The DOI matches its Crossref record; 13 of the 13 references it cites were found in a registry or an index.
Tau, where are we now?
Abstract
Tau is a multifunctional protein that was originally identified as a microtubule-associated protein. Tau is primarily a neuronal protein, but it is becoming increasingly evident that tau is present in non-neuronal cells where it also plays important roles. Tau is the primary protein component of the filaments (both paired helical and straight filaments) found in Alzheimer's disease brain. Further there is an ever growing family of neurodegenerative diseases called "tauopathies" where tau pathology is the primary, defining characteristic with little or no Abeta pathology. These findings, along with the fact that mutations in the tau gene cause a group of diseases collectively known as frontotemporal dementia with parkinsonism linked to chromosome 17 (FTDP-17), clearly demonstrate that tau dysfunction results in neuronal dysfunction and death. This review highlights recent findings concerning the normal metabolism and function of tau, as well as the abnormal processing and function of tau in Alzheimer's disease and in the tauopathies, both sporadic and familial.
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Tau is a component of neurofibrillary tangles (NFT) in Alzheimer's disease and related tauopathies.
“The microtubule-binding protein tau is a component of neurofibrillary tangles (NFT) in Alzheimer's disease (AD) and related disorders that are collectively referred to as tauopathies (Morishima-Kawashima et al. 1995), (Johnson and Bailey 2002).”
From TMEM55B downregulation promotes neurodegeneration in Alzheimer’s disease models (2026) · cites this paper as Johnson and Bailey 2002
Tau is a component of neurofibrillary tangles (NFT) in Alzheimer's disease (AD) and related tauopathies.
“The microtubule-binding protein tau is a component of neurofibrillary tangles (NFT) in Alzheimer's disease (AD) and related disorders that are collectively referred to as tauopathies (Morishima-Kawashima et al. 1995), (Johnson and Bailey 2002).”
From TMEM55B downregulation promotes neurodegeneration in Alzheimer’s disease models (2026) · cites this paper as Johnson and Bailey 2002
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Macromolecular crowding: obvious but underappreciated
Ellis, R. J. (2001) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(01)01938-7 · Cited by 2,309
Apoptosis in neurodegenerative disorders
Mattson, M. P. (2000) · Nature Reviews Molecular Cell Biology · doi:10.1038/35040009 · Cited by 1,605
Minton, A. P. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.r100005200 · Cited by 1,474 · cited 2×
“…in vitro studies on the mechanisms of tau filament formation could be carried out in the presence of high concentrations of natural or synthetic macro-molecules to mimic the crowded conditions in situ [45, 145], and thus provide more insight into the processes that may be occurring in AD brain.”
Hiesberger, T., Trommsdorff, M., Howell, B. W., Goffinet, A., Mumby, M. C., Cooper, J. A., & Herz, J. (1999) · Neuron · doi:10.1016/s0896-6273(00)80861-2 · Cited by 916
The prolyl isomerase Pin1 restores the function of Alzheimer-associated phosphorylated tau protein
Lu, P.-J., Wulf, G., Zhou, X. Z., Davies, P., & Lu, K. P. (1999) · Nature · doi:10.1038/21650 · Cited by 721
Tau filament formation in transgenic mice expressing P301L tau
Götz, J., Chen, F., Barmettler, R., & Nitsch, R. M. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m006531200 · Cited by 495
Corticobasal degeneration and progressive supranuclear palsy share a common tau haplotype
Houlden, H., Baker, M., Morris, H. R., MacDonald, N., Pickering–Brown, S., Adamson, J., Lees, A. J., Rossor, M. N., Quinn, N. P., Kertesz, A., et al. (2001) · Neurology · doi:10.1212/wnl.56.12.1702 · Cited by 409
