Hypothesis: microtubules, a key to Alzheimer disease

Matsuyama, S S; Jarvik, L F

doi:10.1073/pnas.86.20.8152

Cited by 95Alzheimer's disease research and treatmentsDementia and Cognitive Impairment ResearchMicrotubule and mitosis dynamics

Hypothesis: microtubules, a key to Alzheimer disease

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Matsuyama, S S, Jarvik, L F·1989·Proceedings of the National Academy of Sciences

DOI 10.1073/pnas.86.20.8152PMC PMC298233

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Abstract

Alzheimer disease (AD) is a clinicopathologic syndrome of unknown etiology with numerous abnormalities in neuronal and nonneuronal cells. A review of the literature suggests that a common basic intracellular defect may underlie many of the reported abnormalities. We hypothesize impairment of the microtubule (MT) system as one explanation for the pathogenesis of AD. Evidence in support of the hypothesis includes the following: MTs are ubiquitous and vital cell components, unequally distributed, with the highest concentration in the brain; various abnormalities, including the key neuropathologic lesions, can be explained by impairments of the MT system; and experiments utilizing pharmacologic agents known to disrupt MTs have reproduced certain abnormalities observed in AD. The hypothesis provides a framework for systematic investigations of MTs at the cellular and molecular levels as well as the basis for in vivo diagnostic tests for AD.

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Abnormal phosphorylation of the microtubule-associated protein tau (tau) in Alzheimer cytoskeletal pathology.
Grundke-Iqbal, I., Iqbal, K., Tung, Y. C., Quinlan, M., Wisniewski, H. M., & Binder, L. I. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.13.4913 · Cited by 3,676 · see citing works
Alzheimer's Disease and Senile Dementia: Loss of Neurons in the Basal Forebrain
Whitehouse, P., Price, D., Struble, R., Clark, A., Coyle, J., & DeLong, M. R. (1982) · Science · doi:10.1126/science.7058341 · Cited by 3,627 · see citing works
Dynamic instability of microtubule growth
Mitchison, T., & Kirschner, M. (1984) · Nature · doi:10.1038/312237a0 · Cited by 3,337 · see citing works
The distribution of tau in the mammalian central nervous system.
Binder, L. I., Frankfurter, A., & Rebhun, L. I. (1985) · The Journal of cell biology · doi:10.1083/jcb.101.4.1371 · Cited by 1,588 · see citing works
Microtubule-associated protein tau (tau) is a major antigenic component of paired helical filaments in Alzheimer disease.
Kosik, K. S., Joachim, C. L., & Selkoe, D. J. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.11.4044 · Cited by 1,462 · see citing works
Nerve growth factor promotes survival of septal cholinergic neurons after fimbrial transections
Hefti, F. F. (1986) · Journal of Neuroscience · doi:10.1523/jneurosci.06-08-02155.1986 · Cited by 1,455 · see citing works
Clinical, pathological, and neurochemical changes in dementia: a subgroup with preserved mental status and numerous neocortical plaques
Katzman, R., Terry, R., DeTeresa, R., Brown, T., Davies, P., Fuld, P., Renbing, X., & Peck, A. (1988) · Annals of Neurology · doi:10.1002/ana.410230206 · Cited by 1,225 · see citing works
Occurrence of neuropathological changes and dementia of Alzheimer’s disease in Down’s syndrome
Wisniewski, K. E., Wisniewski, H. M., & Wen, G. Y. (1985) · Annals of Neurology · doi:10.1002/ana.410170310 · Cited by 1,159 · see citing works
Protease inhibitor domain encoded by an amyloid protein precursor mRNA associated with Alzheimer's disease
Tanzi, R. E., McClatchey, A. I., Lamperti, E. D., Villa‐Komaroff, L., Gusella, J. F., & Neve, R. L. (1988) · Nature · doi:10.1038/331528a0 · Cited by 1,093 · see citing works
A new A4 amyloid mRNA contains a domain homologous to serine proteinase inhibitors
Ponte, P. A., Gonzalez‐DeWhitt, P. A., Schilling, J., Miller, J., Hsu, D. K., Greenberg, B., Davis, K. L., Wallace, W., Lieberburg, I. M., Fuller, F. H., et al. (1988) · Nature · doi:10.1038/331525a0 · Cited by 1,050 · see citing works
Isolation of a fragment of tau derived from the core of the paired helical filament of Alzheimer disease.
