Cited by 430Alzheimer's disease research and treatmentsAdvanced Proteomics Techniques and ApplicationsDementia and Cognitive Impairment Research

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 access

Hasegawa, M, Morishima-Kawashima, M, Takio, K, Suzuki, M, Titani, K, Ihara, Y·1992·Journal of Biological Chemistry

DOI 10.1016/s0021-9258(18)41890-x

Open this paper in CoChat — free account

Abstract

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.

Integrity signals

Registry

Crossref · 10.1016/s0021-9258(18)41890-x

Cites

43 of 43 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

We couldn’t retrieve this paper’s full text, so its claims and self-check weren’t run. The registry and citation checks still apply.

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?

Abnormal phosphorylation of the microtubule-associated protein tau (tau) in Alzheimer cytoskeletal pathology.
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
Multiple isoforms of human microtubule-associated protein tau: sequences and localization in neurofibrillary tangles of Alzheimer's disease
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
Tau proteins of alzheimer paired helical filaments: Abnormal phosphorylation of all six brain isoforms
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
Cloning and sequencing of the cDNA encoding an isoform of microtubule‐associated protein tau containing four tandem repeats: differential expression of tau protein mRNAs in human brain.
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
Isolation of a fragment of tau derived from the core of the paired helical filament of Alzheimer disease.
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
Ion spray interface for combined liquid chromatography/atmospheric pressure ionization mass spectrometry
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-citation
A preparation of Alzheimer paired helical filaments that displays distinct tau proteins by polyacrylamide gel electrophoresis.
Greenberg, S. G., & Davies, P. J. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.15.5827 · Cited by 735

