Microtubule-associated protein tau in development, degeneration and protection of neurons

Progress in Neurobiology

Volumn 85, Issue 2, 2008, Pages 148-175

  Wang, Jian Zhi ^a   Liu, Fei ^b  

^a HUAZHONG UNIVERSITY OF SCIENCE AND TECHNOLOGY   (China)

^b NANTONG UNIVERSITY   (China)

Author keywords

Microtubule associated protein; Neurodegeneration; Phosphorylation; Tau

Indexed keywords

AMYLOID BETA PROTEIN; MICROTUBULE ASSOCIATED PROTEIN 1; MICROTUBULE ASSOCIATED PROTEIN 2; PHOSPHOPROTEIN PHOSPHATASE; PROTEIN KINASE; TAU PROTEIN; WNT PROTEIN;

ALZHEIMER DISEASE; APOPTOSIS; CELL VIABILITY; COGNITIVE DEFECT; DNA POLYMORPHISM; EXON; GENE EXPRESSION; GENE MUTATION; GLYCOSYLATION; HUMAN; MICROTUBULE ASSEMBLY; NERVE CELL DIFFERENTIATION; NERVE DEGENERATION; NEUROFIBRILLARY TANGLE; NEUROPROTECTION; NITRATION; NONHUMAN; OXIDATIVE STRESS; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN PHOSPHORYLATION; PROTEIN PROCESSING; REVIEW; RNA SPLICING; SIGNAL TRANSDUCTION; TAUOPATHY; UBIQUITINATION;

ANIMALS; HUMANS; MICROTUBULES; NEURODEGENERATIVE DISEASES; NEURONS; TAU PROTEINS;

EID: 43249124363     PISSN: 03010082     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pneurobio.2008.03.002     Document Type: Review

References (404)

1. Ackmann M., Wiech H., and Mandelkow E. Nonsaturable binding indicates clustering of tau on the microtubule surface in a paired helical filament-like conformation. J. Biol. Chem. 275 (2000) 30335-30343
2. Alafuzoff I., Iqbal K., Friden H., Adolfsson R., and Winblad B. Histopathological criteria for progressive dementia disorders: clinical-pathological correlation and classification by multivariate data analysis. Acta Neuropathol. 74 (1987) 209-225
3. Al-Bassam J., Ozer R.S., Safer D., Halpain S., and Milligan R.A. MAP2 and tau bind longitudinally along the outer ridges of microtubule protofilaments. J. Cell Biol. 157 (2002) 1187-1196
4. Allen B., Ingram E., Takao M., Smith M.J., Jakes R., Virdee K., Yoshida H., Holzer M., Craxton M., Emson P.C., Atzori C., Migheli A., Crowther R.A., Ghetti B., Spillantini M.G., and Goedert M. Abundant tau filaments and nonapoptotic neurodegeneration in transgenic mice expressing human P301S tau protein. J. Neurosci. 22 (2002) 9340-9351
5. Alonso A.C., Zaidi T., Grundke-Iqbal I., and Iqbal K. Role of abnormally phosphorylated tau in the breakdown of microtubules in Alzheimer disease. Proc. Natl. Acad. Sci. U.S.A. 91 (1994) 5562-5566
6. Alonso A.C., Grundke-Iqbal I., and Iqbal K. Alzheimer's disease hyperphosphorylated tau sequesters normal tau into tangles of filaments and disassembles microtubules. Nat. Med. 2 (1996) 783-787
7. Alonso A.C., Grundke-Iqbal I., Barra H.S., and Iqbal K. Abnormal phosphorylation of tau and the mechanism of Alzheimer neurofibrillary degeneration: sequestration of microtubule-associated proteins 1 and 2 and the disassembly of microtubules by the abnormal tau. Proc. Natl. Acad. Sci. U.S.A. 94 (1997) 298-303
8. Alonso A.C., Zaidi T., Novak M., Barra H.S., Grundke-Iqbal I., and Iqbal K. Interaction of tau isoforms with Alzheimer's disease abnormally hyperphosphorylated tau and in vitro phosphorylation into the disease-like protein. J. Biol. Chem. 276 (2001) 37967-37973
9. Alonso A.C., Zaidi T., Novak M., Grundke-Iqbal I., and Iqbal K. Hyperphosphorylation induces self-assembly of tau into tangles of paired helical filaments/straight filaments. Proc. Natl. Acad. Sci. U.S.A. 98 (2001) 6923-6928
10. Alonso A.C., Mederlyova A., Novak M., Grundke-Iqbal I., and Iqbal K. Promotion of hyperphosphorylation by frontotemporal dementia tau mutations. J. Biol. Chem. 279 (2004) 34873-34881
11. Alonso A.C., Li B., Grundke-Iqbal I., and Iqbal K. Polymerization of hyperphosphorylated tau into filaments eliminates its inhibitory activity. Proc. Natl. Acad. Sci. U.S.A. 103 (2006) 8864-8869
12. Amadoro G., Serafino A.L., Barbato C., Ciotti M.T., Sacco A., Calissano P., and Canu N. Role of N-terminal tau domain integrity on the survival of cerebellar granule neurons. Cell Death Differ. 11 (2004) 217-230
13. Andorfer C., Kress Y., Espinoza M., de Silva R., Tucker K.L., Barde Y.A., Duff K., and Davies P. Hyperphosphorylation and aggregation of tau in mice expressing normal human tau isoforms. J. Neurochem. 86 (2003) 582-590
14. Andorfer C., Acker C.M., Kress Y., Hof P.R., Duff K., and Davies P. Cell-cycle reentry and cell death in transgenic mice expressing nonmutant human tau isoforms. J. Neurosci. 25 (2005) 5446-5454
15. Andreadis A., Broderick J.A., and Kosik K.S. Relative exon affinities and suboptimal splice site signals lead to non-equivalence of two cassette exons. Nucleic Acids Res. 23 (1995) 3585-3593
16. Andreadis A. Tau gene alternative splicing: expression patterns, regulation and modulation of function in normal brain and neurodegenerative diseases. Biochim. Biophys. Acta 1739 (2005) 91-103
17. Arnold C.S., Johnson G.V., Cole R.N., Dong D.L., Lee M., and Hart G.W. The microtubule-associated protein tau is extensively modified with O-linked N-acetylglucosamine. J. Biol. Chem. 271 (1996) 28741-28744
18. Arai H., Ishiguro K., Ohno H., Moriyama M., Itoh N., Okamura N., Matsui T., Morikawa Y., Horikawa E., Kohno H., Sasaki H., and Imahori K. CSF phosphorylated tau protein and mild cognitive impairment: a prospective study. Exp. Neurol. 166 (2000) 201-203
19. Arrasate M., Pérez M., Armas-Portela R., and Avila J. Polymerization of tau peptides into fibrillar structures. The effect of FTDP-17 mutations. FEBS Lett. 446 (1999) 199-202
20. Arrasate M., Pérez M., Valpuesta J.M., and Avila J. Role of glycosaminoglycans in determining the helicity of paired helical filaments. Am. J. Pathol. 151 (1997) 1115-1122
21. Arrasate M., Pérez M., and Avila J. Tau dephosphorylation at tau-1 site correlates with its association to cell membrane. Neurochem. Res. 25 (2000) 43-50
22. Arendt T., Stieler J., Strijkstra A.M., Hut R.A., Rudiger J., Van der Zee E.A., Harkany T., Holzer M., and Hartig W. Reversible paired helical filament-like phosphorylation of tau is an adaptive process associated with neuronal plasticity in hibernating animals. J. Neurosci. 23 (2003) 6972-6981
23. Arrigada P.A., Growdon J.H., Hedley-White E.T., and Hyman B.T. Neurofibrillary tangles but not senile plaques parallel duration and severity of Alzheimer's disease. Neurology 42 (1992) 631-639
24. Avila J., Lucas J.J., Perez M., and Hernandez F. Role of tau protein in both physiological and pathological conditions. Physiol. Rev. 54 (2004) 361-384
25. Avila J., Santa-María I., Pérez M., Hernández F., and Moreno F. Tau phosphorylation, aggregation, and cell toxicity. J. Biomed. Biotechnol. 2006 (2006) 74539
26. Baas P.W., Pienkowski T.P., Cimbalnik K.A., Toyama K., Bakalis S., Ahmad F.J., and Kosik K.S. Tau confers drug stability but not cold stability to microtubules in living cells. J. Cell Sci. 107 (1994) 135-143
27. Bancher C., Brunner C., Lassmann H., Budka H., Jellinger K., Wiche G., Seitelberger F., Grundke-Iqbal I., Iqbal K., and Wisniewski H.M. Accumulation of abnormally phosphorylated tau precedes the formation of neurofibrillary tangles in Alzheimer's disease. Brain Res. 477 (1989) 90-99
28. Bandyopadhyay B., Li G., Yin H., and Kuret J. Tau aggregation and toxicity in a cell culture model of tauopathy. J. Biol. Chem. 282 (2007) 16454-16464
29. Bhat R.V., Budd Haeberlein S.L., and Avila J. Glycogen synthase kinase 3: a drug target for CNS therapies. J. Neurochem. 89 (2004) 1313-1317
30. Blard O., Frebourg T., Campion D., and Lecourtois M. Inhibition of proteasome and Shaggy/glycogen synthase kinase-3beta kinase prevents clearance of phosphorylated tau in Drosophila. J. Neurosci. Res. 84 (2006) 1107-1115
31. Blennow K., Wallin A., Ågren H., Spenger C., Siegfried J., and Vanmechelen E. Tau protein in cerebrospinal fluid: a biochemical marker for axonal degeneration in Alzheimer disease?. Mol. Chem. Neuropathol. 26 (1995) 231-245
32. Blennow K., and Hampel H. CSF markers for incipient Alzheimer's disease. Lancet Neurol. 2 (2003) 605-613
33. Boekhoorn K., Terwel D., Biemans B., Borghgraef P., Wiegert O., Ramakers G.J., de Vos K., Krugers H., Tomiyama T., Mori H., Joels M., van Leuven F., and Lucassen P.J. Improved long-term potentiation and memory in young tau-P301L transgenic mice before onset of hyperphosphorylation and tauopathy. J. Neurosci. 26 (2006) 3514-3523
34. Braak H., and Braak E. Neuropathological stageing of Alzheimer-related changes. Acta Neuropathol. 82 (1991) 239-259
35. Braak E., Braak H., and Mandelkow E.M. A sequence of cytoskeleton changesrelated to the formation of neurofibrillary tangles and neuropil threads. Acta Neuropathol. (Berl.) 87 (1994) 554-567
36. Braak H., and Braak E. Evolution of the neuropathology of Alzheimer's disease. Acta Neurol. Scand. Suppl. 165 (1996) 3-12
37. Brady R.M., Zinkowski R.P., and Binder L.I. Presence of tau in isolated nuclei from human brain. Neurobiol. Aging 16 (1995) 479-486
38. Brion J.P., Tremp G., and 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. 154 (1999) 255-270
39. Brich J., Shie F.S., Howell B.W., Li R., Tus K., Wakeland E.K., Jin L.W., Mumby M., Churchill G., Herz J., and Cooper J.A. Genetic modulation of tau phosphorylation in the mouse. J. Neurosci. 23 (2003) 187-192
40. Broderick J., Wang J., and Andreadis A. Heterogeneous nuclear ribonucleoprotein E2 binds to tau exon 10 and moderately activates its splicing. Gene 331 (2004) 107-114
41. Buee L., Bussiere T., Buee-Scherrer V., Delacourte A., and Hof P.R. Tau protein isoforms, phosphorylation and role in neurodegenerative diseases. Brain Res. Rev. 33 (2000) 95-130
42. Buerger K., Teipel S.J., Zinkowski R., Blennow K., Arai H., Engel R., Hofmann-Kiefer K., McCulloch C., Ptok U., Heun R., Andreasen N., DeBernardis J., Kerkman D., Moeller H., Davies P., and Hampel H. CSF tau protein phosphorylated at threonine 231 correlates with cognitive decline in MCI subjects. Neurology 59 (2002) 627-629
43. Buerger K., Zinkowski R., Teipel S.J., Tapiola T., Arai H., Blennow K., Andreasen N., Hofmann-Kiefer K., DeBernardis J., Kerkman D., McCulloch C., Kohnken R., Padberg F., Pirttila T., Schapiro M.B., Rapoport S.I., Moller H.J., Davies P., and Hampel H. Differential diagnosis of Alzheimer disease with cerebrospinal fluid levels of tau protein phosphorylated at threonine 231. Arch. Neurol. 59 (2002) 1267-1272
44. Buerger K., Ewers M., Pirttilä T., Zinkowski R., Alafuzoff I., Teipel S.J., DeBernardis J., Kerkman D., McCulloch C., Soininen H., and Hampel H. CSF phosphorylated tau protein correlates with neocortical neurofibrillary pathology in Alzheimer's disease. Brain 129 (2006) 3035-3041
45. Bugiani O., Murrell J.R., Giaccone G., Hasegawa M., Ghigo G., Tabaton M., Morbin M., Primavera A., Carella F., Solaro C., Grisoli M., Savoiardo M., Spillantini M.G., Tagliavini F., Goedert M., and Ghetti B. Frontotemporal dementia and corticobasal degeneration in a family with a P301S mutation in tau. J. Neuropathol. Exp. Neurol. 58 (1999) 667-677
46. Bullmann T., de Silva R., Holzer M., Mori H., and Arendt T. Expression of embryonic tau protein isoforms persist during adult neurogenesis in the hippocampus. Hippocampus 17 (2007) 98-102
47. Bunker J.M., Kamath K., Wilson L., Jordan M.A., and Feinstein S.C. FTDP-17 mutations compromise the ability of tau to regulate microtubule dynamics in cells. J. Biol. Chem. 281 (2006) 11856-11863