Wischik, C. M., Novak, M., Thøgersen, H. C., Edwards, P. C., Runswick, M. J., Jakes, R., Walker, J. E., Milstein, C., Roth, M., & Klug, A. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.12.4506 · Cited by 939 · see citing works
Nerve Growth Factor Treatment After Brain Injury Prevents Neuronal Death
Kromer, L. F. (1987) · Science · doi:10.1126/science.3798108 · Cited by 932 · see citing works
Phosphorylation affects the ability of tau protein to promote microtubule assembly.
Lindwall, G., & Cole, R. D. (1984) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)42989-9 · Cited by 901 · see citing works
Accumulation of abnormally phosphorylated τ precedes the formation of neurofibrillary tangles in Alzheimer's disease
Bancher, C., Brunner, C., Lassmann, H., Budka, H., Jellinger, K., Wiche, G., Seitelberger, F., Grundke-Iqbal, I., Iqbal, K., & Wisniewski, H. M. (1989) · Brain Research · doi:10.1016/0006-8993(89)91396-6 · Cited by 818 · see citing works
Alzheimer's disease
Katzman, R. (1986) · New England Journal of Medicine · doi:10.1056/nejm198604103141506 · Cited by 801 · see citing works
Neurofibrillary tangles of Alzheimer disease share antigenic determinants with the axonal microtubule-associated protein tau (tau)
Wood, J. G., Mirra, S. S., Pollock, N. J., & Binder, L. I. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.11.4040 · Cited by 749 · see citing works
Tau protein function in living cells.
Drubin, D. G., & Kirschner, M. W. (1986) · The Journal of Cell Biology · doi:10.1083/jcb.103.6.2739 · Cited by 745 · see citing works
DEFECTIVE BRAIN MICROTUBULE ASSEMBLY IN ALZHEIMER'S DISEASE
Iqbal, K., Zaidi, T., Wen, G. Y., Grundke, I., MERZ, P. A., Shaikh, S., Wisniewski, H., Alafuzoff, I. I., & Winblad, B. G. (1986) · The Lancet · doi:10.1016/s0140-6736(86)92134-3 · Cited by 727 · see citing works
A unifying hypothesis for the cause of amyotrophic lateral sclerosis, parkinsonism, and alzheimer disease
Appel, S. H. (1981) · Annals of Neurology · doi:10.1002/ana.410100602 · Cited by 698 · see citing works
EXPERIMENTAL PRODUCTION OF NEUROFIBRILLARY DEGENERATION
KLATZO, I., Wı́sniewski, H. M., & STREICHER, E. (1965) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/00005072-196504000-00002 · Cited by 612 · see citing works
Microtubule-Associated Proteins
Olmsted, J. B. (1986) · Annual Review of Cell Biology · doi:10.1146/annurev.cb.02.110186.002225 · Cited by 565 · see citing works
Phosphorylated Tau Protein Is Integrated into Paired Helical Filaments in Alzheimer's Disease1
Ihara, Y., Nukina, N., Miura, R., & OGAWARA, M. (1986) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a135662 · Cited by 527 · see citing works
Nerve growth factor-induced neurite outgrowth in PC12 cells involves the coordinate induction of microtubule assembly and assembly-promoting factors.
