Molecular determinants of paired helical filament assembly and its therapeutic implications in Alzheimer's disease

References

• Anderson J.P., Esch F.S., Keim P.S., Sambamurti K., Lieberburg I., Robakis N.K. Exact cleavage site of Alzheimer amyloid precursor in neuronal PC-12 cells. Neuroscience Letters 1991; 128: 126–128
   PubMed Web of Science ®Google Scholar
• Anderson J.P., Chen Y., Kim K.S., Robakis N.K. An alternative secretase cleavage produces soluble Alzheimer amyloid precursor protein containing a potentially amyloidogenic sequence. Journal of Neurochemistry 1992; 2328–2331
   Google Scholar
• Anderton B.H., Breinburg D., Downes M.J., Green P.J., Tomlinson B.E., Ulrich J., Wood J.N., Kahn J. Monoclonal antibodies show that neurofibrillary tangles and neurofilaments share antigenic determinants. Nature 1982; 298: 84–86
   PubMed Web of Science ®Google Scholar
• Ariagada P.W., Growdon J.H., Hedley-White E.T., Hyman B.T. Neurofibrillary tangles but not senile plaques parallel duration and severity of Alzheimer's disease. Neurology 1992; 42: 631–639
   Google Scholar
• Arispe N., Pollard H.B., Rojas E. Giant multilevel cation channels formed by Alzheimer's disease amyloid β-protein [AβP-(1–40)] in bilayer membranes. Proceedings of the National Academy of Sciences, USA 1993; 90: 10573–10577
   PubMed Web of Science ®Google Scholar
• Ashall F., Goate A.M. Role of the β-amyloid precursor protein in Alzheimer's disease. Trends in Biochemical Sciences 1994; 19: 42–46
   PubMed Web of Science ®Google Scholar
• Bancher C., Grundke-Iqbal I., Iqbal K., Kim K.S., Wisniewski H.M. Immunoreactivity of neuronal lipofuscin with monoclonal antibodies to the amyloid β-protein. Neurobiology of Aging 1989; 10: 125–132
   PubMed Web of Science ®Google Scholar
• Barcikowska M., Wisniewski H.M., Bancher C., Grundke-Iqbal I. About the presence of paired helical filaments in dystrophic neurites participating in the plaque formation. Acta Neuropathologica 1989; 78: 225–231
   Google Scholar
• Baudier J., Lee S.-H., Cole R.D. Separation of the different microtubule-associated tau protein species from bovine brain and their mode II phosphorylation by Ca2+ /phospholipid-dependent protein kinase C. Journal of Biological Chemistry 1987; 62: 17584–17590
   Google Scholar
• Baumann K., Mandelkow E.M., Biernat J., Piwnica-Worms H., Mandelkow E. Abnormal Alzheimer-like phosphorylation of tau protein by cyclin-dependent kinases cdk2 and cdk5. FEBS Letters 1993; 336: 417–424
   PubMed Web of Science ®Google Scholar
• Behl C., Davis J., Cole G.M., Schubert D. Vitamin E protects nerve cells from amyloid protein toxicity. Biochemical and Biophysical Research Communications 1992; 186: 944–950
   PubMed Web of Science ®Google Scholar
• Bertoni-Freddari C., Fattoretti P., Pieroni M., Meier-Ruge W., Ulrich J. Enlargement of synaptic site as a compensative reaction in aging and dementia. Pathology and Research in Practice 1992; 188: 612–615
   PubMed Web of Science ®Google Scholar
• Biernat J.M., Mandelkow E.-M., Schroter C., Lichtenberg-Kraag B., Steiner B., Berling B., Meyer H., Mercken M., Vandermeeren A., Goedert M., Mandelkon E. The switch of tau protein to an Alzheimer-like state includes the phosphorylation of two serine-proline motifs upstream of the microtubule binding region. EMBO Journal 1992; 11: 1593–1597
   PubMed Web of Science ®Google Scholar
• 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
   PubMed Web of Science ®Google Scholar
• Binder L.I., Frankfurter A., Rebhun L.I. The distribution of tau in the mammalian central nervous system. Journal of Cell Biology 1985; 101: 1371–1378
   PubMed Web of Science ®Google Scholar
• Blass J.P., Baker A.C., Ko L.-W., Black R.S. Induction of antigens by an uncoupler of oxidative phosphorylation. Archives of Neurology 1990; 47: 864–869
   PubMedGoogle Scholar
• Blessed G., Tomlinson B.E., Roth M. The association between quantitative measures of dementia and of senile change in the cerebral grey matter of elderly subjects. British Journal of Psychiatry 1968; 114: 797–811
   PubMed Web of Science ®Google Scholar
• Bliss T.V., Collingridge G.L. A synaptic model of memory: long-term potentiation in the hippocampus. Nature 1993; 361: 31–39
   PubMed Web of Science ®Google Scholar
• Bondareff W., Wischik C.M., Novak M., Roth M. Sequestration of tau by granulovascular degeneration in Alzheimer's disease. American Journal of Pathology 1991; 139: 641–647
   Google Scholar
• Bondareff W., Mountjoy C.Q., Wischik C.M., Hauser D.L., LaBree L.D., Roth M. Evidence of subtypes of Alzheimer's disease and implications for etiology. Archives of General Psychiatry 1993; 50: 350–356
   PubMedGoogle Scholar
• Braak H., Braak E. Neuropathological stageing of Alzheimer-related changes. Acta Neuropathologica 1991; 82: 239–259
   PubMed Web of Science ®Google Scholar
• Braak H., Braak E., Grundke-Iqbal I., Iqbal K. Occurrence of neuropil threads in the senile human brain and in Alzheimer's disease: a third location of paired helical filaments outside of neurofibrillary tangles and neuritic plaques. Neuroscience Letters 1986; 65: 351–355
   PubMed Web of Science ®Google Scholar
• Bramblett G.T., Trojanowski J.Q., Lee V. M.-Y. Regions with abundant neurofibrillary pathology in human brain exhibit selective reduction in levels of binding-competent τ and accumulation of abnormal τ isoforms (A68 proteins). Laboratory Investigation 1992; 66: 212–222
   Google Scholar
• Brion J.P., Passareiro H., Nunez J., Flament-Durand J. Immunological detection of tau protein in neurofibrillary tangles of Alzheimer's disease. Archives de Biologie 1985; 95: 229–235
   Google Scholar
• Brion J.-P., Hanger D.P., Couck A.-M., Anderton B.M. A68 proteins in Alzheimer's disease are composed of several tau isoforms in a phosphorylated state which affects their electrophoretic mobilities. Biochemistry Journal 1991; 279: 831–836
   Google Scholar
• Brion J.P., Couck A.M., Robertson J., Loviny T.L.F., Anderton B.H. Neurofilament monoclonal antibodies RT97 and 8D8 recognize different modified epitopes in paired helical filament tau in Alzheimer's disease. Journal of Neurochemistry 1993; 60: 1372–1382
   Google Scholar
• Busciglio J., Gabuzda D.H., Matsudaira P., Yankner B.A. Generation of β-amyloid in the secretory pathway in neuronal and nonneuronal cells. Proceedings of the National Academy of Sciences, USA 1993a; 90: 2092–2096