Show all 43 references

Sorted by citations

Items 201–300 of 428

Overexpressed tau protein in cultured cells is phosphorylated without formation of PHF: implication of phosphoprotein phosphatase involvement
Baum, L., Seger, R., Woodgett, J. R., Kawabata, S., Maruyama, K., Koyama, M., Silver, J. E., & Saitoh, T. (1995) · Molecular Brain Research · doi:10.1016/0169-328x(95)00111-5 · Cited by 58
P‐tau235: a novel biomarker for staging preclinical Alzheimer’s disease
Lantero‐Rodriguez, J., Snellman, A., Benedet, A. L., Milà‐Alomà, M., Camporesi, E., Montoliu‐Gaya, L., Ashton, N. J., Vrillon, A., Karikari, T. K., Gispert, J. D., et al. (2021) · EMBO Molecular Medicine · doi:10.15252/emmm.202115098 · Cited by 59
Cdk5 increases MARK4 activity and augments pathological tau accumulation and toxicity through tau phosphorylation at Ser262
Saito, T., Oba, T., Shimizu, S., Asada, A., Iijima, K., & Ando, K. (2019) · Human Molecular Genetics · doi:10.1093/hmg/ddz120 · Cited by 51
A Cellular Model To Monitor Proteasome Dysfunction by α-Synuclein
Nonaka, T., & Hasegawa, M. (2009) · Biochemistry · doi:10.1021/bi900619j · Cited by 57
Self-citation
The complex relationship between soluble and insoluble tau in tauopathies revealed by efficient dephosphorylation and specific antibodies
Hanger, D. P., Gibb, G., de Silva, R., Boutajangout, A., Brion, J., Révész, T., Lees, A. J., & Anderton, B. H. (2002) · FEBS Letters · doi:10.1016/s0014-5793(02)03611-6 · Cited by 55
A combinatorial native MS and LC-MS/MS approach reveals high intrinsic phosphorylation of human Tau but minimal levels of other key modifications
Drepper, F., Biernat, J., Kaniyappan, S., Meyer, H. E., Mandelkow, E., Warscheid, B., & Mandelkow�, E. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra120.015882 · Cited by 56
Tau protein kinase I/GSK-3Β/kinase FA in heparin phosphorylates tau on Ser199, Thr231, Ser235, Ser262, Ser369, and Ser400 sites phosphorylated in Alzheimer disease brain
Song, J., & Yang, S. (1995) · Journal of Protein Chemistry · doi:10.1007/bf01888367 · Cited by 54
Protein Kinase F A /Glycogen Synthase Kinase‐3α After Heparin Potentiation Phosphorylates τ on Sites Abnormally Phosphorylated in Alzheimer's Disease Brain
Yang, S., Yu, J., Shiah, S., & Huang, J. (1994) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1994.63041416.x · Cited by 54
Mechanism of Tau-Promoted Microtubule Assembly As Probed by NMR Spectroscopy
Gigant, B., Landrieu, I., Fauquant, C., Barbier, P., Huvent, I., Wieruszeski, J., Knossow, M., & Lippens, G. M. (2014) · Journal of the American Chemical Society · doi:10.1021/ja504864m · Cited by 54
Tau Potentiates Nerve Growth Factor-induced Mitogen-activated Protein Kinase Signaling and Neurite Initiation without a Requirement for Microtubule Binding
Leugers, C. J., & Lee, G. S. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.105387 · Cited by 60
Comparison of the phosphorylation of microtubule-associated protein tau by non-proline dependent protein kinases
Singh, J., Grundke, I., McDonald, B., & Iqbal, K. (1994) · Molecular and Cellular Biochemistry · doi:10.1007/bf00925955 · Cited by 53
Alzheimer neurofibrillary lesions: Molecular nature and potential roles of different components
Yen, S.-H. C., Liu, W.-K., Hall, F. L., Yan, S., Stern, D. M., & Dickson, D. W. (1995) · Neurobiology of Aging · doi:10.1016/0197-4580(95)00022-7 · Cited by 53
Phosphorylation of Neuronal Cytoskeletal Proteins in Alzheimer's Disease and Lewy Body Dementiasa
Trojanowski, J. Q., & LEE, V. M. ‐. (1994) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1994.tb44403.x · Cited by 54
A novel tau‐tubulin kinase from bovine brain
Takahashi, M., Tomizawa, K., Sato, K., Ohtake, A., & Omori, A. (1995) · FEBS Letters · doi:10.1016/0014-5793(95)00955-9 · Cited by 52