Drubin, D. G., Feinstein, S. C., Shooter, E. M., & Kirschner, M. W. (1985) · The Journal of Cell Biology · doi:10.1083/jcb.101.5.1799 · Cited by 510 · see citing works
Epitopes that span the tau molecule are shared with paired helical filaments
Kosik, K. S., Orecchio, L. D., Binder, L. I., Trojanowski, J. Q., Lee, V. M.-Y., & Lee, G. S. (1988) · Neuron · doi:10.1016/0896-6273(88)90129-8 · Cited by 497 · see citing works
Pathological changes in the nucleus of meynert in Alzheimer's and Parkinson's diseases
Candy, J., Perry, R. H., Perry, E. K., Irving, D., Blessed, G., FAIRBAIRN, A. F., & Tomlinson, B. E. (1983) · Journal of the Neurological Sciences · doi:10.1016/0022-510x(83)90045-x · Cited by 463 · see citing works
ALUMINOSILICATES AND SENILE PLAQUE FORMATION IN ALZHEIMER'S DISEASE
Candy, J., Klinowski, J., Perry, R. H., Perry, E. K., FAIRBAIRN, A. F., Oakley, A. E., Carpenter, T. A., Atack, J. R., Blessed, G., & Edwardson, J. A. (1986) · The Lancet · doi:10.1016/s0140-6736(86)92319-6 · Cited by 450 · see citing works
Interaction of drugs with microtubule proteins.
Wilson, L., Bamburg, Sb, M., et al. (1974) · PubMed · Cited by 354 · see citing works
Axonal disruption and aberrant localization of tau protein characterize the neuropil pathology of Alzheimer's disease
Kowall, N. W., & Kosik, K. S. (1987) · Annals of Neurology · doi:10.1002/ana.410220514 · Cited by 349 · see citing works
Distribution of tau proteins in the normal human central and peripheral nervous system.
Trojanowski, J. Q., Schuck, T., Schmidt, M. L., & Lee, V. M. (1989) · Journal of Histochemistry & Cytochemistry · doi:10.1177/37.2.2492045 · Cited by 329 · see citing works
Alzheimer's disease: Tau proteins, the promoting factors of microtubule assembly, are major components of paired helical filaments
Delacourte, A., & Défossez, A. (1986) · Journal of the Neurological Sciences · doi:10.1016/0022-510x(86)90167-x · Cited by 325 · see citing works
Pathological changes in olfactory neurons in patients with Alzheimer's disease
Talamo, B. R., Rudel, R. A., Kosik, K. S., Lee, V. M. ‐., Neff, S., Adelman, L. S., & Kauer, J. S. (1989) · Nature · doi:10.1038/337736a0 · Cited by 316 · see citing works
Correlation between Scores for Dementia and Counts of ‘Senile Plaques’ in Cerebral Grey Matter of Elderly Subjects
ROTH, M., TOMLINSON, B. E., & BLESSED, G. (1966) · Nature · doi:10.1038/209109a0 · Cited by 298 · see citing works
Alzheimer neurofibrillary tangles in diseases other than senile and presenile dementia
Wisniewski, K. E., Jervis, G. A., Moretz, R. C., & Wı́sniewski, H. M. (1979) · Annals of Neurology · doi:10.1002/ana.410050311 · Cited by 281 · see citing works
Structural analysis of human neutrophil migration: Centriole, microtubule, and microfilament orientation and function during chemotaxis
Malech, H. L., Root, R., & Gallin, J. (1977) · The Journal of Cell Biology · doi:10.1083/jcb.75.3.666 · Cited by 279 · see citing works
Alzheimer's disease: Genetic aspects and associated clinical disorders
Heyman, A., William Ebomoyi, E., Hurwitz, B. J., Schmechel, D. E., Sigmon, A. H., Weinberg, T., Helms, M. J., & Swift, M. (1983) · Annals of Neurology · doi:10.1002/ana.410140503 · Cited by 272 · see citing works
Mitochondria are associated with microtubules and not with intermediate filaments in cultured fibroblasts.
