Cited by 458Alzheimer's disease research and treatmentsCholinesterase and Neurodegenerative DiseasesDementia and Cognitive Impairment Research

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Advances in tau-focused drug discovery for Alzheimer's disease and related tauopathies

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Brunden, Kurt R., Trojanowski, John Q., Lee, Virginia M.-Y.·2009·Nature Reviews Drug Discovery

DOI 10.1038/nrd2959PMC PMC2787232

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Abstract

Neuronal inclusions comprised of the microtubule-associated protein tau are found in numerous neurodegenerative diseases, commonly known as tauopathies. In Alzheimer's disease - the most prevalent tauopathy - misfolded tau is probably a key pathological agent. The recent failure of amyloid-beta-targeted therapeutics in Phase III clinical trials suggests that it is timely and prudent to consider alternative drug discovery strategies for Alzheimer's disease. Here, we focus on strategies directed at reducing misfolded tau and compensating for the loss of normal tau function.

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Neurofibrillary tangles but not senile plaques parallel duration and severity of Alzheimer's disease
Arriagada, P. V., Growdon, J. H., Hedley-Whyte, E. T., & Hyman, B. T. (1992) · Neurology · doi:10.1212/wnl.42.3.631 · Cited by 2,668
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Goedert, M., Spillantini, M. G., Jakes, R., Rutherford, D., & Crowther, R. A. (1989) · Neuron · doi:10.1016/0896-6273(89)90210-9 · Cited by 2,492
Neurodegenerative Tauopathies
Lee, V. M.-Y., Goedert, M., & Trojanowski, J. Q. (2001) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.24.1.1121 · Cited by 2,480
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Tau protein isoforms, phosphorylation and role in neurodegenerative disorders11These authors contributed equally to this work.
Buée, L., Bussière, T., Buée‐Scherrer, V., Delacourte, A., & Hof, P. R. (2000) · Brain Research Reviews · doi:10.1016/s0165-0173(00)00019-9 · Cited by 2,133
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Roberson, E. D., Scearce-Levie, K., Palop, J. J., Yan, F., Cheng, I. H., Wu, T., Gerstein, H., Yu, G.-Q., & Mucke, L. (2007) · Science · doi:10.1126/science.1141736 · Cited by 1,892
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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

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Research works printed but not linked: 3

Avila, J. Tau and tauopathies: tau phosphorylation and tau assembly. FEBS J. 273, 23 (2006).
Alonso, A. D., GrundkeIqbal, I. & Iqbal, K. Abnormally phosphorylated tau from Alzheimer disease brain depolymerizes microtubules. Neurobiol. Aging 15, S37 (1994).
Schneider, A., Biernat, J., von Bergen, M., Mandelkow, E. & Mandelkow, E. M. Phosphorylation that detaches tau from microtubules S262 and S214 protects it against aggregation into Alzheimer paired helical filaments. J. Neurochem. 73, S26 (1999).

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Authors: Brunden, K. R., Trojanowski, J. Q., & Lee, V. M.-Y.
Affiliations: University of Pennsylvania (US)
Corresponding author: Brunden, Kurt R.
ORCID: Brunden, Kurt R.
Trojanowski, John Q.
Lee, Virginia M.-Y.
Venue: Nature Reviews Drug Discovery
Publisher: Springer Science and Business Media LLC
Published: 2009-10
Volume: 8
Issue: 10
Pages: 783-793
ISSN: 1474-1776 (ISSN-L)
1474-1784
DOI: 10.1038/nrd2959
PMC: PMC2787232
OpenAlex: W2021370614
Cited by: 440
References: 140
Citations by year: 2026: 7 · 2025: 12 · 2024: 20 · 2023: 12 · 2022: 17 · 2021: 31 · 2020: 28 · 2019: 23 · 2018: 22 · 2017: 30 · 2016: 30 · 2015: 22 · 2014: 40 · 2013: 31 · 2012: 43
FWCI: 4.24
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: www.springer.com/tdm (tdm)
Locations: Nature Reviews Drug Discovery (publishedVersion)
PubMed (publishedVersion)
Europe PMC (PubMed Central) (acceptedVersion)
PubMed Central (acceptedVersion)
Funders: National Institutes of Health (5u01ag024904-10)
National Institute on Aging (U01-AG-024904, P01AG014382, P01 AG11542, P01-AG09215, P30AG10124, P01AG011542, P01 AG-17586, P01AG014449, P01 AG14382, P30AG010124, P01AG009215, P01AG017586, P01 AG14449, UO1 AG24904, U19AG010483, P01-AG19724, P01AG019724)
National Institute of Neurological Disorders and Stroke (P01NS044233)
Topics: Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
Health Sciences › Medicine › Pharmacology (medical) › Cholinesterase and Neurodegenerative Diseases
Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
Keywords: tau protein, tauopathy, Alzheimer's disease, tau misfolding, neurodegeneration, tau functions, microtubule-associated proteins
MeSH terms: Alzheimer Disease, Animals, Humans, tau Proteins, Tauopathies, Drug Discovery

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Advances in tau-focused drug discovery for Alzheimer's disease and related tauopathies

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