Molecular aging of tau: disulfide‐independent aggregation and non‐enzymatic degradation in vitro and in vivo
Watanabe, A., Hong, W., Dohmae, N., Takio, K., Morishima‐Kawashima, M., & Ihara, Y. (2004) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02611.x · Cited by 51
Self-citation
Post-translational modifications of tau protein
Pevalova, M., Filipčík, P., Novák, M., Ávila, J., & Iqbal, K. (2006) · Bratislavské lekárske listy/Bratislava medical journal · doi:10.1007/bf03656852 · Cited by 50
[6] Purification of paired helical filament tau and normal tau from human brain tissue
Lee, V. M. ‐., Wang, J., & Trojanowski, J. Q. (1999) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(99)09008-4 · Cited by 52
No difference in kinetics of tau or histone phosphorylation by CDK5/p25 versus CDK5/p35 in vitro
Peterson, D. W., Ando, D. M., Taketa, D. A., Zhou, H., Dahlquist, F. W., & Lew, J. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0912718107 · Cited by 51
Relative Resistance of Cdk5-phosphorylated CRMP2 to Dephosphorylation
Cole, A. R., Soutar, M. P. M., Rembutsu, M., van Aalten, L., Hastie, C. J., McLauchlan, H., Peggie, M. W., Balaštík, M., Lu, K. P., & Sutherland, C. D. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m801645200 · Cited by 50
Cellular and molecular pathology in alzheimer's disease
Crutcher, K. A., Anderton, B. H., Barger, S. W., Ohm, T. G., & Snow, A. D. (1993) · Hippocampus · doi:10.1002/hipo.1993.4500030730 · Cited by 50
Stimulation of MAP kinase by v‐raf transformation of fibroblasts fails to induce hyperphosphorylation of transfected tau
Latimer, D. A., Gallo, J.-M., Lovestone, S., Miller, C. C. J., Hugh Reynolds, C., Marquardt, B., Stabel, S., Woodgett, J. R., & Anderton, B. H. (1995) · FEBS Letters · doi:10.1016/0014-5793(95)00434-b · Cited by 48
Chronoregulation by Asparagine Deamidation
Weintraub, S. J., & Deverman, B. E. (2007) · Science s STKE · doi:10.1126/stke.4092007re7 · Cited by 48
Increased tau Phosphorylation on Mitogen-Activated Protein Kinase Consensus Sites and Cognitive Decline in Transgenic Models for Alzheimer's Disease and FTDP-17: Evidence for Distinct Molecular Processes Underlying tau Abnormalities
Lambourne, S. L., Sellers, L. A., Bush, T. G., Choudhury, S. K., Emson, P. C., Suh, Y., & Wilkinson, L. S. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.25.1.278-293.2005 · Cited by 47
Glycogen synthase kinase 3 phosphorylates recombinant human tau protein at serine‐262 in the presence of heparin (or tubulin)
Moreno, F. J., Medina, M., Pérez, M., de Garcini, E. M., & Ávila, J. (1995) · FEBS Letters · doi:10.1016/0014-5793(95)00934-2 · Cited by 47
Transgenic models of Alzheimer's disease: Better utilization of existing models through viral transgenesis
Platt, T. L., Reeves, V. L., & Murphy, M. P. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2013.04.017 · Cited by 48
Genetic Dissection of Alzheimer’s Disease Using Drosophila Models
Jeon, Y., Lee, J., Choi, B., Won, S.-Y., & Cho, K. S. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21030884 · Cited by 46
Regulation of Tau Phosphorylation in Alzheimer's Disease
Lee, V. M. ‐. (1996) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1996.tb34408.x · Cited by 46
Isolation and Biochemical Characterization of Amyloid Plaques and Paired Helical Filaments
Rostagno, A. A., & Ghiso, J. A. (2009) · Current Protocols in Cell Biology · doi:10.1002/0471143030.cb0333s44 · Cited by 44
Microtubule affinity–regulating kinase 4 with an Alzheimer's disease-related mutation promotes tau accumulation and exacerbates neurodegeneration
Oba, T., Saito, T., Asada, A., Shimizu, S., Iijima, K., & Ando, K. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra120.014420 · Cited by 44
