The DOI matches its Crossref record; 23 of the 24 references it cites were found in a registry or an index.
Monoclonal antibody AT8 recognises tau protein phosphorylated at both serine 202 and threonine 205
Abstract
Hyperphosphorylated microtubule-associated protein tau is the major component of the paired helical filament of Alzheimer's disease. Phosphorylation-dependent anti-tau antibodies are being used to identify specific amino acids that are phosphorylated in tau from normal brain and Alzheimer's disease brain. As such, monoclonal antibody AT8 is widely used. By a combination of site-directed mutagenesis of recombinant tau and in vitro phosphorylation, we show that AT8 requires tau protein to be phosphorylated at both serine 202 and threonine 205 (using the numbering of the longest human brain tau isoform.
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In the citing paper
“However, no significant difference was observed between PS19 and PS19;ApoeCh mice at both 5 and 9 mo of age (Fig. 5a-d, Supp. Figure 14a-c) [45, 67–69].”
From APOE Christchurch enhances a disease-associated microglial response to plaque but suppresses response to tau pathology (2025) · cites this paper as [67]
In the citing paper
“AT8, which recognizes Tau that is phosphorylated at Ser202 and Thr205 (Goedert et al., 1995) or Ser199, Ser202, and Thr205 (Hanger et al., 2009).”
From Regulation of Mitochondrial Transport and Inter-Microtubule Spacing by Tau Phosphorylation at the Sites Hyperphosphorylated in Alzheimer's Disease (2012) · cites this paper as Goedert et al., 1995
In the citing paper
“their detection by this antibody is commonly used as a marker of abnormal phosphorylation in brains of Alzheimer's patients.”
From Regulation of Mitochondrial Transport and Inter-Microtubule Spacing by Tau Phosphorylation at the Sites Hyperphosphorylated in Alzheimer's Disease (2012) · cites this paper as Goedert et al., 1995
Citations
Cites
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Self-citationA68: a Major Subunit of Paired Helical Filaments and Derivatized Forms of Normal Tau
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Goedert, M., & Jakes, R. (1990) · The EMBO Journal · doi:10.1002/j.1460-2075.1990.tb07870.x · Cited by 929
Self-citationBramblett, G. T., Goedert, M., Jakes, R., Merrick, S. E., Trojanowski, J. Q., & Lee, V. M. Y. (1993) · Neuron · doi:10.1016/0896-6273(93)90057-x · Cited by 903
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Tau protein and the neurofibrillary pathology of Alzheimer's disease
Goedert, M. (1993) · Trends in Neurosciences · doi:10.1016/0166-2236(93)90078-z · Cited by 721
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Mitogen activated protein (MAP) kinase transforms tau protein into an Alzheimer‐like state.
Drewes, G., Lichtenberg‐Kraag, B., Döring, F., Mandelkow, E. M., Biernat, J., Goris, J., Dorée, M., & Mandelkow, E. (1992) · The EMBO Journal · doi:10.1002/j.1460-2075.1992.tb05272.x · Cited by 565
Glycogen synthase kinase‐3 and the Alzheimer‐like state of microtubule‐associated protein tau
Mandelkow, E.-M., Drewes, G., Biernat, J., Gustke, N., Van Lint, J., Vandenheede, J. R., & Mandelkow, E. (1992) · FEBS Letters · doi:10.1016/0014-5793(92)81496-9 · Cited by 515
Research works printed but not linked: 1
- Trojanowski, 1993, PHF-Tau (A68): From pathological marker to potential mediator of neuronal dysfunction and de generation in Alzheimer's disease, Clin. Neurosci., 1, 184191
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Sorted by citations
Braak, H., Alafuzoff, I., Arzberger, T., Kretzschmar, H., & Del Tredici, K. (2006) · Acta Neuropathologica · doi:10.1007/s00401-006-0127-z · Cited by 3,172
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 2,142
Transmission and spreading of tauopathy in transgenic mouse brain
Clavaguera, F., Bolmont, T., Crowther, R. A., Abramowski, D., Frank, S., Probst, A., Fraser, G., Stalder, A. K., Beibel, M., Staufenbiel, M., et al. (2009) · Nature Cell Biology · doi:10.1038/ncb1901 · Cited by 1,803
Self-citationFormation of Neurofibrillary Tangles in P301L Tau Transgenic Mice Induced by Aβ42 Fibrils
Götz, J., Chen, F., van Dorpe, J., & Nitsch, R. M. (2001) · Science · doi:10.1126/science.1062097 · Cited by 1,526
Two amyloid precursor protein transgenic mouse models with Alzheimer disease-like pathology
Sturchler-Pierrat, C., Abramowski, D., Duke, M., Wiederhold, K.-H., Mistl, C., Rothacher, S., Ledermann, B., Bürki, K., Frey, P., Paganetti, P. A., et al. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.24.13287 · Cited by 1,507
Metadata
- Authors
- Goedert, M., Jakes, R., & Vanmechelen, E.
- Affiliations
- MRC Laboratory of Molecular Biology (GB)
- Fujirebio (Belgium) (BE)
- Corresponding author
- Goedert, M.
- Venue
- Neuroscience Letters
- Publisher
- Elsevier BV
- Published
- 1995-04
- Volume
- 189
- Issue
- 3
- Pages
- 167-170
- ISSN
- 0304-3940 (ISSN-L)
- OpenAlex
- W2062772621
- Cited by
- 608
- References
- 24
- Citations by year
- 2026: 36 · 2025: 33 · 2024: 20 · 2023: 30 · 2022: 27 · 2021: 26 · 2020: 20 · 2019: 20 · 2018: 20 · 2017: 15 · 2016: 12 · 2015: 22 · 2014: 12 · 2013: 17 · 2012: 14
- FWCI
- 11.08
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Neuroscience Letters (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
- tau protein, tau phosphorylation, paired helical filaments, Alzheimer's disease, anti-tau antibodies, site-directed mutagenesis, in vitro phosphorylation
- MeSH terms
- Amino Acid Sequence, Antibodies, Monoclonal, Cloning, Molecular, Escherichia coli, Humans, Molecular Sequence Data, Phosphorylation, Protein Kinases, Recombinant Proteins, Serine, Threonine, tau Proteins, DNA, Complementary
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