Cited by 404Alzheimer's disease research and treatmentsDementia and Cognitive Impairment ResearchNeuroinflammation and Neurodegeneration Mechanisms

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THE FINE STRUCTURE OF NEUROFIBRILLARY TANGLES IN ALZHEIMERʼS DISEASE

Terry, Robert D.·1963·Journal of Neuropathology and Experimental Neurology

DOI 10.1097/00005072-196310000-00005

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Abstract

Robert D. Terry, M.D.; The Fine Structure of Neurofibrillary Tangles in Alzheimer's Disease*†‡, Journal of Neuropathology & Experimental Neurology, Volume

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Sue‐A‐Quan, A. K., Fialkow, L., Vlahos, C. J., Schelm, J. A., Grinstein, S., Butler, J. R., & Downey, G. P. (1997) · Journal of Cellular Physiology · doi:10.1002/(sici)1097-4652(199707)172:1 · Cited by 63
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Ayola, R., Condorelli, D. F., Ragusa, N., et al. (1988) · Neurochemical Research · doi:10.1007/bf00972483 · Cited by 26
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Ghetti, B. F. (1979) · Brain Research · doi:10.1016/0006-8993(79)90147-1 · Cited by 26
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Castellani, R. J. (2020) · Brain Sciences · doi:10.3390/brainsci10120972 · Cited by 25
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Blázquez‐Llorca, L. (2010) · Frontiers in Neuroanatomy · doi:10.3389/fnana.2010.00020 · Cited by 26
“NFT were first described ultrastructurally in the 1960s, showing them to be bundles of abnormal cytoplasmic filaments that accumulate in nerve cell bodies and their processes (Kidd, 1963, 1964; Terry, 1963; Terry et al., 1964; reviewed in Goedert and Spillantine, 2006).”
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Bennett, P. M., Starr, R., Elliott, A., & Offer, G. (1985) · Journal of Molecular Biology · doi:10.1016/0022-2836(85)90381-x · Cited by 25
Subcellular Pathology of Human Neurodegenerative Disorders: Alzheimer‐Type Dementia and Huntington's Disease
Cross, A. J., Crow, T. J., Dawson, J. M., et al. (1986) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1986.tb00693.x · Cited by 25
Neurofibrillary changes in the cerebral cortex of a patient with subacute sclerosing panencephalitis (SSPE)
Paula-Barbosa, M. M., Brito, R., Silva, C. A., Faria, R., & Cruz, C. (1979) · Acta Neuropathologica · doi:10.1007/bf00691159 · Cited by 23
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Higgins, R., Rings, D. M., Fenner, W. R., et al. (1983) · Acta Neuropathologica · doi:10.1007/bf00691495 · Cited by 24
“Paired helical filaments were not found [31].”
[37] Isolation of paired helical filaments and amyloid fibers from human brain
Selkoe, D. J., & Abraham, C. R. (1986) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(86)34105-3 · Cited by 24
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Brion, J., Couck, A. M., & Flament-Durand, J. (1984) · Acta Neuropathologica · doi:10.1007/bf00695578 · Cited by 26
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Sun, C., González, B., & Jiang, W. (2022) · Scientific Reports · doi:10.1038/s41598-022-11382-7 · Cited by 24
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Furgerson, M., Clark, J. K., Crystal, J. D., Wagner, J. J., Fechheimer, M., & Furukawa, R. (2014) · Acta Neuropathologica Communications · doi:10.1186/s40478-014-0131-9 · Cited by 25
“The brains of Alzheimer’s disease patients develop extracellular amyloid beta plaques and intracellular neurofibrillary tangles (NFTs) [4,5].”