Troglitazone, a peroxisome proliferator‐activated receptor‐γ agonist, decreases tau phosphorylation in CHOtau4R cells
d’Abramo, C., Ricciarelli, R., Pronzato, M. A., & Davies, P. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.03931.x · Cited by 46
Ceruloplasmin functional changes in Parkinson’s disease-cerebrospinal fluid
Barbariga, M., Curnis, F., Andolfo, A., Zanardi, A., Lazzaro, M., Conti, A., Magnani, G., Volonté, M. A., Ferrari, L. D., Comı, G., et al. (2015) · Molecular Neurodegeneration · doi:10.1186/s13024-015-0055-2 · Cited by 47
Phosphorylated α‐synuclein in normal mouse brain
Hirai, Y., Fujita, S. C., Iwatsubo, T., & Hasegawa, M. (2004) · FEBS Letters · doi:10.1016/j.febslet.2004.07.046 · Cited by 45
Self-citation
Structure, function, and regulation of neuronal Cdc2-like protein kinase
Lew, J., Qi, R. Z., Huang, Q.-Q., Paudel, H. K., Matsuura, I., Matsushita, M., Zhu, X., & Wang, J. H.-C. (1995) · Neurobiology of Aging · doi:10.1016/0197-4580(95)00014-6 · Cited by 44
Tau phosphorylation at Alzheimer's disease-related Ser356 contributes to tau stabilization when PAR-1/MARK activity is elevated
Ando, K., Oka, M., Ohtake, Y., Motoki, H., Shimizu, S., Hisanaga, S., & Iijima, K. (2016) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2016.08.053 · Cited by 40
Regions of Tau Implicated in the Paired Helical Fragment Core as Defined by NMR
Sillen, A., Leroy, A., Wieruszeski, J., Loyens, A., Beauvillain, J., Buée, L., Landrieu, I., & Lippens, G. M. (2005) · ChemBioChem · doi:10.1002/cbic.200400452 · Cited by 49
miR-143-3p Inhibits Aberrant Tau Phosphorylation and Amyloidogenic Processing of APP by Directly Targeting DAPK1 in Alzheimer’s Disease
Wang, L., Shui, X., Mei, Y., Xia, Y., Lan, G., Hu, L., Zhang, M., Gan, C., Li, R., Tian, Y., et al. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23147992 · Cited by 42
Hyperphosphorylation of microtubule-associated tau protein plays dual role in neurodegeneration and neuroprotection
Zhang, Y., Tian, Q., Zhang, Q., Zhou, X., Liu, S., & Wang, J. (2009) · Pathophysiology · doi:10.1016/j.pathophys.2009.02.003 · Cited by 42
Effects of grape seed proanthocyanidin on Alzheimer's disease in vitro and in vivo
Lian, Q., Nie, Y., Zhang, X., Tan, B., Cao, H., Chen, W., Gao, W., Chen, J., Liang, Z., Lai, H., et al. (2016) · Experimental and Therapeutic Medicine · doi:10.3892/etm.2016.3530 · Cited by 41
Mass Spectrometry for Neurobiomarker Discovery: The Relevance of Post-Translational Modifications
Azevedo, R., Jacquemin, C., Villain, N., Fenaille, F., Lamari, F., & Bécher, F. (2022) · Cells · doi:10.3390/cells11081279 · Cited by 45
The Role of Synaptic Proteins in Alzheimer's Disease
Masliah, E. (2000) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2000.tb05562.x · Cited by 39
Visualization of Newly Deposited tau in Neurofibrillary Tangles and Neuropil Threads
Miyasaka, T., Watanabe, A., Saito, Y., Murayama, S., Mann, D. M. A., Yamazaki, M., Ravid, R., Morishima‐Kawashima, M., Nagashima, K., & Ihara, Y. (2005) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/01.jnen.0000173890.79058.1d · Cited by 45
Self-citation
Zebrafish models of Tauopathy
Bai, Q., & Burton, E. A. (2010) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2010.09.004 · Cited by 42
Argyrophilic grain disease
Tolnay, M., & Probst, A. (2008) · Handbook of clinical neurology · doi:10.1016/s0072-9752(07)01251-1 · Cited by 41
Reduction of calcineurin activity in brain by antisense oligonucleotides leads to persistent phosphorylation of tau protein at Thr181 and Thr231.
Garver, T. D., Kincaid, R. L., Conn, R. A., & Billingsley, M. L. (1999) · PubMed · Cited by 40
