The DOI matches its Crossref record; 52 of the 52 references it cites were found in a registry or an index.
Microtubule-associated protein tau. Abnormal phosphorylation of a non-paired helical filament pool in Alzheimer disease.
Open accessAbstract
The major protein subunit of the paired helical filaments (PHF) of Alzheimer disease (AD) is the microtubule-associated protein tau. Tau is a family of phosphopolypeptides that are abnormally phosphorylated in PHF. In this study, a non-PHF pool of tau abnormally phosphorylated at Ser-199/202, and tau not phosphorylated at this site (AD P-tau and AD tau, respectively) were isolated from the 27,000 x g to 200,000 x g fraction of AD brain homogenate by extraction in 8 M urea, followed by dialysis against Tris buffer. AD P-tau and AD tau were further purified and separated from each other by acid precipitation, glial fibrillary acidic protein affinity chromatography, and phosphocellulose chromatography. The resulting AD P-tau and AD tau preparations were free of cytoskeletal proteins, ubiquitin, and beta-amyloid peptide. Immunochemical and morphological analysis of AD P-tau preparations revealed that most of the protein was of non-PHF origin. The AD P-tau was about 3-4-fold (approximately 8 mol P04/mol protein, M(r) 41,318) more phosphorylated than cytosolic tau from AD and control brains. Unlike PHF, the AD P-tau lacked ubiquitin. In AD brain the levels of cytosolic tau were about half of those in control aged cases. These findings suggest that the abnormal phosphorylation of tau in AD occurs in the cytosol.
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
“In the normal adult brain, there are 2–3 mol of phosphate per mole of tau, but in the AD brain, tau protein is twofold to threefold hyperphosphorylated [35].”
From Tau and neuroinflammation in Alzheimer’s disease: interplay mechanisms and clinical translation (2023) · cites this paper as [35]
Citations
Cites
Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
LAEMMLI, U. K. (1970) · Nature · doi:10.1038/227680a0 · Cited by 249,961
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
Self-citationAssay of proteins in the presence of interfering materials
Bensadoun, A., & Weinstein, D. (1976) · Analytical Biochemistry · doi:10.1016/s0003-2697(76)80064-4 · Cited by 3,191
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
Microtubule-associated protein tau. A component of Alzheimer paired helical filaments.
Grundke, I., Iqbal, K., Quinlan, M., Tung, Y. C., Zaidi, M. S., & Wisniewski, H. M. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)38495-8 · Cited by 1,780
Self-citationThe 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
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
Rat monoclonal antitubulin antibodies derived by using a new nonsecreting rat cell line.
Kilmartin, J. V., Wright, B., & Milstein, C. (1982) · The Journal of Cell Biology · doi:10.1083/jcb.93.3.576 · Cited by 942
Goedert, M., & Jakes, R. (1990) · The EMBO Journal · doi:10.1002/j.1460-2075.1990.tb07870.x · Cited by 929
Research works printed but not linked: 4
- Himmler, 1989, Mol. Cell. Biol., 9, 1381
- Papasozomenos, 1989, Lab. Invest., 60, 375
- Kim, 1988, Neurosci. Res. Comm., 2, 121
- Goldstein, 1987, J. Immunol., 14, 149
Cited by
Sorted by citations
Amyloid oligomers exacerbate tau pathology in a mouse model of tauopathy
Selenica, M.-L. B., Brownlow, M., Jimenez, J. P., Lee, D. C., Pena, G., Dickey, C. A., Gordon, M. N., & Morgan, D. (2013) · Neurodegenerative Diseases · doi:10.1159/000337230 · Cited by 10,359
Inflammation as a central mechanism in Alzheimer's disease
Kinney, J. W., Bemiller, S. M., Murtishaw, A. S., Leisgang, A. M., Salazar, A. M., & Lamb, B. T. (2018) · Alzheimer's & Dementia: Translational Research & Clinical Interventions · doi:10.1016/j.trci.2018.06.014 · Cited by 2,253
Tau in physiology and pathology
Wang, Y., & Mandelkow, E. (2016) · Nature Reviews Neuroscience · doi:10.1038/nrn.2015.1 · Cited by 2,251
Tau in Alzheimer Disease and Related Tauopathies
Iqbal, K., Liu, F., Gong, C., & Grundke, I. (2010) · Current Alzheimer Research · doi:10.2174/156720510793611592 · Cited by 1,163
Self-citationTau pathology in Alzheimer disease and other tauopathies
Iqbal, K., del C. Alonso, A., Chen, S., Chohan, M. O., El-Akkad, E., Gong, C.-X., Khatoon, S., Li, B., Liu, F., Rahman, A., et al. (2005) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2004.09.008 · Cited by 1,037
Self-citationRole of tau protein in both physiological and pathological conditions
AVILA, J., LUCAS, J. J., PÉREZ, M., & HERNÁNDEZ, F. (2004) · Physiological Reviews · doi:10.1152/physrev.00024.2003 · Cited by 1,005
Roles of tau protein in health and disease
Guo, T., Noble, W., & Hanger, D. P. (2017) · Acta Neuropathologica · doi:10.1007/s00401-017-1707-9 · Cited by 1,003
Alonso, A. D. C., Zaidi, T., Novak, M., Grundke-Iqbal, I., & Iqbal, K. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.121119298 · Cited by 827
Self-citationAlonso, A. D. C., Grundke-Iqbal, I., & Iqbal, K. (1996) · Nature Medicine · doi:10.1038/nm0796-783 · Cited by 859
Self-citationBiochemistry and Cell Biology of Tau Protein in Neurofibrillary DegenerationPreprint
Mandelkow, E., & Mandelkow, E. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006247 · Cited by 897
Tau and neurodegenerative disease: the story so far
Iqbal, K., Liu, F., & Gong, C.-X. (2016) · Nature Reviews Neurology · doi:10.1038/nrneurol.2015.225 · Cited by 806
Self-citationAmbadipudi, S., Biernat, J., Riedel, D., Mandelkow, E., & Zweckstetter, M. (2017) · Nature Communications · doi:10.1038/s41467-017-00480-0 · Cited by 782
O-GlcNAcylation regulates phosphorylation of tau: A mechanism involved in Alzheimer's disease
Liu, F., Iqbal, K., Grundke-Iqbal, I., Hart, G. W., & Gong, C.-X. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0400348101 · Cited by 775
Self-citationLiu, F., Grundke‐Iqbal, I., Iqbal, K., & Gong, C. (2005) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2005.04391.x · Cited by 759
Self-citationRole of abnormally phosphorylated tau in the breakdown of microtubules in Alzheimer disease.
Alonso, A. C., Zaidi, T., Grundke-Iqbal, I., & Iqbal, K. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.12.5562 · Cited by 738
Self-citationZempel, H., Thies, E., Mandelkow, E., & Mandelkow, E.-M. (2010) · The Journal of Neuroscience · doi:10.1523/jneurosci.2357-10.2010 · Cited by 686
Gong, C., & Iqbal, K. (2008) · Current Medicinal Chemistry · doi:10.2174/092986708785909111 · Cited by 672
Self-citationPost-translational modifications of tau protein: Implications for Alzheimer's disease
Martin, L., Latypova, X., & Terro, F. (2011) · Neurochemistry International · doi:10.1016/j.neuint.2010.12.023 · Cited by 683
Mechanisms of tau-induced neurodegeneration
Iqbal, K., Liu, F., Gong, C.-X., Alonso, A. D. C., & Grundke-Iqbal, I. (2009) · Acta Neuropathologica · doi:10.1007/s00401-009-0486-3 · Cited by 628
Self-citationArendt, T., Stieler, J. T., & Holzer, M. (2016) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2016.08.018 · Cited by 609
Amyloid cascade hypothesis: Pathogenesis and therapeutic strategies in Alzheimer's disease
Barage, S. H., & Sonawane, K. D. (2015) · Neuropeptides · doi:10.1016/j.npep.2015.06.008 · Cited by 579
Extrasynaptic NMDA Receptor Involvement in Central Nervous System Disorders
Parsons, M. P., & Raymond, L. A. (2014) · Neuron · doi:10.1016/j.neuron.2014.03.030 · Cited by 567
Kinases and phosphatases and tau sites involved in Alzheimer neurofibrillary degeneration
Wang, J., Grundke, I., & Iqbal, K. (2007) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2006.05226.x · Cited by 569
Self-citationThe preclinical phase of the pathological process underlying sporadic Alzheimer’s disease
Braak, H., & Del Tredici, K. (2015) · Brain · doi:10.1093/brain/awv236 · Cited by 540
Lee, W., Loo, C., Bebawy, M., Luk, F., Mason, R. S., & Rohanizadeh, R. (2013) · Current Neuropharmacology · doi:10.2174/1570159x11311040002 · Cited by 552
Wang, J., Xia, Y., Grundke, I., & Iqbal, K. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2012-129031 · Cited by 547
Self-citationTau and neuroinflammation in Alzheimer’s disease: interplay mechanisms and clinical translation
Chen, Y., & Yu, Y. (2023) · Journal of Neuroinflammation · doi:10.1186/s12974-023-02853-3 · Cited by 516
Zhang, Z., Song, M., Liu, X., Kang, S. S., Kwon, I.-S., Duong, D. M., Seyfried, N. T., Hu, W. T., Liu, Z., Wang, J.-Z., et al. (2014) · Nature Medicine · doi:10.1038/nm.3700 · Cited by 494
Morris, M., Knudsen, G. M., Maeda, S., Trinidad, J. C., Ioanoviciu, A., Burlingame, A. L., & Mucke, L. (2015) · Nature Neuroscience · doi:10.1038/nn.4067 · Cited by 472
The role of tau in neurodegeneration
Gendron, T. F., & Petrucelli, L. (2009) · Molecular Neurodegeneration · doi:10.1186/1750-1326-4-13 · Cited by 478
Structure and Pathology of Tau Protein in Alzheimer Disease
Kolarova, M., García‐Sierra, F., Bartoš, A., Říčný, J., & Řípová, D. (2012) · International Journal of Alzheimer s Disease · doi:10.1155/2012/731526 · Cited by 526
A current view on Tau protein phosphorylation in Alzheimer's disease
Wegmann, S., Biernat, J., & Mandelkow�, E. (2021) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2021.03.003 · Cited by 486
Billingsley, M. L., & Kincaid, R. L. (1997) · Biochemical Journal · doi:10.1042/bj3230577 · Cited by 466
Liu, F., Shi, J., Tanimukai, H., Gu, J., Gu, J., Grundke-Iqbal, I., Iqbal, K., & Gong, C.-X. (2009) · Brain · doi:10.1093/brain/awp099 · Cited by 439
Self-citationPost-translational modifications of tau protein in Alzheimer’s disease
Gong, C.-X., Liu, F., Grundke-Iqbal, I., & Iqbal, K. (2005) · Journal of Neural Transmission · doi:10.1007/s00702-004-0221-0 · Cited by 437
Self-citationAlonso, A. D. C., Grundke-Iqbal, I., Barra, H. S., & Iqbal, K. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.1.298 · Cited by 437
Self-citationThe Role of Tau in Alzheimer's Disease and Related Disorders
Medeiros, R., Baglietto‐Vargas, D., & LaFerla, F. M. (2010) · CNS Neuroscience & Therapeutics · doi:10.1111/j.1755-5949.2010.00177.x · Cited by 484
Gong, C.-X., Lidsky, T., Wegiel, J., Zuck, L., Grundke-Iqbal, I., & Iqbal, K. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.8.5535 · Cited by 405
Self-citationMicrotubule-associated protein tau in development, degeneration and protection of neurons
Wang, J., & Liu, F. (2008) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2008.03.002 · Cited by 405
Liquid-liquid phase separation induces pathogenic tau conformations in vitro
Kanaan, N. M., Hamel, C., Grabinski, T., & Combs, B. (2020) · Nature Communications · doi:10.1038/s41467-020-16580-3 · Cited by 397
Hofweber, M., & Dormann, D. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.tm118.001189 · Cited by 398
Hanger, D. P., Betts, J. C., Loviny, T. L. F., Blackstock, W. P., & Anderton, B. H. (1998) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1998.71062465.x · Cited by 386
Amyloid-β and tau complexity — towards improved biomarkers and targeted therapies
Polanco, J. C., Li, C., Bodea, L., Martínez‐Mármol, R., Meunier, F. A., & Götz, J. (2017) · Nature Reviews Neurology · doi:10.1038/nrneurol.2017.162 · Cited by 386
Wang, J.-Z., Grundke-Iqbal, I., & Iqbal, K. (1996) · Nature Medicine · doi:10.1038/nm0896-871 · Cited by 360
Self-citationSnead, W. T., & Gladfelter, A. S. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.09.016 · Cited by 356
Inducible Expression of Tau Repeat Domain in Cell Models of Tauopathy
Khlistunova, I., Biernat, J., Wang, Y., Pickhardt, M., von Bergen�, M., Gažová, Z., Mandelkow�, E., & Mandelkow, E. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m507753200 · Cited by 366
Oxidative stress in Alzheimer's disease
Chauhan, V. P. S., & Chauhan, A. (2006) · Pathophysiology · doi:10.1016/j.pathophys.2006.05.004 · Cited by 349
Immune Signaling in Neurodegeneration
Hammond, T. R., Marsh, S. E., & Stevens, B. (2019) · Immunity · doi:10.1016/j.immuni.2019.03.016 · Cited by 336
Analysis of microtubule-associated protein tau glycation in paired helical filaments.
Ledesma, M. D., Bonay, P., Colaço, C., & Avila, J. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)31849-5 · Cited by 333
Promotion of Hyperphosphorylation by Frontotemporal Dementia Tau Mutations
Alonso, A. D. C., Mederlyova, A., Novák, M., Grundke, I., & Iqbal, K. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m405131200 · Cited by 330
Self-citationYamamoto, A., Shin, R., Hasegawa, K., Naiki, H., Sato, H., Yoshimasu, F., & Kitamoto, T. (2002) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2002.t01-1-01061.x · Cited by 313
An, W.-L., Cowburn, R. F., Li, L., Braak, H., Alafuzoff, I., Iqbal, K., Iqbal, I.-G., Winblad, B., & Pei, J.-J. (2003) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)63687-5 · Cited by 312
Self-citationRole of Amyloid-β and Tau Proteins in Alzheimer’s Disease: Confuting the Amyloid Cascade
Gulisano, W., Maugeri, D., Baltrons, M. A., Fà, M., Amato, A., Palmeri, A., D’Adamio, L., Grassi, C., Devanand, D. P., Honig, L. S., et al. (2018) · Journal of Alzheimer's Disease · doi:10.3233/jad-179935 · Cited by 313
Illenberger, S., Zheng‐Fischhöfer, Q., Preuß, U., Stamer, K., Baumann, K., Trinczek, B., Biernat, J., Godemann, R., Mandelkow, E., & Mandelkow�, E. (1998) · Molecular Biology of the Cell · doi:10.1091/mbc.9.6.1495 · Cited by 305
DYRK1A-mediated Hyperphosphorylation of Tau
Ryoo, S., Jeong, H. K., Radnaabazar, C., Yoo, J.-J., Cho, H.-J., Lee, H. W., Kim, I.-S., Cheon, Y. H., Ahn, Y. S., Chung, S., et al. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m707358200 · Cited by 285
Hyperphosphorylation of Tau Associates With Changes in Its Function Beyond Microtubule Stability
Alonso, A. D., Cohen, L. S., Corbo, C., Morozova, V., ElIdrissi, A., Phillips, G., & Kleiman, F. E. (2018) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2018.00338 · Cited by 278
Self-citationTau-based therapies in neurodegeneration: opportunities and challenges
Li, C., & Götz, J. (2017) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2017.155 · Cited by 272
Polanco, J. C., Scicluna, B. J., Hill, A. F., & Götz, J. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.709485 · Cited by 280
Dephosphorylation of Alzheimer paired helical filaments by protein phosphatase-2A and -2B
Wang, J.-Z., Gong, C.-X., Zaidi, T., Grundke-Iqbal, I., & Iqbal, K. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.9.4854 · Cited by 269
Self-citationTheunis, C., Crespo-Biel, N., Gafner, V., Pihlgren, M., López-Deber, M. P., Reis, P., Hickman, D. T., Adolfsson, O., Chuard, N., Ndao, D. M., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0072301 · Cited by 259
Where, when, and in what form does sporadic Alzheimerʼs disease begin?
Braak, H., & Tredici, K. D. (2012) · Current Opinion in Neurology · doi:10.1097/wco.0b013e32835a3432 · Cited by 261
The Excitotoxin Quinolinic Acid Induces Tau Phosphorylation in Human Neurons
Rahman, A., Ting, K., Cullen, K. M., Braidy, N., Brew, B. J., & Guillemin, G. J. (2009) · PLoS ONE · doi:10.1371/journal.pone.0006344 · Cited by 257
Yamamoto, A., Shin, R., Hasegawa, K., Naiki, H., Sato, H., YOSHIMASU, F., & Kitamoto, T. (2003) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2002.01061.x · Cited by 245
Mechanisms of Aβ mediated neurodegeneration in Alzheimer's disease
Crouch, P. J., Harding, S.-M. E., White, A. R., Camakaris, J., Bush, A. I., & Masters, C. L. (2007) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2007.07.013 · Cited by 254
Cellular and pathological functions of tau
Bravo, C. P., Naguib, S. A., & Gan, L. (2024) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-024-00753-9 · Cited by 271
Alzheimer neurofibrillary degeneration: significance, etiopathogenesis, therapeutics and prevention
Iqbal, K., & Grundke, I. (2008) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2008.00225.x · Cited by 243
Self-citationLuo, H.-B., Xia, Y.-Y., Shu, X.-J., Liu, Z.-C., Feng, Y., Liu, X.-H., Yu, G., Yin, G., Xiong, Y.-S., Zeng, K., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1417548111 · Cited by 236
Neuroprotective Natural Products for Alzheimer’s Disease
Chen, X., Drew, J., Berney, W., & Lei, W. (2021) · Cells · doi:10.3390/cells10061309 · Cited by 236
Phosphorylation of tau at Thr212, Thr231, and Ser262 combined causes neurodegeneration
Alonso, A. D., Di Clerico, J., Li, B., Corbo, C. P., Alaniz, M. E., Grundke-Iqbal, I., & Iqbal, K. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.110957 · Cited by 236
Self-citationThe Formation of Straight and Twisted Filaments from Short Tau Peptides
Goux, W. J., Kopplin, L., Nguyen, A. D., Leak, K., Rutkofsky, M., Shanmuganandam, V. D., Sharma, D., Inouye, H., & Kirschner, D. A. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m402379200 · Cited by 227
14-3-3ζ Is an Effector of Tau Protein Phosphorylation
Hashiguchi, M., Sobue, K., & Paudel, H. K. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m003738200 · Cited by 223
Novel diffusion barrier for axonal retention of Tau in neurons and its failure in neurodegeneration
Li, X., Kumar, Y., Zempel, H., Mandelkow, E., Biernat, J., & Mandelkow, E. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.376 · Cited by 232
Tau Protein Interaction Partners and Their Roles in Alzheimer’s Disease and Other Tauopathies
Sinsky, J., Pichlerova, K., & Hanes, J. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22179207 · Cited by 220
Xia, Y., Prokop, S., & Giasson, B. I. (2021) · Molecular Neurodegeneration · doi:10.1186/s13024-021-00460-5 · Cited by 227
Regulation of microtubule-associated proteins
Cassimeris, L., & Spittle, C. S. (2001) · International review of cytology · doi:10.1016/s0074-7696(01)10006-9 · Cited by 231
Inflammation in the early stages of neurodegenerative pathology
Khandelwal, P. J., Herman, A. M., & Moussa, C. (2011) · Journal of Neuroimmunology · doi:10.1016/j.jneuroim.2011.07.002 · Cited by 218
Liu, F., Li, B., Tung, E., Grundke‐Iqbal, I., Iqbal, K., & Gong, C. (2007) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2007.05955.x · Cited by 208
Self-citationLi, Y., Zhang, J., Wan, J., Liu, A., & Sun, J. (2020) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2020.110887 · Cited by 214
AGEs induce Alzheimer-like tau pathology and memory deficit via RAGE-mediated GSK-3 activation
Li, X., Lv, B.-L., Xie, J., Liu, J., Zhou, X., & Wang, J. (2011) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2011.02.003 · Cited by 207
Polymerization of hyperphosphorylated tau into filaments eliminates its inhibitory activity
Alonso, A. D. C., Li, B., Grundke-Iqbal, I., & Iqbal, K. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0603214103 · Cited by 206
Self-citationUpdates in Alzheimer's disease: from basic research to diagnosis and therapies
Liu, E., Zhang, Y., & Wang, J. (2024) · Translational Neurodegeneration · doi:10.1186/s40035-024-00432-x · Cited by 241
Involvement of aberrant glycosylation in phosphorylation of tau by cdk5 and GSK‐3β
Liu, F., Iqbal, K., Grundke, I., & Gong, C. (2002) · FEBS Letters · doi:10.1016/s0014-5793(02)03487-7 · Cited by 197
Self-citationFlavonoids as Therapeutic Compounds Targeting Key Proteins Involved in Alzheimer’s Disease
Baptista, F. I., Henriques, A. G., Silva, A. M. S., Wiltfang, J., & Silva, O. A. B. D. C. E. (2013) · ACS Chemical Neuroscience · doi:10.1021/cn400213r · Cited by 195
Tau Becomes a More Favorable Substrate for GSK-3 When It Is Prephosphorylated by PKA in Rat Brain
Liu, S. J., Zhang, J. Y., Li, H. L., Fang, Z., Wang, Q., Deng, H. M., Gong, C. X., Grundke, I., Iqbal, K., & Wang, J. Z. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m406109200 · Cited by 186
Self-citationUltrastructure and biochemical composition of paired helical filaments in corticobasal degeneration.
Ksiȩżak-Reding, H., Morgan, K., Mattiace, L. A., Davies, P., Liu, W. K., Yen, S. H., Weidenheim, K. M., & Dickson, D. W. (1994) · PubMed Central · Cited by 183
Hu, Y., He, S., Wang, X., Duan, Q., Grundke, I., Iqbal, K., & Wang, J. (2002) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)62554-0 · Cited by 180
Self-citationCurrent Concepts of Neurodegenerative Mechanisms in Alzheimer’s Disease
Magalingam, K. B., Radhakrishnan, A., Ping, N. S., & Haleagrahara, N. (2018) · BioMed Research International · doi:10.1155/2018/3740461 · Cited by 178
Disruption of microtubule network by Alzheimer abnormally hyperphosphorylated tau
Li, B., Chohan, M. O., Grundke, I., & Iqbal, K. (2007) · Acta Neuropathologica · doi:10.1007/s00401-007-0207-8 · Cited by 173
Self-citationSun, L., Liu, S. Y., Zhou, X. W., Wang, X. C., Liu, R., Wang, Q., & Wang, J. Z. (2003) · Neuroscience · doi:10.1016/s0306-4522(02)00697-8 · Cited by 168
Eckermann, K., Mocanu, M.-M., Khlistunova, I., Biernat, J., Nissen, A., Hofmann, A., Schönig, K., Bujard, H., Haemisch, A., Mandelkow, E., et al. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m705282200 · Cited by 168
Role of glycosylation in hyperphosphorylation of tau in Alzheimer's disease
Liu, F., Zaidi, T., Iqbal, K., Grundke-Iqbal, I., Merkle, R. K., & Gong, C.-X. (2002) · FEBS Letters · doi:10.1016/s0014-5793(02)02228-7 · Cited by 167
Self-citationKhatoon, S., Grundke, I., & Iqbal, K. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)00829-9 · Cited by 167
Self-citationRole of protein kinase B in Alzheimer's neurofibrillary pathology
Pei, J.-J., Khatoon, S., An, W., Nordlinder, M., Tanaka, T., Braak, H., Tsujio, I., Takeda, M., Alafuzoff, I. I., Winblad, B. G., et al. (2002) · Acta Neuropathologica · doi:10.1007/s00401-002-0657-y · Cited by 169
Self-citationTau – an inhibitor of deacetylase HDAC6 function
Perez, M., Santa‐Maria, I., De Barreda, E. G., Zhu, X., Cuadros, R., Cabrero, J. R., Sanchez‐Madrid, F., Dawson, H. N., Vitek, M. P., Perry, G., et al. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.06102.x · Cited by 182
Limorenko, G., & Lashuel, H. A. (2021) · Chemical Society Reviews · doi:10.1039/d1cs00127b · Cited by 168
Merkwirth, C., Martinelli, P., Korwitz, A., Morbin, M., Brönneke, H. S., Jordan, S. D., Rugarli, E. I., & Langer, T. (2012) · PLoS Genetics · doi:10.1371/journal.pgen.1003021 · Cited by 162
Alonso, A. D. C., Zaidi, T., Novák, M., Barra, H. S., Grundke, I., & Iqbal, K. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m105365200 · Cited by 160
Self-citationHo, C., Troncoso, J. C., Knox, D. L., Stark, W. J., & Eberhart, C. G. (2013) · Brain Pathology · doi:10.1111/bpa.12070 · Cited by 157
Dephosphorylation of Alzheimer's disease abnormally phosphorylated tau by protein phosphatase-2A
Gong, C., Grundke, I., & Iqbal, K. (1994) · Neuroscience · doi:10.1016/0306-4522(94)90400-6 · Cited by 156
Self-citationBasheer, N., Smolek, T., Hassan, I., Liu, F., Iqbal, K., Zilka, N., & Novak, P. (2023) · Molecular Psychiatry · doi:10.1038/s41380-023-02113-z · Cited by 159
Self-citation
Metadata
- Authors
- Köpke, E., Tung, Y. C., Shaikh, S., Alonso, A. C., Iqbal, K., & Grundke-Iqbal, I.
- Affiliations
- Regeneron (United States) (US)
- ORCID
- Iqbal, K
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1993-11
- Volume
- 268
- Issue
- 32
- Pages
- 24374-24384
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1601433695
- Cited by
- 779
- References
- 52
- Citations by year
- 2026: 22 · 2025: 40 · 2024: 44 · 2023: 42 · 2022: 24 · 2021: 45 · 2020: 49 · 2019: 45 · 2018: 43 · 2017: 29 · 2016: 30 · 2015: 30 · 2014: 29 · 2013: 22 · 2012: 29
- FWCI
- 7.79
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (5r01ns018105-17, 5p01ag004220-12)
- National Institute on Aging (F32 AGO 5541, AGO4220)
- National Institute of Neurological Disorders and Stroke (NS 18105)
- 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, Alzheimer's disease, tau phosphorylation, paired helical filaments, ubiquitin
- MeSH terms
- Aged, Aged, 80 and over, Alzheimer Disease, Brain, Chromatography, Affinity, Chromatography, Ion Exchange, Electrophoresis, Polyacrylamide Gel, Humans, Microscopy, Electron, Phosphorylation, Protein Denaturation, Solubility, Ubiquitins, Urea, 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