Background
Alzheimer paired helical filaments, untreated and pronase digested, studied by vertical platinum-carbon replication and high resolution transmission electron microscopy
Ruben, G. C., Novak, M., Edwards, P. C., & Iqbal, K. (1995) · Brain Research · doi:10.1016/0006-8993(94)01437-m · Cited by 23
Reversible β-pleated sheet formation of a phosphorylated synthetic τ peptide
Láng, E., Szendrei, G. I., Elekes, I., Lee, V. M. ‐., & Ötvös, L. (1992) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(05)80112-3 · Cited by 22
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Rao, K. S. J., Katsetos, C. D., Herman, M. M., & Savory, J. (1998) · Clinics in Laboratory Medicine · doi:10.1016/s0272-2712(18)30144-6 · Cited by 22
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DeTure, M. A., Di Noto, L., & Purich, D. L. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m201201200 · Cited by 21
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EGAN, D. A., Flumerfelt, B. A., & Gwyn, D. G. (1977) · Neuropathology and Applied Neurobiology · doi:10.1111/j.1365-2990.1977.tb00602.x · Cited by 21
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Láng, E., & Ötvös, L. (1992) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(92)92364-4 · Cited by 21
Alzheimer’s disease is an inherent, natural part of human brain aging: an integrated perspective
Ferrer, I. (2022) · Free Neuropathology · doi:10.17879/freeneuropathology-2022-3806 · Cited by 25
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Lampert, P. W. (1971) · Springer eBooks · doi:10.1007/978-3-642-47449-1_6 · Cited by 20
Senile changes in the human neocortex and hippocampus compared by the use of the electron and light microscopes
Gibson, P. H., Stones, M., & Tomlinson, B. E. (1976) · Journal of the Neurological Sciences · doi:10.1016/0022-510x(76)90011-3 · Cited by 20
Are alzheimer neurofibrillary tangles insoluble polymers?
Iqbal, K., Grundke, I., Zaidi, T., Ali, N., & Wı́sniewski, H. M. (1986) · Life Sciences · doi:10.1016/0024-3205(86)90414-5 · Cited by 20
Neurochemistry of Aging
Samorajski, T., & Ordy, J. M. (1972) · Advances in behavioral biology · doi:10.1007/978-1-4684-8503-5_5 · Cited by 21
Ultrastructure of neurofibrillary tangles in Alzheimer’s disease
Miyakawa, T., Katsuragi, S., Araki, K., Hashimura, T., Kimura, T., & Kuramoto, R. (1989) · Virchows Archiv B Cell Pathology Including Molecular Pathology · doi:10.1007/bf02899091 · Cited by 20
“Terry (1963) reported the ultrastructure of neurofibrillary tangles in Alzheimer's disease.”
Background
Disturbances of Axoplasmic Transport in Alzheimer’s Disease
Dustin, P., & Flament-Durand, J. (1982) · Proceedings in life sciences · doi:10.1007/978-3-642-85714-0_17 · Cited by 20
Asparagine residue 368 is involved in Alzheimer's disease tau strain–specific aggregation
Shimonaka, S., Matsumoto, S., Elahi, M., Ishiguro, K., Hasegawa, M., Hattori, N., & Motoi, Y. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra120.013271 · Cited by 18
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Shoham, S., & Ebstein, R. P. (1997) · Experimental Neurology · doi:10.1006/exnr.1997.6622 · Cited by 19
The Sixth International Conference on Alzheimer's Disease, Amsterdam, The Netherlands, July 1998. The amyloid cascade hypothesis debate: Emerging consensus on the role of Aβ and amyloid in Alzheimer's disease
Small, D. H. (1998) · Amyloid · doi:10.3109/13506129809007304 · Cited by 19
Ultrastructural studies in experimental kernicterus.
