The DOI matches its Crossref record; 43 of the 43 references it cites were found in a registry or an index.
Protein sequence and mass spectrometric analyses of tau in the Alzheimer's disease brain
Open accessAbstract
Tau with unusually slow mobilities in sodium dodecyl sulfate-polyacrylamide gel electrophoresis was purified from the Sarkosyl-insoluble pellet of Alzheimer's disease brain homogenates. Such species of tau (PHF-tau) are considered to construct the framework of the sodium dodecyl sulfate-soluble form of paired helical filaments (PHF). Detailed comparison of peptide maps of PHF-tau and normal tau before and after dephosphorylation pointed to three anomalously eluted peaks which contained abnormally phosphorylated peptides, residues 191-225, 226-240, 260-267, and 386-438, according to the numbering of the longest tau isoform (Goedert, M., Spillantini, M. G., Jakes, R., Rutherford, D., and Crowther, R. A. (1989) Neuron 3, 519-526). Protein sequence and mass spectrometric analyses localized Thr-231 and Ser-235 as the abnormal phosphorylation sites and further indicated that each tau 1 site (residues 191-225) and the most carboxyl-terminal portion of the protein (residues 386-438) carries more than two abnormal phosphates. Ser-262 was also phosphorylated in a fraction of PHF-tau. Modifications other than phosphorylation, removal of the initiator methionine, and N alpha-acetylation at the amino terminus and deamidation at 2 asparaginyl residues were found in PHF-tau, but these modifications were also present in normal tau.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“Prior studies have shown that many phosphorylated residues in PHF-tau are serines or threonines followed by a proline [1,6,8,11].”
From Glycogen synthase kinase-3β phosphorylates tau protein at multiple sites in intact cells (1995) · cites this paper as [8]
Citations
Cites
Grundke-Iqbal, I., Iqbal, K., Tung, Y. C., Quinlan, M., Wisniewski, H. M., & Binder, L. I. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.13.4913 · Cited by 3,676
A protein factor essential for microtubule assembly
Weingarten, M. D., Lockwood, A. H., Hwo, S. Y., & Kirschner, M. W. (1975) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.72.5.1858 · Cited by 3,089
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
A68: a Major Subunit of Paired Helical Filaments and Derivatized Forms of Normal Tau
Lee, V. M.-Y., Balin, B. J., Otvos, L., & Trojanowski, J. Q. (1991) · Science · doi:10.1126/science.1899488 · Cited by 1,418
Goedert, M., Spillantini, M. G., Cairns, N. J., & Crowther, R. A. (1992) · Neuron · doi:10.1016/0896-6273(92)90117-v · Cited by 1,122
Goedert, M., Spillantini, M. G., Potier, M. C., Ulrich, J., & Crowther, R. A. (1989) · The EMBO Journal · doi:10.1002/j.1460-2075.1989.tb03390.x · Cited by 1,037
Wischik, C. M., Novak, M., Thøgersen, H. C., Edwards, P. C., Runswick, M. J., Jakes, R., Walker, J. E., Milstein, C., Roth, M., & Klug, A. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.12.4506 · Cited by 939
Bruins, A. P., Covey, T. R., & Henion, J. D. (1987) · Analytical Chemistry · doi:10.1021/ac00149a003 · Cited by 874
Ubiquitin Is a Component of Paired Helical Filaments in Alzheimer's Disease
Mori, H., Kondo, J., & Ihara, Y. (1987) · Science · doi:10.1126/science.3029875 · Cited by 843
Self-citationGreenberg, S. G., & Davies, P. J. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.15.5827 · Cited by 735
Cited by
Sorted by citations
Items 401–428 of 428
[Regulation of phosphorylation of tau by insulin and Ca2+ signals].
Yamamoto, H. (2005) · Folia Pharmacologica Japonica · doi:10.1254/fpj.125.129
Biochemical Analysis of Tau and α-Synuclein in Neurodegenerative Diseases
Hasegawa, M., Taniguchi, S., Aoyagi, H., Fujiwara, H., & Iwatsubo, T. (2002) · Advances in behavioral biology · doi:10.1007/978-0-306-47593-1_91
Self-citationPathological Changes in the Elderly Human Brain
Mann, D. M. A. (1997) · Springer eBooks · doi:10.1007/978-1-4615-6001-2_2
Detection and conformational characterization of misfolded proteins in neurodegenerative diseases
Morozova, O. A. (2016) · Library, Museums and Press - UDSpace (University of Delaware) · doi:10.58088/yt52-dk03
The Analysis of Exosomal Tau Release and its Regulation
Bradshaw, A. (2018) · UCL Discovery (University College London)
Tau proteolysis mechanisms and relevance for tauopathies
Quinn, J. P. (2019) · Research Explorer (The University of Manchester)
Tau Protein and the Neurofibrillary Pathology of Alzheimer’s Disease
Goedert, M. (1996) · Springer eBooks · doi:10.1007/978-3-642-80109-9_9 · Cited by 1
Faculty Opinions recommendation of Near-atomic model of microtubule-tau interactions.