Ca2+/calmodulin-dependent protein kinase II promotes neurodegeneration caused by tau phosphorylated at Ser262/356 in a transgenic Drosophila model of tauopathy
Oka, M., Fujisaki, N., Akiko, M.-O., Ohtake, Y., Shimizu, S., Saito, T., Hisanaga, S., Iijima, K., & Ando, K. (2017) · The Journal of Biochemistry · doi:10.1093/jb/mvx038 · Cited by 41
PKR kinase directly regulates tau expression and Alzheimer's disease‐related tau phosphorylation
Reimer, L., Betzer, C., Kofoed, R. H., Volbracht, C., Fog, K., Kurhade, C., Nilsson, E., Överby, A. K., & Jensen, P. H. (2020) · Brain Pathology · doi:10.1111/bpa.12883 · Cited by 39
Phosphorylation of microtubule-associated protein tau by Ca2+/calmodulin-dependent protein kinase II in its tubulin binding sites
Yamamoto, H., Yamauchi, E., Taniguchi, H., Ono, T., & Miyamoto, E. (2002) · Archives of Biochemistry and Biophysics · doi:10.1016/s0003-9861(02)00556-8 · Cited by 39
Effects of curcumin and demethoxycurcumin on amyloid-β precursor and tau proteins through the internal ribosome entry sites: A potential therapeutic for Alzheimer's disease
Villaflores, O. B., Chen, Y., Chen, C., Yeh, J., & Wu, T. (2012) · Taiwanese Journal of Obstetrics and Gynecology · doi:10.1016/j.tjog.2012.09.010 · Cited by 38
Molecular Pathology of Alzheimer’s Disease and Related Disorders
Ginsberg, S. D., Schmidt, M. L., Crino, P. B., Eberwine, J. H., Lee, V. M. ‐., & Trojanowski, J. Q. (1999) · Cerebral cortex · doi:10.1007/978-1-4615-4885-0_17 · Cited by 38
Asparagine deamidation: a regulatory hourglass
Weintraub, S. J. (2004) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2004.03.002 · Cited by 37
Involvement of WAVE Accumulation in Aβ/APP Pathology-Dependent Tangle Modification in Alzheimer’s Disease
Takata, K., Kitamura, Y., Nakata, Y., Matsuoka, Y., Tomimoto, H., Taniguchi, T., & Shimohama, S. (2009) · The American Journal of Pathology · doi:10.2353/ajpath.2009.080908 · Cited by 36
Tau in Alzheimer’s Disease: Pathological Alterations and an Attractive Therapeutic Target
Gu, J., & Liu, F. (2020) · Current Medical Science · doi:10.1007/s11596-020-2282-1 · Cited by 41
Oxidation-induced Structural Changes of Ceruloplasmin Foster NGR Motif Deamidation That Promotes Integrin Binding and Signaling
Barbariga, M., Curnis, F., Spitaleri, A., Andolfo, A., Zucchelli, C., Lazzaro, M., Magnani, G., Musco, G., Corti, A., & Alessio, M. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.520981 · Cited by 35
Monocyte adhesion to atherosclerotic matrix proteins is enhanced by Asn-Gly-Arg deamidation
Dutta, B., Park, J. E., Kumar, S., Hao, P., Gallart‐Palau, X., Serra, A., Ren, Y., Sorokin, V. A., Lee, C. N., Ho, H. H., et al. (2017) · Scientific Reports · doi:10.1038/s41598-017-06202-2 · Cited by 35
NMR Meets Tau: Insights into Its Function and Pathology
Lippens, G. M., Landrieu, I., Smet‐Nocca, C., Huvent, I., Gandhi, N. S., Gigant, B., Despres, C., Qi, H., & Lopez, J. M. (2016) · Biomolecules · doi:10.3390/biom6020028 · Cited by 35
Beta-amyloidolysis and glutathione in Alzheimer's disease
Lasierra-Cirujeda, J., Coronel, Gimeno, & Aza (2013) · Journal of Blood Medicine · doi:10.2147/jbm.s35496 · Cited by 35
Site-specific Microtubule-associated Protein 4 Dephosphorylation Causes Microtubule Network Densification in Pressure Overload Cardiac Hypertrophy
Panneerselvam, C., Samanna, V., Cheng, G., Ablonczy, Z., Baicu, C. F., Bethard, J. R., Menick, D. R., Kuppuswamy, D., & Cooper, G. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.120709 · Cited by 34
PKA Phosphorylations on Tau: Developmental Studies in the Mouse
Andorfer, C. A., & Davies, P. (2000) · Developmental Neuroscience · doi:10.1159/000017454 · Cited by 34
Site-specific regulation of Alzheimer-like tau phosphorylation in living neurons