Chen, H. C., Lin, C. S., & Lein, I. N. (1966) · PubMed · Cited by 19
Anti-amnesic effect of ESP-102 on Aβ1–42-induced memory impairment in mice
Kim, D., Jung, W. Y., Park, S. J., Kim, J. M., Lee, S., Kim, Y. C., & Ryu, J. H. (2010) · Pharmacology Biochemistry and Behavior · doi:10.1016/j.pbb.2010.08.005 · Cited by 18
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Krishna‐K, K., Baby, N., Raghuraman, R., Navakkode, S., Behnisch, T., & Sajikumar, S. (2020) · The FASEB Journal · doi:10.1096/fj.201902844rr · Cited by 18
In vitro polymerization of embryonic MAP-2c and fragments of the MAP-2 microtubule binding region into structures resembling paired helical filaments
DeTure, M. A., Yi Zhang, E., Bubb, M. R., & Purich, D. L. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.51.32702 · Cited by 18
Immunocytochemical studies of Alzheimer neuronal perikarya with intermediate filament antisera
Elovaara, I., Paetau, A. E., Lehto, V.-P., Dahl, D. R., Virtanen, I., & Palo, J. (1983) · Journal of the Neurological Sciences · doi:10.1016/0022-510x(83)90208-3 · Cited by 18
Three-dimensional structure of Alzheimer's neurofibrillary tangles of the aged human brain revealed by the quick-freeze, deep-etch and replica method
Ohtsubo, K., Izumiyama, N., Shimada, H., TACHIKAWA, T., & Nakamura, H. (1990) · Acta Neuropathologica · doi:10.1007/bf00296106 · Cited by 18
“In the earliest reports, Kidd [7, 8] described the filaments as two anti-coiled, anti-parallel right-hand helices, making full turn in 160 nm, the individual strands of the helix being 10 nm in diameter and their center to center separation 15 nm. Terry [ 11 ] and Terry et al. [12] presented the paired helical structu…”
BackgroundResultInfluential
Chapter 24 Hippocampal grafts derived from embryonic trisomy 16 mice exhibit amyloid (A4) and neurofibrillary pathology
Richards, S.-J., Waters, J. J., Rogers, D. C., Martel, F. L., Sparkman, D. R., White, C. L., Beyreuther, K. T., Masters, C. L., & Dunnett, S. B. (1990) · Progress in brain research · doi:10.1016/s0079-6123(08)62607-2 · Cited by 18
History in perspective: How Alzheimer's Disease came to be where it is?
Ahmed, T. F., Ahmed, A., & Imtiaz, F. (2021) · Brain Research · doi:10.1016/j.brainres.2021.147342 · Cited by 21
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Dikranian, K. T., Kim, J., Stewart, F. R., Levy, M. A., & Holtzman, D. M. (2012) · Europe PMC (PubMed Central) · Cited by 17
Ultrastructural study of Betz cells in the primary motor cortex of the human brain
Sasaki, S., & Iwata, M. (2001) · Journal of Anatomy · doi:10.1046/j.1469-7580.2001.19960699.x · Cited by 17
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Background
CDK5RAP2 gene and tau pathophysiology in late‐onset sporadic Alzheimer's disease
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“109 the accumulation of neurofibrillary tangles (NFTs) in neurons [5].”
RNA content and volume of nerve cell bodies in human brain
Uemura, E., & Hartmann, H. A. (1979) · Experimental Neurology · doi:10.1016/0014-4886(79)90252-8 · Cited by 17
Neuronal aging in tissue and cell cultures: A review
Kim, S. U. (1983) · In Vitro Cellular & Developmental Biology - Plant · doi:10.1007/bf02621889 · Cited by 17
“Electron microscope studies revealed that these fibrils are composed of linear structures that twisted every 80 nm and had a diameter at these nodes of 9 nm and a maximum diameter between the nodes of almost 20 nm (40, 41 ).”
Background
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Kanagasingam, S., von Ruhland, C. J., Welbury, R. R., & Singhrao, S. K. (2022) · Journal of Alzheimer s Disease · doi:10.3233/jad-220486 · Cited by 17
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DEMİR, Z., & Türkan, F. (2022) · Iğdır Üniversitesi Fen Bilimleri Enstitüsü Dergisi · doi:10.21597/jist.1161271 · Cited by 16
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Mishra, S. (2023) · Journal of Molecular Biology · doi:10.1016/j.jmb.2023.168361 · Cited by 16
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Weickert, S., Cattani, J., & Drescher, M. (2018) · Royal Society of Chemistry eBooks · doi:10.1039/9781788013888-00001 · Cited by 18
Neuronal Thread Protein Gene Modulation With Cerebral Infarction
de la Monte, S. M., Garner, W., & Wands, J. R. (1997) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1097/00004647-199706000-00004 · Cited by 16
Disulfide-Cross-Linked Tau and MAP2 Homodimers Readily Promote Microtubule Assembly
Noto, L. D., Deture, M. A., & Purich, D. L. (1999) · Molecular Cell Biology Research Communications · doi:10.1006/mcbr.1999.0153 · Cited by 17
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Díaz‐Espinoza, R. (2021) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2021.782617 · Cited by 17
“In addition to Aβ42 plaques, AD-affected brains can also contain intracellular inclusions composed of misfolded Tau protein Frontiers in Aging Neuroscience | www.frontiersin.org 3 November 2021 | Volume 13 | Article 782617 (Terry, 1963; Lee et al., 1991).”
