • 0029965781 scopus 로고    scopus 로고
    • Phosphorylation of microtubule-associated proteins MAP2 and MAP4 by the protein kinase p110mark. Phosphorylation sites and regulation of microtubule dynamics
    • Illenberger, S.; Drewes, G.; Trinczek, B.; Biernat, J.; Meyer, H. E.; Olmsted, J. B.; Mandelkow, E. M.; Mandelkow, E. Phosphorylation of microtubule-associated proteins MAP2 and MAP4 by the protein kinase p110mark. Phosphorylation sites and regulation of microtubule dynamics. J. Biol. Chem. 1996, 271, 10834-10843.
    • (1996) J. Biol. Chem. , vol.271 , pp. 10834-10843
    • Illenberger, S.1    Drewes, G.2    Trinczek, B.3    Biernat, J.4    Meyer, H.E.5    Olmsted, J.B.6    Mandelkow, E.M.7    Mandelkow, E.8
  • 147
    • 0033596946 scopus 로고    scopus 로고
    • Phosphorylation that detaches tau protein from microtubules (Ser262, Ser214) also protects it against aggregation into Alzheimer paired helical filaments
    • Schneider, A.; Biernat, J.; von Bergen, M.; Mandelkow, E.; Mandelkow, E. M. Phosphorylation that detaches tau protein from microtubules (Ser262, Ser214) also protects it against aggregation into Alzheimer paired helical filaments. Biochemistry 1999, 38, 3549-3558.
    • (1999) Biochemistry , vol.38 , pp. 3549-3558
    • Schneider, A.1    Biernat, J.2    von Bergen, M.3    Mandelkow, E.4    Mandelkow, E.M.5
  • 148
    • 5444273804 scopus 로고    scopus 로고
    • MARK/PAR1 kinase is a regulator of microtubule-dependent transport in axons
    • Mandelkow, E. M.; Thies, E.; Trinczek, B.; Biernat, J.; Mandelkow, E. MARK/PAR1 kinase is a regulator of microtubule-dependent transport in axons. J. Cell. Biol. 2004, 167, 99-110.
    • (2004) J. Cell. Biol. , vol.167 , pp. 99-110
    • Mandelkow, E.M.1    Thies, E.2    Trinczek, B.3    Biernat, J.4    Mandelkow, E.5
  • 149
  • 150
    • 1542358900 scopus 로고    scopus 로고
    • PAR-1 for the course of neurodegeneration
    • Fortini, M. E. PAR-1 for the course of neurodegeneration. Cell 2004, 116, 631-632.
    • (2004) Cell , vol.116 , pp. 631-632
    • Fortini, M.E.1
  • 152
    • 0030614508 scopus 로고    scopus 로고
    • The regulatory Ser262 of microtubule-associated protein tau is phosphorylated by phosphorylase kinase
    • Paudel, H. K. The regulatory Ser262 of microtubule-associated protein tau is phosphorylated by phosphorylase kinase. J. Biol. Chem. 1997, 272, 1777-1785.
    • (1997) J. Biol. Chem. , vol.272 , pp. 1777-1785
    • Paudel, H.K.1
  • 153
    • 0026625670 scopus 로고
    • Microtubule-associated protein Tau is phosphorylated by protein kinase C on its tubulin binding domain
    • Correas, I; Diaz-Nido, J.; Avila, J. Microtubule-associated protein Tau is phosphorylated by protein kinase C on its tubulin binding domain. J. Biol. Chem. 1992, 267, 15721-15728.
    • (1992) J. Biol. Chem. , vol.267 , pp. 15721-15728
    • Correas, I.1    Diaz-Nido, J.2    Avila, J.3
  • 154
    • 0027508998 scopus 로고
    • Phosphorylation of recombinant Tau by cAMP-dependent protein kinase. Identification of phosphorylation sites and effect on microtubule assembly
    • Scott, C. W.; Spreen, R. C.; Herman, J. L.; Chow, F. P.; Davison, M. D.; Young, J.; Caputo, C. B. Phosphorylation of recombinant Tau by cAMP-dependent protein kinase. Identification of phosphorylation sites and effect on microtubule assembly. J. Biol. Chem. 1993, 268, 1166-1173.
    • (1993) J. Biol. Chem. , vol.268 , pp. 1166-1173
    • Scott, C.W.1    Spreen, R.C.2    Herman, J.L.3    Chow, F.P.4    Davison, M.D.5    Young, J.6    Caputo, C.B.7
  • 155
    • 0028364256 scopus 로고
    • Differential effect of phosphorylation and substrate modulation on tau's ability to promote microtubule growth and nucleation
    • Brandt, R.; Lee, G.; Teplow, D. B.; Shalloway, D.; Abdel-Ghany, M. Differential effect of phosphorylation and substrate modulation on tau's ability to promote microtubule growth and nucleation. J. Biol. Chem. 1994, 269, 11776-11782.