Burack, M. A., & Halpain, S. (1996) · Neuroscience · doi:10.1016/0306-4522(95)00546-3 · Cited by 36
The Amyloid Peptide and Its Precursor in Alzheimer's Disease
Octave, J. N. (1995) · Reviews in the Neurosciences · doi:10.1515/revneuro.1995.6.4.287 · Cited by 34
Examination of phosphorylated tau protein as a PHF-precursor at early stage alzheimer's disease
Lai, R. Y. K., Gertz, H. N.-J., Wischik, D., Xuereb, J. H., Mukaetova-Ladinska, E. B., Harrington, C. R., Edwards, P. C., Mena, R., Paykel, E. S., Brayne, C., et al. (1995) · Neurobiology of Aging · doi:10.1016/0197-4580(95)00041-c · Cited by 33
Cholinergic Muscarinic Receptor Signaling by the Phosphoinositide Signal Transduction System in Alzheimer's Disease
Jope, R. S. (1999) · Journal of Alzheimer s Disease · doi:10.3233/jad-1999-14-505 · Cited by 33
Pathological Tau proteins of Alzheimer's disease as a biochemical marker of neurofibrillary degeneration
Delacourte, A. (1994) · Biomedicine & Pharmacotherapy · doi:10.1016/0753-3322(94)90174-0 · Cited by 33
Neuronal Cdc2-like kinase: from cell cycle to neuronal function
Tang, D., Matsuura, I., Wang, J. H.-C., Lee, K.-Y., & Qi, R. Z. (1996) · Biochemistry and Cell Biology · doi:10.1139/o96-046 · Cited by 32
3R and 4R tau isoforms in paired helical filaments in Alzheimer’s disease
Hasegawa, M., Watanabe, S., Kondo, H., Akiyama, H., Mann, D. M. A., Saito, Y., & Murayama, S. (2013) · Acta Neuropathologica · doi:10.1007/s00401-013-1191-9 · Cited by 33
Self-citation
Conformation of paired helical filaments blocks dephosphorylation of epitopes shared with fetal tau except Ser199/202 and Ser202/Thr205
Gordon‐Krajcer, W., Yang, L., & Ksiȩżak-Reding, H. (2000) · Brain Research · doi:10.1016/s0006-8993(99)02391-4 · Cited by 31
Distinct phosphorylation profiles of tau in brains of patients with different tauopathies
Samimi, N., Sharma, G., Kimura, T., Matsubara, T., Huo, A., Chiba, K., Saito, Y., Murayama, S., Akatsu, H., Hashizume, Y., et al. (2021) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2021.08.011 · Cited by 28
Self-citation
Reassessment of Neuronal Tau Distribution in Adult Human Brain and Implications for Tau Pathobiology
Paterno, G., Bell, B. M., Gorion, K.-M. M., Prokop, S., & Giasson, B. I. (2022) · Acta Neuropathologica Communications · doi:10.1186/s40478-022-01394-9 · Cited by 30
Phosphorylation-Induced Structural Reorganization in Tau-Paired Helical Filaments
Rani, L., & Mallajosyula, S. S. (2021) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.1c00084 · Cited by 28
Alzheimer abnormally phosphorylated tau is more hyperphosphorylated than the fetal tau and causes the disruption of microtubules
Iqbal, K., & Grundke, I. (1995) · Neurobiology of Aging · doi:10.1016/0197-4580(95)00033-b · Cited by 29
β‐Amyloid Protein Precursor and τ mRNA Levels Versus β‐Amyloid Plaque and Neurofibrillary Tangles in the Aged Human Brain
Oyama, F., Shimada, H., Oyama, R., Titani, K., & Ihara, Y. (1993) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1993.tb13388.x · Cited by 28
Self-citation
High-Resolution Magic Angle Spinning NMR of the Neuronal Tau Protein Integrated in Alzheimer's-Like Paired Helical Fragments
Sillen, A., Wieruszeski, J., Leroy, A., Younes‐Chennoufi, A. B., Landrieu, I., & Lippens, G. M. (2005) · Journal of the American Chemical Society · doi:10.1021/ja0516211 · Cited by 31
Secreted β-APP stimulates MAP kinase and phosphorylation of tau in neurons
Greenberg, S. M., & Kosik, K. S. (1995) · Neurobiology of Aging · doi:10.1016/0197-4580(94)00172-w · Cited by 28
Dorothy Russell Memorial Lecture The molecular pathology of Alzheimer's disease: are we any closer to understanding the neurodegenerative process?
Smith, C. J., & Anderton, B. H. (1994) · Neuropathology and Applied Neurobiology · doi:10.1111/j.1365-2990.1994.tb00977.x · Cited by 27