Ball, E. H., & Singer, S. J. (1982) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.79.1.123 · Cited by 267 · see citing works
Radioimmunoassay for tubulin: a quantitative comparison of the tubulin content of different established tissue culture cells and tissues
Hiller, G., & Weber, K. K. (1978) · Cell · doi:10.1016/0092-8674(78)90335-5 · Cited by 261 · see citing works
Biochemistry of altered brain proteins in Alzheimer's disease.
Selkoe, D. (1989) · Annual Review of Neuroscience · doi:10.1146/annurev.ne.12.030189.002335 · Cited by 261 · see citing works
Microtubule Assembly and Nucleation
Kirschner, M. W. (1978) · International review of cytology · doi:10.1016/s0074-7696(08)60164-3 · Cited by 256 · see citing works
Tubulin microheterogeneity increases with rat brain maturation
Gozes, I., & Littauer, U. Z. (1978) · Nature · doi:10.1038/276411a0 · Cited by 233 · see citing works
In vivo microtubules are copolymers of available beta-tubulin isotypes: localization of each of six vertebrate beta-tubulin isotypes using polyclonal antibodies elicited by synthetic peptide antigens.
Lopata, M. A., & Cleveland, D. W. (1987) · The Journal of Cell Biology · doi:10.1083/jcb.105.4.1707 · Cited by 232 · see citing works
The multitubulin hypothesis revisited: what have we learned?
Cleveland, D. W. (1987) · The Journal of Cell Biology · doi:10.1083/jcb.104.3.381 · Cited by 215 · see citing works
NEURONAL CHANGES INDUCED BY INTRATHECAL VINCRISTINE SULFATE
Schochet, S. S., Lampert, P. W., & Earle, K. M. (1968) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/00005072-196810000-00008 · Cited by 205 · see citing works
The nucleus basalis of Meynert in neurological disease: A quantitative morphological study
Rogers, J., BROGAN, D. R., & Mirra, S. S. (1985) · Annals of Neurology · doi:10.1002/ana.410170210 · Cited by 202 · see citing works
Is Alzheimer disease caused by lack of nerve growth factor?
Hefti, F. F. (1983) · Annals of Neurology · doi:10.1002/ana.410130127 · Cited by 179 · see citing works
Promotion of Tubulin Assembly by Aluminum Ion in Vitro
Macdonald, T. L., Humphreys, W. G., & Martin, R. B. (1987) · Science · doi:10.1126/science.3105058 · Cited by 177 · see citing works
ALZHEIMER'S DISEASE: PAIRED HELICAL FILAMENTS AND CYTOMEMBRANES
Gray, E. G., Paula-Barbosa, M., & Roher, A. (1987) · Neuropathology and Applied Neurobiology · doi:10.1111/j.1365-2990.1987.tb00174.x · Cited by 165 · see citing works
Regulation of microtubule protein levels during cellular morphogenesis in nerve growth factor-treated PC12 cells.
Drubin, D. G., Kobayashi, S., Kellogg, D. R., & Kirschner, M. W. (1988) · The Journal of Cell Biology · doi:10.1083/jcb.106.5.1583 · Cited by 160 · see citing works
Heterogeneity of Microtubule‐Associated Proteins and Brain Development
Francon, J., Lennon, A. M., Fellous, A., Mareck, A., Pierre, M., & Nunez, J. (1982) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1982.tb07072.x · Cited by 155 · see citing works
Regulation of microtubule composition and stability during nerve growth factor-promoted neurite outgrowth.
Black, M. M., Aletta, J. M., & Greene, L. (1986) · The Journal of Cell Biology · doi:10.1083/jcb.103.2.545 · Cited by 154 · see citing works
Autoregulated changes in stability of polyribosome-bound beta-tubulin mRNAs are specified by the first 13 translated nucleotides.
