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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“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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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
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1 of the 24 references couldn’t be matched to a known paper.
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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Lipka, J., Shan, X., Zhang, Q., Dutka, P., Phu, L., Johnson, M. C., Wendorff, T. J., Adrian, M., Biton, A., Sun, D., et al. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.09.07.749799
Böken, D., Beltran-Lobo, P., Wu, Y., Rowe, L. A., Fertan, E., Croft, C. L., Jiménez-Sánchez, M., Cox, D., & Klenerman, D. (2026) · Advanced Science · doi:10.1002/advs.77822 · Cited by 1
Gatto, R. G., Youssef, H., Uruk, G., Carlos, A. F., Reichard, R. R., Lowe, V. J., Whitwell, J. L., & Josephs, K. A. (2026) · Brain Sciences · doi:10.3390/brainsci16101013
Kjar, A., Kim, H., Spetz, M. R., Jarrett, Z., Fernandez, M., Wang, J., Russotti, M. L., Bodnya, C., Chavarría, D., Hohman, T. J., et al. (2026) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.6c00376
An age-preserving neuronal iSpheroid platform for modeling human aging and Alzheimer’s diseasePreprint
Alsolami, S., Wang, M., Sabedot, T. S., Singh, U., Kirk, B., Mitchell, L. E., Hernandez, M., Skvir, N. J., Bowman, C., Oiwa, K., et al. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.09.30.755853
Nimavard, R. T., Sadeghi, S. A., Colón-Rosado, J. A., Yue, Y., Fang, F., Hagar, H. C., Kuo, M.-H., & Sun, L. (2026) · Journal of Proteome Research · doi:10.1021/acs.jproteome.6c00539
Design of readers for pathological PTM proteoforms in Alzheimer’s diseasePreprint
Wu, K., Schantz, T., Chang, L., Chabria, P., Bashaw, E., Kalatturu, T. R., Kim, D. Y., Chen, A., Corley, N., Bera, A. K., et al. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.10.20.760520
Second-generation tau PET tracer in situ binding assessed with fluorescence imagingPreprint
Antic, A., Dreos, A., Lashley, T., Yo-Ap, S. Y., Sander, K., Schöll, M., & Hanrieder, J. (2026) · Research Square · doi:10.21203/rs.3.rs-11153643/v1
Duong (2000) · doi:10.1002/1097-0169(200011)47:3
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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