   PubMed Web of Science ®Google Scholar
• Busciguo J., Yeh J., Yankner B.A. β-Amyloid neurotoxicity in human cortical culture is not mediated by excitotoxins. Journal of Neurochemistry 1993b; 61: 1565–1568
   Google Scholar
• Butner K.A., Kirschner M.W. Tau protein binds to microtubules through a flexible array of distributed weak sites. Journal of Cell Biology 1991; 15: 717–730
   Google Scholar
• Butterfield D.A., Hensley K., Harris M., Mattson M., Carney J. β-Amyloid peptide free radical fragments initiate synaptosomal lipoperoxidation in a sequence-specific fashion: implications to Alzheimer's disease. Biochemical and Biophysical Research Communications 1994; 200: 710–715
   PubMed Web of Science ®Google Scholar
• Buxbaum J.D., Gandy S.E., Cicchetti P., Ehruch M.E., Czernik A.J., Fracasso R.P., Ramabhadran T.V., Unterbeck A.J., Greengard P. Processing of Alzheimer β/A4 amyloid precursor protein: Modulation by agents that regulate protein phosphorylation. Proceedings of the National Academy of Sciences, USA 1990; 87: 6003–6006
   PubMed Web of Science ®Google Scholar
• Caceres A., Kosik K.S. Inhibition of neurite polarity by tau antisense oligonucleotides in primary cerebellar neurons. Nature 1990; 343: 461–463
   PubMed Web of Science ®Google Scholar
• Caporaso G.L., Gandy S.E., Buxbaum J.D., Ramabhadran T.V., Greengard P. Protein phosphorylation regulates secretion of Alzheimer β/A4 amyloid precursor protein. Proceedings of the National Academy of Sciences, USA 1992; 89: 3055–3059
   PubMed Web of Science ®Google Scholar
• Caputo C.B., Wischik C.M., Novak M., Scott C.W., Brunner W.F., Montejo de Garcini E., Lo M.S., Norris T.E., Salama A.I. Immunological characterization of the region of tau protein that is bound to Alzheimer paired helical filaments. Neurobiology and Aging 1992a; 13: 267–274
   Google Scholar
• Caputo C.B., Sygowski L.A., Scott C.W., Sobel I.R. Role of tau in the polymerisation of peptides from β-amyloid precursor protein. Brain Research 1992b; 597: 227–232
   Google Scholar
• Citron M., Oltersdorf T., Haas C., McConlogue L., Hunt A.Y., Seubert P., Vigopelfrey C., Leiberburg I., Selkoe D.J. Mutation of the β-amyloid precursor protein in familial Alzheimer's disease increased β-protein production. Nature 1992; 360: 672–674
   PubMed Web of Science ®Google Scholar
• Cleveland D.W., Hwo S.Y., Kirschner M. Purification of tau, a microtubule-associated protein that induces assembly of microtubules from purified tubulin. Journal of Molecular Biology 1977; 116: 207–225
   PubMed Web of Science ®Google Scholar
• Coleman P.D., Flood D.G. Neuron numbers and dendritic extent in normal aging and Alzheimer's disease. Neurobiology and Aging 1987; 8: 521–545
   PubMed Web of Science ®Google Scholar
• Coria F., Moreno A., Rubio I., Garcia M.A., Morato E., Mayor F., Jr. The cellular pathology associated with Alzheimer β-amyloid deposits in non-demented aged individuals. Neuropathology and Applied Neurobiology 1993; 19: 261–268
   PubMed Web of Science ®Google Scholar
• Corral-Debrinski M., Horton T., Lott M.T., Schoffner J.M., McKee A.C., Beal M.F., Graham B.H., Wallace D.C. Marked changes in mitochondrial DNA deletion levels in Alzheimer brains. Genomics 1994; 23: 471–476
   PubMedGoogle Scholar
• Correas I., Diaz-Nido J., Avila J. Microtubule-associated protein tau is phosphorylated by protein kinase C on its tubulin binding domain. Journal of Biological Chemistry 1992; 267: 15721–15728
   PubMed Web of Science ®Google Scholar
• Couchie D., Mavilia C., Georgieff I.S., Liem R.K.H., Shelanski M.L., Nunez J. Primary structure of high molecular weight tau present in the peripheral nervous system. Proceedings of the National Academy of Sciences, USA 1992; 89: 4378–4381
   Google Scholar
• Couchie D., Nunez J. Immunological characterization of microrubule-associated proteins for the immature brain. FEBS Letters 1985; 188: 331–335
   Google Scholar
• Crowther R.A. Tau protein and paired helical filaments of Alzheimer's disease. Current Opinion in Structural Biology 1993; 3: 202–206
   Google Scholar
• Crowther R.A., Wischik C.M. Image reconstruction of the Alzheimer paired helical filament. EMBO Journal 1985; 4: 3661–3665
   PubMed Web of Science ®Google Scholar
• Crowther R.A., Oleson O.F., Smith M.J., Jakes R., Goedert M. Assembly of Alzheimerlike filaments from full-length tau protein. FEBS Letters 1994; 337: 135–138
   PubMed Web of Science ®Google Scholar
• Crystal H., Dickson D., Fuld P., Masur D., Scott R., Mehler M., Masdew J., Kwas C., Aronson M., Wolfson L. Clinico-pathologic studies in dementia: Non-demented subjects with pathologically confirmed Alzheimer's disease. Neurology 1988; 38: 1682–1687
   PubMed Web of Science ®Google Scholar
• Davies C.A., Mann D.M.A., Sumpter P.Q., Yates P.O. A quantitative morphometric analysis of the normal and synaptic content of the frontal and temporal cortex in patients with Alzheimer's disease. Journal of Neurological Science 1987; 78: 151–164
   PubMed Web of Science ®Google Scholar
• Davies D.C., Horwood N., Isaacs S.L., Mann D.M.A. The effect of age and Alzheimer's disease on pyramidal neuron density in the individual fields of the hippocampal formation. Acta Neuropathologica 1992; 83: 510–517
   PubMedGoogle Scholar
• DeKosky S.T., Scheff S.W. Synapse loss in frontal cortex biopsies in Alzheimer's disease: correlation with cognitive severity. Annals of Neurology 1990; 7: 457–464
   Google Scholar
• Delacourte, Defossez. Alzheimer's disease: tau proteins, the promoting factors of microtubule assembly, a major component of paired helical filaments. Journal of Neurological Science 1986; 76: 173–186
   PubMed Web of Science ®Google Scholar
• Delaère P., Duyckaerts C., Masters C., Beyreuther K., Piette F., Hauw J.-J. Large amounts of neocortical βA4 deposits without neuritic plaques nor tangles in a psychometrically assessed, non-demented person. Neuroscience Letters 1990; 116: 87–93
   Google Scholar
• Delaère P., He Y., Fayet G., Duyckaerts C., Hauw J.-J. βA4 deposits are constant in the brain of the oldest old: an immunocytochemical study of 20 French centenarians. Neurobiology and Aging 1993; 14: 191–194
   PubMedGoogle Scholar
• Dickson D.W., Farlo J., Davies P., Crystal H., Fuld P., Yen S.-H.H2. Alzheimer's disease: a double-labeling immunohistochemical study of senile plaques. American Journal of Pathology 1988; 132: 86–101