Background
Multivesicular bodies in cortical dendrites of two patients with Alzheimer's disease
Paula-Barbosa, M. M., Cardoso, R. M., Faria, R., & Cruz, C. (1978) · Journal of the Neurological Sciences · doi:10.1016/0022-510x(78)90086-2 · Cited by 14
Atomic force microscopy of paired helical filaments isolated from the autopsied brains of patients with Alzheimer's disease and immunolabeled against microtubule-associated protein tau.
Ikonomović, M. D., Armstrong, D. M., Yen, S.-H. C., Obcemea, C. H., & Vidić, B. (1995) · Europe PMC (PubMed Central) · Cited by 15
Non-enzymatic posttranslational protein modifications in protein aggregation and neurodegenerative diseases
Baldensperger, T., Preissler, M., & Becker, C. F. W. (2024) · RSC Chemical Biology · doi:10.1039/d4cb00221k · Cited by 17
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Kaur, B., Biby, S., Namme, J. N., More, S., Xu, Y., & Zhang, S. (2024) · Advances in pharmacology · doi:10.1016/bs.apha.2024.10.004 · Cited by 15
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Miron, J., Picard, C., Labonté, A., Auld, D. S., & Poirier, J. (2022) · Journal of Alzheimer s Disease · doi:10.3233/jad-215410 · Cited by 16
Neurofibrillary degeneration in a case of quadriplegia and myoclonic movement
Kuroda, S., Otsuki, S., Tateishi, J., & Hirano, A. (1979) · Acta Neuropathologica · doi:10.1007/bf00691887 · Cited by 14
Biochemistry of Senile Dementia
DeKosky, S. T., & Bass, N. H. (1985) · Springer eBooks · doi:10.1007/978-1-4757-0797-7_23 · Cited by 14
The Neuronal Cytoskeleton
Pachter, J. S., Liem, R. K. H., & Shelanski, M. L. (1984) · Advances in cellular neurobiology · doi:10.1016/b978-0-12-008305-3.50008-8 · Cited by 14
MAP2 caps tau fibrils and inhibits aggregation
Holden, M. R., Krzesinski, B. J., Weismiller, H. A., Shady, J. R., & Margittai, M. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.104891 · Cited by 13
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Dickson, D. W. (1997) · Europe PMC (PubMed Central) · Cited by 13
Alzheimer's disease: Microtubule‐associated proteins 2 (MAP 2) are not components of paired helical filaments
Rosemblatt, M. S., Fellous, A., Mazié, J. C., Delacourte, A., & Défossez, A. (1989) · FEBS Letters · doi:10.1016/0014-5793(89)80895-6 · Cited by 13
ASPECTS OF THE PATHOLOGY OF PRESENILE DEMENTIA
TORVIK, A. (2009) · Acta Neurologica Scandinavica · doi:10.1111/j.1600-0404.1970.tb02154.x · Cited by 13
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Hirano, A. (1970) · Novartis Foundation symposium · doi:10.1002/9780470719749.ch12 · Cited by 20
Human Nervous System
Katzman, R. (1995) · Comprehensive physiology · doi:10.1002/cphy.cp110112 · Cited by 15
Altern des Zentralnervensystems
Arendt, A. (1972) · Handbuch der allgemeinen Pathologie · doi:10.1007/978-3-642-80637-7_10 · Cited by 14
Amyloid-like (Congophilic) neurofibrillary tangles do not react with neurofilament antisera in Alzheimer's cerebral cortex
Bignami, A., Selkoe, D. J., & Dahl, D. R. (1984) · Acta Neuropathologica · doi:10.1007/bf00688115 · Cited by 12
“The chemical composition of the paired helical filaments (PHF) in Alzheimer's disease (Kidd 1963; Terry 1963 ) is stil controversial.”
