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Mapt  -  microtubule-associated protein tau

Rattus norvegicus

Synonyms: Microtubule-associated protein tau, Mtapt, Neurofibrillary tangle protein, PHF-tau, Paired helical filament-tau, ...
 
 
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Chemical compound and disease context of Mapt

 

Biological context of Mapt

 

Anatomical context of Mapt

 

Associations of Mapt with chemical compounds

 

Other interactions of Mapt

References

  1. Hyperphosphorylation and aggregation of tau in experimental autoimmune encephalomyelitis. Schneider, A., Araújo, G.W., Trajkovic, K., Herrmann, M.M., Merkler, D., Mandelkow, E.M., Weissert, R., Simons, M. J. Biol. Chem. (2004) [Pubmed]
  2. 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.Y., Wang, Q., Deng, H.M., Gong, C.X., Grundke-Iqbal, I., Iqbal, K., Wang, J.Z. J. Biol. Chem. (2004) [Pubmed]
  3. Secreted beta-APP stimulates MAP kinase and phosphorylation of tau in neurons. Greenberg, S.M., Kosik, K.S. Neurobiol. Aging (1995) [Pubmed]
  4. Specific tau phosphorylation sites in hippocampus correlate with impairment of step-down inhibitory avoidance task in rats. Chen, Y.G. Behav. Brain Res. (2005) [Pubmed]
  5. Pituitary adenylate cyclase-activating polypeptide prevents the effects of ceramides on migration, neurite outgrowth, and cytoskeleton remodeling. Falluel-Morel, A., Vaudry, D., Aubert, N., Galas, L., Benard, M., Basille, M., Fontaine, M., Fournier, A., Vaudry, H., Gonzalez, B.J. Proc. Natl. Acad. Sci. U.S.A. (2005) [Pubmed]
  6. Functional implications for the microtubule-associated protein tau: localization in oligodendrocytes. LoPresti, P., Szuchet, S., Papasozomenos, S.C., Zinkowski, R.P., Binder, L.I. Proc. Natl. Acad. Sci. U.S.A. (1995) [Pubmed]
  7. Cloning of a big tau microtubule-associated protein characteristic of the peripheral nervous system. Goedert, M., Spillantini, M.G., Crowther, R.A. Proc. Natl. Acad. Sci. U.S.A. (1992) [Pubmed]
  8. Dynamic regulation of expression and phosphorylation of tau by fibroblast growth factor-2 in neural progenitor cells from adult rat hippocampus. Tatebayashi, Y., Iqbal, K., Grundke-Iqbal, I. J. Neurosci. (1999) [Pubmed]
  9. Corticosterone exacerbates kainate-induced alterations in hippocampal tau immunoreactivity and spectrin proteolysis in vivo. Elliott, E.M., Mattson, M.P., Vanderklish, P., Lynch, G., Chang, I., Sapolsky, R.M. J. Neurochem. (1993) [Pubmed]
  10. Role of protein phosphatase-2A and -1 in the regulation of GSK-3, cdk5 and cdc2 and the phosphorylation of tau in rat forebrain. Bennecib, M., Gong, C.X., Grundke-Iqbal, I., Iqbal, K. FEBS Lett. (2000) [Pubmed]
  11. The slow axonal transport of the microtubule-associated protein tau and the transport rates of different isoforms and mutants in cultured neurons. Utton, M.A., Connell, J., Asuni, A.A., van Slegtenhorst, M., Hutton, M., de Silva, R., Lees, A.J., Miller, C.C., Anderton, B.H. J. Neurosci. (2002) [Pubmed]
  12. Acute anoxia induces tau dephosphorylation in rat brain slices and its possible underlying mechanisms. Liu, R., Pei, J.J., Wang, X.C., Zhou, X.W., Tian, Q., Winblad, B., Wang, J.Z. J. Neurochem. (2005) [Pubmed]
  13. 4-Hydroxynonenal, a product of lipid peroxidation, inhibits dephosphorylation of the microtubule-associated protein tau. Mattson, M.P., Fu, W., Waeg, G., Uchida, K. Neuroreport (1997) [Pubmed]
  14. Tau associates with actin in differentiating PC12 cells. Yu, J.Z., Rasenick, M.M. FASEB J. (2006) [Pubmed]
  15. The microtubule binding of Tau and high molecular weight Tau in apoptotic PC12 cells is impaired because of altered phosphorylation. Davis, P.K., Johnson, G.V. J. Biol. Chem. (1999) [Pubmed]
  16. Distribution and trafficking of JHM coronavirus structural proteins and virions in primary neurons and the OBL-21 neuronal cell line. Pasick, J.M., Kalicharran, K., Dales, S. J. Virol. (1994) [Pubmed]
  17. Overactivation of glycogen synthase kinase-3 by inhibition of phosphoinositol-3 kinase and protein kinase C leads to hyperphosphorylation of tau and impairment of spatial memory. Liu, S.J., Zhang, A.H., Li, H.L., Wang, Q., Deng, H.M., Netzer, W.J., Xu, H., Wang, J.Z. J. Neurochem. (2003) [Pubmed]
  18. Differential axonal transport of soluble and insoluble tau in the rat sciatic nerve. Tashiro, T., Sun, X., Tsuda, M., Komiya, Y. J. Neurochem. (1996) [Pubmed]
  19. Effect of inhibiting melatonin biosynthesis on spatial memory retention and tau phosphorylation in rat. Zhu, L.Q., Wang, S.H., Ling, Z.Q., Wang, D.L., Wang, J.Z. J. Pineal Res. (2004) [Pubmed]
  20. Ceramide selectively decreases tau levels in differentiated PC12 cells through modulation of calpain I. Xie, H., Johnson, G.V. J. Neurochem. (1997) [Pubmed]
  21. The phosphorylation state of the microtubule-associated protein tau as affected by glutamate, colchicine and beta-amyloid in primary rat cortical neuronal cultures. Davis, D.R., Brion, J.P., Couck, A.M., Gallo, J.M., Hanger, D.P., Ladhani, K., Lewis, C., Miller, C.C., Rupniak, T., Smith, C. Biochem. J. (1995) [Pubmed]
  22. Modulation of the phosphorylation state of tau in situ: the roles of calcium and cyclic AMP. Fleming, L.M., Johnson, G.V. Biochem. J. (1995) [Pubmed]
  23. Opposite effects of lithium and valproic acid on trophic factor deprivation-induced glycogen synthase kinase-3 activation, c-Jun expression and neuronal cell death. Jin, N., Kovács, A.D., Sui, Z., Dewhurst, S., Maggirwar, S.B. Neuropharmacology (2005) [Pubmed]
  24. Neurotoxic calcium transfer from endoplasmic reticulum to mitochondria is regulated by cyclin-dependent kinase 5-dependent phosphorylation of tau. Darios, F., Muriel, M.P., Khondiker, M.E., Brice, A., Ruberg, M. J. Neurosci. (2005) [Pubmed]
  25. Interaction of Tau with Fe65 links tau to APP. Barbato, C., Canu, N., Zambrano, N., Serafino, A., Minopoli, G., Ciotti, M.T., Amadoro, G., Russo, T., Calissano, P. Neurobiol. Dis. (2005) [Pubmed]
  26. Isoform-specific interactions of apolipoprotein E with the microtubule-associated protein MAP2c: implications for Alzheimer's disease. Huang, D.Y., Goedert, M., Jakes, R., Weisgraber, K.H., Garner, C.C., Saunders, A.M., Pericak-Vance, M.A., Schmechel, D.E., Roses, A.D., Strittmatter, W.J. Neurosci. Lett. (1994) [Pubmed]
 
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