   PubMed Web of Science ®Google Scholar
• Dlouhy S.R., Hsiao K., Farlow M.R., Faroud T., Conneally P.M., Johnson P., Prusiner S.B., Ghettt B. Linkage of the Indiana kindred of Gerstmann-Sträussler-Scheinker disease to the prion protein gene. Nature Genetics 1992; 1: 64–67
   PubMed Web of Science ®Google Scholar
• Dreschel D.N., Hyman A.A., Cobb M.H., Kirschner M.W. Modulation of the dynamic instability of tubulin assembly by the microtubule-associated protein tau. Molecular and Cellular Biology 1992; 3: 1141–1154
   Google Scholar
• Drewes G., Lichtenberg-Kraag B., Doring F., Mandelkow E.M., Biernat J., Doree M., Mandelkow E. Mitogen activated protein (MAP) kinase transforms tau protein into an Alzheimer-like state. EMBO Journal 1992; 11: 2131–2138
   PubMed Web of Science ®Google Scholar
• Drewes G., Mandelkow E.-M., Baumann K., Goris J., Merlevede W., Mandelkow E. Dephosphorylation of tau protein and Alzheimer paired helical filaments by calcineurin and phosphatase-2A. FEBS Letters 1993; 336: 425–432
   Google Scholar
• Drubin D.G., Kirschner M.W. Tau protein function in living cells. Journal of Cell Biology 1986; 103: 2739–2746
   PubMed Web of Science ®Google Scholar
• Dyrks T., Dyrks E., Hartmann T., Masters C.L., Beyreuther K. Amyloidogenicity of β/A4 and β/A4-bearing amyloid protein precursor fragments by metal-catalyzed oxidation. Journal of Biological Chemistry 1992; 267: 18210–18217
   PubMed Web of Science ®Google Scholar
• Englund E., Brun A., Alling C. White matter changes in dementia of Alzheimer's type. Biochemical and neuropathological correlates. Brain 1988; 111: 1425–1439
   PubMed Web of Science ®Google Scholar
• Esch F.S., Keim P.S., Beattie E.C., Blacher R.W., Culwell A.R., Oltersdorf T., McClure D., Ward P.J. Cleavage of amyloid β peptide during constitutive processing of its precursor. Science 1990; 248: 1122–1124
   PubMed Web of Science ®Google Scholar
• Flament S., Delacourte A., Delaère P., Duyckaerts C., Hauw J.-J. Correlation between microscopical changes and tau 64 and 69 biochemical detection in senile dementia of the Alzheimer type. Tau 64 and 69 are reliable markers of the neurofibrillary degeneration. Acta Neuropathologica 1990; 80: 212–215
   Google Scholar
• Folstein M.F., Folstein S.E., McHugh P.R. Mini-Mental State, a practical method for grading the cognitive state of patients for the clinican. Journal of Psychiatric Research 1975; 12: 189–198
   PubMed Web of Science ®Google Scholar
• Francon J., Lennon A.M., Fellous A., Mareck A., Pierre M., Nunez J. Heterogeneity of microrubule-associated proteins and brain development. European Journal of Biochemistry 1982; 129: 465–471
   Google Scholar
• Gabuzda D., Buscigua J., Chen L.B., Matsudaira P., Yankner B.A. Inhibition of energy metabolism alters the processing of amyloid precursor protein and induces a potentially amyloidogenic derivative. Journal of Biological Chemistry 1994; 269: 133623–13628
   Google Scholar
• Gambetti P., Perry G., Authjo-Gambetti L. Paired helical filaments: do they contain neurofilament epitopes?. Neurobiology of Aging 1986; 7: 451–452
   Google Scholar
• Geixerstedt N. Zue Kenntnis der Hirnveranderungen bei der normalen Altersinvolution. Upsala Läkaref, forh. 1933; 38: 193–408
   Google Scholar
• Gibson P.H. EM study of the numbers of cortical synapses in the brains of ageing people and people with Alzheimer-type dementia. Acta Neuropathologica 1983; 62: 127–133
   PubMed Web of Science ®Google Scholar
• Goedert M. Tau protein and the neurofibrillary pathology of Alzheimer's disease. Trends in Neuroscience 1993; 16: 460–465
   PubMed Web of Science ®Google Scholar
• Goedert M., Wischik C.M., Crowther R.A., Walker J.E., Klug A. Cloning and sequencing of the cDNA encoding a core protein of the paired helical filament of Alzheimer disease: identification as the microtubule-associated protein tau. Proceedings of the National Academy of Sciences, USA 1988; 85: 4051–4055
   PubMed Web of Science ®Google Scholar
• Goedert M., Spillantini M.G., Potier M.C., Ulrich J., 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 Journal 1989a; 8: 393–399
   PubMed Web of Science ®Google Scholar
• Goedert M., Spillantini M.G., Jakes R., Rutherford D., Crowther R.A. Multiple isoforms of human microtubule-associated protein tau: sequences and localization in neurofibrillary tangles of Alzheimer's disease. Neuron 1989b; 3: 519–526
   PubMed Web of Science ®Google Scholar
• Goedert M., Spillantini M.G., Jakes R. Localization of the Alz-50 epitope in recombinant human microtubule. Neuroscience Letters 1991; 126: 149–154
   Google Scholar
• Goedert M., Spillantini M.G., Cairns N.J., Crowther R.A. Tau proteins of Alzheimer paired helical filaments: abnormal phosphorylation of all six brain isoforms. Neuron 1992a; 8: 159–168
   PubMed Web of Science ®Google Scholar
• Goedert M., Cohen E.S., Jakes R., Cohen P. p42 MAP kinase phosphorylation sites in microtubule-associated protein tau are dephosphorylated by protein phosphatase 2A1. Implications for Alzheimer's disease. FEBS Letters 1992b; 312: 95–99
   PubMedGoogle Scholar
• Goedert M., Jakes R., Crowther R.A., Six J., Lubke U., Vandermeeren M., Cras P., Trojanowski J.Q., Lee V.M.Y. The abnormal phosphorylation of tau protein at Ser-202 in Alzheimer disease recapitulates phosphorylation during development. Proceedings of the National Academy of Sciences, USA 1993; 90: 5066–5070
   PubMedGoogle Scholar
• Goedert M., Jakes R., Spillantini M.-G., Crowther R.A. Tau proteins and Alzheimer's disease. Microtubules, J.S. Hyams, C.W. Lloyd. Alan R. Liss, New York 1994
   Google Scholar
• Golde T.E., Estus S., Younkin L.H., Selkoe D.J., Younkin S.G. Processing of the amyloid protein precursor to potentially amyloidogenic derivatives. Science 1992; 255: 728–730
   PubMed Web of Science ®Google Scholar
• Gong C.-X., Sing H.T.J., Grundke-Iqbal I., Iqbal K. Phosphoprotein phosphatase activities in Alzheimer disease brain. Journal of Neurochemistry 1993; 61: 921–927
   PubMed Web of Science ®Google Scholar
• Greenberg S.G., Davies P. A preparation of Alzheimer paired helical filaments that displays distinct tau proteins by polyacrylamide gel electrophoresis. Proceedings of the National Academy of Sciences, USA 1990; 87: 5827–5831
   PubMed Web of Science ®Google Scholar