Yen, T. J., Gay, D. A., Pachter, J. S., et al. (1988) · Molecular and Cellular Biology · doi:10.1128/mcb.8.3.1224 · Cited by 140 · see citing works
Cytotypic differences in the protein composition of the axonally transported cytoskeleton in mammalian neurons
Oblinger, M., Brady, S., McQuarrie, I. G., & Lasek, R. (1987) · Journal of Neuroscience · doi:10.1523/jneurosci.07-02-00453.1987 · Cited by 130 · see citing works
Multiple tubulin forms are expressed by a single neurone
Gozes, I., & Sweadner, K. J. (1981) · Nature · doi:10.1038/294477a0 · Cited by 130 · see citing works
Working memory and secondary memory deficits in Alzheimer's disease
Becker, J. T. (1988) · Journal of Clinical and Experimental Neuropsychology · doi:10.1080/01688638808402811 · Cited by 125 · see citing works
Studies in aging of the brain
Cook-Deegan, R. M., Ward, B. E., & Austin, J. H. (1979) · Neurology · doi:10.1212/wnl.29.10.1402 · Cited by 117 · see citing works
Phosphorylation of tubulin by a calmodulin-dependent protein kinase.
Wandosell, F. G., Serrano, L. G., Hernández, M. A., & Ávila, J. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)67528-3 · Cited by 110 · see citing works
Alzheimer's Disease, Trisomy 21, and Myeloproliferative Disorders: Associations Suggesting a Genetic Diathesis
Heston, L. L. (1977) · Science · doi:10.1126/science.196.4287.322 · Cited by 110 · see citing works
Family Study of Platelet Membrane Fluidity in Alzheimer's Disease
Zubenko, G. S., Wusylko, M., Cohen, B. M., Boller, F., & Teply, I. (1987) · Science · doi:10.1126/science.3659926 · Cited by 108 · see citing works
Microheterogeneity of Micro tubule‐Associated τ Proteins Is Due to Differences in Phosphorylation
Butler, M., & Shelanski, M. L. (1986) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1986.tb00788.x · Cited by 106 · see citing works
The Control of Microtubule Assembly in Vivo
Raff, E. C. (1979) · International review of cytology · doi:10.1016/s0074-7696(08)61660-5 · Cited by 105 · see citing works
Phase dynamics at microtubule ends: the coexistence of microtubule length changes and treadmilling
Farrell, K., Jordan, M. A., Miller, H., & Wilson, L. (1987) · The Journal of Cell Biology · doi:10.1083/jcb.104.4.1035 · Cited by 101 · see citing works
Defective neutrophil chemotaxis in patients with Down syndrome
Khan, A. J., Evans, H. E., Glass, L., et al. (1975) · The Journal of Pediatrics · doi:10.1016/s0022-3476(75)80077-1 · Cited by 99 · see citing works
INHIBITION OF AXOPLASMIC TRANSPORT BY COLCHICINE, PODOPHYLLOTOXIN, AND VINBLASTINE: AN EFFECT ON MICROTUBULES*
Paulson, J. C., & McClure, W. O. (1975) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1975.tb19225.x · Cited by 95 · see citing works
Association of Tau Protein with Microtubules in Living Cells
Drubin, D. G., KOBAYASHI, S., & Kirschner, M. W. (1986) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1986.tb38398.x · Cited by 91 · see citing works
Axonal transport of a subclass of tau proteins: evidence for the regional differentiation of microtubules in neurons.