    • (1994) J. Biol. Chem. , vol.269 , pp. 11776-11782
    • Brandt, R.1    Lee, G.2    Teplow, D.B.3    Shalloway, D.4    Abdel-Ghany, M.5
  • 158
    • 0023715473 scopus 로고
    • Inhibition by cyclic AMP of phorbol ester-potentiated norepinephrine release from guinea pig brain cortical synaptosomes
    • Shuntoh, H.; Taniyama, K.; Fukuzaki, H.; Tanaka, C. Inhibition by cyclic AMP of phorbol ester-potentiated norepinephrine release from guinea pig brain cortical synaptosomes. J. Neurochem. 1988, 51, 1565-1572.
    • (1988) J. Neurochem. , vol.51 , pp. 1565-1572
    • Shuntoh, H.1    Taniyama, K.2    Fukuzaki, H.3    Tanaka, C.4
  • 159
    • 3843085169 scopus 로고    scopus 로고
    • Human SAD1 kinase is involved in UV-induced DNA damage checkpoint function
    • Lu, R.; Niida, H.; Nakanishi, M. Human SAD1 kinase is involved in UV-induced DNA damage checkpoint function. J. Biol. Chem. 2004, 279, 31164-31170.
    • (2004) J. Biol. Chem. , vol.279 , pp. 31164-31170
    • Lu, R.1    Niida, H.2    Nakanishi, M.3
  • 160
    • 0035137995 scopus 로고    scopus 로고
    • The SAD-1 kinase regulates presynaptic vesicle clustering and axon termination
    • Crump, J. G.; Zhen, M.; Jin, Y.; Bargmann, C. I. The SAD-1 kinase regulates presynaptic vesicle clustering and axon termination. Neuron 2001, 29, 115-129
    • (2001) Neuron , vol.29 , pp. 115-129
    • Crump, J.G.1    Zhen, M.2    Jin, Y.3    Bargmann, C.I.4
  • 161
    • 13644267037 scopus 로고    scopus 로고
    • Mammalian SAD Kinases Are Required for Neuronal Polarization
    • Kishi, M.; Pan, Y. A.; Crump, J. G.; Sanes, J. R. Mammalian SAD Kinases Are Required for Neuronal Polarization. Science 2005, 307, 929-932
    • (2005) Science , vol.307 , pp. 929-932
    • Kishi, M.1    Pan, Y.A.2    Crump, J.G.3    Sanes, J.R.4
  • 162
    • 0036769791 scopus 로고    scopus 로고
    • Role of Serine/threonine protein phosphatase in Alzheimer's disease
    • Tian, Q.; Wang, J. Role of Serine/threonine protein phosphatase in Alzheimer's disease. Neurosignals 2002, 11, 262-269.
    • (2002) Neurosignals , vol.11 , pp. 262-269
    • Tian, Q.1    Wang, J.2
  • 163
    • 0035075793 scopus 로고    scopus 로고
    • PP2A mRNA Expression Is Quantitatively Decreased in Alzheimer's Disease Hippocampus
    • Vogelsberg-Ragaglia, V.; Schuck, T.; Trojanowski, J. Q.; Lee, V. M. Y. PP2A mRNA Expression Is Quantitatively Decreased in Alzheimer's Disease Hippocampus. Exp. Neurol. 2001, 168, 402-412.
    • (2001) Exp. Neurol. , vol.168 , pp. 402-412
    • Vogelsberg-Ragaglia, V.1    Schuck, T.2    Trojanowski, J.Q.3    Lee, V.M.Y.4
  • 164
    • 0029113874 scopus 로고
    • Phosphatase activity toward abnormally phosphorylated tau: Decrease in Alzheimer disease brain
    • Gong, C. X.; Shaikh, S.; Wang, J. Z.; Zaidi, T.; Grundke-Iqbal, I.; Iqbal, K. Phosphatase activity toward abnormally phosphorylated tau: decrease in Alzheimer disease brain. J. Neurochem. 1995, 65, 732-738.
    • (1995) J. Neurochem. , vol.65 , pp. 732-738
    • Gong, C.X.1    Shaikh, S.2    Wang, J.Z.3    Zaidi, T.4    Grundke-Iqbal, I.5    Iqbal, K.6
  • 165
    • 0027214404 scopus 로고
    • Phosphoprotein phosphatase activities in Alzheimer disease brain
    • Gong, C. X.; Singh, T. J.; Grundke-Iqbal, I.; Iqbal, K. Phosphoprotein phosphatase activities in Alzheimer disease brain. J. Neurochem. 1993, 61, 921-927.
    • (1993) J. Neurochem. , vol.61 , pp. 921-927
    • Gong, C.X.1    Singh, T.J.2    Grundke-Iqbal, I.3    Iqbal, K.4
  • 166
    • 0028064431 scopus 로고
    • Dephosphorylation of Alzheimer's disease abnormally phosphorylated tau by protein phosphatase-2A
    • Gong, C. X.; Grundke-Iqbal, I.; Iqbal, K. Dephosphorylation of Alzheimer's disease abnormally phosphorylated tau by protein phosphatase-2A. Neuroscience 1994, 61, 765-772.
    • (1994) Neuroscience , vol.61 , pp. 765-772
    • Gong, C.X.1    Grundke-Iqbal, I.2    Iqbal, K.3
  • 168
    • 0030865642 scopus 로고    scopus 로고
    • An Efficient Total Synthesis of Okadaic Acid
    • Forsyth, C. J.; Sabes, S. F.; Urbanek, R. A. An Efficient Total Synthesis of Okadaic Acid. J. Am. Chem. Soc. 1997, 119, 8381-8382.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 8381-8382
    • Forsyth, C.J.1    Sabes, S.F.2    Urbanek, R.A.3
  • 169
    • 0024397415 scopus 로고
    • The structure and regulation of protein phosphatases
    • Cohen, P. The structure and regulation of protein phosphatases. Annu. Rev. Biochem. 1989, 58, 453-508.
    • (1989) Annu. Rev. Biochem. , vol.58 , pp. 453-508
    • Cohen, P.1
  • 170
    • 0025994387 scopus 로고
    • Protein phosphorylation and neuronal function
    • Walaas, S. I.; Greengard, P. Protein phosphorylation and neuronal function. Pharmacol. Rev. 1991, 43, 299-349.
    • (1991) Pharmacol. Rev. , vol.43 , pp. 299-349
    • Walaas, S.I.1    Greengard, P.2
  • 171
    • 0029665228 scopus 로고    scopus 로고
    • Molecular Identification of I1PP2A, a Novel Potent Heat-Stable Inhibitor Protein of Protein Phosphatase 2A
    • Li, M.; Makkinje, A.; Damuni, Z. Molecular Identification of I1PP2A, a Novel Potent Heat-Stable Inhibitor Protein of Protein Phosphatase 2A. Biochemistry 1996, 35, 6998-7002.
    • (1996) Biochemistry , vol.35 , pp. 6998-7002
    • Li, M.1    Makkinje, A.2    Damuni, Z.3
  • 172
    • 0029889342 scopus 로고    scopus 로고
    • The myeloid leukemia-associated protein SET is a potent inhibitor of protein phosphatase 2A
    • Li, M.; Makkinje, A.; Damuni, Z. The myeloid leukemia-associated protein SET is a potent inhibitor of protein phosphatase 2A. J. Biol. Chem. 1996, 271, 11059-11062.
    • (1996) J. Biol. Chem. , vol.271 , pp. 11059-11062
    • Li, M.1    Makkinje, A.2    Damuni, Z.3
  • 173
    • 19544362550 scopus 로고    scopus 로고
    • Up-regulation of inhibitors of protein phosphatase-2A in Alzheimer's disease
    • Tanimukai, H.; Grundke-Iqbal, I.; Iqbal, K. Up-regulation of inhibitors of protein phosphatase-2A in Alzheimer's disease. Am. J. Pathol. 2005, 166, 1761-1771.
    • (2005) Am. J. Pathol. , vol.166 , pp. 1761-1771
    • Tanimukai, H.1    Grundke-Iqbal, I.2    Iqbal, K.3
  • 174
    • 11844273281 scopus 로고    scopus 로고
    • Inhibitors of protein phosphatase-2A from human brain structures, inummocytological localization and activities towards dephosphorylation of the Alzheimer type hyperphosphorylated tau
    • Tsujio, I.; Zaidi, T.; Xu, J.; Kotula, L.; Grundke-Iqbal, I.; Iqbal, K. Inhibitors of protein phosphatase-2A from human brain structures, inummocytological localization and activities towards dephosphorylation of the Alzheimer type hyperphosphorylated tau. FEBS Lett. 2004, 579, 363-372.
    • (2004) FEBS Lett. , vol.579 , pp. 363-372
    • Tsujio, I.1    Zaidi, T.2    Xu, J.3    Kotula, L.4    Grundke-Iqbal, I.5    Iqbal, K.6
  • 175
    • 2442465965 scopus 로고    scopus 로고
    • Memantine inhibits and reverses the Alzheimer type abnormal hyperphosphorylation of tau and associated neurodegeneration
    • Li, L.; Sengupta, A.; Haque, N.; Grundke-Iqbal, I.; Iqbal, K. Memantine inhibits and reverses the Alzheimer type abnormal hyperphosphorylation of tau and associated neurodegeneration. FEBS Lett. 2004, 566, 261-269.
    • (2004) FEBS Lett. , vol.566 , pp. 261-269
    • Li, L.1    Sengupta, A.2    Haque, N.3    Grundke-Iqbal, I.4    Iqbal, K.5
  • 177
    • 33646181674 scopus 로고    scopus 로고
    • presented at Alzheimer's and Parkinson's Diseases: Insights, Progress and Perspectives; 7th International Conference, Sorrento, Italy, March 9-13
    • Hutton, M. presented at Alzheimer's and Parkinson's Diseases: Insights, Progress and Perspectives; 7th International Conference, Sorrento, Italy, March 9-13, 2005.
    • (2005)
    • Hutton, M.1


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