• Grundke-Iqbal I., Iqbal K., Quinlan M., Tung Y.-C., Zaidi M.S., Wisniewski H.M. Microtubule-associated protein tau, a component of Alzheimer paired helical filaments. Journal of Biological Chemistry 1986a; 261: 6084–6089
   PubMed Web of Science ®Google Scholar
• Grundke-Iqbal I., Iqbal K., Tung Y.C., Quinlan M., Wisniewski H.M., Binder L.I. Abnormal phosphorylation of the microtubule-associated protein tau in Alzheimer cytoskeletal pathology. Proceedings of the National Academy of Sciences, USA 1986b; 83: 4913–4917
   PubMed Web of Science ®Google Scholar
• Gustke N., Steiner B., Mandelkow E.-M., Biernat J., Meyer H.E., Goedert M., Mandelkow E. The Alzheimer-like phosphorylation of tau protein reduces microtubule binding and involves Ser-Pro and Thr-Pro motifs. FEBS Letters 1992; 307: 199–205
   PubMed Web of Science ®Google Scholar
• Hanger D.P., Hughes K., Woodgett J.R., Brion J.P., Anderton B.H. Glycogen synthase kinase-3 induces Alzheimer's disease-like phosphorylation of tau: generation of paired helical filament epitopes and neuronal localization of the kinase. Neuroscience Letters 1992; 147: 58–62
   PubMed Web of Science ®Google Scholar
• Harrington C.R., Edwards P.C., Wischik C.M. Competitive ELISA for measurement of tau proteins in Alzheimer's disease. Journal of Immunological Methods 1990; 134: 261–271
   Google Scholar
• Harrington C.R., Mukaetova-Ladinska E.B., Hills R., Edwards P.C., Montejo de Garcini E., Novak M., Wischik C.M. Measurement of distinct immunochemical presentations of tau protein in Alzheimer disease. Proceedings of the National Academy of Sciences, USA 1991; 88: 5842–5846
   Google Scholar
• Harrington C.R., Wischik C.M., McArthur F.K., Taylor G.A., Edwardson J.A., Candy J.M. Alzheimer's-disease-like changes in tau protein processing: association with aluminium accumulation in brains of renal dialysis patients. The Lancet 1994a; 343: 993–997
   PubMedGoogle Scholar
• Harrington C.R., Perry R.H., Perry E.K., Hurt J., McKeith I.G., Roth M., Wischik C.M. Senile dementia of Lewy Body type and Alzheimer type are biochemically distinct in terms of paired helical filaments and hyperphosphorylated tau protein. Dementia 1994b; 5: 215–228
   PubMedGoogle Scholar
• Harrington C.R., Louwagie J., Rossau R., Vanmechelen E., Perry R.H., Perry E.K., Xuereb J., Roth M., Wischik C.M. The influence of apolipoprotein E genotype on senile dementia of the Alzheimer and Lewy body-types: significance for aetiological theories of Alzheimer's disease. American Journal of Pathology 1994c; 145: 1472–1484
   Google Scholar
• Harrington C.R., Roth M., Xuereb J.H., McKenna P.J., Wischik C. Apolipo-protein E type E4 allele frequency is increased in patients with schizophrenia. Neuroscience Letters 1995; 202: 101–104
   PubMed Web of Science ®Google Scholar
• Hasegawa M., Morishjma-Kawashima M., Takio K., Suzuki M., Titani K., Ihara Y. Protein sequence and mass spectrometric analyses of tau in Alzheimer's disease brain. Journal of Biological Chemistry 1992; 267: 17047–17054
   PubMedGoogle Scholar
• Hensley K., Carney J.M., Mattson M.P., Aksenova M., Harris M., Wu J.F., Floyd R.A., Butterfield D.A. A model for β-amyloid aggregation and neurotoxicity based on free radical generation by the peptide: relevance to Alzheimer disease. Proceedings of the National Academy of Sciences, USA 1994; 91: 3270–3274
   PubMed Web of Science ®Google Scholar
• Honer W.G., Dickson D.W., Gleeson J., Davies P. Regional synaptic pathology in Alzheimer's disease. Neurobiology and Aging 1992; 13: 375–382
   Google Scholar
• Huang D.Y., Weisgraber K.H., Goedert M., Saunders A.M., Roses A.D., Strittmatter W.J. ApoE3 binding to tau tandem repeat I is abolished by tau serine262 phosphorylation. Neuroscience Letters 1995; 192: 209–212
   Google Scholar
• Hubbard B.M., Anderson J.M. Age-related variations in the neuron content of the cerebral cortex in senile dementia of the Alzheimer type. Neuropathology, & Applied Neurobiology 1985; 11: 369–382
   Google Scholar
• Ihara Y., Nukina N., Miurar Ogawarra M. Phosphorylated tau protein is integrated into paired helical filaments in Alzheimer's disease. Journal of Biochemistry 1986; 99: 1807–1810
   PubMed Web of Science ®Google Scholar
• Ishiguro K., Ihara Y., Uchida T., Imahori K. A novel tubulin-dependent protein kinase forming a paired helical filament epitope on tau. Journal of Biochemistry 1988; 104: 319–321
   Google Scholar
• Ishiguro K., Omori A., Kato K., Tomizawa K., Imahori K., Uchida T. A serine/threonine proline kinase activity is included in the tau protein kinase fraction forming a paired helical filament epitope. Neuroscience Letters 1991; 128: 195–198
   Google Scholar
• Ishiguro K., Takamatsu M., Tomizawa K., Omori A., Takahashi M., Arioka M., Uchida T., Imahori K. Tau protein kinase I converts normal tau protein into A68-like component of paired helical filaments. Journal of Biological Chemistry 1992; 267: 10897–10901
   PubMed Web of Science ®Google Scholar
• Jacoby R.J., Levy R. Computed tomography in the elderly. 2. Senile-dementia: Diagnosis and functional impact. British Journal of Psychiatry 1980; 136: 256–269
   PubMed Web of Science ®Google Scholar
• Jakes R., Novak M., Edwards P., Wischik C.M. Identification of 3- and 4-repeat tau isoforms within the PHF in Alzheimer's disease. EMBO Journal 1991; 10: 2725–2729
   PubMed Web of Science ®Google Scholar
• Jancsik V., Filliol D., Felter S., Rendon A. Binding of microtubule-associated proteins to rat brain mitochondria: a comparative study of binding of MAP2, its microtubule-binding and projection domains, and tau proteins. Cell Motility and Cytoskeleton 1989; 14: 372–381
   Google Scholar
• Jarret J.T., Lansbury P.T. Seeding one-dimensional crystallization of amyloid—a pathogenic mechanism in Alzheimer's disease and scrapie. Cell 1993; 73: 1055–1058
   PubMedGoogle Scholar
• Jobst K.A., Smith A.D., Szatmari M., Esiri M.M., Jaskowski A., Hindley N., McDonald B., Molyneux A.J. Rapidly progressing atrophy of medial temporal lobe in Alzheimer's disease. The Lancet 1994; 343: 829–830
   Google Scholar
• Katzman R., Terry R.D., DeTeresa R., Brown T., Davies P., Fuld P., Renbing X., Peck A. Clinical, pathological, and neurochemical changes in dementia: A subgroup with preserved mental status and numerous neocortical plaques. Annals of Neurology 1988; 23: 138–144
   PubMed Web of Science ®Google Scholar