Slep, K. C. (2018) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.733205353.793546066
Authors' response to commentaries
Morishima‐Kawashima, M., & Ihara, Y. (1995) · Neurobiology of Aging · doi:10.1016/0197-4580(95)00032-a
Self-citationProteomics for Novel Biomarker and Drug Target Discovery in Alzheimer Disease
Zhu, H., Cai, M., Chen, D., Sha, J., Du, L., Chen, Y., Liu, S., Zheng, Q., Wei, X., & Bai, B. (2025) · Springer eBooks · doi:10.1007/978-3-031-80849-4_12
Aβ Modulates Extracellular Vesicles Proteomic Profile Impacting Phosphorylation Mediators
Vaz, M., Martins, T. S., Trigo, D., Silva, O. A. B. D. C. E., Amado, F. M. L., Vitorino, R. M. P., & Henriques, A. G. (2025) · Molecular Neurobiology · doi:10.1007/s12035-025-05343-0 · Cited by 1
MAPK family members differentially regulate pThr175 tau-mediated pathogenicity
Donison, N. S., Hintermayer, M. A., Palik, J., Fisher, J., Volkening, K., & Strong, M. J. (2025) · Neurobiology of Disease · doi:10.1016/j.nbd.2025.107223
Gobom, J., Benedet, A. L., Mattsson, N., Montoliu‐Gaya, L., Schultz, N., Ashton, N. J., Janelidze, S., Servaes, S., Sauer, M., Pascoal, T. A., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26553350
Tau nucléaire : un acteur clé dans le stress neuronal
Sultan, A. (2010) · theses.fr (ABES) · doi:10.70675/98c582c8z1d31z4edazbbfaz92750b338b46
Rôle des modifications post-traductionnelles dans le processus d’agrégation de la protéine Tau
Despres, C. (2017) · theses.fr (ABES) · doi:10.70675/de10f843z8572z4295zb672z763dbf30e2b5
Identification et caractérisation fonctionnelle de nouveaux sites de clivage de la protéine Tau
Derisbourg, M. J. (2015) · theses.fr (ABES) · doi:10.70675/ef5f45b0zf4e8z433fz9beaz8d2cc6de65bc
Altered neuronal activity in the hippocampal CA3 region in an in vitro model of tauopathy
Goncalves, A. (2020) · theses.fr (ABES) · doi:10.70675/b42db6dez88a0z4a14z93eez8f51d19d46f5
The emerging role of polo-like kinase 2 in Alzheimer's disease
Martínez-Drudis, L., Sheta, R., Musiol, D., Teixeira, M., & Oueslati, A. (2026) · Experimental Neurology · doi:10.1016/j.expneurol.2026.115806
Molekulargenetik und Molekularbiologie der Alzheimer-Krankheit
Sandbrink, R., & Beyreuther, K. T. (1999) · Springer eBooks · doi:10.1007/978-3-642-60175-0_7
Microtubules, Tau Protein,and Paired Helical Filaments in Alzheimer’s Disease
Mandelkow�, E., Biernat, J., Lichtenberg-Kraag, B., Drewes, G., Wille, H., Gustke, N., Baumann, K., & Mandelkow�, E. (1995) · Springer eBooks · doi:10.1007/978-3-642-79482-7_16
The dual role of tau in cell polarisation and organelle trafficking
Mandelkow, E., Biernat, J., Stamer, K., Trinczek, B., & Mandelkow�, E. (2001) · Birkhäuser Basel eBooks · doi:10.1007/978-3-0348-8225-5_12
- Self-citation
Metadata
- Authors
- Hasegawa, M., Morishima-Kawashima, M., Takio, K., Suzuki, M., Titani, K., & Ihara, Y.
- Affiliations
- The University of Tokyo (JP)
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1992-10
- Volume
- 267
- Issue
- 24
- Pages
- 17047-17054
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1598318710
- Cited by
- 430
- References
- 43
- Citations by year
- 2026: 4 · 2025: 10 · 2024: 8 · 2023: 10 · 2022: 7 · 2021: 8 · 2020: 19 · 2019: 14 · 2018: 10 · 2017: 3 · 2016: 17 · 2015: 11 · 2014: 5 · 2013: 10 · 2012: 9
- FWCI
- 22.71
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Keywords
- tau protein, Alzheimer's disease, paired helical filaments, phosphorylation sites, dephosphorylation, peptide mapping, protein modification, N-terminal acetylation, deamidation
- MeSH terms
- Alzheimer Disease, Amino Acid Sequence, Brain, Brain Chemistry, Electrophoresis, Polyacrylamide Gel, Humans, Molecular Sequence Data, Peptide Fragments, Peptide Mapping, Mass Spectrometry, tau Proteins
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