Tytell, M., Brady, S. T., & Lasek, R. J. (1984) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.81.5.1570 · Cited by 90 · see citing works
Alzheimer's Disease
Wurtman, R. J. (1985) · Scientific American · doi:10.1038/scientificamerican0185-62 · Cited by 90 · see citing works
Radial-arm maze deficits produced by colchicine administered into the area of the nucleus basalis are ameliorated by cholinergic agents
Tilson, H. A., McLamb, R. L., Shaw, S., Rogers, B. C., Pediaditakis, P., & Cook, L. L. (1988) · Brain Research · doi:10.1016/0006-8993(88)91326-1 · Cited by 80 · see citing works
AMYLOID PRECURSOR PROTEIN IN SENILE PLAQUES OF ALZHEIMER DISEASE
Perry, G. L., Lipphardt, S., Kancherla, M., et al. (1988) · The Lancet · doi:10.1016/s0140-6736(88)90219-x · Cited by 75 · see citing works
Altered response of fibroblasts from aged and Alzheimer donors to drugs that elevate cytosolic free calcium
Peterson, C. M., Ratan, R. R., Shelanski, M. L., et al. (1988) · Neurobiology of Aging · doi:10.1016/s0197-4580(88)80063-0 · Cited by 73 · see citing works
Neuroplasmic transport in dendrites: effect of colchicine on morphology and physiology of motoneurones in the cat
Schubert, P., Kreutzberg, G. W., & Lux, H. D. (1972) · Brain Research · doi:10.1016/0006-8993(72)90643-9 · Cited by 73 · see citing works
ALZHEIMER'S DISEASE AND TAU PROTEINS
Brion, J., Flament-Durand, J., & Dustin, P. (1986) · The Lancet · doi:10.1016/s0140-6736(86)90495-2 · Cited by 72 · see citing works
Altered expression of genes for amyloid and cytoskeletal proteins in alzheimer cortex
Clark, A. W., Krekoski, C. A., Parhad, I. M., Liston, D. R., Julien, J., & Hoar, D. I. (1989) · Annals of Neurology · doi:10.1002/ana.410250404 · Cited by 70 · see citing works
Neurofibrillary tangles induced by vincristine and vinblastine sulfate in central and peripheral neurons in vitro
Seil, F. J., & Lampert, P. W. (1968) · Experimental Neurology · doi:10.1016/0014-4886(68)90140-4 · Cited by 65 · see citing works
Colchicine lesions in the rat hippocampus mimic the alterations of several markers in Alzheimer's disease
Nakagawa, Y., Nakamura, S., Kasé, Y., Noguchi, T., & Ishihara, T. (1987) · Brain Research · doi:10.1016/0006-8993(87)90358-1 · Cited by 62 · see citing works
Microtubule disarray in cortical dendrites and neurobehavioral failure. I. Golgi and electron microscopic studies
Purpura, D. P., Bodick, N. C., Suzuki, K., Rapin, I., & Wurzelmann, S. (1982) · Developmental Brain Research · doi:10.1016/0165-3806(82)90128-6 · Cited by 61 · see citing works
Antemortem markers of Alzheimer's disease
Hollander, E., Mohs, R. C., & Davis, K. L. (1986) · Neurobiology of Aging · doi:10.1016/0197-4580(86)90164-8 · Cited by 60 · see citing works
Translation in vitro of Rat Brain mRNA Coding for a Variety of Tubulin Forms
Gozes, I., de Baetselier, A., & Littauer, U. Z. (1980) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1980.tb04283.x · Cited by 60 · see citing works
Phosphorylation of tubulin enhances its interaction with membranes
Hargreaves, A. J., Wandosell, F. G., & Ávila, J. (1986) · Nature · doi:10.1038/323827a0 · Cited by 57 · see citing works
Transmission studies from blood of Alzheimer disease patients and healthy relatives.
Manuelidis, E. E., de Figueiredo, J. M., Kim, J. H., et al. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.13.4898 · Cited by 56 · see citing works
Sequestration of Tubulin in Neurons in Alzheimer's disease
Price, D. L., Altschuler, R. J., Struble, R. G., Casanova, M. F., Cork, L. C., & Murphy, D. B. (1986) · Brain Research · doi:10.1016/0006-8993(86)91077-2 · Cited by 55 · see citing works
Comparison of the temperature‐dependence of rapid axonal transport and microtubules in nerves of the rabbit and bullfrog.