• Kidd M., Allsop D., Landon M. Senile plaque amyloid, paired helical filaments and cerebrovascular amyuloid, in Alzheimer's disease are all deposits of the same protein. The Lancet 1985; 1: 278
   Google Scholar
• Kocisko D.A., Come J.H., Priola S.A., Chesebro B., Raymond G.J., Lansbury P.T., Caughey B. Cell-free formation of protease-resistant prior protein. Nature 1994; 370: 471–474
   PubMed Web of Science ®Google Scholar
• Kosik K.S., Joachim C.L., Selkoe D.J. Microtubule associated protein tau is a major antigenic component of paired helical filaments in Alzheimer disease. Proceedings of the National Academy of Sciences, USA 1986; 83: 4044–4048
   PubMed Web of Science ®Google Scholar
• Kosik K.S., Orecchio L.D., Binder L., Trojanowski J.Q., Lee V.M.Y., Lee G. Epitopes that span the tau molecule are shared with paired helical filaments. Neuron 1988; 1: 817–825
   PubMedGoogle Scholar
• Ksiezak-Reding H., Wall J.S. Mass and physical dimensions of two distinct populations of paired helical filaments. Neurobiology of Aging 1994; 15: 11–19
   Google Scholar
• Kzieszak-Reding H., Binder L.I., Yen S.H. Immunochemical and biochemical characterization of τ proteins in normal and Alzheimer's disease brains with Alz50 and Tau-1. Journal of Biological Chemistry 1988; 263: 7948–7953
   Google Scholar
• Lai R.Y.K. Role of phosphorylation of tau protein in neurofibrillary pathology in Alzheimer's disease. PhD Thesis, University of Cambridge, Cambridge 1995
   Google Scholar
• Lai R.Y.K., Gertz H.J., Wischik D.J., Xuereb J.H., Mukaetova-Ladinska E.B., Harrington C.R., Edwards P.C., Mena R., Paykel E.S., Brayne C., Huppert F.A., Roth M., Wischik C.M. Examination of phosphorylated tau protein as a PHF-precursor at early stage Alzheimer's disease. Neurobiology of Aging 1995; 16: 433–445
   Google Scholar
• Ledesma M.D., Correas I., Avila J., Diaz-Nido J. Implication of brain cdc2 and MAP2 kinases in the phosphorylation of tau protein in Alzheimer's disease. FEBS Letters 1992; 308: 218–224
   Google Scholar
• Lee V. M.-Y., Trojanowski J.Q. The disordered neuronal cytoskeleton in Alzheimer's disease. Current Opinion in Neurobiology 1992; 2: 653–656
   PubMed Web of Science ®Google Scholar
• Lee V. M.-Y., Balin B.J., Otvos L., Trojanowski J.Q. A68: a major subunit of paired helical filaments and derivatized forms of normal tau. Science 1991; 251: 675–678
   PubMed Web of Science ®Google Scholar
• Lichtenberg-Kraag B., Mandelkow E.M., Biernat J., Steiner B., Schroter C., Gustke N., Meyer H.E., Mandelkow E. Phosphory-larion-dependent epitopes of neurofilament antibodies on tau protein and relationship with Alzheimer tau. Proceedings of the National Academy of Sciences, USA 1992; 89: 5384–5388
   Google Scholar
• Linnane A.W., Marzuki S., Ozawa T., Tanaka M. Mitochondrial DNA mutations as an important contribution to aging and degenerative diseases. The Lancet 1989; i: 642–645
   Google Scholar
• Lippa C.F., Hamos J.E., Pulaski-Salo D., Degennaro L.J., Drachman D.A. Alzheimer's disease and aging: Effects of perforant pathway perikarya and synapses. Neurobiology of Aging 1992; 13: 405–411
   Google Scholar
• Liu W.K., Moore W.T., Williams R.T., Hall F.L., Yen S.H. Application of synthetic phospho- and unphosphopeptides to identify phosphorylation sites in a subregion of the tau molecule, which is modified in Alzheimer's disease. Journal of Neuroscience Research 1993; 34: 371–376
   Google Scholar
• Mandelkow E.-M., Drewes G., Biernat J., Gustke N., Van Lint J., Vandenheede J.R., Mandelkow E. Glycogen synthase kinase-3 and the Alzheimer-like state of microtubule-associated protein tau. FEBS Letters 1992; 314: 315–321
   PubMed Web of Science ®Google Scholar
• Mann D.M.A., Marcyniuk B., Yates P.O., Neary D., Snowdon J.S. The progression of the pathological changes of Alzheimer's disease in frontal and temporal neocortex examined both at biopsy and at autopsy. Neuropathology and Applied Neurobiology 1988; 14: 177–195
   PubMed Web of Science ®Google Scholar
• Masliah E., Terry R.D. The role of synaptic proteins in the pathogenesis of disorders of the central nervous system. Brain Pathology 1993; 3: 77–85
   PubMed Web of Science ®Google Scholar
• Masliah E., Terry R.D., DeTeresa R., Hauser L.A. Immunohistochemical quantification of the synapse-related protein synaptophysin in Alzheimer's disease. Neuroscience Letters 1989; 103: 234–239
   PubMed Web of Science ®Google Scholar
• Masliah E., Terry R.D., Mallory M., Alford M., Hansen L.A. Diffuse plaques do not accentuate synapse loss in Alzheimer's disease. American Journal of Pathology 1990; 137: 1293–1297
   PubMed Web of Science ®Google Scholar
• Masliah E., Terry R.D., Alford M., DeTeresa R., Hansen L.A. Conical and subcortical patterns of synaptophysin-like immunoreactivity in Alzheimer's disease. American Journal of Pathology 1991; 138: 235–246
   PubMed Web of Science ®Google Scholar
• Masliah E., Miller A., Terry R.D. The synaptic organization of the neocortex in Alzheimer's disease. Medical Hypotheses 1993; 41: 334–340
   Google Scholar
• Masters C.L., Multhaup G., Simms G., Pottgiesser J., Martins R.N., Beyreuther K. Neuronal origin of a cerebral amyloid: neurofibrillary tangles of Alzheimer's disease contain the same protein as the amyloid of plaque cores and blood vessels. EMBO Journal 1985; 4: 2757–2763
   PubMed Web of Science ®Google Scholar
• Matsuo E.S., Shin R.-W., Billingsley M.L., Van DeVoorde A., O'Connor M., Trojanowski J.Q., Lee V. M.-Y. Biopsy-derived adult human brain tau is phosphorylated at many of the same sites as Alzheimer's disease paired helical filament tau. Neuron 1994; 13: 989–1002
   PubMedGoogle Scholar
• Mattis S. Geriatric Psychiatry, L. Bellak, T.B. Karasu. Grune, & Stratton, New York 1976; 77–121
   Google Scholar
• Mattson M.P., Engle M.G., Rychlik B. Effects of elevated intracellular calcium levels on the cytoskeleton and tau in cultured human cerebral cortical neurons. Molecular Chemistry and Neuropathology 1991; 15: 117–142
   PubMedGoogle Scholar
• Mattson M.P., Cheng B., Davis D., Bryant K., Lieberburg I., Rydel R.E. β-amyloid peptides destabilize calcium homeostasis and render human cortical neurons vulnerable to excitotoxicity. Journal of Neuroscience 1992; 12: 376–389
   PubMed Web of Science ®Google Scholar
• Mattson M.P., Barger S.W., Cheng B., Lieberburg I., Smith-Swintosky V.L., Rydel R.E. β-amyloid precursor protein metabolites and loss of neuronal Ca2+ homeostasis in Alzheimer's disease. Trends in Neuroscience 1993; 16: 409–414