Background
Dementias
Katzman, R. (1978) · Postgraduate Medicine · doi:10.1080/00325481.1978.11714904 · Cited by 12
Curly fibers are tau-positive strands in the pre- and post-synaptic neurites, consisting of paired helical filaments: observations by the freeze-etch and replica method
Ohtsubo, K., Izumiyama, N., Kuzuhara, S., Mori, H., & Shimada, H. (1990) · Acta Neuropathologica · doi:10.1007/bf00334498 · Cited by 12
“Our present findings as well as previous ones [12] apparently contradict the twisted tubule model of Terry [ 17 ] and, recently, Of Miyakawa et al. [10] that the fibrils of NFT consist of hollow tubules with periodical constrictions, and rather support the idea of Kidd [6] and many others [2] that they are helical fil…”
Result
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Kumari, R., Goel, S., & Das, S. (2023) · AIP conference proceedings · doi:10.1063/5.0163400 · Cited by 11
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Zhou, H., Yin, X., Zhang, G., Yang, Z., & Zhou, R. (2025) · JACS Au · doi:10.1021/jacsau.5c00002 · Cited by 15
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Lee, H. E., Lim, D., Lee, J. Y., Lim, S. M., & Pae, A. N. (2019) · Pharmaceutical Patent Analyst · doi:10.4155/ppa-2019-0003 · Cited by 11
Age-related changes in RNA content and volume of the human hypoglossal neuron
Uemura, E., & Hartmann, H. A. (1978) · Brain Research Bulletin · doi:10.1016/0361-9230(78)90115-6 · Cited by 11
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Jones, G. R. N. (2014) · Inflammation & Allergy - Drug Targets · doi:10.2174/1871528112666131219163405 · Cited by 11
“An ultrastructural study of synaptic regions in cortical biopsies from F-AD patients demonstrated loss of anastomoses [173]; peroxynitriteinduced damage to synaptosomal membranes has also been reported [72].”
Background
Chapter 17 Neuronal cytoskeleton in aging and dementia
Iqbal, K., Grundke, I., & Wisniewski, H. M. (1986) · Progress in brain research · doi:10.1016/s0079-6123(08)64310-1 · Cited by 11
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Selkoe, D. J. (2002) · Neurochemistry International · doi:10.1016/s0197-0186(01)00057-2 · Cited by 11
Alzheimer paired helical filaments: a comparison with the twisted ribbon model
Pollanen, M. S., Markiewicz, P., Goh, M. C., & Bergeron, C. (1995) · Acta Neuropathologica · doi:10.1007/bf00294320 · Cited by 11
Changes in expression of lymphocyte amyloid precursor protein mRNA isoforms in normal aging and Alzheimer's disease
Ebstein, R. P., Nemanov, L., Lubarski, G., Dano, M., Trevis, T., & Korczyn, A. D. (1996) · Molecular Brain Research · doi:10.1016/0169-328x(95)00227-j · Cited by 11
Tau protein as a therapeutic target in Alzheimer’s disease and other neurodegenerative disorders
Larner, A. J. (1999) · Expert Opinion on Therapeutic Patents · doi:10.1517/13543776.9.10.1359 · Cited by 11
Immunoreactivity patterns in neurofibrillary tangles of the inferior temporal cortex in Alzheimer disease
Duong, T., & Gallagher, K. A. (1994) · Molecular and Chemical Neuropathology · doi:10.1007/bf03160099 · Cited by 11
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Sasaki, S., & Maruyama, S. (1993) · Neuroscience Letters · doi:10.1016/0304-3940(93)90185-n · Cited by 10
Progressive Supranuclear Palsy and Corticobasal Degeneration
Dickson, D. W. (2001) · Elsevier eBooks · doi:10.1016/b978-012351830-9/50015-9 · Cited by 10
Research Advances in the Biology of Alzheimer’s Disease
Tabaton, M. (1994) · Clinics in Geriatric Medicine · doi:10.1016/s0749-0690(18)30344-6 · Cited by 11
ELECTRON MICROSCOPE STUDIES ON PUROMYCIN-INDUCED CHANGES IN NERVE CELLS OF THE MEDULLA OBLONGATA
Kishi, K. (1974) · The Journal of Cell Biology · doi:10.1083/jcb.63.3.1091 · Cited by 9
“tubules in the affected neurons of Alzheimer's disease (30, 34).”