The Microtubule-associated Protein Tau Is Extensively Modified with O-linked N-acetylglucosamine
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Self-citationUbiquitin is conjugated with amino-terminally processed tau in paired helical filaments
Morishima-Kawashima, M., Hasegawa, M., Takio, K., Suzuki, M., Titani, K., & Ihara, Y. (1993) · Neuron · doi:10.1016/0896-6273(93)90063-w · Cited by 332
Tau Cleavage and Dephosphorylation in Cerebellar Granule Neurons Undergoing Apoptosis
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Maas, T., Eidenmüller, J., & Brandt, R. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m000389200 · Cited by 226
Different distribution of phosphorylated tau protein isoforms in Alzheimer's and Pick's diseases
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Tau phosphorylation in neuronal cell function and dysfunction
Johnson, G. V. W., & Stoothoff, W. H. (2004) · Journal of Cell Science · doi:10.1242/jcs.01558 · Cited by 624
Self-citationUntangling tau hyperphosphorylation in drug design for neurodegenerative diseases
Mazanetz, M. P., & Fischer, P. M. (2007) · Nature Reviews Drug Discovery · doi:10.1038/nrd2111 · Cited by 459
Histone deacetylase 6 interacts with the microtubule‐associated protein tau
Ding, H., Dolan, P. J., & Johnson, G. V. W. (2008) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2008.05564.x · Cited by 387
Self-citationCho, J., & Johnson, G. V. W. (2004) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02155.x · Cited by 282
Self-citationBlalock, E. M., Buechel, H. M., Popovic, J., Geddes, J. W., & Landfield, P. W. (2011) · Journal of Chemical Neuroanatomy · doi:10.1016/j.jchemneu.2011.06.007 · Cited by 211
Cdk5 is involved in NFT-like tauopathy induced by transient cerebral ischemia in female rats
Wen, Y., Yang, S.-H., Liu, R., Perez, E. J., Brun-Zinkernagel, A. M., Koulen, P., & Simpkins, J. W. (2007) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2006.10.011 · Cited by 162
Stress is critical for LPS-induced activation of microglia and damage in the rat hippocampus
Espinosa-Oliva, A. M., de Pablos, R. M., Villarán, R. F., Argüelles, S., Venero, J. L., Machado, A., & Cano, J. (2011) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2009.01.012 · Cited by 151
Wei, Y., Qu, M.-H., Wang, X.-S., Chen, L., Wang, D.-L., Liu, Y., Hua, Q., & He, R.-Q. (2008) · PLoS ONE · doi:10.1371/journal.pone.0002600 · Cited by 129
Differential Incorporation of Tau Isoforms in Alzheimer's Disease
Espinoza, M., de Silva, R., Dickson, D. W., & Davies, P. (2008) · Journal of Alzheimer's Disease · doi:10.3233/jad-2008-14101 · Cited by 119
Azorsa, D. O., Robeson, R. H., Frost, D., hoovet, B. M., Brautigam, G. R., Dickey, C., Beaudry, C., Basu, G. D., Holz, D. R., Hernandez, J. A., et al. (2010) · BMC Genomics · doi:10.1186/1471-2164-11-25 · Cited by 88
Qu, L., Li, S., Ji, L., Luo, S., Ding, M., Yin, F., Wang, C., Luo, H., Lu, D., Liu, X., et al. (2021) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2021.113889 · Cited by 61
Tau phosphorylation in human brain: relationship to behavioral disturbance in dementia
Guadagna, S., Esiri, M. M., Williams, R. J., & Francis, P. T. (2012) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2012.01.015 · Cited by 48
TMEM55B downregulation promotes neurodegeneration in Alzheimer’s disease models
Roy, B., Contu, V. R., Jeziorek, M., Friedman, W. J., & Wong, C.-O. (2026) · doi:10.64898/2026.10.21.760809
Metadata
- Authors
- Johnson, G. V. W., & Bailey, C. D. C.
- Affiliations
- Department of Psychiatry, University of Alabama at Birmingham School of Medicine, Birmingham, AL 35294-0017, USA
- Venue
- Journal of Alzheimer's Disease
- Publisher
- SAGE Publications
- Published
- 2002-11-01
- Volume
- 4
- Issue
- 5
- Pages
- 375-398
- ISSN
- 1875-8908
- 1387-2877
- Cited by
- 61
- References
- 13
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