Cerebrospinal fluid: A specific biofluid for the biosensing of Alzheimer's diseases biomarkers
Mirzaie, A., Nasrollahpour, H., Khalilzadeh, B., Jamali, A. A., Spiteri, R. J., Yousefi, H., Işıldak, İ., & Rahbarghazi‬, R. (2023) · TrAC Trends in Analytical Chemistry · doi:10.1016/j.trac.2023.117174 · Cited by 28
Multiple asparagine deamidation of Bacillus anthracis protective antigen causes charge isoforms whose complexity correlates with reduced biological activity
Powell, B. S., Enama, J. T., Ribot, W. J., Webster, W. M., Little, S. F., Hoover, T. A., Adamovicz, J. J., & Andrews, G. P. (2007) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.21432 · Cited by 27
Phosphorylation of human microtubule‐associated protein tau by protein kinases of the AGC subfamily
Virdee, K., Yoshida, H., Peak‐Chew, S., & Goedert, M. (2007) · FEBS Letters · doi:10.1016/j.febslet.2007.05.009 · Cited by 27
Decreased Synthesis of Matrix Metalloproteinase-7 and Adhesion to the Extracellular Matrix Proteins of Human Colon Cancer Cells Treated with Troglitazone
Sunami, E., Tsuno, N. H., Kitayama, J., Saito, S., Osada, T., Yamaguchi, H., Tomozawa, S., Tsuruo, T., Shibata, Y., & Nagawa, H. (2002) · Surgery Today · doi:10.1007/s005950200049 · Cited by 27
Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins
Danis, C., Despres, C., Bessa, L. M., Malki, I., Merzougui, H., Huvent, I., Qi, H., Lippens, G. M., Cantrelle, F., Schneider, R. C., et al. (2016) · Journal of Visualized Experiments · doi:10.3791/55001 · Cited by 34
Acute inhibition of the CNS-specific kinase TTBK1 significantly lowers tau phosphorylation at several disease relevant sites
Dillon, G. M., Henderson, J. L., Bao, C., Joyce, J. A., Calhoun, M. E., Amaral, B., King, K. W., Bajrami, B., & Rabah, D. (2020) · PLoS ONE · doi:10.1371/journal.pone.0228771 · Cited by 26
Argyrophilic Grain Disease
Tolnay, M., Monsch, A. U., & Probst, A. (2001) · Advances in experimental medicine and biology · doi:10.1007/978-1-4615-1249-3_4 · Cited by 26
Passive immunization targeting the N-terminal region of phosphorylated tau (residues 68–71) improves spatial memory in okadaic acid induced tauopathy model rats
Subramanian, S., Savanur, G., & Madhavadas, S. (2016) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2016.12.101 · Cited by 25
Specific binding of Hsp27 and phosphorylated Tau mitigates abnormal Tau aggregation-induced pathology
Zhang, S., Zhu, Y., Lu, J., Liu, Z., Lobato, A. G., Zeng, W., Liu, J., Qiang, J., Zeng, S., Zhang, Y., et al. (2022) · eLife · doi:10.7554/elife.79898 · Cited by 25
Tau protein and Alzheimer's disease
Mandelkow, E., & Mandelkow�, E. (1994) · Neurobiology of Aging · doi:10.1016/0197-4580(94)90178-3 · Cited by 27
Immunohistochemical detection of tau protein in various non‐human animal brains
Kuroki, K., Uchida, K., Kiatipattanasakul, W., Nakamura, S., Yamaguchi, R., Nakayama, H., Doi, K., & TATEYAMA, S. (1997) · Neuropathology · doi:10.1111/j.1440-1789.1997.tb00034.x · Cited by 27
Loss of amyloid precursor protein in a mouse model of Niemann–Pick type C disease exacerbates its phenotype and disrupts tau homeostasis
Nunes, A. F., Pressey, S. N., Cooper, J. D., & Soriano, S. (2011) · Neurobiology of Disease · doi:10.1016/j.nbd.2011.01.028 · Cited by 24
Locations and immunoreactivities of phosphorylation sites on bovine and porcine tau proteins and a PHF-tau fragment
Poulter, L., Barratt, D., Scott, C. W., & Caputo, C. B. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)98397-3 · Cited by 24
Brain microdialysis of GABA and glutamate: What does it signify?
Timmerman, W., & Westerink, B. H. C. (1997) · Synapse · doi:10.1002/(sici)1098-2396(199711)27:3 · Cited by 387