Background
Etude anatomo-pathologique et ultrastructurale de divers processus de vieillissement cérébral chez l'homme revue critique, 1
Foncin, J. F. (1980) · Revue d Electroencé phalographie et de Neurophysiologie Clinique · doi:10.1016/s0370-4475(80)80003-7 · Cited by 8
Caspase-2 and tau—a toxic partnership?
Troy, C. M., & Shelanski, M. L. (2016) · Nature Medicine · doi:10.1038/nm.4227 · Cited by 10
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Iqbal, K., Grundke, I., & Wı́sniewski, H. M. (1987) · Advances in behavioral biology · doi:10.1007/978-1-4613-1657-2_9 · Cited by 8
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Trullén, J. M. P. (2007) · Revista Española de Patología · doi:10.1016/s1699-8855(07)70058-2 · Cited by 8
Vacuolar degeneration in neurons of aging rats
de Estable‐Puig, R. F., & Estable-Puig, J. F. (1975) · Virchows Archiv B Cell Pathology Including Molecular Pathology · doi:10.1007/bf02912859 · Cited by 7
My own experience in early research on Alzheimer disease
Terry, R. D. (2006) · Journal of Alzheimer s Disease · doi:10.3233/jad-2006-9s313 · Cited by 7
Self-citation
in Alzheimer’s Disease
Weiner, M., Edland, S. D., & Luszczynska, H. (2014) · Cited by 7
Chapter 25 Neuronal responses to injury and aging: lessons from animal models
Price, D. L., Koo, E. H., Sisodia, S. S., Martin, L. J., Koliatsos, V. E., Muma, N. A., Walker, L. C., & Cork, L. C. (1990) · Progress in brain research · doi:10.1016/s0079-6123(08)63186-6 · Cited by 8
A hypothesis concerning the role of endogenous colchicine-like factors in the etiology of Alzheimer's disease
Gorenstein, C. (1987) · Medical Hypotheses · doi:10.1016/0306-9877(87)90057-0 · Cited by 7
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David, E., Marx, I., & David, H. (1967) · Acta Neuropathologica · doi:10.1007/bf00687932 · Cited by 7
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“that Dr Robert Terry and co-workers [25,26] thought I was referring to all neurofilaments and not simply the tangle filaments (which I immediately had recognised were not neurofilaments); and both those publications recorded that the tangle filaments were ‘not different from normal neurofilaments’ in appearance – thes…”
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What's new in the pathology of neuronal cytoskeleton: The significance of neurofibrillary tangles
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Authors: Terry, R. D.
Corresponding author: Terry, Robert D.
Venue: Journal of Neuropathology and Experimental Neurology
Publisher: Oxford University Press (OUP)
Published: 1963-10
Volume: 22
Issue: 4
Pages: 629-642
ISSN: 0022-3069 (ISSN-L)
DOI: 10.1097/00005072-196310000-00005
OpenAlex: W2070494722
Cited by: 403
References: 0
Citations by year: 2026: 4 · 2025: 5 · 2024: 6 · 2023: 8 · 2022: 10 · 2021: 9 · 2020: 13 · 2019: 10 · 2018: 6 · 2017: 8 · 2016: 3 · 2015: 7 · 2014: 10 · 2013: 4 · 2012: 6
FWCI: 3.13
Type: journal article
Language: en
Open access: closed
Locations: Journal of Neuropathology & Experimental Neurology (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
Keywords: neurofibrillary tangles, Alzheimer's disease, fine structure, ultrastructure, neurofibrillary pathology
MeSH terms: Alzheimer Disease, Cerebral Cortex, Dementia, Electrons, Humans, Microscopy, Microscopy, Electron, Neurons, Pathology, Psychotic Disorders, Neurofibrillary Tangles

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THE FINE STRUCTURE OF NEUROFIBRILLARY TANGLES IN ALZHEIMERʼS DISEASE

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