Brimijoin, S., Olsen, J., & Rosenson, R. S. (1979) · The Journal of Physiology · doi:10.1113/jphysiol.1979.sp012660 · Cited by 52 · see citing works
Red Blood Cell Abnormalities in Alzheimer Disease
Blass, J. P., Hanin, I., Barclay, L., et al. (1985) · Journal of the American Geriatrics Society · doi:10.1111/j.1532-5415.1985.tb07150.x · Cited by 48 · see citing works
A quantitative study of frontal cortex dendritic microtubules in patients with Alzheimer's disease
Paula-Barbosa, M., Ferreira, M. A., & Cadete‐Leite, A. (1987) · Brain Research · doi:10.1016/0006-8993(87)90188-0 · Cited by 47 · see citing works
Philothermal response of polymorphonuclear leukocytes in dementia of the Alzheimer type
Jarvik, L. F., Matsuyama, S. S., Kessler, J. O., et al. (1982) · Neurobiology of Aging · doi:10.1016/0197-4580(82)90002-1 · Cited by 47 · see citing works
Self-citation
Role of the tubulin-microtubule system in lymphocyte activation
SHERLINE, P., & Mundy, G. R. (1977) · The Journal of Cell Biology · doi:10.1083/jcb.74.2.371 · Cited by 42 · see citing works
Autoregulated Changes in Stability of Polyribosome-Bound β-Tubulin mRNAs Are Specified by the First 13 Translated Nucleotides
Yen, T. J., Gay, D. A., Pachter, J. S., et al. (1988) · Molecular and Cellular Biology · doi:10.1128/mcb.8.3.1224-1235.1988 · Cited by 40 · see citing works
Spindle microtubular dysfunction in mothers of Down syndrome children
Ford, J. H. (1984) · Human Genetics · doi:10.1007/bf00292587 · Cited by 30 · see citing works
A review of neuropathological and neurochemical correlates of Alzheimer's disease
Perry, E. K., & Perry, R. H. (1985) · PubMed · doi:10.25405/ncl.34082031 · Cited by 30 · see citing works
Defective neutrophil motility in patients with primary ciliary dyskinesia
Valerius, N. H., Knudsen, B. B., & Pedersen, M. (1983) · European Journal of Clinical Investigation · doi:10.1111/j.1365-2362.1983.tb00134.x · Cited by 26 · see citing works
Recent advances in the neurochemistry of Alzheimer's disease.
Davies, P., & Wolozin, B. L. (1987) · PubMed · Cited by 26 · see citing works
Neuronal transformations in Alzheimer's disease
Metuzals, J., Robitaille, Y., Houghton, S., Gauthier, S. G., Kang, C. Y., & Leblanc, R. (1988) · Cell and Tissue Research · doi:10.1007/bf00214366 · Cited by 22 · see citing works
Defects in granulocyte function in various chromosome abnormalities (down's-, edwards'-, cri-du-chat syndrome)
Seger, R. A., Wildfeuer, A., Buchinger, G., et al. (1976) · Journal of Molecular Medicine · doi:10.1007/bf01468883 · Cited by 19 · see citing works
Reduced Proteins in Temporal Cortex in Alzheimer's Disease: An Electrophoretic Study
Borthwick, N. M., Yates, C. M., & Gordon, A. (1985) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1985.tb08780.x · Cited by 18 · see citing works
Inhibition of axonal transport ‘in vivo’ by a tubulin-specific antibody
Johnston, K. M., Connolly, J. A., & van der Kooy, D. (1986) · Brain Research · doi:10.1016/0006-8993(86)91544-1 · Cited by 17 · see citing works
Philothermal response, microtubules and dementia
Fu, T.-K., Matsuyama, S. S., Kessler, J. O., & Jarvik, L. F. (1986) · Neurobiology of Aging · doi:10.1016/0197-4580(86)90025-4 · Cited by 13 · see citing works
Self-citation
Altered Expression of Different Tubulin Electrophoretic Variants During Human Cortex Development
Morrison, M. R., Pardue, S., & Griffin, W. S. T. (1983) · Journal of Neurogenetics · doi:10.3109/01677068309107076 · Cited by 12 · see citing works
Induction of neurofibrillary tangles in cultured mouse neurons by maytanprine
Sato, Y., Kim, S. U., & Ghetti, B. F. (1985) · Journal of the Neurological Sciences · doi:10.1016/0022-510x(85)90100-5 · Cited by 10 · see citing works
VARIATION IN DNA CONTENT OF MONONUCLEAR CELLS OF PATIENTS WITH DEMENTIA OF THE ALZHEIMER TYPE
Matsuyama, S. S., & Bohman, R. (1988) · Alzheimer Disease & Associated Disorders · doi:10.1097/00002093-198802020-00004 · Cited by 9 · see citing works
Self-citation
BRAIN “TRANSPLANTS”, NEUROTROPHIC FACTORS AND BEHAVIOR
Russell, R. W. (1988) · Alzheimer Disease & Associated Disorders · doi:10.1097/00002093-198802020-00001 · Cited by 7 · see citing works
Reductions in soluble brain proteins in older subjects with Down's syndrome
Borthwick, N. M., Gordon, A., & Yates, C. M. (1985) · Journal of the Neurological Sciences · doi:10.1016/0022-510x(85)90101-7 · Cited by 6 · see citing works

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Consciousness in the universe
Hameroff, S., & Penrose, R. (2014) · Physics of Life Reviews · doi:10.1016/j.plrev.2013.08.002 · Cited by 983 · see citing works
“Neurons have a rich and uniquely organized cytoskeleton, the major components being microtubules, well-positioned and uniquely arrayed (e.g. in dendrites and soma) to mediate consciousness and regulate firing.”
Background
Orchestrated reduction of quantum coherence in brain microtubules: a model for consciousness
Hameroff, S., & Penrose, R. (1996) · Mathematics and Computers in Simulation · doi:10.1016/0378-4754(96)80476-9 · Cited by 641 · see citing works
How quantum brain biology can rescue conscious free will
Hameroff, S. (2012) · Frontiers in Integrative Neuroscience · doi:10.3389/fnint.2012.00093 · Cited by 95 · see citing works
Microtubule disruption and cognitive defects: Effect of colchicine on learning behavior in rats
Bensimon, G., & Chermat, R. (1991) · Pharmacology Biochemistry and Behavior · doi:10.1016/0091-3057(91)90602-x · Cited by 69 · see citing works

Authors: Matsuyama, S. S., & Jarvik, L. F.
Affiliations: VA West Los Angeles Medical Center (US)
Venue: Proceedings of the National Academy of Sciences
Publisher: National Academy of Sciences
Published: 1989-10
Volume: 86
Issue: 20
Pages: 8152-8156
ISSN: 0027-8424 (ISSN-L)
1091-6490
DOI: 10.1073/pnas.86.20.8152
PMC: PMC298233
OpenAlex: W2050744977
Cited by: 95
References: 100
Citations by year: 2026: 1 · 2023: 1 · 2022: 5 · 2021: 2 · 2020: 2 · 2019: 4 · 2018: 1 · 2017: 1 · 2016: 4 · 2015: 4 · 2014: 3 · 2013: 3 · 2012: 3
FWCI: 5.43
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Locations: Proceedings of the National Academy of Sciences (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Topics: Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
Keywords: Alzheimer's disease, microtubules, microtubule disruption, pathogenesis, neurofibrillary tangles, amyloid plaques, in vivo diagnosis, microtubule inhibitors
MeSH terms: Alzheimer Disease, Brain, Humans, Microtubules, Models, Neurological

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