Interactions between Microtubule-Associated Protein Tau (MAPT) and Small MoleculesPreprint
Rauch, J. N., Olson, S. H., & Gestwicki, J. E. (2016) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a024034 · Cited by 22
The Abundance of Nonphosphorylated Tau in Mouse and Human Tauopathy Brains Revealed by the Use of Phos-Tag Method
Kimura, T., Hatsuta, H., Masuda‐Suzukake, M., Hosokawa, M., Ishiguro, K., Akiyama, H., Murayama, S., Hasegawa, M., & Hisanaga, S. (2015) · American Journal Of Pathology · doi:10.1016/j.ajpath.2015.10.009 · Cited by 23
Self-citation
Reduction of Calcineurin Activity in Brain by Antisense Oligonucleotides Leads to Persistent Phosphorylation of τ Protein at Thr181 and Thr231
Garver, T. D., Kincaid, R. L., Conn, R. A., & Billingsley, M. L. (1999) · Molecular Pharmacology · doi:10.1016/s0026-895x(24)23024-8 · Cited by 41
Interplay Between Aging and Tau Pathology in Alzheimer’s Disease: Mechanisms and Translational Perspectives
Alrouji, M., Alshammari, M. S., Syed, T., & Shamsi, A. (2025) · Antioxidants · doi:10.3390/antiox14070774 · Cited by 21
Neurofibrillary changes undergoing morphological and biochemical changes – How does tau with the profile shift of from four repeat to three repeat spread in Alzheimer brain?
Uchihara, T. (2020) · Neuropathology · doi:10.1111/neup.12669 · Cited by 22
Isolation of a phosphorylated soluble Tau fraction from Alzheimer's disease brain
Ledesma, M. D. (1995) · Neurobiology of Aging · doi:10.1016/0197-4580(95)00075-p · Cited by 22
In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein
Sui, D., Liu, M., & Kuo, M. (2015) · Journal of Visualized Experiments · doi:10.3791/51537 · Cited by 28
Positional Effects of Phosphorylation on the Stability and Morphology of Tau-Related Amyloid Fibrils
Inoue, M., Konno, T., Tainaka, K., Nakata, E., Yoshida, H.-O., & Morii, T. (2012) · Biochemistry · doi:10.1021/bi201451z · Cited by 22
The Study of Posttranslational Modifications of Tau Protein by Nuclear Magnetic Resonance Spectroscopy: Phosphorylation of Tau Protein by ERK2 Recombinant Kinase and Rat Brain Extract, and Acetylation by Recombinant Creb-Binding Protein
Qi, H., Despres, C., Prabakaran, S., Cantrelle, F., Chambraud, B., Gunawardena, J., Lippens, G. M., Smet‐Nocca, C., & Landrieu, I. (2016) · Methods in molecular biology · doi:10.1007/978-1-4939-6598-4_11 · Cited by 20
Structure of NFT: Biochemical Approach
Hasegawa, M. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-981-32-9358-8_2 · Cited by 22
Self-citation
Methionine-Mediated Protein Phosphatase 2A Catalytic Subunit (PP2Ac) Methylation Ameliorates the Tauopathy Induced by Manganese in Cell and Animal Models
Wu, B., Cai, H., Tang, S., Xu, Y., Shi, Q., Wei, L., Meng, L., Zhang, N., Wang, X., Xiao, D., et al. (2020) · Neurotherapeutics · doi:10.1007/s13311-020-00930-6 · Cited by 19
Identification of cis-acting determinants mediating the unconventional secretion of tau
Katsinelos, T., McEwan, W. A., Jahn, T. R., & Nickel, W. (2021) · Scientific Reports · doi:10.1038/s41598-021-92433-3 · Cited by 16

Authors: Hasegawa, M., Morishima-Kawashima, M., Takio, K., Suzuki, M., Titani, K., & Ihara, Y.
Affiliations: The University of Tokyo (JP)
ORCID: Hasegawa, M
Suzuki, M
Ihara, Y
Venue: Journal of Biological Chemistry
Publisher: Elsevier BV
Published: 1992-10
Volume: 267
Issue: 24
Pages: 17047-17054
ISSN: 0021-9258 (ISSN-L)
DOI: 10.1016/s0021-9258(18)41890-x
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: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 10240 d)
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

Protein sequence and mass spectrometric analyses of tau in the Alzheimer's disease brain

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks