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Brain proline-directed protein kinase phosphorylates tau on sites that are abnormally phosphorylated in tau associated with Alzheimer's paired helical filaments.
Open accessAbstract
Brain proline-directed protein kinase (BPDK), which contains a catalytic subunit homologous to and displaying site-specific phosphorylation similar to p34cdc2 kinase (Lew, J., Winkfein, R. J., Paudel, H. K., and Wang, J. H. (1992) J. Biol. Chem. 267, 25922-25926), has been examined for possible involvement in tau phosphorylation. Immunoblot analyses using peptide antibodies specific for BPDK have revealed the presence of the kinase in bovine brain microtubules purified extensively by repeated polymerization and depolymerization cycles. When the microtubule proteins are separated into the tubulin and microtubule-associated protein fractions, BPDK is found exclusively in the latter fraction. BPDK phosphorylates both tau and MAP2, the former protein being phosphorylated to a stoichiometry of 3.8 mol of phosphate/mol of tau. Analysis of the phosphopeptides isolated from the tryptic digest of the phosphorylated bovine tau has revealed seven phosphorylation sites. Based on the sequence alignment between bovine and human tau proteins, these sites correspond to Ser-195, Ser-202, Thr-205, Thr-231, Ser-235, Ser-396, and Ser-404 of human tau. Mass spectrometric analysis of the tau protein isolated from Alzheimer's paired helical filaments (PHFs) has determined three abnormal phosphorylation sites and two phosphopeptides containing a total of five abnormal phosphates (Hasegawa, M., Morishima-Kawashima, M., Takio, K., Suzuki, M., Titani, K., and Ihara, Y. (1992) J. Biol. Chem. 267, 17047-…
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“However, without exception, these studies have been carried out in vitro.”
From Glycogen synthase kinase-3β phosphorylates tau protein at multiple sites in intact cells (1995) · cites this paper as [14]
In the citing paper
“They extend results obtained in vitro [7,12,14] to an in vivo model system, and indicate that GSK3fl may be involved in the phosphorylation of tau in vivo.”
From Glycogen synthase kinase-3β phosphorylates tau protein at multiple sites in intact cells (1995) · cites this paper as [14]
In the citing paper
“Mitogen-activated protein kinase, glycogen synthase kinase-3 (GSK3) and neuronal cdc2-1ike kinase have been shown to phosphorylate tau protein in vitro at a number of sites that are phosphorylated in PHFs.”
From Glycogen synthase kinase-3β phosphorylates tau protein at multiple sites in intact cells (1995) · cites this paper as [14]
In the citing paper
“However, since in vitro studies [7,12,14] have demonstrated that tau can be directly phosphorylated by GSK3fl at many of the sites we observed in transfected cells, GSK3fl probably was directly responsible for the increased immunoreactivities and mobility shifts observed here.”
From Glycogen synthase kinase-3β phosphorylates tau protein at multiple sites in intact cells (1995) · cites this paper as [14]
Citations
Cites
Bradford, M. M. (1976) · Analytical Biochemistry · doi:10.1016/0003-2697(76)90527-3 · Cited by 255,302
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
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
Transforming gene product of Rous sarcoma virus phosphorylates tyrosine
Hunter, T. R., & Sefton, B. M. (1980) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.77.3.1311 · Cited by 2,333
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
Xiong, Y., Zhang, H., & Beach, D. (1992) · Cell · doi:10.1016/0092-8674(92)90518-h · Cited by 1,021
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
A family of human cdc2‐related protein kinases.
Meyerson, M. M., Enders, G. H., Wu, C. L., Su, L., Gorka, C., Nelson, C. E., Harlow, E., & Tsai, L. (1992) · The EMBO Journal · doi:10.1002/j.1460-2075.1992.tb05360.x · Cited by 925
Physical and chemical properties of purified tau factor and the role of tau in microtubule assembly
Cleveland, D. W., Hwo, S. Y., & Kirschner, M. W. (1977) · Journal of Molecular Biology · doi:10.1016/0022-2836(77)90214-5 · Cited by 881
Research works printed but not linked: 4
- Ksiezak-Reding, 1991, Neuron, 6, 717, 10.1016/0896-6273(91)90169-Z · DOI
- Grundke-Iqbal, 1986, Proc. Natl. Acad. Sci. U.S.A., 83, 4913, 10.1073/pnas.83.13.4913 · DOI · Paper page
- Himmler, 1989, Mol. Cell. Biol., 9, 1381
- Hayes, 1991, New Biol., 3, 259
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Lew, J., Huang, Q.-Q., Qi, R. Z., Winkfein, R. J., Aebersold, R. H., Hunt, T., & Wang, J. H.-C. (1994) · Nature · doi:10.1038/371423a0 · Cited by 580
Self-citationMatsuo, E. S., Shin, R., Billingsley, M., de Voorde, A. V., O'Connor, M., Trojanowski, J., & Lee, V. (1994) · Neuron · doi:10.1016/0896-6273(94)90264-x · Cited by 588
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Noble, W. J., Olm, V., Takata, K., Casey, E., Mary, O., Meyerson, J. L., Gaynor, K., LaFrancois, J. J., Wang, L., Kondo, T., et al. (2003) · Neuron · doi:10.1016/s0896-6273(03)00259-9 · Cited by 511
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Vincent, I. J., Jicha, G. A., Rosado, M., & Dickson, D. W. (1997) · Journal of Neuroscience · doi:10.1523/jneurosci.17-10-03588.1997 · Cited by 444
Götz, J., Probst, A., Spillantini, M. G., Schäfer, T., Jakes, R., Bürki, K., & Goedert, M. (1995) · The EMBO Journal · doi:10.1002/j.1460-2075.1995.tb07116.x · Cited by 441
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Goedert, M., Jakes, R., Crowther, R. A., Cohen, P., Vanmechelen, E., Vandermeeren, M., & Cras, P. (1994) · Biochemical Journal · doi:10.1042/bj3010871 · Cited by 375
Targeting Cyclin-Dependent Kinases in Human Cancers: From Small Molecules to Peptide Inhibitors
Peyressatre, M., Prével, C., Pellerano, M., & Morris, M. C. (2015) · Cancers · doi:10.3390/cancers7010179 · Cited by 358
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Seubert, P., Mawal-Dewan, M., Barbour, R., Jakes, R., Goedert, M., Johnson, G. V. W., Litersky, J. M., Schenk, D., Lieberburg, I., Trojanowski, J. Q., et al. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.32.18917 · Cited by 345
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Ahlijanian, M. K., Barrezueta, N. X., Williams, R. D., Jakowski, A. B., Kowsz, K. P., McCarthy, S. A., Coskran, T., Carlo, A. A., Seymour, P. A., Burkhardt, J. E., et al. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.040577797 · Cited by 339
Domains of tau protein, differential phosphorylation, and dynamic instability of microtubules.
Trinczek, B., Biernat, J., Baumann, K., Mandelkow, E. M., & Mandelkow, E. (1995) · Molecular Biology of the Cell · doi:10.1091/mbc.6.12.1887 · Cited by 340
Sengupta, A., Kabat, J., Novak, M., Wu, Q., Grundke-Iqbal, I., & Iqbal, K. (1998) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1998.0813 · Cited by 363
Tau domains, phosphorylation, and interactions with microtubules
Mandelkow, E.-M., Biernat, J., Drewes, G., Gustke, N., Trinczek, B., & Mandelkow, E. (1995) · Neurobiology of Aging · doi:10.1016/0197-4580(95)00025-a · Cited by 308
Smith, P. D., Crocker, S. J., Jackson-Lewis, V. R., Jordan‐Sciutto, K. L., Hayley, S. P., Mount, M. P., O'Hare, M. J., Callaghan, S. M., Slack, R. S., Przedborski, S., et al. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2232515100 · Cited by 310
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Meyer, H. E., Mandelkow, E.-M., Drewes, G., Trinczek, B., Illenberger, S., Biernat, J., Schmitt-Ulms, G., & Mandelkow, E. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.13.7679 · Cited by 388
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
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Judging a Protein by More Than Its Name: GSK-3
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Wagner, U., Utton, M. A., Gallo, J., & Miller, C. C. J. (1996) · Journal of Cell Science · doi:10.1242/jcs.109.6.1537 · Cited by 258
Physiology and pathology of tau protein kinases in relation to Alzheimer's disease.
Imahori, K., & Uchida, T. (1997) · PubMed · Cited by 236
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
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Cassimeris, L., & Spittle, C. S. (2001) · International review of cytology · doi:10.1016/s0074-7696(01)10006-9 · Cited by 231
cAMP-Dependent Protein Kinase Phosphorylations on Tau in Alzheimer’s Disease
Jicha, G. A., Weaver, C. L., Lane, E., Vianna, C., Kress, Y., Rockwood, J. M., & Davies, P. (1999) · Journal of Neuroscience · doi:10.1523/jneurosci.19-17-07486.1999 · Cited by 207
Glycogen synthase kinase-3β phosphorylates tau protein at multiple sites in intact cells
Sperbera, B. R., Leight, S., Goedert, M., & Lee, V. M.-Y. (1995) · Neuroscience Letters · doi:10.1016/0304-3940(95)11902-9 · Cited by 204
Alzheimer-like Changes in Microtubule-associated Protein Tau Induced by Sulfated Glycosaminoglycans
Hasegawa, M., Crowther, R. A., Jakes, R., & Goedert, M. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.52.33118 · Cited by 207
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Liu, F., Iqbal, K., Grundke, I., & Gong, C. (2002) · FEBS Letters · doi:10.1016/s0014-5793(02)03487-7 · Cited by 197
Arendt, T. (2003) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2003.09.007 · Cited by 189
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Humbert, S., Dhavan, R., & Tsai, L. (2000) · Journal of Cell Science · doi:10.1242/jcs.113.6.975 · Cited by 188
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Piedrahita, D., Hernández, I., Tobon, A., Fedorov, D., Obara, B., Manjunath, B. S., Boudreau, R. L., Davidson, B. L., LaFerla, F. M., Gallego-Gómez, J. C., et al. (2010) · Journal of Neuroscience · doi:10.1523/jneurosci.3637-10.2010 · Cited by 188
Hirokawa, N., Funakoshi, T., Sato-Harada, R., & Kanai, Y. (1996) · The Journal of cell biology · doi:10.1083/jcb.132.4.667 · Cited by 179
Chatterjee, S., Sang, T.-K., Lawless, G. M., & Jackson, G. R. (2009) · Human Molecular Genetics · doi:10.1093/hmg/ddn326 · Cited by 178
Ferreira, A., Lu, Q., Orecchio, L., & Kosik, K. S. (1997) · Molecular and Cellular Neuroscience · doi:10.1006/mcne.1997.0615 · Cited by 178
Lew, J., & Wang, J. H.-C. (1995) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(00)88948-3 · Cited by 177
Self-citationCdk5 is involved in neuregulin-induced AChR expression at the neuromuscular junction
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Elevated neuronal Cdc2-like kinase activity in the Alzheimer disease brain
Lee, K., Clark, A. W., Rosales, J. L., Chapman, K. R., Fung, T. S., & Johnston, R. N. (1999) · Neuroscience Research · doi:10.1016/s0168-0102(99)00026-7 · Cited by 169
Tau mutations in frontotemporal dementia FTDP-17 and their relevance for Alzheimer’s disease
Goedert, M., & Spillantini, M. G. (2000) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/s0925-4439(00)00037-5 · Cited by 175
An Unusual Member of the Cdk Family: Cdk5
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Wen, Y., Yang, S.-H., Liu, R., Perez, E. J., Brun-Zinkernagel, A. M., Koulen, P., & Simpkins, J. W. (2007) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2006.10.011 · Cited by 162
Potentiation of GSK-3-catalyzed Alzheimer-like phosphorylation of human tau by cdk5
Sengupta, A., Wu, Q., Grundke, I., Iqbal, K., & Singh, T. J. (1997) · Molecular and Cellular Biochemistry · doi:10.1023/a:1006883924775 · Cited by 160
Hasegawa, M., Jakes, R., Crowther, R. A., Lee, V. M.-Y., Ihara, Y., & Goedert, M. (1996) · FEBS Letters · doi:10.1016/0014-5793(96)00271-2 · Cited by 163
EVANS, D. B., Rank, K. B., Bhattacharya, K., Thomsen, D. R., Gurney, M. E., & Sharma, S. K. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m000808200 · Cited by 155
Litersky, J. M., Johnson, G. V. W., Jakes, R., Goedert, M., Lee, M., & Seubert, P. A. (1996) · Biochemical Journal · doi:10.1042/bj3160655 · Cited by 150
Phosphorylation of MEK1 by cdk5/p35 Down-regulates the Mitogen-activated Protein Kinase Pathway
Sharma, P., Veeranna, Sharma, M., Amin, N. D., Sihag, R. K., Grant, P. G., Ahn, N. G., Kulkarni, A. B., & Pant, H. C. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m109324200 · Cited by 150
Truncation of CDK5 Activator p35 Induces Intensive Phosphorylation of Ser202/Thr205 of Human Tau
Hashiguchi, M., Saito, T., Hisanaga, S., & Hashiguchi, T. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m207426200 · Cited by 149
Dynamic association of tau with neuronal membranes is regulated by phosphorylation
Pooler, A. M., Usardi, A., Evans, C. J., Philpott, K. L., Noble, W., & Hanger, D. P. (2012) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2011.01.005 · Cited by 148
Maccioni, R. B., Carola Otth, L., Concha, I. I., & Muñoz, J. P. (2001) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.2001.02024.x · Cited by 173
Ishiguro, K., Kobayashi, S., Onion, A., Takamatsu, M., Yonekura, S., Anzai, K., Imahori, K., & Uchida, T. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)80501-6 · Cited by 147
Specific tau variants in the brains of patients with myotonic dystrophy
Vermersch, P., Sergeant, N., Ruchoux, M., Hofmann-Radvanyi, H., Wattez, A., Petit, H., Dewailly, P., & Delacourte, A. (1996) · Neurology · doi:10.1212/wnl.47.3.711 · Cited by 146
Cyclin‐dependent kinase‐5 in neurodegeneration
Shelton, S. B., & Johnson, G. V. W. (2004) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2003.02328.x · Cited by 146
JNK Plays a Key Role in Tau Hyperphosphorylation in Alzheimer's Disease Models
Ploia, C., Antoniou, X., Sclip, A., Grande, V., Cardinetti, D., Colombo, A., Canu, N., Benussi, L., Ghidoni, R., Forloni, G., et al. (2011) · Journal of Alzheimer's Disease · doi:10.3233/jad-2011-110320 · Cited by 145
Structure, Microtubule Interactions, and Phosphorylation of Tau Proteina
Mandelkow�, E., Schweers, O., Drewes, G., Biernat, J., Gustke, N., Trinczek, B., & Mandelkow, E. (1996) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1996.tb34407.x · Cited by 142
Involvement of microtubules in the regulation of neuronal growth cone morphologic remodeling
Gallo, G. (1998) · Journal of Neurobiology · doi:10.1002/(sici)1097-4695(199805)35:2 · Cited by 30
Calpain‐mediated degradation of p35 to p25 in postmortem human and rat brains
Taniguchi, S., Fujita, Y., Hayashi, S., Kakita, A., Takahashi, H., Murayama, S., Saido, T. C., Hisanaga, S., Iwatsubo, T., & Hasegawa, M. (2001) · FEBS Letters · doi:10.1016/s0014-5793(00)02431-5 · Cited by 141
Mawal-Dewan, M., Henley, J., VOORDE, A. V. D., Trojanowski, J. Q., & Lee, V. M. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)47378-4 · Cited by 140
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Ohshima, T., Gilmore, E. C., Longenecker, G., Jacobowitz, D. M., Brady, R. O., Herrup, K., & Kulkarni, A. B. (1999) · Journal of Neuroscience · doi:10.1523/jneurosci.19-14-06017.1999 · Cited by 142
Chen, S., Pelletier, D. B., Peng, A., & Boynton, A. L. (1995) · PubMed · Cited by 140
Feijoo, C., Campbell, D. G., Jakes, R., Goedert, M., & Cuenda, A. (2005) · Journal of Cell Science · doi:10.1242/jcs.01655 · Cited by 133
Arendt, T., Holzer, M., Fruth, R., Brückner, M. K., & Gärtner, U. (1995) · Neuroscience · doi:10.1016/0306-4522(95)00347-l · Cited by 132
Down-regulation of WW Domain-containing Oxidoreductase Induces Tau Phosphorylation in Vitro
Sze, C.-I., Su, M., Pugazhenthi, S., Jambal, P., Hsu, L.-J., Heath, J., Schultz, L., & Chang, N.-S. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m401399200 · Cited by 130
Regulation of cyclin-dependent kinase 5 catalytic activity by phosphorylation
Sharma, P., Sharma, M., Amin, N. D., Albers, R. W., & Pant, H. C. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.20.11156 · Cited by 131
Cortical and brainstem-type Lewy bodies are immunoreactive for the cyclin-dependent kinase 5.
Brion, J., & Couck, A. M. (1995) · Europe PMC (PubMed Central) · Cited by 125
Starvation induces tau hyperphosphorylation in mouse brain: implications for Alzheimer's disease
Yanagisawa, M., Planel, E., Ishiguro, K., & Fujita, S. C. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)01480-5 · Cited by 123
Ohshima, T., Ogawa, M., Veeranna, Hirasawa, M., Longenecker, G., Ishiguro, K., Pant, H. C., Brady, R. O., Kulkarni, A. B., & Mikoshiba, K. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.051628498 · Cited by 122
Identification of Functional Domains in the Neuronal Cdk5 Activator Protein
Poon, R. Y. C., Lew, J., & Hunter, T. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.9.5703 · Cited by 116
Self-citationAmbegaokar, S. S., & Jackson, G. R. (2011) · Human Molecular Genetics · doi:10.1093/hmg/ddr432 · Cited by 113
“Cdk5 is a known tau kinase (28,279), which may indicate a common regulatory mechanism between Cdk5 and Cyclin E/Cdk2.”
BackgroundInvolvement of calpain in the neuropathogenesis of Alzheimer’s disease
Mahaman, Y. A. R., Huang, F., Afewerky, H. K., Salissou, M. T. M., Bishwajit, G., & Wang, X. (2018) · Medicinal Research Reviews · doi:10.1002/med.21534 · Cited by 110
Dendritic changes in Alzheimer's disease and factors that may underlie these changes
Anderton, B. H., Callahan, L. M., Coleman, P. D., Davies, P., Flood, D. G., Jicha, G. A., Ohm, T. G., & Weaver, C. L. (1998) · Progress in Neurobiology · doi:10.1016/s0301-0082(98)00022-7 · Cited by 113
Glycogen Synthase Kinase-3β Is Complexed with Tau Protein in Brain Microtubules
Sun, W., Qureshi, H. Y., Cafferty, P. W., Sobue, K., Agarwal-Mawal, A., Neufield, K. D., & Paudel, H. K. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m107182200 · Cited by 110
Self-citationGodemann, R., Biernat, J., Mandelkow, E., & Mandelkow�, E. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)00741-3 · Cited by 110
Mitotic-like Tau Phosphorylation by p25-Cdk5 Kinase Complex
Hamdane, M., Sambo, A., Delobel, P., Bégard, S., Violleau, A., Delacourte, A., Bertrand, P., Bénavidès, J., & Buée, L. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m302872200 · Cited by 107
Zeng, K., Ko, H., Yang, H. O., & Wang, X. (2010) · Neuropharmacology · doi:10.1016/j.neuropharm.2010.07.020 · Cited by 106
Li, B., Zhang, L., Gu, J., Amin, N. D., & Pant, H. C. (2000) · Journal of Neuroscience · doi:10.1523/jneurosci.20-16-06055.2000 · Cited by 106
Preuß, U., Döring, F., Illenberger, S., & Mandelkow�, E. (1995) · Molecular Biology of the Cell · doi:10.1091/mbc.6.10.1397 · Cited by 101
Axonopathy, tau abnormalities, and dyskinesia, but no neurofibrillary tangles in p25‐transgenic mice
Bian, F., Nath, R., Sobocinski, G. P., Booher, R. N., Lipinski, W. J., Callahan, M. J., Pack, A., Wang, K., & Walker, L. C. (2002) · The Journal of Comparative Neurology · doi:10.1002/cne.10186 · Cited by 101
Qi, R. Z., Huang, Q., Lee, K., Lew, J., & Wang, J. H.-C. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.18.10847 · Cited by 99
Self-citationTau as a Therapeutic Target for Alzheimers Disease
Boutajangout, A., Sigurdsson, E. M., & Krishnamurthy, P. K. (2011) · Current Alzheimer Research · doi:10.2174/156720511796717195 · Cited by 102
Interaction of Cyclin-dependent Kinase 5 (Cdk5) and Neuronal Cdk5 Activator in Bovine Brain
Lee, K., Rosales, J. L., Tang, D., & Wang, J. H.-C. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.3.1538 · Cited by 93
Self-citationMolecular dissection of the paired helical filament
Goedert, M., Spillantini, M. G., Jakes, R., Crowtherp, R. A., Vanmechelen, E., Probst, A., Götz, J., Bürki, K., & Cohen, P. (1995) · Neurobiology of Aging · doi:10.1016/0197-4580(95)00017-9 · Cited by 94
The cell cycle as a therapeutic target for Alzheimer's disease
Neve, R. L., & McPhie, D. L. (2006) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2005.09.005 · Cited by 92
Cdc2 phosphorylation of nucleolin demarcates mitotic stages and Alzheimer’s disease pathology
Dranovsky, A., Vincent, I. J., Gregori, L. L., Schwarzman, A. L., Colflesh, D. E., Enghild, J. J., Strittmatter, W. J., Davies, P., & Goldgaber, D. (2001) · Neurobiology of Aging · doi:10.1016/s0197-4580(00)00248-7 · Cited by 92
Paudel, H. K., & Li, W. S. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.12.8029 · Cited by 89
Self-citation
Metadata
- Authors
- Paudel, H. K., Lew, J., Ali, Z., & Wang, J. H.
- Affiliations
- University of Calgary (CA)
- ORCID
- Ali, Z
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1993-11
- Volume
- 268
- Issue
- 31
- Pages
- 23512-23518
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1568595238
- Cited by
- 285
- References
- 49
- Citations by year
- 2023: 4 · 2022: 3 · 2021: 2 · 2020: 1 · 2018: 3 · 2017: 3 · 2016: 5 · 2015: 2 · 2014: 5 · 2013: 7 · 2012: 6
- FWCI
- 12.99
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Rare & Special e-Zone (The Hong Kong University of Science and Technology) (submittedVersion)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Keywords
- tau phosphorylation, paired helical filaments, Alzheimer's disease, MAP2, microtubule-associated proteins, phosphorylation sites
- MeSH terms
- Alzheimer Disease, Amino Acid Sequence, Animals, Brain, Cattle, Humans, Microtubule-Associated Proteins, Molecular Sequence Data, Phosphoproteins, Phosphorylation, Phosphoserine, Phosphothreonine, tau Proteins, Protein Serine-Threonine Kinases, Calcium-Calmodulin-Dependent Protein Kinases, Proline-Directed Protein Kinases
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