   PubMed Web of Science ®Google Scholar
• Mawal-Dewan M., Sen P.C., Abdel-Ghany M., Shalloway D., Racker F. Phosphorylation of tau protein by purified p34cdc28 and a related protein kinase from neurofilaments. Journal of Biological Chemistry 1992; 267: 19705–19709
   Google Scholar
• Mecocci P., MacGarvey U., Beal M.F. Oxidative damage to mitochondrial DNA is increased in Alzheimer's disease. Annals of Neurology 1994; 36: 747–751
   PubMed Web of Science ®Google Scholar
• Mena R., Wischik C.M., Novak M., Milstein C., Cuello A.C. A progressive deposition of paired helical filaments (PHF) in the brain characterizes the evolution of dementia in Alzheimer's disease: An immunocytochemical study with a monoclonal antibody against the PHF core. Journal of Neuropathology and Experimental Neurology 1991; 50: 474–490
   Google Scholar
• Mena R., Edwards P., Perez-Olvera O., Wischik C.M. Monitoring padiological assembly of tau and β-amyloid proteins in Alzheimer's disease. Acta Neuropathologica 1995; 89: 50–56
   Google Scholar
• Mena R., Edwards P., Harrington C.R., Mukaetova-Ladinska E., Wischik C.M. Staging the pathological assembly of truncated tau protein into paired helical filaments in Alzheimer's disease. Acta Neuropathologica 1996, in press
   Google Scholar
• Miller C.C.J., Brion J.-P., Calvert R., Chin T.K., Eagles P.A.M., Downes M.J., Flament-Durant J., Haugh M., Kahn J., Probst A., Ulrich J., Anderton B.H. Alzheimer's paired helical filaments share epitopes wim neurofilament sidearms. EMBO Journal 1986; 5: 269–276
   Google Scholar
• Montejo de Garcini E., Corrachano L., Wischik C.M., Diaz Nido J., Correas I., Avila J. Differentiation of neuroblastoma cells correlates widi an altered splicing pattern of tau RNA. FEBS Letters 1992; 299: 10–14
   PubMedGoogle Scholar
• Mori H., Kondo J., Ihara Y. Ubiquitin is a component of paired helical filaments in Alzheimer's disease. Science 1987; 235: 1641–1644
   PubMed Web of Science ®Google Scholar
• Morris R.G.M. Does synaptic plasticity play a role in information storage in the vertebrate brain?. Parallel Distributed Processing: Implications for Psychology and Neurobiology, R.G.M. Morris. Oxford University Press, Oxford 1989
   Google Scholar
• Mountjoy C.Q., Roth M., Evans N.J.R., Evans H.M. Cortical neuronal counts in normal elderly controls and demented patients. Neurobiology and Aging 1983; 4: 1–11
   PubMed Web of Science ®Google Scholar
• Mukaetova-Ladinska E.B., Harrington C.R., Roth M., Wischik C.M. Biochemical and anatomical redistribution of tau protein in Alzheimer's disease. American Journal of Pathology 1993; 143: 565–578
   PubMed Web of Science ®Google Scholar
• Murayama S., Bouldin T.W., Suzuki K. Diffuse plaques in non-demented population. Journal of Neuropathology and Experimental Neurology 1991; 50: 303, abstract
   Google Scholar
• Neary D., Snowdon J.S., Mann D.M.A., Bowen D.M., Sims N.R., Northen B., Yates P.O., Davison A.N. Alzheimer's disease: a correlative study. Journal of Neurology, Neurosurgery and Psychiatry 1986; 49: 229–237
   PubMed Web of Science ®Google Scholar
• Neupert W. Transport of proteins across mitochondrial membranes. Clinical Investment 1994; 72: 251–261
   PubMedGoogle Scholar
• Neve R.L., Kammesheidt A., Hohmann C.F. Brain transplants of cells expressing the carboxyl-terminal fragment of the Alzheimer amyloid protein precursor cause specific neuropathology in vivo. Proceedings of the National Academy of Sciences, USA 1992; 89: 3448–3452
   PubMedGoogle Scholar
• Novak M., Kabat J., Wischik C.M. Molecular characterization of the minimal protease resistant tau unit of the Alzheimer's disease paired helical filament. EMBO Journal 1993; 12: 365–370
   PubMed Web of Science ®Google Scholar
• Nukina N., Ihara Y. One of the antigenic determinants of paired helical filaments is related to tau protein. Journal of Biochemistry 1986; 99: 1541–1544
   PubMed Web of Science ®Google Scholar
• Nukina N., Kosik K.S., Selkoe D.J. The monoclonal antibody, Alz 50, recognizes tau proteins in Alzheimer's disease brain. Neuroscience Letters 1988; 87: 240–246
   Google Scholar
• Ouver C., Holland A.J. Down's syndrome and Alzheimer's disease: a review. Psychologicial Medicine 1986; 16: 307–322
   Google Scholar
• Oltersdorf T., Fritz L.C., Schenk D.B., Lieberburg I., Johnson-Wood K.L., Beattie E.C., Ward P.J., Blacher R.W., Dovey H.F., Sinha S. The secreted form of Alzheimer's amyloid precursor protein with the Kunitz domain to protease nexin-II. Nature 1989; 341: 144–147
   PubMed Web of Science ®Google Scholar
• Palmer D.N., Martinus R.D., Cooper S.M., Midwinter G.G., Reid J.C., Jolly R.D. Ovine ceroid lipofuscinosis. The major lipopigment protein and the lipid-binding subunit of mitochondrial ATP synthetase have the same NH2-terminal sequence. Journal of Biological Chemistry 1989; 264: 5736–5740
   PubMed Web of Science ®Google Scholar
• Pan K.-M., Baldwin M., Nguyen I., Gasset M., Serban A., Groth D., Melhorn I., Huang Z., Fletterick R.J., Cohen F.E., Prusiner S.B. Conversion of α-helices into β-sheets features in the formation of scrapie prion proteins. Proceedings of the National Academy of Sciences, USA 1993; 90: 10962–10966
   PubMed Web of Science ®Google Scholar
• Papasozomenos S. Ch., Binder L.I. Phosphorylation determines two distinct species of tau in the central nervous system. Cell Motility and Cytoskeleton 1987; 8: 210–226
   PubMed Web of Science ®Google Scholar
• Paykel E.S., Brayne C., Huppert F.A., Gill C., Barkley C., Gehlaar E., Beardsall L., Girling D.M., Pullitt P., O'Connor D. Incidence of dementia in a population older than 75 years in the United Kingdom. Archives of General Psychiatry 1994; 51: 325–332
   PubMedGoogle Scholar
• Perry E.K., Perry R.H., Blessed G., Tomlinson B.E. Necropsy evidence of central cholinergic deficits in senile dementia. The Lancet 1977; i: 189
   Google Scholar
• Perry G., Rizzuto N., Autilio-Gambetti L., Gambetti P. Paired helical filaments from Alzheimer disease patients contain cytoskeletal components. Proceedings of the National Academy of Sciences, USA 1985; 82: 3916–3920
   PubMed Web of Science ®Google Scholar
• Perry G., Friedman R., Shaw G., Chau V. Ubiquitin is detected in neurofibrillary tangles and senile plaque neurons of Alzheimer's disease brains. Proceedings of the National Academy of Sciences, USA 1987; 84: 3033–3036
   PubMed Web of Science ®Google Scholar
• Pfefferbaum A., Sullivan E.V., Jemigan T.L., Zipursky R.B., Rosenbloom M.J., Yesavage J.A., Tinklenberg J.R. A quantitative analysis of CT and cognitive measures in normal aging, & Alzheimer's disease. Psychiatric Research 1990; 35: 115–136
   Google Scholar
• Pierre M., Nunez J. Multisite phosphorylation of tau proteins from rat brain. Biochemical and Biophysical Research Communication 1983; 115: 212–219
   Google Scholar
• Pike C.J., Burdick WalencewiczA.J., Glabe C.J., Cotman C.W. Neurodegeneration induced by β-amyloid peptides in vitro: The role of peptide assembly state. Journal of Neuroscience 1993; 13: 1676–1687
   PubMed Web of Science ®Google Scholar
• Pizzi M., Valerio A., Arrighi V., Galu P., Belloni M., Ribola M., Alberici A., Spano P.F., Memo M. Inhibition of glutamate-induced neurotoxicity by a tau antisense oligonucleotide in primary culture of rat cerebellar granule cells. European Journal of Neuroscience 1995; 7: 1603–1613
   Google Scholar
• Poulter L., Barratt D., Scott C.W., Caputo C.B. Locations and immunoreactivities of phosphorylation sites on bovine and porcine tau proteins and a PHF-tau fragment. Journal of Biological Chemistry 1993; 268: 9636–9644
   Google Scholar
• Prusiner S.B. Biology and genetics of prion diseases. Annual Review of Microbiology 1994; 48: 655–686
   PubMed Web of Science ®Google Scholar
• Rendon A., Jung D., Jancsik V. Interactions of microtubules and microtubule-associated proteins (MAPs) with rat brain mitochondria. Journal of Biochemistry 1990; 269: 555–556
   Google Scholar
• Resch J.F., Lehr G.S., Wischik C.M. Design and synthesis of a potential affinity/cleaving reagent for beta-pleated sheet protein structures. Biorganic and Medicinal Chemistry Letters 1991; 1: 519–522
   Google Scholar
• Riederer B.M., Innocenti G.M. Differential distribution of tau proteins in developing cat cerebral cortex and corpus callosum. European Journal of Neuroscience 1991; 3: 1134–1145
   Google Scholar
• Roder H.M., Ingram V.M. Two novel kinases phosphorylate tau and the KSP site of heavy neurofilament subunits in high stoichiometric ratios. Journal of Neuroscience 1991; 11: 3325–3343
   PubMedGoogle Scholar
• Rubenstein R., Kascsak R.J., Merz P.A., Wisniewski H.M., Carp R.I., Iqbal K. Paired helical filaments associated with Alzheimer's disease are readily soluble structures. Brain Research 1986; 372: 80–88
   Google Scholar
• Saitoh T., Sundsmo M., Roch J.-M., Kimura M., Cole G., Schubert D., Oltersdorf T., Schenk D.B. Secreted form of amyloid β-protein precursor is involved in the growth regulation of fibroblasts. Cell 1989; 58: 615–622
   PubMed Web of Science ®Google Scholar
• Scheff S.W., Price D.A. Synapse loss in the temporal lobe in Alzheimer's disease. Annals of Neurology 1993; 33: 190–199
   PubMed Web of Science ®Google Scholar
• Schellenberg G.D. Genetic dissection of Alzheimer disease, a heterogeneous disorder. Proceedings of the National Academy of Sciences, USA 1995; 92: 8552–8559
   PubMed Web of Science ®Google Scholar
• 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 asssembly. Journal of Biological Chemistry 1993; 268: 1166–1173
   PubMed Web of Science ®Google Scholar
• Seubert P., Oltersdorf T., Lee M.G., Barbour R., Blomquist C., Davis D.L., Bryant K., Fritz L.C., Galasko D., Thal L.J., Schenk D.B. Secretion of β-amyloid precursor protein cleaved at the amino terminus of the β-amyloid precursor protein cleaved at the amino terminus of the β-amyloid peptide. Nature 1993; 361: 260–263
   PubMed Web of Science ®Google Scholar
• Shankar S.Y., Yanagihara R., Garruto R.M., Grundke-Iqbal I., Kosik K.S., Gajdusek D.C. Immunocytochemical characterization of neurofibrillary tangles in amyotrophic lateral sclerosis in parkinsonism-dementia of Guam. Annals of Neurology 1989; 225: 146–151
   Google Scholar
• Shaw G., Chau V. Ubiquitin and microtubule-associated protein tau immunoreactivity each define distinct structures with differing distributions and solubility properties in Alzheimer brain. Proceedings of the National Academy of Sciences, USA 1988; 85: 2854–2858
   PubMedGoogle Scholar
• Shearman M.S., Ragan C.I., Iversen I.I. Inhibition of PC 12 cell redox activity is a specific, early indicator of the mechanism of β-amyloid mediated cell death. Proceedings of the National Academy of Sciences, USA 1994; 91: 1470–1474
   PubMed Web of Science ®Google Scholar
• Shin R.-W., Bramblett G.T., Lee V. M.-Y., Trojanowski J.Q. Alzheimer disease A68 proteins injected into rat brain induce codeposits of β-amyloid, ubiquitin, and 1-antichymotrypsin. Proceedings of the National Academy of Sciences, USA 1993; 90: 6825–6828
   PubMed Web of Science ®Google Scholar
• Simchowitz T. Histologische Studien über die senile Demenz. Histologische und Histopathologische Arbeiten über die Grosshimrinde mix besonderer Berucksichtlgung der pathologischen Anatomic der Geisteskraukheiten, F. Nissl, A. Alzheimer. Fischer, Jena 1911; vol. 4: 267–444
   Google Scholar
• Steiner B., Mandelkow E.-M., Biernat J., Gustke N., Meyer H.E., Schmidt B., Mieskes G., Soling H.D., Drechsel D., Kirschner M.W., Goedert M., Mandelkow E. Phosphorylation of microtubule-associated protein tau: identification of the site of Ca2+ -calmodulin dependent kinase and the relationship with tau phosphorylation in Alzheimer tangles. EMBO Journal 1990; 9: 3539–3544
   PubMed Web of Science ®Google Scholar
• Sternberger N.H., Sternberger L.A., Ulrich J. Aberrant neurofilament phosphorylation in Alzheimer's disease. Proceedings of the National Academy of Sciences, USA 1985; 82: 4272–4276
   Google Scholar
• Strittmatter W.J., Weisgraber K.H., Huang D.Y., Dong L.-M., Salvesen G.S., Pericak-Vance M., Schmechel D., Saunders A.M., Goldgaber D., Roses A.D. Binding of human apolipoprotein E to symhetic amyloid β-peptide: isoform-specific effects and implications for the late-onset Alzheimer disease. Proceedings of the National Academy of Sciences, USA 1993; 90: 8089–8102
   Google Scholar
• Tabaton M., Mandybur T.I., Perry G., Onorato M., Autiuo-Gambetti L., Gambetti I. The widespread alteration of neurites in Alzheimer's disease may be unrelated to amyloid deposition. Annals of Neurology 1989; 26: 771–778
   PubMed Web of Science ®Google Scholar
• Takashima A., Noguchi K., Sato K., Hoshino T., Imahori K. Tau protein kinase I is essential for amyloid β-protein induced neurotoxicity. Proceedings of the National Academy of Sciences, USA 1993; 90: 7789–7793
   PubMed Web of Science ®Google Scholar
• Terry R.D., Masuah E., Salmon D.P., Butters N., DeTeresa R., Hill R., Hansen L.A., Katzman R. Physical basis of cognitive alterations in Alzheimer's disease: synapse loss is the major correlate of cognitive impairment. Annals of Neurology 1991; 30: 572–580
   PubMed Web of Science ®Google Scholar
• Troncoso J.C., Costello A., Watson A. L., Jr., Johnson G.V.W. In vitro polymerization of oxidised tau into filaments. Brain Research 1993; 613: 313–316
   PubMedGoogle Scholar
• Ueda K., Fukui Y., Kageyama H. Compromise of mitochondrial function induced by amyloid β-protein in PC 12 cells and protection by cyclic AMP-dependent protein kinase inhibitors. Neuroscience Research Communication 1994; 15: 195–200
   Google Scholar
• Ulrich J. Alzheimer changes in nondemented patients younger than sixy-five: possible early stages of Alzheimer's disease and senile dementia of Alzheimer type. Annals of Neurology 1985; 17: 273–277
   PubMed Web of Science ®Google Scholar
• Van Hoesen G.W., Damasio A.R. Neural correlates of cognitive impairment in Alzheimer's disease. Handbook of Physiology. The Nervous System 1990; V: 871–898
   Google Scholar
• Vogelsang G.D., Zemlan F.P., Dean G.E. Untangling the insoluble: a characterisation of Alzheimer's paired helical filaments. The Molecular Biology of Alzheimer's Disease, C.E. Finch, T. Davies. Current Communications in Molecular Biology, Cold Spring Harbor Publications. 1988; 150–158
   Google Scholar
• Vulliet R., Halbran S.M., Braun R.K., Smith A.J., Lee G. Proline-directed phosphorylation of human tau protein. Journal of Biological Chemistry 1992; 267: 22570–22574
   PubMedGoogle Scholar
• Wallace D.C. Mitochondrial DNA sequence variation in human evolution and disease. Proceedings of the National Academy of Sciences, USA 1994; 91: 8739–8746
   PubMed Web of Science ®Google Scholar
• White P., Hiley C.R., Goodhardt M.J., Carrasco L.H., Williams I.E.I., Bowen D.M. Neocortical cholinergic neurons in elderly people. The Lancet 1977; i: 668–670
   Google Scholar
• Wilcock G.K., Esiri M.M. Plaques, tangles and dementia: a quantitative study. Journal of Neurological Sciences 1982; 56: 407–417
   Google Scholar
• Wischik C.M., Crowther R.A., Stewart M., Roth M. Subunit structure of paired helical filaments in Alzheimer's disease. Journal of Cell Biology 1985; 100: 1905–1912
   Google Scholar
• Wischik C.M., Novak M., Thogersen H.C., Edwards P.C., Runswick M.J., Jakes R., Walker J.E., Milstein C., Roth M., Klug A. Isolation of a fragment of tau derived from the core of the paired helical filament of Alheimer disease. Proceedings of the National Academy of Sciences, USA 1988a; 85: 4506–4510
   PubMed Web of Science ®Google Scholar
• Wischik C.M., Novak M., Edwards P.C., Klug A., Tichelaar W., Crowther R.A. Structural characterization of the core of the paired helical filament of Alzheimer disease. Proceedings of the National Academy of Sciences, USA 1988b; 85: 4884–4888
   PubMed Web of Science ®Google Scholar
• Wischik C.M., Edwards P.C., Lai R.Y.K., Gertz H.J., Xuereb J.H., Paykel E.S., Brayne C., Huppert F.A., Mukaetova-Ladinska E.B., Mena R., Roth M., Harrington C.R. Quantitative analysis of tau protein in paired helical filament preparations: implications for the role of tau protein phosphorylation in PHF assembly in Alzheimer's disease. Neurobiology of Aging 1995a; 16: 409–417
   PubMed Web of Science ®Google Scholar
• Wischik C.M., Harrington C.R., Lai R.Y.K., Mukaetova-Ladinska E.B., Xuereb J.H., Gertz H., Wischik D.J., Edwards P.C., Mena R., Roth M., et al. Authors' response to commentaries. Neurobiology of Aging 1995b; 16: 423–431
   Google Scholar
• Wischik C.M., Edwards P.C., Harrington C.R. The tau protein amyloidosis of Alzheimer's disease: its mechanisms, potential trigger factors and consequences. Neurobiology of Alzheimer's Disease, D. Dawbarn, S.J. Allen. BIOS Scientific, Oxford 1995c
   Google Scholar
• Wischik C.M., Lai R., Harrington C.R., Mukaetova-Ladinska E.B., Xuereb J.H., Mena R., Edwards P.C., Roth M. Structure and biochemistry and molecular pathogenesis of paired helical filaments in Alzheimer's disease. Pathology of Alzheimer's disease, A. Goate, F. Ashall. Academic Press, USA 1995d
   Google Scholar
• Wisniewski K.E., Masunska D., Kttaguchi T., Kim K.S., Goebel H.H., Haltia M. Topographic heterogeneity of amyloid β-protein epitopes in brains with various forms of neuronal ceroid lipofuscinoses, suggesting defective processing of amyloid precursor protein. Acta Neuropathologica 1990; 80: 26–34
   PubMed Web of Science ®Google Scholar
• Wolozin B.L., Pruchnicki A., Dickson D.W., Davies P. A neuronal antigen in the brains of Alzheimer patients. Science 1986; 232: 648–650
   PubMed Web of Science ®Google Scholar
• Wood J.G., Mirra S.S., Pollock N.J., Binder L.I. Neurofibrillary tangles of Alzheimer disease share antigenic determinants with the axonal microtubule-associated protein tau. Proceedings of the National Academy of Sciences, USA 1986; 83: 4040–4043
   PubMed Web of Science ®Google Scholar
• Yamamoto H., Fukunaga K., Tanaka E., Miyamoto E. Ca2+- and calmodulin-dependent phosphorylation of microtubule-associated protein 2 and tau factor, and inhibition of microtubule assembly. Journal of Neurochemistry 1983; 41: 1119–1126
   Google Scholar
• Yankner B.A., Caceres A., Duffy L.K. Nerve growth factor potentiates the neurotoxicity of β-amyloid. Proceedings of the National Academy of Sciences, USA 1990; 87: 9020–9023
   PubMed Web of Science ®Google Scholar
• Yen S.-H., Gaskin F., Fu S.M. Neurofibrillary tangles in senile dementia of the Alzheimer type share an antigenic determinant with intermediate filaments of the vimentin class. American Journal of Pathology 1983; 113: 373–381
   Google Scholar
• Yen S.-H., Dickson D.W., Butler M., Shelanski M.L. Alzheimer's neurofibrillary tangles contain unique epitopes and epitopes in common with the heat-stable microtubule associated proteins tau and MAP2. American Journal of Pathology 1987; 126: 81–91
   PubMedGoogle Scholar
• Zhan S.S., Beyreuther K., Schmitt H.P. Quantitative assessment of the synaptophysin immuno-reactivity of the cortical neuropil in various neurodegenerative disorders with dementia. Dementia 1993; 4: 66–74
   PubMedGoogle Scholar