48. Cai Q., Pan P.Y., and Sheng Z.H. Syntabulin-kinesin-1 family member 5B-mediated axonal transport contributes to activity-dependent presynaptic assembly. J. Neurosci. 27 (2007) 7284-7296
49. Caceres A., and Kosik K.S. Inhibition of neurite polarity by tau antisense oligonucleotides in primary cerebellar neurons. Nature 343 (1990) 461-463
50. Calingasan N.Y., Uchida K., and Gibson G.E. Protein-bound acrolein: a novel marker of oxidative stress in Alzheimer's disease. J. Neurochem. 72 (1999) 751-756
51. Caricasole A., Copani A., Caraci F., Aronica E., Rozemuller A.J., Caruso A., Storto M., Gaviraghi G., Terstappen G.C., and Nicoletti F. Induction of Dickkopf-1, a negative modulator of the Wnt pathway, is associated with neuronal degeneration in Alzheimer's brain. J. Neurosci. 24 (2004) 6021-6027
52. Cash A.D., Aliev G., Siedlak S.L., Nunomura A., Fujioka H., Zhu X., Raina A.K., Vinters H.V., Tabaton M., Johnson A.B., Paula-Barbosa M., Avila J., Jones P.K., Castellani R.J., Smith M.A., and Perry G. Microtubule reduction in Alzheimer's disease and aging is independent of tau filament formation. Am. J. Pathol. 162 (2003) 1623-1627
53. Castegna A., Thongboonkerd V., Klein J.B., Lynn B., Markesbery W.R., and Butterfield D.A. Proteomic identification of nitrated proteins in Alzheimer's disease brain. J. Neurochem. 85 (2003) 1394-1401
54. Castellani R.J., Harris P.L., Sayre L.M., Fujii J., Taniguchi N., Vitek M.P., Founds H., Atwood C.S., Perry G., and Smith M.A. Active glycation in neurofibrillary pathology of Alzheimer disease: N(epsilon)-(carboxymethyl) lysine and hexitol-lysine. Free Radic. Biol. Med. 31 (2001) 175-180
55. Castellani R.J., Lee H.G., Zhu X., Nunomura A., Perry G., and Smith M.A. Neuropathology of Alzheimer disease: pathognomonic but not pathogenic. Acta Neuropathol. 111 (2006) 503-509
56. Chau K.W., Chan W.Y., Shaw P.C., and Chan H.Y. Biochemical investigation of tau protein phosphorylation status and its solubility properties in Drosophila. Biochem. Biophys. Res. Commun. 346 (2006) 150-159
57. Chen J., Kanai Y., Cowan N.J., and Hirokawa N. Projection domains of MAP2 and tau determine spacings between microtubules in dendrites and axons. Nature 360 (1992) 674-677
58. Chen Y.G. Specific tau phosphorylation sites in hippocampus correlate with impairment of step-down inhibitory avoidance task in rats. Behav. Brain Res. 158 (2005) 277-284
59. Chin S.S., and Goldman J.E. Glial inclusions in CNS degenerative diseases. J. Neuropathol. Exp. Neurol. 55 (1996) 499-508
60. Cho J.H., and Johnson G.V. Glycogen synthase kinase 3beta phosphorylates tau at both primed and unprimed sites. Differential impact on microtubule binding. J. Biol. Chem. 278 (2003) 187-193
61. Cho J.H., and Johnson G.V. Glycogen synthase kinase 3 beta induces caspase-cleaved tau aggregation in situ. J. Biol. Chem. 279 (2004) 54716-54723
62. Cho J.H., and Johnson G.V. Primed phosphorylation of tau at Thr231 by glycogen synthase kinase 3β (GSK-3β) plays a critical role in regulating tau's ability to bind and stabilize microtubules. J. Neurochem. 88 (2004) 349-358
63. Cho U.S., and Xu W. Crystal structure of a protein phosphatase 2A heterotrimeric holoenzyme. Nature 445 (2007) 53-57
64. Chun W., and Johnson G.V. Activation of glycogen synthase kinase 3β promotes the intermolecular association of tau. The use of fluorescence resonance energy transfer microscopy. J. Biol. Chem. 282 (2007) 23410-23417
65. Chung C.W., Song Y.H., Kim I.K., Yoon W.J., Ryu B.R., Jo D.G., Woo H.N., Kwon Y.K., Kim H.H., Gwag B.J., Mook-Jung I.H., and Jung Y.K. Proapoptotic effects of tau cleavage product generated by caspase-3. Neurobiol. Dis. 8 (2001) 162-172
66. Churcher I. Tau therapeutic strategies for the treatment of Alzheimer's disease. Curr. Top. Med. Chem. 6 (2006) 579-595
67. Cleveland D.W., Hwo S.Y., and Kirschner M.W. Physical and chemical properties of purified tau factor and the role of tau in microtubule assembly. J. Mol. Biol. 116 (1977) 227-247
68. Clodfelder-Miller B.J., Zmijewska A.A., Johnson G.V., and Jope R.S. Tau is hyperphosphorylated at multiple sites in mouse brain in vivo after streptozotocin-induced insulin deficiency. Diabetes 55 (2006) 3320-3325
69. Coleman P.D., and Yao P.J. Synaptic slaughter in Alzheimer's disease. Neurobiol. Aging 24 (2003) 1023-1027
70. Conrad C., Vianna C., Freeman M., and Davies P. A polymorphic gene nested within an intron of the tau gene: implications for Alzheimer's disease. Proc. Natl. Acad. Sci. U.S.A. 99 (2002) 7751-7756
71. Cripps D., Thomas S., Jeng Y., Yang F., Davies P., and Yang A. Alzheimer disease-specific conformation of hyperphosphorylated paired helical filament-tau is polyubiquitinated through Lys-48, Lys-11, and Lys-6 ubiquitin conjugation. J. Biol. Chem. 281 (2006) 10825-10838
72. David D.C., Layfield R., Serpell L., Narain Y., Goedert M., and Spillantini M.G. Proteasomal degradation of tau protein. J. Neurochem. 83 (2002) 176-185
73. Davis D.R., Anderton B.H., Brion J.P., Reynolds C.H., and Hanger D.P. Oxidative stress induces dephosphorylation of tau in rat brain primary neuronal cultures. J. Neurochem. 68 (1997) 1590-1597
74. Dawson H.N., Ferreira A., Eyster M.V., Ghoshal N., Binder L.I., and Vitek M.P. Inhibition of neuronal maturation in primary hippocampal neurons from tau deficient mice. J. Cell Sci. 114 (2001) 1179-1187
75. Dayanandan R., Van Slegtenhorst M., Mack T.G., Ko L., Yen S.H., Leroy K., Brion J.P., Anderton B.H., Hutton M., and Lovestone S. Mutations in tau reduce its microtubule binding properties in intact cells and affect its phosphorylation. FEBS Lett. 446 (1999) 228-232
76. Delisle M.B., Murrell J.R., Richardson R., Trofatter J.A., Rascol O., Soulages X., Mohr M., Calvas P., and Ghetti B. A mutation at codon 279 (N279K) in exon 10 of the tau gene causes a tauopathy with dementia and supranuclear palsy. Acta Neuropathol. 98 (1999) 62-77
77. Delobel P., Flament S., Hamdane M., Mailliot C., Sambo A.V., Begard S., Sergeant N., Delacourte A., Vilain J.P., and Buee L. Abnormal Tau phosphorylation of the Alzheimer-type also occurs during mitosis. J. Neurochem. 83 (2002) 412-420
78. Deng Y.Q., Xu G.G., Duan P., Zhang Q., and Wang J.Z. Effects of melatonin on wortmannin-induced tau hyperphosphorylation. Acta Pharmacol. Sin. 6 (2005) 519-526
79. De Sarno P., Bijur G.N., Zmijewska A.A., Li X., and Jope R.S. In vivo regulation of GSK3 phosphorylation by cholinergic and NMDA receptors. Neurobiol. Aging 27 (2006) 413-422
80. De Vrij F.M.S., Fischer D.F., van Leeuwen F.W., and Hol E.M. Protein quality control in Alzheimer's disease by the ubiquitin proteasome system. Prog. Neurobiol. 74 (2004) 249-270
81. Dickey C.A., Yue M., Lin W.L., Dickson D.W., Dunmore J.H., Lee W.C., Zehr C., West G., Cao S., Clark A.M., Caldwell G.A., Caldwell K.A., Eckman C., Patterson C., Hutton M., and Petrucelli L. Deletion of the ubiquitin ligase CHIP leads to the accumulation, but not the aggregation, of both endogenous phospho- and caspase-3-cleaved tau species. J. Neurosci. 26 (2006) 6985-6996
82. Di Maria E., Tabaton M., Vigo T., Abbruzzese G., Bellone E., Donati C., Frasson E., Marchese R., Montagna P., Munoz D.G., Pramstaller P.P., Zanusso G., Ajmar F., and Mandich P. Corticobasal degeneration shares a common genetic background with progressive supranuclear palsy. Ann. Neurol. 47 (2000) 374-377
83. Donahue C.P., Muratore C., Wu J.Y., Kosik K.S., and Wolfe M.S. Stabilization of the tau exon 10 stem loop alters pre-mRNA splicing. J. Biol. Chem. 281 (2006) 23302-23306
84. Donahue C.P., Ni J., Rozners E., Glicksman M.A., and Wolfe M.S. Identification of tau stem loop RNA stabilizers. J. Biomol. Screen. 12 (2007) 789-799
85. Dotti C.G., Banker G.A., and Binder L.I. The expression and distribution of the microtubule-associated proteins tau and microtubule-associated protein 2 in hippocampal neurons in the rat in situ and in cell culture. Neuroscience 23 (1987) 121-130
86. Drewes G., Trinczek B., Illenberger S., Biernat J., Schmitt-Ulms G., Meyer H.E., Mandelkow E.M., and 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. 270 (1995) 7679-7688
87. D'Souza I., and Schellenberg G.D. Determinants of 4-repeat tau expression. Coordination between enhancing and inhibitory splicing sequences for exon 10 inclusion. J. Biol. Chem. 275 (2000) 17700-17709
88. D'Souza I., and Schellenberg G.D. Tau Exon 10 expression involves a bipartite intron 10 regulatory sequence and weak 5′ and 3′ splice sites. J. Biol. Chem. 277 (2002) 26587-26599
89. D'Souza I., and Schellenberg G.D. Regulation of tau isoform expression and dementia. Biochim. Biophys. Acta 1739 (2005) 104-115
90. Duchowicz P.R., and Castro E.A. QSAR studies for the pharmacological inhibition of glycogen synthase kinase-3. Med. Chem. 3 (2007) 393-417
91. Duff K., and Planel E. Untangling memory deficits. Nat. Med. 11 (2005) 826-827
92. Ebneth A., Godemann R., Stamer K., Illenberger S., Trinczek B., and Mandelkow E. Overexpression of tau protein inhibits kinesin-dependent trafficking of vesicles, mitochondria and endoplasmic reticulum: implications for Alzheimer's disease. J. Cell Biol. 143 (1998) 777-794
93. Ekinci F.J., and Shea T.B. Phosphorylation of tau alters its association with the plasma membrane. Cell Mol. Neurobiol. 20 (2000) 497-508
94. Eldar-Finkelman H. Glycogen synthase kinase 3: an emerging therapeutic target. Trends Mol. Med. 8 (2002) 126-132
95. Elder G.A., Friedrich Jr. V.L., Bosco P., Kang C., Gourov A., Tu P.H., Lee V.M., and Lazzarini R.A. Absence of the mid-sized neurofilament subunit decreases axonal calibers, levels of light neurofilament (NF-L), and neurofilament content. J. Cell Biol. 141 (1998) 727-739
96. Engel T., Lucas J.J., Gomez-Ramos P., Moran M.A., Avila J., and Hernandez F. Cooexpression of FTDP-17 tau and GSK-3beta in transgenic mice induce tau polymerization and neurodegeneration. Neurobiol. Aging 27 (2006) 1258-1268
97. Evans D.B., Rank K.B., Bhattacharya K., Thomsen D.R., Gurney M.E., and Sharma S.K. Tau phosphorylation at serine 396 and serine 404 by human recombinant tau protein kinase II inhibits tau's ability to promote microtubule assembly. J. Biol. Chem. 275 (2000) 24977-24983
98. Fath T., Eidenmuller J., and Brandt R. Tau-mediated cytotoxicity in a pseudohyperphosphorylation model of Alzheimer's disease. J. Neurosci. 22 (2002) 9733-9741
99. Feijoo C., Campbell D.G., Jakes R., Goedert M., and Cuenda A. Evidence that phosphorylation of the microtubule-associated protein Tau by SAPK4/p38delta at Thr50 promotes microtubule assembly. J. Cell Sci. 118 (2005) 397-408
100. Feinstein S.C., and 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 1739 (2005) 268-279
101. Fellous A., Francon J., Lennon A.M., and Nunez J. Microtubule assembly in vitro. Purification of assembly-promoting factors. Eur. J. Biochem. 78 (1977) 167-174
102. Forman M.S., Lal D., Zhang B., Dabir D.V., Swanson E., Lee V.M., and Trojanowski J.Q. Transgenic mouse model of tau pathology in astrocytes leading to nervous system degeneration. J. Neurosci. 25 (2005) 3539-3550
103. Gao Q.S., Memmott J., Lafyatis R., Stamm S., Screaton G., and Andreadis A. Complex regulation of tau exon 10, whose missplicing causes frontotemporal dementia. J. Neurochem. 74 (2000) 490-500
104. Gamblin T.C., Chen F., Zambrano A., Abraha A., Lagalwar S., Guillozet A.L., Lu M., Fu Y., Garcia-Sierra F., LaPointe N., Miller R., Berry R.W., Binder L.I., and Cryns V.L. Caspase cleavage of tau: linking amyloid and neurofibrillary tangles in Alzheimer's disease. Proc. Natl. Acad. Sci. U.S.A. 100 (2003) 10032-10037
105. Goedert M., Spillantini M.G., Jakes R., Rutherford D., and Crowther R.A. Multiple isoforms of human microtubule-associated protein tau: sequences and localization in neurofibrillary tangles of Alzheimer's disease. Neuron 3 (1989) 519-526
106. Goedert M., Spillantini M.G., Potier M.C., Ulrich J., and Crowther R.A. Cloning and sequencing of the cDNA encoding an isoform of microtubule-associated protein tau containing four tandem repeats: differential expression of tau protein mRNAs in human brain. EMBO J. 8 (1989) 393-399
107. Goedert M., and Jakes R. Expression of separate isoforms of human tau protein: correlation with the tau pattern in brain and effects on tubulin polymerization. EMBO J. 9 (1990) 4225-4230
108. Goedert M., Spillantini M.G., Cairns N.J., and Crowther R.A. Tau proteins of Alzheimer paired helical filaments: abnormal phosphorylation of all six brain isoforms. Neuron 8 (1992) 159-168
109. Goedert M., Jakes R., Crowther R.A., Six J., Lubke U., Vandermeeren M., Cras P., Trojanowski J.Q., and Lee V.M.Y. The abnormal phosphoryla-tion of tau protein at Ser-202 in Alzheimer disease recapitulates phos-phorylation during development. Proc. Natl. Acad. Sci. U.S.A. 90 (1993) 5066-5070
110. Goedert M., Hasegawa M., Jakes R., Lawler S., Cuenda A., and Cohen P. Phosphorylation of microtubule-associated protein tau by stress activated protein kinases. FEBS Lett. 409 (1997) 57-66
111. Goedert M., and Spillantini M.G. Tau mutations in frontotemporal dementia FTDP-17 and their relevance for Alzheimer's disease. Biochim. Biophys. Acta 1502 (2000) 110-121
112. Goldbaum O., Oppermann M., Handschuh M., Dabir D., Zhang B., Forman M.S., Trojanowski J.Q., Lee V.M., and Richter-Landsberg C. Proteasome inhibition stabilizes Tau inclusions in oligodendroglial cells that occur after treatment with okadaic acid. J. Neurosci. 23 (2003) 8872-8880
113. Goldbaum O., and Richter-Landsberg C. Proteolytic stress causes heat shock protein induction, tau ubiquitination, and the recruitment of ubiquitin to tau-positive aggregates in oligodendrocytes in culture. J. Neurosci. 24 (2004) 5748-5757
114. Goldberg D.J., and Wu D.Y. Tyrosine phosphorylation and protrusive structures of the growth cone. Perspect. Dev. Neurobiol. 4 (1996) 183-192
115. Gomez-Ramos A., Diaz-Nido J., Smith M.A., Perry G., and Avila J. Effect of the lipid peroxidation product acrolein on tau phosphorylation in neural cells. J. Neurosci. Res. 71 (2003) 863-870
116. Gomez-Ramos A., Dominguez J., Zafra D., Corominola H., Gomis R., Guinovart J.J., and Avila J. Sodium tungstate decreases the phosphorylation of tau through GSK3 inactivation. J. Neurosci. Res. 83 (2006) 264-273
117. Gong C.X., Singh T.J., Grundke-Iqbal I., and Iqbal K. Phosphoprotein phosphatase activities in Alzheimer disease brain. J. Neurochem. 61 (1993) 921-927
118. Gong C.X., Shaikh S., Wang J.Z., Zaidi T., Grundke-Iqbal I., and Iqbal K. Phosphatase activity toward abnormally phosphorylated tau: decrease in Alzheimer disease brain. J. Neurochem. 65 (1995) 732-738
119. Gong C.X., Lidsky T., Wegiel J., Zuck L., Grundke-Iqbal I., and Iqbal K. Phosphorylation of microtubule-associated protein tau is regulated by protein phosphatase 2A in mammalian brain. Implications for neurofibrillary degeneration in Alzheimer's disease. J. Biol. Chem. 275 (2000) 5535-5544
120. Gong C.X., Liu F., Wu G., Rossie S., Wegiel J., Li L., Grundke-Iqbal I., and Iqbal K. Dephosphorylation of microtubule-associated protein tau by protein phosphatase 5. J. Neurochem. 88 (2004) 298-310
121. Gong C.X., Liu F., Grundke-Iqbal I., and Iqbal K. Post-translational modifications of tau protein in Alzheimer's disease. J. Neural Transm. 112 (2005) 813-838
122. Gong C.X., Liu F., Grundke-Iqbal I., and Iqbal K. Impaired brain glucose metabolism leads to Alzheimer neurofibrillary degeneration through a decrease in tau O-GlcNAcylation. J. Alzheimers Dis. 9 (2006) 1-12
123. Good P.F., Werner P., Hsu A., Olanow C.W., and Perl D.P. Evidence of neuronal oxidative damage in Alzheimer's disease. Am. J. Pathol. 149 (1996) 21-28
124. Goode B.L., and Feinstein S.C. Identification of a novel microtubule binding and assembly domain in the developmentally regulated inter-repeat region of tau. J. Cell Biol. 124 (1994) 769-782
125. Goode B.L., Denis P.E., Panda D., Radeke M.J., Miller H.P., Wilson L., and Feinstein S.C. Functional interactions between the prolinerich and repeat regions of tau enhance microtubule binding and assembly. Mol. Biol. Cell 8 (1997) 353-365
126. Gould T.D., and Manji H.K. Glycogen synthase kinase-3: a putative molecular target for lithium mimetic drugs. Neuropsychopharmacology 30 (2005) 1223-1237
127. Götz J., Probst A., Spillantini M.G., Schäfer T., Jakes R., Bürki K., and Goedert M. Somatodendritic localization and hyperphosphorylation of tau protein in transgenic mice expressing the longest human brain tau isoform. EMBO J. 14 (1995) 1304-1313
128. Götz J., Chen F., Barmettler R., and Nitsch R.M. Tau filament formation in transgenic mice expressing P301L tau. J. Biol. Chem. 276 (2001) 529-534
129. Götz J., Tolnay M., Barmettler R., Chen F., Probst A., and Nitsch R.M. Oligodendroglial tau filament formation in transgenic mice expressing G272V tau. Eur. J. Neurosci. 13 (2001) 2131-2140
130. Götz J., Deters N., Doldissen A., Bokhari L., Ke Y., Wiesner A., Schonrock N., and Ittner L.M. A decade of tau transgenic animal models and beyond. Brain Pathol. 17 (2007) 91-103
131. Greenberg S.G., Davies P., Schein J.D., and Binder L.I. Hydrofluoric acid-treated tau PHF proteins display the same biochemical properties as normal tau. J. Biol. Chem. 267 (1992) 564-569
132. Greenwood I.A., Helliwell R.M., and Large W.A. Modulation of Ca(2+)-activated Cl- currents in rabbit portal vein smooth muscle by an inhibitor of mitochondrial Ca2+ uptake. J. Physiol. 505 (1997) 53-64
133. Grover A., Houlden H., Baker M., Adamson J., Lewis J., Prihar G., Pickering-Brown S., Duff K., and Hutton M. 5′ splice site mutations in tau associated with the inherited dementia FTDP-17 affect a stem-loop structure that regulates alternative splicing of exon 10. J. Biol. Chem. 274 (1999) 5134-15143
134. Grundke-Iqbal I., Iqbal K., Tung Y.C., and Wisniewski H.M. Alzheimer paired helical filaments: immunochemical identification of polypeptides. Acta Neuropathol. (Berl.) 62 (1984) 259-267
135. Grundke-Iqbal I., Iqbal K., Quinlan M., Tung Y.C., Zaidi M.S., and Wisniewski H.M. Microtubule-associated protein tau: a component of Alzheimer paired helical filaments. J. Biol. Chem. 261 (1986) 6084-6089
136. Grundke-Iqbal I., Iqbal K., Tung Y.C., Quinlan M., Wisniewski H.M., and Binder L.U. Abnormal phosphorylation of the microtubule-associated protein tau (tau) in Alzheimer cytoskeletal pathology. Proc. Natl. Acad. Sci. U.S.A. 83 (1986) 4913-4917
137. Guillozet-Bongaarts A.L., Garcia-Sierra F., Reynolds M.R., Horowitz P.M., Fu Y.F., Wang T.Y., Cahill M.E., Bigio E.H., Berry R.W., and Binder L.I. Tau truncation during neurofibrillary tangle evolution in Alzheimer's disease. Neurobiol. Aging 26 (2005) 1015-1022
138. Guillozet-Bongaarts A.L., Cahill M.E., Cryns V.L., Reynolds M.R., Berry R.W., and Binder L.I. Pseudophosphorylation of tau at serine 422 inhibits caspase cleavage: in vitro evidence and implications for tangle formation in vivo. J. Neurochem. 97 (2006) 1005-1014
139. Guo H., Albrecht S., Bourdeau M., Petzke T., Bergeron C., and LeBlanc A.C. Active caspase-6 and caspase-6-cleaved tau in neuropil threads, neuritic plaques, and neurofibrillary tangles of Alzheimer's disease. Am. J. Pathol. 165 (2004) 523-531
140. Hampel H., Buerger K., Zinkowski R., Teipel S.J., Goernitz A., Andreasen N., Sjoegren M., DeBernardis J., Kerkman D., Ishiguro K., Ohno H., Vanmechelen E., Vanderstichele H., McCulloch C., Moller H.J., Davies P., and Blennow K. Measurement of phosphorylated tau epitopes in the differential diagnosis of Alzheimer disease: a comparative cerebrospinal fluid study. Arch. Gen. Psychiatry 61 (2004) 95-102
141. Hampel H., Burger K., Pruessner J.C., Zinkowski R., DeBernardis J., Kerkman D., Leinsinger G., Evans A.C., Davies P., Moller H.J., and Teipel S.J. Correlation of cerebrospinal fluid levels of tau protein phosphorylated at threonine 231 with rates of hippocampal atrophy in Alzheimer disease. Arch. Neurol. 62 (2005) 770-773
142. Hanger D.P., Betts J.C., Loviny T.L., Blackstock W.P., and 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. 71 (1998) 2465-2476
143. Hanger D.P., Byers H.L., Wray S., Leung K.Y., Saxton M.J., Seereeram A., Reynolds C.H., Ward M.A., and Anderton B.H. Novel phosphorylation sites in tau from Alzheimer brain support a role for casein kinase 1 in disease pathogenesis. J. Biol. Chem. 282 (2007) 23645-23654
144. Hansson O., Zetterberg H., Buchhave P., Londos E., Blennow K., and Minthon L. Association between CSF biomarkers and incipient Alzheimer's disease in patients with mild cognitive impairment: a follow-up study. Lancet Neurol. 5 (2006) 228-234
145. Harada A., Oguchi K., Okabe S., Kuno J., Terada S., Ohshima T., Sato-Yoshitake R., Takei Y., Noda T., and Hirokawa N. Altered microtubule organization in small-calibre axons of mice lacking tau protein. Nature 369 (1994) 488-491
146. Hardy J. Has the amyloid cascade hypothesis for Alzheimer's disease been proved?. Curr. Alzheimer Res. 3 (2006) 71-73
147. Hartmann A.M., Rujescu D., Giannakouros T., Nikolakaki E., Goedert M., Mandelkow E.M., Gao Q.S., Andreadis A., and Stamm S. Regulation of alternative splicing of human tau exon 10 by phosphorylation of splicing factors. Mol. Cell. Neurosci. 18 (2001) 80-90
148. Hasegawa M., Morishima-Kawashima M., Takio K., Suzuki M., Titani K., and Ihara Y. Protein sequence and mass spectrometric analyses of tau in the Alzheimer's disease brain. J. Biol. Chem. 267 (1992) 17047-17054
149. Hasegawa M., Smith M.J., and Goedert M. Tau proteins with FTDP-17 mutations have a reduced ability to promote microtubule assembly. FEBS Lett. 437 (1998) 207-210
150. Helmke S., and Pfenninger K.H. Growth cone enrichment and cytoskeletal association of non-receptor tyrosine kinases. Cell Motil. Cytoskeleton 30 (1995) 194-207
151. Hensley K., Maidt M.L., Yu Z., Sang H., Markesbery W.R., and Floyd R.A. Electrochemical analysis of protein nitrotyrosine and dityrosine in the Alzheimer brain indicates region-specific accumulation. J. Neurosci. 18 (1998) 8126-8132
152. Hernández F., Pérez M., Lucas J.J., Mata A.M., Bhat R., and Avila J. Glycogen synthase kinase-3 plays a crucial role in tau exon 10 splicing and intranuclear distribution of SC35. Implications for Alzheimer's disease. J. Biol. Chem. 279 (2004) 3801-3806
153. Heutink P. Untangling tau-related dementia. Hum. Mol. Genet. 9 (2000) 979-986
154. Higuchi M., Ishihara T., Zhang B., Hong M., Andreadis A., Trojanowski J., and Lee V.M. Transgenic mouse model of tauopathies with glial pathology and nervous system degeneration. Neuron 35 (2002) 433-446
155. Higuchi M., Zhang B., Forman M.S., Yoshiyama Y., Trojanowski J.Q., and Lee V.M.Y. Axonal degeneration induced by targeted expression of mutant human tau in oligodendrocytes of transgenic mice that model glial tauopathies. J. Neurosci. 25 (2005) 9434-9443
156. Himmler A. Structure of the bovine tau gene: alternatively spliced transcripts generate a protein family. Mol. Cell. Biol. 9 (1989) 1389-1396
157. Hirokawa N., Shiomura Y., and Okabe S. Tau proteins: the molecular structure and mode of binding on microtubules. J. Cell Biol. 107 (1988) 1449-1459
158. Hoenicka J., Perez M., PerezTur J., Barabash A., Godoy M., Vidal L., Astarloa R., Avila J., Nygaard T., and deYebenes J.G. The tau gene A0 allele and progressive supranuclear palsy. Neurology 53 (1999) 1219-1225
159. Hogg M., Grujic Z.M., Baker M., Demirci S., Guillozet A.L., Sweet A.P., Herzog L.L., Weintraub S., Mesulam M.M., LaPointe N.E., Gamblin T.C., Berry R.W., Binder L.I., de Silva R., Lees A., Espinoza M., Davies P., Grover A., Sahara N., Ishizawa T., Dickson D., Yen S.H., Hutton M., and Bigio E.H. The L266V tau mutation is associated with frontotemporal dementia and Pick-like 3R and 4R tauopathy. Acta Neuropathol. (Berl.) 106 (2003) 323-336
160. Hong M., Zhukareva V., Vogelsberg-Ragaglia V., Wszolek Z., Reed L., Miller B.I., Geschwind D.H., Bird T.D., McKeel D., Goate A., Morris J.C., Wilhelmsen K.C., Schellenberg G.D., Trojanowski J.Q., and Lee V.M. Mutation-specific functional impairments in distinct tau isoforms of hereditary FTDP-17. Science 282 (1998) 1914-1917
161. Horiguchi T., Uryu K., Giasson B.I., Ischiropoulos H., LightFoot R., Bellmann C., Richter-Landsberg C., Lee V.M., and Trojanowski J.Q. Nitration of tau protein is linked to neurodegeneration in tauopathie. Am. J. Pathol. 163 (2003) 1021-1031
162. Hua Q., and He R.Q. Effect of phosphorylation and aggregation on tau binding to DNA. Protein Pept. Lett. 9 (2002) 249-357
163. Hua Q., He R.Q., Haque N., Qu M.H., del Carmen Alonso A., Grundke-Iqbal I., and Iqbal K. Microtubule associated protein tau binds to double-stranded but not single-stranded DNA. Cell. Mol. Life Sci. 60 (2003) 413-421
164. Hutton M., Lendon C.L., Rizzu P., Baker M., Froelich S., Houlden H., Pickering-Brown S., Chakraverty S., Isaacs A., Grover A., Hackett J., Adamson J., Lincoln S., Dickson D., Davies P., Petersen R.C., Stevens M., de Graaff E., Wauters E., van Baren J., Hillebrand M., Joosse M., Kwon J.M., Nowotny P., Heutink P., Che L.K., Norton J., Morris J.C., Reed L.A., Trojanowski J., Basul H., Lannfelt L., Neystar M., Fahn S., Dark F., Tannenberg T., Dodd P.R., Hayward N., Kwok J.B.J., Schofield P.R., Andreadis A., Snowden J., Craufurd D., Neary D., Owen F., Oostra B.A., Hardy J., Goate A., van Swieten J., Mann D., Timothy L., and Heutink P. Association of missense and 5′ splice site mutations in tau with the inherited dementia FTDP-17. Nature 393 (1998) 702-705
165. Hu Y.Y., He S.S., Wang X., Duan Q.H., Grundke-Iqbal I., Iqbal K., and Wang J.Z. Levels of nonphosphorylated and phosphorylated tau in cerebrospinal fluid of Alzheimer's disease patients: an ultrasensitive bienzyme-substrate-recycle enzyme-linked immunosorbent assay. Am. J. Pathol. 160 (2002) 1269-1278
166. Hu Y.Y., He S.S., Wang X.C., Duan Q.H., Khatoon S., Iqbal K., Grundke-Iqbal I., and Wang J.Z. Elevated levels of phosphorylated neurofilament proteins in cerebrospinal fluid of Alzheimer disease patients. Neurosci. Lett. 320 (2002) 156-160
167. Ignelzi Jr. M.A., Miller D.R., Soriano P., and Maness P.F. Impaired neurite outgrowth of src-minus cerebellar neurons on the cell adhesion molecule L1. Neuron 12 (1994) 873-884
168. Ikeda M., Shoji M., Kawarai T., Kawarabayashi T., Matsubara E., Murakami T., Sasaki A., Tomidokoro Y., Ikarashi Y., Kuribara H., Ishiguro K., Hasegawa M., Yen S.H., Chishti M.A., Harigaya Y., Abe K., Okamoto K., St George-Hyslop P., and Westaway D. Accumulation of filamentous tau in the cerebral cortex of human tau R406W transgenic mice. Am. J. Pathol. 166 (2005) 521-531
169. Iliev A.I., Ganesan S., Bunt G., and Wouters F.S. Removal of pattern-breaking sequences in microtubule binding repeats produces instantaneous tau aggregation and toxicity. J. Biol. Chem. 281 (2006) 37195-371204
170. Illenberger S., Zheng-Fischhofer Q., Preuss U., Stamer K., Baumann K., Trinczek B., Biernat J., Godemann R., Mandelkow E.M., and Mandelkow E. The endogenous and cell cycle-dependent phosphorylation of tau protein in living cells: implications for Alzheimer's disease. Mol. Biol. Cell 9 (1998) 1495-1512
171. Iqbal K., Grundke-Iqbal I., Smith A.J., George L., Tung Y.C., and Zaidi T. Identification and localization of a tau peptide to paired helical filaments of Alzheimer disease. Proc. Natl. Acad. Sci. U.S.A. 86 (1989) 5646-5650
172. Iqbal K., Flory M., Khatoon S., Soininen H., Pirttila T., Lehtovirta M., Alafuzoff I., Blennow K., Andreasen N., Vanmechelen E., and Grundke-Iqbal I. Subgroups of Alzheimer's disease based on cerebrospinal fluid molecular markers. Ann. Neurol. 5 (2005) 748-757
173. Iqbal K., and Grundke-Iqbal I. Developing pharmacological therapies for Alzheimer disease. Cell. Mol. Life Sci. 64 (2007) 2234-2244
174. Iseki E., Yamamoto R., Murayama N., Minegishi M., Togo T., Katsuse O., Kosaka K., Akiyama H., Tsuchiya K., de Silva R., Andrew L., and Arai H. Immunohistochemical investigation of neurofibrillary tangles and their tau isoforms in brains of limbic neurofibrillary tangle dementia. Neurosci. Lett. 405 (2006) 29-33
175. Ishiguro K., Ohno H., Arai H., Yamaguchi H., Urakami K., Park J.M., Sato K., Kohno H., and Imahori K. Phosphorylated tau in human cerebrospinal fluid is a diagnostic marker for Alzheimer's disease. Neurosci. Lett. 270 (1999) 91-94
176. Ishihara T., Hong M., Zhang B., Nakagawa Y., Lee M.K., Trojanowski J.Q., and Lee V.M.Y. Age-dependent emergence and progression of a tauopathy in transgenic mice overexpressing the shortest human tau isoform. Neuron 24 (1999) 751-762
177. Jackson G.R., Wiedau-Pazos M., Sang T.K., Wagle N., Brown C.A., Massachi S., and Geschwind D.H. Human wild-type tau interacts with wingless pathway components and produces neurofibrillary pathology in Drosophila. Neuron 34 (2002) 509-519
178. Jancsik V., Filliol D., and Rendon A. Tau proteins bind to kinesin and modulate its activation by microtubules. Neurobiology (Bp) 4 (1996) 417-429
179. Jiang Z., Tang H., Havlioglu N., Zhang X., Stamm S., Yan R., and Wu J.Y. Mutations in tau gene exon 10 associated with FTDP-17 alter the activity of an exonic splicing enhancer to interact with Tra2 beta. J. Biol. Chem. 278 (2003) 18997-19007
180. Jicha G.A., O'Donnell A., Weaver C., Angeletti R., and Davies P. Hierarchical phosphorylation of recombinant tau by the paired-helical filament-associated protein kinase is dependent on cyclic AMP-dependent protein kinase. J. Neurochem. 72 (1999) 214-224
181. Kanai Y., Chen J., and Hirokawa N. Microtubule bundling by tau proteins in vivo: analysis of functional domains. EMBO J. 11 (1992) 3953-3961
182. Kar S., Fan J., Smith M.J., Goedert M., and Amos L.A. Repeat motifs of tau bind to the insides of microtubules in the absence of taxol. EMBO J. 22 (2003) 70-77
183. Kar A., Kuo D., He R., Zhou J., and Wu J.Y. Tau alternative splicing and frontotemporal dementia. Alzheimer Dis. Assoc. Disord. 19 (2005) S29-S36
184. Kaspar B.K., Vissel B., Bengoechea T., Crone S., Randolph-Moore L., Muller M., Brandon E.P., Schaffer D., Verma I.M., Lee K., Heinemann S.F., and Gage F.H. Adeno-associated virus effectively mediates conditional gene modification in the brain. Proc. Natl. Acad. Sci. U.S.A. 99 (2002) 2320-2325
185. Keck S., Nitsch R., Grune T., and Ullrich O. Proteasome inhibition by paired helical filament-tau in brains of patients with Alzheimer's disease. J. Neurochem. 85 (2003) 115-122
186. Keller J.N., Hanni K.B., and Markesbery W.R. Impaired proteasome function in Alzheimer's disease. J. Neurochem. 75 (2000) 436-439
187. Kerr F., Rickle A., Nayeem N., Brandner S., Cowburn R.F., and Lovestone S. PTEN, a negative regulator of PI3 kinase signalling, alters tau phosphorylation in cells by mechanisms independent of GSK-3. FEBS Lett. 580 (2006) 3121-3128
188. Khatoon S., Grundke-Iqbal I., and Iqbal K. Brain levels of microtubule associated protein tau are elevated in Alzheimer's disease brain: a radioimmunoslot-blot assay for nanograms of the protein. J. Neurochem. 59 (1992) 750-753
189. Khatoon S., Grundke-Iqbal I., and Iqbal K. Levels of normal and abnormally phosphorylated tau in different cellular and regional compartments of Alzheimer disease and control brains. FEBS Lett. 351 (1994) 80-84
190. Khlistunova I., Biernat J., Wang Y., Pickhardt M., von Bergen M., Gazova Z., Mandelkow E., and Mandelkow E.M. Inducible expression of tau repeat domain in cell models of tauopathy: aggregation is toxic to cells but can be reversed by inhibitor drugs. J. Biol. Chem. 281 (2006) 1205-1214
191. Khurana V., Lu Y., Steinhilb M.L., Oldham S., Shulman J.M., and Feany M.B. TOR-mediated cell-cycle activation causes neurodegeneration in a Drosophila tauopathy model. Curr. Biol. 16 (2006) 230-241
192. Kim H.S., Kim E.M., Lee J.P., Park C.H., Kim S., Seo J.H., Chang K.A., Yu E., Jeong S.J., Chong Y.H., and Suh Y.H. C-terminal fragments of amyloid precursor protein exert neurotoxicity by inducing glycogen synthase kinase-3beta expression. FASEB J. 17 (2003) 1951-1953
193. King M.E., Ghoshal N., Wall J.S., Binder L.I., and Ksiezak-Reding H. Structural analysis of Pick's disease-derived and in vitro-assembled tau filaments. Am. J. Pathol. 158 (2001) 1481-1490
194. Knops J., Kosik K.S., Lee G., Pardee J.D., Cohen-Gould L., and McConlogue L. Overexpression of tau in a nonneuronal cell induces long cellular processes. J. Cell Biol. 114 (1991) 725-733
195. Knowles R., LeClerc N., and Kosik K.S. Organization of actin and microtubules during process formation in tau-expressing Sf9 cells. Cell Motil. Cytoskeleton 28 (1994) 256-264
196. Kohnken R., Buerger K., Zinkowski R., Miller C., Kerkman D., DeBernardis J., Shen J., Möller H.J., Davies P., and Hampel H. Detection of tau phosphorylated at threonine 231 in cerebrospinal fluid of Alzheimer's disease patients. Neurosci. Lett. 287 (2000) 187-190
197. Kondratick C.M., and Vandre D.D. Alzheimer's disease neurofibrillary tangles contain mitosis-specific phosphoepitopes. J. Neurochem. 67 (1996) 405-416
198. Kopke E., Tung Y.C., Shaikh S., Alonso A.C., Iqbal K., and Grundke-Iqbal I. Microtubule associated protein tau: abnormal phosphorylation of a non-paired helical filament pool in Alzheimer disease. J. Biol. Chem. 268 (1993) 24374-24384
199. Kosik K.S., Joachim C.L., and Selkoe D.J. Microtubule-associated protein tau (tau) is a major antigenic component of paired helical filaments in Alzheimer disease. Proc. Natl. Acad. Sci. U.S.A. 83 (1986) 4044-4048
200. Kraemer B.C., Zhang B., Leverenz J.B., Thomas J.H., Trojanowski J.Q., and Schellenberg G.D. Neurodegeneration and defective neurotransmission in a Caenorhabditis elegans model of tauopathy. Proc. Natl. Acad. Sci. U.S.A. 100 (2003) 9980-9985
201. Kuhla B., Haase C., Lüth H.J., Arendt T., and Münch G. Effect of pseudophosphorylation and crosslinking by lipid peroxidation and advanced glycation endproduct precursors on tau aggregation and filament formation. J. Biol. Chem. 282 (2007) 6984-6991
202. Kumar P., Wu H., McBride J.L., Jung K., Kim M.H., Davidson B.L., Lee S.K., Shankar P., and Manjunath N. Transvascular delivery of small interfering RNA to the central nervous system. Nature 448 (2007) 39-44
203. Lassmann H., Bancher C., Breitschopf H., Wegiel J., Bobinski M., Jellinger K., and Wisniewski H.M. Cell death in Alzheimer's disease evaluated by DNA fragmentation in situ. Acta Neuropathol. (Berl.) 89 (1995) 35-41
204. Latimer D.A., Gallo J.M., Lovestone S., Miller C.C., Reynolds C.H., Marquardt B., Stabel S., Woodgett J.R., and Anderton B.H. Stimulation of MAP kinase by v-raf transformation of fibroblasts fails to induce hyperphosphorylation of transfected tau. FEBS Lett. 365 (1995) 42-46
205. Le Corre S., Klafki H.W., Plesnila N., Hubinger G., Obermeier A., Sahagun H., Monse B., Seneci P., Lewis J., Eriksen J., Zehr C., Yue M., McGowan E., Dickson D.W., Hutton M., and Roder H.M. An inhibitor of tau hyperphosphorylation prevents severe motor impairments in tau transgenic mice. Proc. Natl. Acad. Sci. U.S.A. 103 (2006) 9673-9678
206. Ledesma M.D., Bonay P., Colaco C., and Avila J. Analysis of microtubule-associated protein tau glycation in paired helical filaments. J. Biol. Chem. 269 (1994) 21614-21619
207. Lee G., Cowan N., and Kirschner M. The primary structure and heterogeneity of tau protein from mouse brain. Science 239 (1988) 285-288
208. Lee G., Neve R.L., and Kosik K.S. The microtubule binding domain of tau protein. Neuron 2 (1989) 1615-1624
209. Lee G., Thangavel R., Sharma V.M., Litersky J.M., Bhaskar K., Fang S.M., Do L.H., Andreadis A., Van Hoesen G., and Ksiezak-Reding H. Phosphorylation of tau by fyn: implications for Alzheimer's disease. J. Neurosci. 24 (2004) 2304-23012
210. Lee G. Tau and src family tyrosine kinases. Biochim. Biophys. Acta 1739 (2005) 323-330
211. Lee H.G., Perry G., Moreira P.I., Garrett M.R., Liu Q., Zhu X., Takeda A., Nunomura A., and Smith M.A. Tau phosphorylation in Alzheimer's disease: pathogen or protector?. Trends Mol. Med. 11 (2005) 164-169
212. Lee V.M., Balin B.J., Otvos L., and Trojanowski J.Q. A68: a major subunit of paired helical filaments and derivatized forms of normal tau. Science 251 (1991) 675-678
213. Lee V.M.Y., Goedert M., and Trojanowski J.Q. Neurodegenerative tauopathies. Annu. Rev. Neurosci. 24 (2001) 1121-1159
214. Lefebvre T., Ferreira S., Dupont-Wallois L., Bussiere T., Dupire M.J., Delacourte A., Michalski J.C., and Caillet-Boudin M.L. Evidence of a balance between phosphorylation and O-GlcNAc glycosylation of Tau proteins: a role in nuclear localization. Biochim. Biophys. Acta 1619 (2003) 167-176
215. Leszek J., Malyszczak K., Bartys A., Staniszewska M., and Gamian A. Analysis of serum of patients with Alzheimer's disease for the level of advanced glycation end products. Am. J. Alzheimers Dis. Other Demen. 21 (2006) 360-365
216. Levites Y., Jansen K., Smithson L.A., Dakin R., Holloway V.M., Das P., and Golde T.E. Intracranial adeno-associated virus-mediated delivery of anti-Pan amyloid β, amyloid β40, and amyloid β42 single-chain variable fragments attenuates plaque pathology in amyloid precursor protein mice. J. Neurosci. 26 (2006) 11923-111928
217. Lewis J., McGowan E., Rockwood J., Melrose H., Nacharaju P., Van Slegtenhorst M., Gwinn-Hardy K., Paul Murphy M., Baker M., Yu X., Duff K., Hardy J., Corral A., Lin W.L., Yen S.H., Dickson D.W., Davies P., and Hutton M. Neurofibrillary tangles, amyotrophy and progressive motor disturbance in mice expressing mutant (P301L) tau protein. Nat. Genet. 25 (2000) 402-405
218. Liao X.M., Zhang Y.C., Wang Y.P., and Wang J.Z. The effect of cdk-5 overexpression on tau phosphorylation and spatial memory of rat. Sci. China C Life Sci. 47 (2004) 251-257
219. Li H.L., Wang H.H., Liu S.J., Deng Y.Q., Zhang Y.J., Tian Q., Wang X.C., Chen X.Q., Yang Y., Zhang J.Y., Wang Q., Xu H., Liao F.F., and Wang J.Z. Phosphorylation of tau antagonizes apoptosis by stabilizing beta-catenin, a mechanism involved in Alzheimer's neurodegeneration. Proc. Natl. Acad. Sci. U.S.A. 104 (2007) 3591-3596
220. Li G., Yin H., and Kuret J. Casein kinase 1 delta phosphorylates tau and disrupts its binding to microtubules. J. Biol. Chem. 279 (2004) 15938-15945
221. Li T., and Paudel H.K. Glycogen synthase kinase 3beta phosphorylates Alzheimer's disease-specific Ser396 of microtubule-associated protein tau by a sequential mechanism. Biochemistry 45 (2006) 3125-3133
222. Li W., Wang X.S., Qu M.H., Liu Y., and He R.Q. Human protein tau represses DNA replication in vitro. Biochim. Biophys. Acta 1726 (2005) 280-286
223. Li X., Lu F., Wang J.Z., and Gong C.X. Concurrent alterations of O-GlcNAcylation and phosphorylation of tau in mouse brains during fasting. Eur. J. Neurosci. 23 (2006) 2078-2086
224. Li X., Lu F., Tian Q., Yang Y., Wang Q., and Wang J.Z. Activation of glycogen synthase kinase-3 induces Alzheimer-like tau hyperphosphorylation in rat hippocampus slices in culture. J. Neural Transm. 113 (2006) 93-102
225. Lim F., Hernandez F., Lucas J.J., Gomez-Ramos P., Moran M.A., and Avila J. FTDP-17 mutations in tau transgenic mice provoke lysosomal abnormalities and Tau filaments in forebrain. Mol. Cell. Neurosci. 18 (2001) 702-714
226. Lippa C.F., Zhukareva V., Kawarai T., Uryu K., Shafiq M., Nee L.E., Grafman J., Liang Y., St George-Hyslop P.H., Trojanowski J.Q., and Lee V.M. Frontotemporal dementia with novel tau pathology and a Glu342Val tau mutation. Ann. Neurol. 48 (2000) 850-858
227. Liu F., Zaidi T., Grundke-Iqbal I., Iqbal K., and Gong C.X. Aberant glycosylation modulates phosphorylation of tau by protein kinase A and dephosphorylation of tau by protein phosphatase 2A and 5. Neuroscience 115 (2002) 829-837
228. Liu F., Zaidi T., Iqbal K., Grundke-Iqbal I., Merkle R.K., and Gong C.X. Role of glycosylation in hyperphosphorylation of tau in Alzheimer's disease. FEBS Lett. 512 (2002) 101-106
229. Liu F., Iqbal K., Grundke-Iqbal I., Hart G.W., and Gong C.X. O-GlcNAcylation regulates phosphorylation of tau: a mechanism involved in Alzheimer's disease. Proc. Natl. Acad. Sci. U.S.A. 101 (2004) 10804-10809
230. Liu F., Iqbal K., Grundke-Iqbal I., Rossie S., and Gong C.X. Dephosphorylation of tau by protein phosphatase 5: impairment in Alzheimer's disease. J. Biol. Chem. 280 (2005) 1790-1796
231. Liu F., Liang Z., and Gong C.X. Hyperphosphorylation of tau and protein phosphatases in Alzheimer disease. Panminerva Med. 48 (2006) 97-108
232. Liu G.P., Zhang Y., Yao X.Q., Zhang C.E., Fang J., Wang Q., and Wang J.Z. Activation of glycogen synthase kinase-3 inhibits protein phosphatase-2A and the underlying mechanisms. Neurobiol. Aging (April 2007) (Epub ahead of print)
233. Liu Q., Smith M.A., Avila J., DeBernardis J., Kansal M., Takeda A., Zhu X., Nnomura A., Honda K., Oreira P.I., liveira C.R., Sntos M.S., Shimohama S., Aliev G., Torre J., Ghanbari H.A., Siedlak S.L., Harris P.L., Sayre L.M., and Perry G. Alzheimer-specific epitopes of tau represent lipid peroxidation-induced conformations. Free Radic. Biol. Med. 38 (2005) 746-754
234. Liu R., Pei J.J., Wang X.C., Zhou X.W., Tian Q., Winblad B., and Wang J.Z. Acute anoxia induces tau dephosphorylation in rat brain slices and its possible underlying mechanisms. J. Neurochem. 94 (2005) 1225-1234
235. Liu S.J., and Wang J.Z. Alzheimer-like tau phosphorylation induced by wortmannin in vivo and its attenuation by melation. Acta Pharmacol. Sin. 23 (2002) 183-187
236. Liu S.J., Zhang A.H., Li H.L., Wang Q., Deng H.M., Netzer W.J., Xu H., and Wang J.Z. Overactivation of glycogen synthase kinase-3 by inhibition of phosphoinositol-3 kinase and protein kinase C leads to hyperphosphorylation of tau and impairment of spatial memory. J. Neurochem. 87 (2003) 1333-1344
237. Liu S.J., Zhang J.Y., Li H.L., Fang Z.Y., Wang Q., Deng H.M., Gong C.X., Grundke-Iqbal I., Iqbal K., and Wang J.Z. Tau becomes a more favorable substrate for GSK-3 when it is prephosphorylated by PKA in rat brain. J. Biol. Chem. 279 (2004) 50078-50088
238. LoPresti P., and Konat G.W. Hydrogen peroxide induces transient dephosphorylation of tau protein in cultured rat oligodendrocytes. Neurosci. Lett. 311 (2001) 142-144
239. Lovestone S., Reynolds C.H., Latimer D., Davis D.R., Anderton B.H., Gallo J.M., Hanger D., Mulot S., Marquardt B., Stabel S., et al. Alzheimer's disease-like phosphorylation of the microtubule-associated protein tau by glycogen synthase kinase-3 in transfected mammalian cells. Curr. Biol. 4 (1994) 1077-1086
240. Lu M., and Kosik K.S. Competition for microtubule-binding with dual expression of tau missense and splice isoforms. Mol. Biol. Cell 12 (2001) 171-184
241. Lucas J.J., Hernández F., Gómez-Ramos P., Morán M.A., Hen R., and Avila J. Decreased nuclear beta-catenin, tau hyperphosphorylation and neurodegeneration in GSK-3beta conditional transgenic mice. EMBO J. 20 (2001) 27-39
242. Maj M., Pirozzi R., Bartoli L., and Magliano L. Long-term outcome of lithium prophylaxis in bipolar disorder with mood-incongruent psychotic features: a prospective study. J. Affect. Disord. 71 (2002) 195-198
243. Mandell J.W., and Banker G.A. A spatial gradient of tau protein phosphorylation in nascent axons. J. Neurosci. 16 (1996) 5727-5740
244. Marx J. Neuroscience. New leads on the 'how' of Alzheimer's. Science 293 (2001) 2192-2194
245. Mazanetz M.P., and Fischer P.M. Untangling tau hyperphosphorylation in drug design for neurodegenerative diseases. Nat. Rev. Drug Discov. 6 (2007) 464-479
246. McShea A., Lee H.G., Petersen R.B., Casadesus G., Vincent I., Linford N.J., Funk J.O., Shapiro R.A., and Smith M.A. Neuronal cell cycle re-entry mediates Alzheimer disease-type changes. Biochim. Biophys. Acta 1772 (2007) 467-472
247. Morishima-Kawashima M., Hasegawa M., Takio K., Suzuki M., Titani K., and Ihara Y. Ubiquitin is conjugated with amino-terminally processed tau in paired helical filaments. Neuron 10 (1993) 1151-1160
248. Morishima-Kawashima M., Hasegawa M., Takio K., Suzuki M., Yoshida H., Titani K., and Ihara Y. Proline-directed and non-proline-directed phosphorylation of PHF-tau. J. Biol. Chem. 270 (1995) 823-829
249. Morsch R., Simon W., and Coleman P.D. Neurons may live for decades with neurofibrillary tangles. J. Neuropathol. Exp. Neurol. 58 (1999) 188-197
250. Motter R., Vigo-Pelfrey C., Kholodenko D., Barbour R., Johnson-Wood K., Galasko D., Chang L., Miller B., Clark C., Green R., et al. Reduction of ß-amyloid peptide42 in the cerebrospinal fluid of patients with Alzheimer's disease. Ann. Neurol. 38 (1995) 643-648
251. Mudher A., Shepherd D., Newman T.A., Mildren P., Jukes J.P., Squire A., Mears A., Drummond J.A., Berg S., MacKay D., Asuni A.A., Bhat R., and Lovestone S. GSK-3beta inhibition reverses axonal transport defects and behavioural phenotypes in Drosophila. Mol. Psychiatry 9 (2004) 522-530
252. Mukrasch M.D., von Bergen M., Biernat J., Fischer D., Griesinger C., Mandelkow E., and Zweckstetter M. The "jaws" of the tau-microtubule interaction. J. Biol. Chem. 282 (2007) 12230-12239
253. Munch G., Deuther-Conrad W., and Gasic-Milenkovic J. Glycoxidative stress creates a vicious cycle of neurodegeneration in Alzheimer's disease: a target for neuroprotective treatment strategies?. J. Neural Transm. 62 (2002) 303-307
254. Murrell J.R., Spillantini M.G., Zolo P., Guazzelli M., Smith M.J., Hasegawa M., Redi F., Crowther R.A., Pietrini P., Ghetti B., and Goedert M. Tau gene mutation G389R causes a tauopathy with abundant pick body-like inclusions and axonal deposits. J. Neuropathol. Exp. Neurol. 58 (1999) 1207-1226
255. Muyllaert D., Terwel D., Borghgraef P., Devijver H., Dewachter I., and Van Leuven F. Transgenic mouse models for Alzheimer's disease: the role of GSK-3B in combined amyloid and tau-pathology. Rev. Neurol. 162 (2006) 903-907
256. Nayeem N., Kerr F., Naumann H., Linehan J., Lovestone S., and Brandner S. Hyperphosphorylation of tau and neurofilaments and activation of cdk5 and ERK1/2 in PTEN-deficient cerebella. Mol. Cell. Neurosci. 34 (2007) 400-408
257. Neve R.L., Harris P., Kosik K.S., Kurnit D.M., and Donlon T.A. Identification of cDNA clones for the human microtubule-associated protein tau and chromosomal localization of the genes for tau and microtubule-associated protein 2. Brain Res. 387 (1986) 271-280
258. Noble W.J., Derkinderen P., Scales T., Price C., Bird I.N., Kellie S., Varndell I.M., Sheppard P.W., Williamson R., Reynolds H., and Anderson B.H. The microtubule-associated tau is phosphorylated on tyrosine 394. Neurobiol. Aging 25 (2004) S419
259. Noble W., Planel E., Zehr C., Olm V., Meyerson J., Suleman F., Gaynor K., Wang L., LaFrancois J., Feinstein B., Burns M., Krishnamurthy P., Wen Y., Bhat R., Lewis J., Dickson D., and Duff K. Inhibition of glycogen synthase kinase-3 by lithium correlates with reduced tauopathy and degeneration in vivo. Proc. Natl. Acad. Sci. U.S.A. 102 (2005) 6990-69995
260. Novak M., Kabat J., and Wischik C.M. Molecular characterization of the minimal protease resistant tau unit of the Alzheimer's disease paired helical filament. EMBO J. 12 (1993) 365-370
261. Nuňez J. Immature and mature variants of MAP2 and tau proteins and neuronal plasticity. Trends Neurosci. 11 (1988) 477-479
262. Nunomura A., Perry G., Pappolla M.A., Wade R., Hirai K., Chiba S., and Smith M.A. RNA oxidation is a prominent feature of vulnerable neurons in Alzheimer's disease. J. Neurosci. 19 (1999) 1959-1964
263. Nunomura A., Perry G., Aliev G., Hirai K., Takeda A., Balraj E.K., Jones P.K., Ghanbari H., Wataya T., Shimohama S., Chiba S., Atwood C.S., Petersen R.B., and Smith M.A. Oxidative damage is the earliest event in Alzheimer disease. J. Neuropathol. Exp. Neurol. 60 (2001) 759-767
264. Oddo S., Caccamo A., Shepherd J.D., Murphy M.P., Golde T.E., Kayed R., Metherate R., Mattson M.P., Akbari Y., and LaFerla F.M. Triple-transgenic model of Alzheimer s disease with plaques and tangles. Intracellular abeta and synaptic dysfunction. Neuron 39 (2003) 409-421
265. Olsson A., Vanderstichele H., Andreasen N., De Meyer G., Wallin A., Holmberg B., Rosengren L., Vanmechelen E., and Blennow K. Simultaneous measurement of beta-amyloid (1-42), total tau, and phosphorylated tau (Thr181) in cerebrospinal fluid by the xMAP technology. Clin. Chem. 51 (2005) 336-345
266. Oyama F., Kotliarova S., Harada A., Ito M., Miyazaki H., Ueyama Y., Hirokawa N., Nukina N., and Ihara Y. Gem GTPase and tau: morphological changes induced by gem GTPase in cho cells are antagonized by tau. J. Biol. Chem. 279 (2004) 27272-27277
267. Parnetti L., Lanari A., Amici S., Gallai V., Vanmechelen E., and Hulstaert F. CSF phosphorylated tau is a possible marker for discriminating Alzheimer's disease from dementia with Lewy bodies. Phospho-Tau International Study Group. Neurol. Sci. 22 (2001) 77-78
268. Pei J.J., Tanaka T., Tung Y.C., Braak E., Iqbal K., and Grundke-Iqbal I. Distribution, levels, and activity of glycogen synthase kinase-3 in the Alzheimer disease brain. J. Neuropathol. Exp. Neurol. 56 (1997) 70-78
269. Pei J.J., Braak E., Braak H., Grundke-Iqbal I., Iqbal K., Winblad B., and Cowburn R.F. Distribution of active glycogen synthase kinase 3beta (GSK-3beta) in brains staged for Alzheimer disease neurofibrillary changes. J. Neuropathol. Exp. Neurol. 58 (1999) 1010-1019
270. Peng J.H., Zhang C.E., Wei W., Hong X.P., Pan X.P., and Wang J.Z. Dehydroevodiamine attenuates tau hyperphosphorylation and memory deficit induced by activation of glycogen synthase kinase-3 in rats. Neuropharmacology 52 (2007) 1521-1527
271. Perez M., Cuadros R., Smith M.A., Perry G., and Avila J. Phosphorylated, but not native, tau protein assembles following reaction with the lipid peroxidation product, 4-hydroxy-2-nonenal. FEBS Lett. 486 (2000) 270-274
272. Perez M., Hernandez F., Gomez-Ramos A., Smith M., Perry G., and Avila J. Formation of aberrant phosphotau fibrillar polymers in neural cultured cells. Eur. J. Biochem. 269 (2002) 1484-1489
273. Perez M., Hernandez F., Lim F., Diaz-Nido J., and Avila J. Chronic lithium treatment decreases mutant tau protein aggregation in a transgenic mouse model. J. Alzheimers Dis. 5 (2003) 301-308
274. Perry G., Friedman R., Shaw G., and Chau V. Ubiquitin is detected in neurofibrillary tangles and senile plaque neurites of Alzheimer disease brains. Proc. Natl. Acad. Sci. U.S.A. 84 (1987) 3033-3036
275. Perry G., Nunomura A., Lucassen P., Lassmann H., and Smith M.A. Apoptosis and Alzheimer's disease. Science 282 (1998) 1268-1269
276. Perry G., Nunomura A., and Smith M.A. A suicide note from Alzheimer disease neurons?. Nat. Med. 4 (1998) 897-898
277. Perry G., Zhu X., and Smith M.A. Do neurons have a choice in death?. Am. J. Pathol. 158 (2001) 1-2
278. Petrucelli L., Dickson D., Kehoe K., Taylor J., Snyder H., Grover A., De Lucia M., McGowan E., Lewis J., Prihar G., Kim J., Dillmann W.H., Browne S.E., Hall A., Voellmy R., Tsuboi Y., Dawson T.M., Wolozin B., Hardy J., and Hutton M. CHIP and Hsp70 regulate tau ubiquitination, degradation and aggregation. Hum. Mol. Genet. 13 (2004) 703-714
279. Poorkaj P., Muma N.A., Zhukareva V., Cochran E.J., Shannon K.M., Hurtig H., Koller W.C., Bird T.D., Trojanowski J.Q., Lee V.M., and Schellenberg G.D. An R5L tau mutation in a subject with a progressive supranuclear palsy phenotype. Ann. Neurol. 52 (2002) 511-516
280. Poppek D., Keck S., Ermak G., Jung T., Stolzing A., Ullrich O., Davies K.J., and Grune T. Phosphorylation inhibits turnover of the tau protein by the proteasome: influence of RCAN1 and oxidative stress. Biochem. J. 400 (2006) 511-520
281. Probst A., Götz J., Wiederhold K.H., Tolnay M., Mistl C., Jaton A.L., Hong M., Ishihara T., Lee V.M.Y., Trojanowski J.Q., Jakes R., Crowther R.A., Spillantini M.G., Bürki K., and Goedert M. Axonopathy and amyotrophy in mice transgenic for human four-repeat tau protein. Acta Neuropathol. (Berl.) 99 (2000) 469-481
282. Preuss U., and Mandelkow E.M. Mitotic phosphorylation of tau protein in neuronal cell lines resembles phosphorylation in Alzheimer's disease. Eur. J. Cell Biol. 76 (1998) 176-184
283. Rahman A., Grundke-Iqbal I., and Iqbal K. PP2B isolated from human brain preferentially dephosphorylates Ser-262 and Ser-396 of the Alzheimer disease abnormally hyperphosphorylated tau. J. Neural Transm. 113 (2006) 219-230
284. Raina A.K., Hochman A., Ickes H., Zhu X., Ogawa O., Cash A.D., Shimohama S., Perry G., and Smith M.A. Apoptotic promoters and inhibitors in alzheimer's disease: who wins out?. Prog. Neuropsychopharmacol. Biol. Psychiatry 27 (2003) 251-254
285. Raina A.K., Zhu X., Shimohama S., Perry G., and Smith M.A. Tipping the apoptotic balance in Alzheimer's disease: the abortosis concept. Cell Biochem. Biophys. 39 (2003) 249-255
286. Rao M.V., Houseweart M.K., Williamson T.L., Crawford T.O., Folmer J., and Cleveland D.W. Neurofilament-dependent radial growth of motor axons and axonal organization of neurofilaments does not require the neurofilament heavy subunit (NF-H) or its phosphorylation. J. Cell Biol. 143 (1998) 171-181
287. Ren Q.G., Liao X.M., Wang Z.F., Qu Z.S., and Wang J.Z. The involvement of glycogen synthase kinase-3 and protein phosphatase-2A in lactacystin-induced tau accumulation. FEBS Lett. 580 (2006) 2503-2511
288. Ren Q.G., Liao X.M., Chen X.Q., Liu G.P., and Wang J.Z. Effects of tau phosphorylation on proteasome activity. FEBS Lett. 581 (2007) 1521-1528
289. Reusche E. Silver staining of senile plaques and neurofibrillary tangles in paraffin sections. Pathol. Res. Pract. 187 (1991) 1045-1049
290. Reynolds C.H., Betts J.C., Blackstock W.P., Nebreda A.R., and Anderton B.H. Phosphorylation sites on tau identified by nanoelectrospray mass spectrometry: differences in vitro between the mitogen-activated protein kinases ERK2, c-Jun N-terminal kinase and P38, and glycogen synthase kinase-3beta. J. Neurochem. 74 (2000) 1587-1595
291. Reynolds M.R., Berry R.W., and Binder L.I. Site-specific nitration and oxidative dityrosine bridging of the tau protein by peroxynitrite: implications for Alzheimer's disease. Biochemistry 44 (2005) 1690-1700
292. Reynolds M.R., Berry R.W., and Binder L.I. Site-specific nitration differentially influences tau assembly in vitro. Biochemistry 44 (2005) 13997-14009
293. Reynolds M.R., Reyes J.F., Fu Y., Bigio E.H., Guillozet-Bongaarts A.L., Berry R.W., and Binder L.I. Tau nitration occurs at tyrosine 29 in the fibrillar lesions of Alzheimer's disease and other tauopathies. J. Neurosci. 26 (2006) 10636-10645
294. Richter-Landsberg C., and Goldbaum O. Stress proteins in neural cells: functional roles in health and disease. Cell. Mol. Life Sci. 60 (2003) 337-349
295. Rissman R.A., Poon W.W., Blurton-Jones M., Oddo S., Torp R., Vitek M.P., LaFerla F.M., Rohn T.T., and Cotman C.W. Caspase-cleavage of tau is an early event in Alzheimer disease tangle pathology. J. Clin. Invest. 114 (2004) 121-130
296. Rizzini C., Goedert M., Hodges J.R., Smith M.J., Jakes R., Hills R., Xuereb J.H., Crowther R.A., and Spillantini M.G. Tau gene mutation K257T causes a tauopathy similar to Pick's disease. J. Neuropathol. Exp. Neurol. 59 (2000) 990-1001
297. Rizzu P., Van Swieten J.C., Joosse M., Hasegawa M., Stevens M., Tibben A., Niermeijer M.F., Hillebrand M., Ravid R., Oostra B.A., Goedert M., van Duijn C.M., and Heutink P. High prevalence of mutations in the microtubule-associated protein tau in a population study of frontotemporal dementia in the Netherlands. Am. J. Hum. Genet. 64 (1999) 414-421
298. Roberson E.D., Scearce-Levie K., Palop J.J., Yan F., Cheng I.H., Wu T., Gerstein H., Yu G.Q., and Mucke L. Reducing endogenous tau ameliorates amyloid beta-induced deficits in an Alzheimer's disease mouse model. Science 316 (2007) 750-754
299. Robertson L.A., Moya K.L., and Breen K.C. The potential role of tau protein O-glycosylation in Alzheimer's disease. J. Alzheimers Dis. 6 (2004) 489-495
300. Rohn T.T., Head E., Su J.H., Anderson A.J., Bahr B.A., Cotman C.W., and Cribbs D.H. Correlation between caspase activation and neurofibrillary tangle formation in Alzheimer's disease. Am. J. Pathol. 158 (2001) 189-198
301. Sahara N., Murayama M., Mizoroki T., Urushitani M., Imai Y., Takahashi R., Murata S., Tanaka K., and Takashima A. In vivo evidence of CHIP up-regulation attenuating tau aggregation. J. Neurochem. 94 (2005) 1254-1263
302. Salehi A., Delcroix J.D., and Mobley W.C. Traffic at the intersection of neurotrophic factor signaling and neurodegeneration. Trends Neurosci. 26 (2003) 73-80
303. Santacruz K., Lewis J., Spires T., Paulson J., Kotilinek L., Ingelsson M., Guimaraes A., DeTure M., Ramsden McGowan E., Forster C., Yue M., Orne J., Janus C., Mariash A., Kuskowski M., Hyman B., Hutton M., and Ashe H. Tau suppression in a neurodegenerative mouse model improves memory function. Science 309 (2005) 476-481
304. Sasaki N., Fukatsu R., Tsuzuki K., Hayashi Y., Yoshida T., Fujii N., Koike T., Wakayama I., Yanagihara R., Garruto R., Amano N., and Makita Z. Advanced glycation end products in Alzheimer's disease and other neurodegenerative diseases. Am. J. Pathol. 153 (1998) 1149-1155
305. Schaefer A., O'Carroll D., Tan C.L., Hillman D., Sugimori M., Llinas R., and Greengard P. Cerebellar neurodegeneration in the absence of microRNA. J. Exp. Med. 204 (2007) 1553-1558
306. Schild A., Ittner L.M., and Gotz J. Altered phosphorylation of cytoskeletal proteins in mutant protein phosphatase 2A transgenic mice. Biochem. Biophys. Res. Commun. 343 (2006) 1171-1178
307. Schindowski K., Bretteville A., Leroy K., Begard S., Brion J.P., Hamdane M., and Buee L. Alzheimer's disease-like tau neuropathology leads to memory deficits and loss of functional synapses in a novel mutated tau transgenic mouse without any motor deficits. Am. J. Pathol. 169 (2006) 599-616
308. Schwartz A.L., and Ciechanover A. The ubiquitin-proteasome pathway and pathogenesis of human diseases. Annu. Rev. Med. 50 (1999) 57-74
309. Sengupta A., Wu Q., and Grundke-Iqbal I. Potentiation of GSK-3-catalyzed Alzheimer-like phosphorylation of human tau by cdk5. Mol. Cell. Biochem. 167 (1997) 99-105
310. Sengupta A., Kabat J., Novak M., Wu Q., Grundke-Iqbal I., and Iqbal K. Phosphorylation of tau at both Thr 231 and Ser 262 is required for maximal inhibition of its binding to microtubules. Arch. Biochem. Biophys. 357 (1998) 299-309
311. Sergeant N., Wattez A., and Delacourte A. Neurofibrillary degeneration in progressive supranuclear palsy and corticobasal degeneration: tau pathologies with exclusively 'exon 10' isoforms. J. Neurochem. 72 (1999) 1243-1249
312. Sergeant N., Sablonniere B., Schraen-Maschke S., Ghestem A., Maurage C.A., Wattez A., Vermersch P., and Delacourte A. Dysregulation of human brain microtubule-associated tau mRNA maturation in myotonic dystrophy type 1. Hum. Mol. Genet. 10 (2001) 2143-2155
313. Shahani N., Subramaniam S., Wolf T., Tackenberg C., and Brandt R. Tau aggregation and progressive neuronal degeneration in the absence of changes in spine density and morphology after targeted expression of Alzheimer's disease-relevant tau constructs in organotypic hippocampal slices. J. Neurosci. 26 (2006) 6103-6114
314. Shimura H., Schwartz D., Gygi S.P., and Kosik K.S. CHIP-Hsc70 complex ubiquitinates phosphorylated tau and enhances cell survival. J. Biol. Chem. 279 (2004) 4869-4876
315. Singh T.J., Zaidi T., and Grundke-Iqbal I. Modulation of GSK-3-catalyzed phosphorylation of microtubule-associated protein tau by non-proline-dependent protein kinases. FEBS Lett. 358 (1995) 4-8
316. Singh T.J., Wang J.Z., Novak M., Kontzekova E., Grundke-Iqbal I., and Iqbal K. Calcium/calmodulin-dependent protein kinase II phosphorylates tau at Ser-262 but only partially inhibits its binding to microtubules. FEBS Lett. 387 (1996) 145-148
317. Singh T.J., Zaidi T., Grundke-Iqbal I., and Iqbal K. Non-proline-dependent protein kinases phosphorylate several sites found in tau from Alzheimer disease brain. Mol. Cell. Biochem. 154 (1996) 143-151
318. Sjögren M., Davidsson P., Tullberg M., Minthon L., Wallin A., Wikkelso C., Granérus A.K., Vanderstichele H., Vanmechelen E., and Blennow K. Both total and phosphorylated tau are increased in Alzheimer's disease. J. Neurol. Neurosurg. Psychiatry 70 (2001) 360-624
319. Skrabana R., Kontsek P., Mederlyova A., Iqbal K., and Novak M. Folding of Alzheimer's core PHF subunit revealed by monoclonal antibody 423. FEBS Lett. 568 (2004) 178-182
320. Smith M.A., Taneda S., Richey P.L., Miyata S., Yan S.D., Stern D., Sayre L.M., Monnier V.M., and Perry G. Advanced Maillard reaction end products are associated with Alzheimer disease pathology. Proc. Natl. Acad. Sci. U.S.A. 91 (1994) 5710-5714
321. Smith M.A., Siedlak S.L., Richey P.L., Mulvihill P., Ghiso J., Frangione B., Tagliavini F., Giaccone G., Bugiani O., and Praprotnik D. Tau protein directly interacts with the amyloid beta-protein precursor: implications for Alzheimer's disease. Nat. Med. 1 (1995) 365-369
322. Smith M.A., Perry G., Richey P.L., Sayre L.M., Anderson V.E., Beal M.F., and Kowall N. Oxidative damage in Alzheimer's. Nature 382 (1996) 120-121
323. Smith M.A., Richey Harris P.L., Sayre L.M., Beckman J.S., and Perry G. Widespread peroxynitrite-mediated damage in Alzheimer's disease. J. Neurosci. 17 (1997) 2653-2657
324. Smith M.A., Casadesus G., Joseph J.A., and Perry G. Amyloid-beta and tau serve antioxidant functions in the aging and Alzheimer brain. Free Radic. Biol. Med. 33 (2002) 1194-1199
325. Sontag E., Hladik C., Montgomery L., Luangpirom A., Mudrak I., Ogris E., and White III C.L. Downregulation of protein phosphatase 2A carboxyl methylation and methyltransferase may contribute to Alzheimer disease pathogenesis. J. Neuropathol. Exp. Neurol. 63 (2004) 1080-1091
326. Spillantini M.G., Murrell J.R., Goedert M., Farlow M.R., Klug A., and Ghetti B. Mutation in the tau gene in familial multiple system tauopathy with presenile dementia. Proc. Natl. Acad. Sci. U.S.A. 95 (1998) 737-7741
327. Spires T.L., Orne J.D., SantaCruz K., Pitstick R., Carlson G.A., Ashe K.H., and Hyman B.T. Region-specific dissociation of neuronal loss and neurofibrillary pathology in a mouse model of tauopathy. Am. J. Pathol. 168 (2006) 1598-1607
328. Spittaels K., Van den Haute C., Van Dorpe J., Bruynseels K., Vandezande K., Laenen I., Geerts H., Mercken M., Sciot R., Van Lommel A., Loos R., and Van Leuven F. Prominent axonopathy in the brain and spinal cord of transgenic mice overexpressing four-repeat human tau protein. Am. J. Pathol. 155 (1999) 2153-2165
329. Stamer K., Vogel R., Thies E., Mandelkow E., and Mandelkow E.M. Tau blocks traffic of organelles, neurofilaments, and APP vesicles in neurons and enhances oxidative stress. J. Cell Biol. 156 (2002) 1051-1063
330. Stanford P.M., Shepherd C.E., Halliday G.M., Brooks W.S., Schofield P.W., Brodaty H., Martins R.N., Kwok J.B., and Schofield P.R. Mutations in the tau gene that cause an increase in three repeat tau and frontotemporal dementia. Brain 126 (2003) 814-826
331. Steinhilb M.L., Dias-Santagata D., Mulkearns E.E., Shulman J.M., Biernat J., Mandelkow E.M., and Feany M.B. S/P and T/P phosphorylation is critical for tau neurotoxicity in Drosophila. J. Neurosci. Res. 85 (2007) 1271-1278
332. Sun L., Liu S.Y., Zhou X.W., Wang X.C., Liu R., Wang Q., and Wang J.Z. Inhibition of protein phosphatase 2a- and protein phosphatase 1-induced tau hyperphosphorylation and impairment of spatial memory retention in rats. Neuroscience 118 (2003) 1175-1182
333. Sun L., Wang X., Liu S., Wang Q., Wang J., Bennecib M., Gong C.X., Sengupta A., Grundke-Iqbal I., and Iqbal K. Bilateral injection of isoproterenol into hippocampus induces Alzheimer-like hyperphosphorylation of tau and spatial memory deficit in rat. FEBS Lett. 579 (2005) 251-258
334. Suo Z., Wu M., Citron B.A., Palazzo R.E., and Festoff B.W. Rapid tau aggregation and delayed hippocampal neuronal death induced by persistent thrombin signaling. J. Biol. Chem. 278 (2003) 37681-37689
335. Takashima A. GSK-3 is essential in the pathogenesis of Alzheimer's disease. J. Alzheimers Dis. 9 (2006) 309-317
336. Takeda A., Perry G., Abraham N.G., Dwyer B.E., Kutty R.K., Laitinen J.T., Petersen R.B., and Smith M.A. Overexpression of heme oxygenase in neuronal cells, the possible interaction with tau. J. Biol. Chem. 275 (2000) 5395-5399
337. Takeda A., Smith M.A., Avila J., Nunomura A., Siedlak S.L., Zhu X., Perry G., and Sayre L.M. In Alzheimer's disease, heme oxygenase is coincident with Alz50, an epitope of tau induced by 4-hydroxy-2-nonenal modification. J. Neurochem. 75 (2000) 1234-1241
338. Takeuchi M., Watai T., Sasaki N., Choei H., Iwaki M., Ashizawa T., Inagaki Y., Yamagishi S., Kikuchi S., Riederer P., Saito T., Bucala R., and Kameda Y. Neurotoxicity of acetaldehyde-derived advanced glycation end products for cultured cortical neurons. J. Neuropathol. Exp. Neurol. 62 (2003) 486-496
339. Takuma H., Arawaka S., and Mori H. Isoforms changes of tau protein during development in various species. Brain Res. Dev. Brain Res. 142 (2003) 121-127
340. Tanaka T., Zhong J., Iqbal K., Trenkner E., and Grundke-Iqbal I. The regulation of phosphorylation of tau in SY5Y neuroblastoma cells: the role of protein phosphatases. FEBS Lett. 426 (1998) 248-254
341. Tanemura K., Akagi T., Murayama M., Kikuchi N., Murayama O., Hashikawa T., Yoshiike Y., Park J.M., Matsuda K., Nakao S., Sun X., Sato S., Yamaguchi H., and Takashima A. Formation of filamentous tau aggregations in transgenic mice expressing V337M human tau. Neurobiol. Dis. 8 (2001) 1036-1045
342. Tanimukai H., Grundke-Iqbal I., and Iqbal K. Up-regulation of inhibitors of protein phosphatase-2A in Alzheimer's disease. Am. J. Pathol. 166 (2005) 1761-1771
343. Terwel D., Lasrado R., Snauwaert J., Vandeweert E., Van Haesendonck C., Borghgraef P., and Van Leuven F. Changed conformation of mutant Tau-P301L underlies the moribund tauopathy, absent in progressive, non-lethal axonopathy of Tau-4R/2N transgenic mice. J. Biol. Chem. 280 (2005) 3963-3973
344. Tatebayashi Y., Haque N., Tung Y.C., Iqbal K., and Grundke-Iqbal I. Role of tau phosphorylation by glycogen synthase kinase-3β in the regulation of organelle transport. J. Cell Sci. 117 (2004) 1653-1663
345. Tatebayashi Y., Miyasaka T., Chui D.H., Akagi T., Mishima K., Iwasaki K., Fujiwara M., Tanemura K., Murayama M., Ishiguro K., Planel E., Sato S., Hashikawa T., and Takashima A. Tau filament formation and associative memory deficit in aged mice expressing mutant (R406W) human tau. Proc. Natl. Acad. Sci. U.S.A. 99 (2002) 13896-13901
346. Tian Q., and Wang J.Z. Role of protein phosphatases on Alzheimer disease. Neurosignals 11 (2002) 262-269
347. Tian Q., Lin Z.Q., Wang X.C., Chen J., Wang Q., Gong C.X., and Wang J.Z. Injection of okadaic acid into the meynert nucleus basalis of rat brain induces decreased acetylcholine level and spatial memory deficit. Neuroscience 126 (2004) 277-284
348. Togo T., Akiyama H., Iseki E., Uchikado H., Kondo H., Ikeda K., Tsuchiya K., de Silva R., Lees A., and Kosaka K. Immunohistochemical study of tau accumulation in early stages of Alzheimer-type neurofibrillary lesions. Acta Neuropathol. (Berl.) 107 (2004) 504-508
349. Tohgi H., Abe T., Yamazaki K., Murata T., Ishizaki E., and Isobe C. Alterations of 3-nitrotyrosine concentration in the cerebrospinal fluid during aging and in patients with Alzheimer's disease. Neurosci. Lett. 269 (1999) 52-54
350. Trinczek B., Biernat J., Baumann K., and Mandelkow E.M. Domains of tau protein, differential phosphorylation, and dynamic instability of microtubules. Mol. Biol. Cell 6 (1995) 1887-1902
351. Tsujio I., Zaidi T., Xu J., Kotula L., Grundke-Iqbal I., and Iqbal K. Inhibitors of protein phosphatase-2A from human brain structures, immunocytological localization and activities towards dephosphorylation of the Alzheimer type hyperphosphorylated tau. FEBS Lett. 579 (2005) 363-372
352. Tucker K.L., Meyer M., and Barde Y.A. Neurotrophins are required for nerve growth during development. Nat. Neurosci. 4 (2001) 29-37
353. Vandebroek T., Terwel D., Vanhelmont T., Gysemans M., Van Haesendonck C., Engelborghs Y., Winderickx J., and Van Leuven F. Microtubule binding and clustering of human Tau-4R and Tau-P301L proteins isolated from yeast deficient in orthologues of glycogen synthase kinase-3beta or cdk5. J. Biol. Chem. 281 (2006) 25388-25397
354. Vanmechelen E., Vanderstichele H., Davidsson P., Van Kerschaver E., Van Der Perre B., Sjogren M., Andreasen N., and Blennow K. Quantification of tau phosphorylated at threonine 181 in human cerebrospinal fluid: a sandwich ELISA with a synthetic phosphopeptide for standardization. Neurosci. Lett. 285 (2000) 49-52
355. Varani L., Hasegawa M., Spillantini M.G., Smith M.J., Murrell J.R., Ghetti B., Klug A., Goedert M., and Varani G. Structure of tau exon 10 splicing regulatory element RNA and destabilization by mutations of frontotemporal dementia and parkinsonism linked to chromosome 17. Proc. Natl. Acad. Sci. U.S.A. 96 (1999) 8229-8234
356. Vega I.E., Cui L., Propst J.A., Hutton M.L., Lee G., and Yen S.H. Increase in tau tyrosine phosphorylation correlates with the formation of tau aggregates. Brain Res. Mol. Brain Res. 138 (2005) 135-144
357. Verpillat P., Ricard S., Hannequin D., Dubois B., Bou J., Camuzat A., Pradier L., Frebourg T., Brice A., Clerget-Darpoux F., Deleuze J.F., and Campion D. Is the Saitohin gene involved in neurodegenerative diseases?. Ann. Neurol. 52 (2002) 829-832
358. Vershinin M., Carter B.C., Razafsky D.S., King S.J., and Gross S.P. Multiple-motor based transport and its regulation by tau. Proc. Natl. Acad. Sci. U.S.A. 104 (2007) 87-92
359. Vigo-Pelfrey C., Seubert P., Barbour R., Blomquist C., Lee M., Lee D., Coria F., Chang L., Miller B., Lieberburg I., and Schenk D. Elevation of microtubule-associated protein tau in the cerebrospinal fluid of patients with Alzheimer's disease. Neurology 45 (1995) 788-793
360. Wang J.Z., Gong C.X., Zaidi T., Grundke-Iqbal I., and Iqbal K. Dephosphorylation of Alzheimer paired helical filaments by protein phosphatase-2A and -2B. J. Biol. Chem. 270 (1995) 4854-4860
361. Wang J.Z., Grundke-Iqbal I., and Iqbal K. Glycosylation of microtubule-associated protein tau: an abnormal posttranslational modification in Alzheimer's disease. Nat. Med. 2 (1996) 871-875
362. Wang J.Z., Grundke-Iqbal I., and Iqbal K. Restoration of biological activity of Alzheimer abnormally phosphorylated tau by dephosphorylation with protein phosphatase-1, -2A and -2B. Mol. Brain Res. 38 (1996) 200-208
363. Wang J.Z., Grundke-Iqbal I., and Iqbal K. Tau is phosphorylated by GSK-3 at several sites found in AD and its biological activity markedly inhibited only after it is prephosphorylated by A-kinase. FEBS Lett. 436 (1998) 28-34
364. Wang J.Z., Grundke-Iqbal I., and Iqbal K. Kinases and phosphatases and tau sites involved in Alzheimer neurofibrillary degeneration. Eur. J. Neurosci. 25 (2007) 59-68
365. Wang Q.B., and Wang J.Z. Injection of bradykinin or cyclosporine A to hippocampus induces Alzheimer-like phosphorylation of tau and abnormal behavior in rats. Chin. Med. J. 115 (2002) 884-887
366. Wang Y., Wang J., Gao L., Lafyatis R., Stamm S., and Andreadis A. Tau exons 2 and 10, which are misregulated in neurodegenerative diseases, are partly regulated by silencers which bind a SRp30c, SRp55 complex that either recruits or antagonizes htra2β1. J. Biol. Chem. 280 (2005) 14230-14239
367. Wang Y.P., Biernat J., Pickhardt M., Mandelkow E., and Mandelkow E.M. Stepwise proteolysis liberates tau fragments that nucleate the Alzheimer-like aggregation of full-length tau in a neuronal cell model. Proc. Natl. Acad. Sci. U.S.A. 104 (2007) 10252-10257
368. Wang Z.F., Li H.L., Li X.C., Zhang Q., Tian Q., Wang Q., Xu H., and Wang J.Z. Effects of endogenous beta-amyloid overproduction on tau phosphorylation in cell culture. J. Neurochem. 98 (2006) 1167-1175
369. Wataya T., Nunomura A., Smith M.A., Siedlak S.L., Harris P.L., Shimohama S., Szweda L.I., Kaminski M.A., Avila J., Price D.L., Cleveland D.W., Sayre L.M., and Perry G. High molecular weight neurofilament proteins are physiological substrates of adduction by the lipid peroxidation product hydroxynonenal. J. Biol. Chem. 277 (2002) 4644-4648
370. Weingarten M.D., Lockwood A.H., Hwo S.Y., and Kirschner M.W. A protein factor essential for microtubule assembly. Proc. Natl. Acad. Sci. U.S.A. 72 (1975) 1858-1862
371. Wen Y., Yang S., Liu R., Brun-Zinkernagel A.M., Koulen P., and Simpkins J.W. Transient cerebral ischemia induces aberrant neuronal cell cycle re-entry and Alzheimer's disease-like tauopathy in female rats. J. Biol. Chem. 279 (2004) 22684-22692
372. Williams A., Jahreiss L., Sarkar S., Saiki S., Menzies F.M., Ravikumar B., and Rubinsztein D.C. Aggregate-prone proteins are cleared from the cytosol by autophagy: therapeutic implications. Curr. Top. Dev. Biol. 76 (2006) 89-101
373. Wittmann C.W., Wszolek M.F., Shulman J.M., Salvaterra P.M., Lewis J., Hutton M., and Feany M.B. Tauopathy in Drosophila: neurodegeneration without neurofibrillary tangles. Science 293 (2001) 711-714
374. Witman G.B., Cleveland D.W., Weingarten M.D., and Kirschner M.W. Tubulin requires tau for growth onto microtubule initiating sites. Proc. Natl. Acad. Sci. U.S.A. 73 (1976) 4070-4074
375. Wood J.G., Mirra S.S., Pollock N.J., and Binder L.I. Neurofibrillary tangles of Alzheimer disease share antigenic determinants with the axonal microtubule-associated protein tau (tau). Proc. Natl. Acad. Sci. U.S.A. 83 (1986) 4040-4043 (erratum in: Proc. Natl. Acad. Sci. U.S.A. 83, 9773)
376. Wu J.Y., Kar A., Kuo D., Yu B., and Havlioglu N. SRp54 (SFRS11), a regulator for tau exon 10 alternative splicing identified by an expression cloning strategy. Mol. Cell. Biol. 26 (2006) 6739-6747
377. Xing Y., Xu Y., Chen Y., Jeffrey P.D., Chao Y., Lin Z., Li Z., Strack S., Stock J.B., and Shi Y. Structure of protein phosphatase 2A core enzyme bound to tumor-inducing toxins. Cell 127 (2006) 341-353
378. Xu G.G., Deng Y.Q., Liu S.J., Li H.L., and Wang J.Z. Prolonged Alzheimer-like tau hyperphosphorylation induced by simultaneous inhibition of phosphoinositol-3 kinase and protein kinase C in N2a cells. Acta Biochim. Biophys. Sin. (Shanghai) 37 (2005) 349-354
379. Xu Y., Xing Y., Chen Y., Chao Y., Lin Z., Fan E., Yu J.W., Strack S., Jeffrey P.D., and Shi Y. Structure of the protein phosphatase 2A holoenzyme. Cell 127 (2006) 1239-1251
380. Xu Y.F., Zhang Y.J., Zhang A.H., Zhang Q., Wu T., and Wang J.Z. Attenuation of okadaic acid-induced hyperphosphorylation of cytoskeletal proteins by heat preconditioning and its possible underlying mechanisms. Cell Stress Chaperones 9 (2004) 304-312
381. Yamagishia S., akamuraa K.N., Inoueb H., Kikuchic S., and akeuchid M. Serum or cerebrospinal fluid levels of glyceraldehyde-derived advanced glycation end products (AGEs) may be a promising biomarker for early detection of Alzheimer's disease. Med. Hypotheses 64 (2005) 1205-1207
382. 2+/calmodulin-dependent protein kinase II in neuronal soma in brain. J. Neurochem. 94 (2005) 1438-1447
383. Yan S.D., Chen X., Schmidt A.M., Brett J., Godman G., Zou Y.S., Scott C.W., Caputo C., Frappier T., Smith M.A., et al. Glycated tau protein in Alzheimer disease: a mechanism for induction of oxidant stress. Proc. Natl. Acad. Sci. U.S.A. 91 (1994) 7787-7791
384. Yan S.D., Yan S.F., Chen X., Fu J., Chen M., Kuppusamy P., Smith M.A., Perry G., Godman G.C., Nawroth P., et al. Non-enzymatically glycated tau in Alzheimer's disease induces neuronal oxidant stress resulting in cytokine gene expression and release of amyloid beta-peptide. Nat. Med. 1 (1995) 693-699
385. Yang Y., Yang X.F., Wang Y.P., Tian Q., Wang X.C., Li H.L., Wang Q., and Wang J.Z. Inhibition of protein phosphatases induces transport deficits and axonopathy. J. Neurochem. 102 (2007) 878-886
386. Yin H., and Kuret J. C-terminal truncation modulates both nucleation and extension phases of s fibrillization. FEBS Lett. 580 (2006) 211-215
387. Yoshida M. Cellular tau pathology and immunohistochemical study of tau isoforms in sporadic tauopathies. Neuropathology 26 (2006) 457-470
388. Yoshida H., and Goedert M. Molecular cloning and functional characterization of chicken brain tau: isoforms with up to five tandem repeats. Biochemistry 41 (2002) 15203-15211
389. Yu D.Y., Luo J., Bu F., Song G.J., Zhang L.Q., and Wei Q. Inhibition of calcineurin by infusion of CsA causes hyperphosphorylation of tau and is accompanied by abnormal behavior in mice. Biol. Chem. 387 (2006) 977-983
390. Zambrano C.A., Egaña J.T., Núñez M.T., Maccioni R.B., and González-Billault C. Oxidative stress promotes tau dephosphorylation in neuronal cells: the roles of cdk5 and PP1. Free Radic. Biol. Med. 36 (2004) 1393-1402
391. Zhang C.E., Tian Q., Wei W., Peng J.H., Liu G.P., Wang Q., Wang D.W., and Wang J.Z. Homocysteine induces tau hyperphosphorylation by inactivating protein phosphatase-2A. Neurobiol. Aging (May 2007) (Epub ahead of print)
392. 2+-dependent proteasome protease system. J. Neural Transm. 112 (2005) 547-555
393. Zhang Y., Li H.L., Wang D.L., Liu S.J., and Wang J.Z. A transitory activation of protein kinase-A induces a sustained tau hyperphosphorylation at multiple sites in N2a cells-imply a new mechanism in Alzheimer pathology. J. Neural Transm. 113 (2006) 1487-1497
394. Zhang Y.J., Xu Y.F., Liu X.H., Li D., Yin J., Liu Y.H., Chen X.Q., and Wang J.Z. Carboxyl terminus of h eat-shock cognate 70-interacting protein degrades tau regardless its phosphorylation status without affecting the spatial memory of the rats. J. Neural Transm. (February 2008) (Epub ahead of print)
395. Zhang Y.J., Xu Y.F., Chen X.Q., Wang X.C., and Wang J.Z. Nitric oxide induces tau hyperphosphorylation via glycogen synathase kinase-3B activation. FEBS Lett. 579 (2005) 6230-6236
396. Zhang Y.J., Xu Y.F., Chen X.Q., Wang X.C., and Wang J.Z. Nitration and oligomerization of tau induced by peroxynitrite inhibit its microtubule-binding activity. FEBS Lett. 579 (2005) 2421-2427
397. Zhang Y.J., Xu Y.F., Liu Y.H., Yin J., Li H.L., Wang Q., and Wang J.Z. Peroxynitrite induces Alzheimer-like tau modifications and accumulation in rat brain and its underlying mechanisms. FASEB J. 20 (2006) 1431-1442
398. Zhang X., Li F., Bulloj A., Zhang Y.W., Tong G., Zhang Z., Liao F.F., and Xu H. Tumor-suppressor PTEN affects tau phosphorylation, aggregation, and binding to microtubules. FASEB J. 20 (2006) 1272-1274
399. Zheng-Fischhofer Q., Biernat J., Mandelkow E.M., Illenberger S., Godemann R., and Mandelkow E. Sequential phosphorylation of tau by glycogen synthase kinase-3beta and protein kinase A at Thr212 and Ser214 generates the Alzheimer-specific epitope of antibody AT100 and requires a paired-helical-filament-like conformation. Eur. J. Biochem. 252 (1998) 542-555
400. Zhou F., Zhu X., Castellani R.J., Stimmelmayr R., Perry G., Smith M.A., and Drew K.L. Hibernation, a model of neuroprotection. Am. J. Pathol. 158 (2001) 2145-2151
401. Zhu L.Q., Wang S.H., Liu D., Yin Y.Y., Tian Q., Wang X.C., Wang Q., Chen J.G., and Wang J.Z. Activation of glycogen synthase kinase-3 inhibits long-term potentiation with synapse-associated impairments. J. Neurosci. 27 (2007) 12211-12220
402. Zhu L.Q., Wang S.H., Ling Z.Q., Wang D.L., and Wang J.Z. Effect of inhibiting melatonin biosynthesis on spatial memory retention and tau phosphorylation in rat. J. Pineal Res. 37 (2004) 71-77
403. Zhou L.X., Zeng Z.Y., Du J.T., Zhao Y.F., and Li Y.M. The self-assembly ability of the first microtubule-binding repeat from tau and its modulation by phosphorylation. Biochem. Biophys. Res. Commun. 348 (2006) 637-642
404. Zilka N., Filipcikm P., Koson P., Fialova L., Skrabana R., Zilkova M., Rolkova G., Kontsekova E., and Novak M. Truncated tau from sporadic Alzheimer's disease suffices to drive neurofibrillary degeneration in vivo. FEBS Lett. 580 (2006) 3582-3588