메뉴 건너뛰기




Volumn 8, Issue 6, 2011, Pages 623-632

Role of protein phosphatase 2A in Alzheimer's disease

Author keywords

Alzheimer's disease; Neurofilaments; Pin1; Protein dephosphorylation; Protein kinases and phosphatases; Protein phosphatase 2a; Tau

Indexed keywords

CALCINEURIN; CANTHARIDIN; GLYCOGEN SYNTHASE KINASE 3; MICROCYSTIN LR; NODULARIN; PHOSPHOPROTEIN PHOSPHATASE 2A; TAU PROTEIN; TAUTOMYCIN;

EID: 80051713257     PISSN: 15672050     EISSN: 18755828     Source Type: Journal    
DOI: 10.2174/156720511796717168     Document Type: Review
Times cited : (31)

References (123)
  • 1
    • 0023200370 scopus 로고
    • Histopathological criteria for progressive dementia disorders: Clinicalpathological correlation and classification by multivariate data analysis
    • Alafuzoff I, Iqbal K, Friden H, Adolfsson R, Winblad B. Histopathological criteria for progressive dementia disorders: clinicalpathological correlation and classification by multivariate data analysis. Acta Neuropathol 74: 209-225 (1987).
    • (1987) Acta Neuropathol , vol.74 , pp. 209-225
    • Alafuzoff, I.1    Iqbal, K.2    Friden, H.3    Adolfsson, R.4    Winblad, B.5
  • 2
    • 0029999787 scopus 로고    scopus 로고
    • Alzheimer's disease hyperphosphorylated Tau sequesters normal Tau into tangles of filaments and disassembles microtubules
    • Alonso AD, Grundke-Iqbal I, Iqbal K. Alzheimer's disease hyperphosphorylated Tau sequesters normal Tau into tangles of filaments and disassembles microtubules. Nat Med 2: 783-787 (1996).
    • (1996) Nat Med , vol.2 , pp. 783-787
    • Alonso, A.D.1    Grundke-Iqbal, I.2    Iqbal, K.3
  • 3
    • 0028227962 scopus 로고
    • Role of abnormally phosphorylated Tau in the breakdown of microtubules in Alzheimer disease
    • Alonso AD, Zaidi T, Grundke-Iqbal I, Iqbal K. Role of abnormally phosphorylated Tau in the breakdown of microtubules in Alzheimer disease. Proc Natl Acad Sci USA 91: 5562-5566 (1994).
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 5562-5566
    • Alonso, A.D.1    Zaidi, T.2    Grundke-Iqbal, I.3    Iqbal, K.4
  • 4
    • 0025993428 scopus 로고
    • Hereditary hypotrophic axonopathy with neurofilament deficiency in a mutant strain of the Japanese quail
    • Yamasaki H, Itakura C, Mizutani M. Hereditary hypotrophic axonopathy with neurofilament deficiency in a mutant strain of the Japanese quail. Acta Neuropathol 82: 427-434 (1991).
    • (1991) Acta Neuropathol , vol.82 , pp. 427-434
    • Yamasaki, H.1    Itakura, C.2    Mizutani, M.3
  • 5
    • 0026529403 scopus 로고
    • Phosphorylation-dependent neurofilament epitopes are reduced in nodes of Ranvier
    • Mata M, Kupina M, Fink DJ. Phosphorylation-dependent neurofilament epitopes are reduced in nodes of Ranvier. Neurocytology 21: 199-210 (1992).
    • (1992) Neurocytology , vol.21 , pp. 199-210
    • Mata, M.1    Kupina, M.2    Fink, D.J.3
  • 6
    • 0027530064 scopus 로고
    • Neurofilament deficiency in quail caused by nonsense mutation in neurofilament- L gene
    • O'Hara O, Gahara Y, Miyake T, Teraoka H, Kitamura T. Neurofilament deficiency in quail caused by nonsense mutation in neurofilament- L gene. J Cell Biol 121: 387-395 (1993).
    • (1993) J Cell Biol , vol.121 , pp. 387-395
    • O'Hara, O.1    Gahara, Y.2    Miyake, T.3    Teraoka, H.4    Kitamura, T.5
  • 7
    • 0026580004 scopus 로고
    • Local modulation of neurofilament phosphorylation, axonal caliber, and slow axonal transport by myelinating Schwann cells
    • DeWaegh SM, Lee VMY, Brady ST. Local modulation of neurofilament phosphorylation, axonal caliber, and slow axonal transport by myelinating Schwann cells. Cell 68: 451-463 (1992).
    • (1992) Cell , vol.68 , pp. 451-463
    • Dewaegh, S.M.1    Lee, V.M.Y.2    Brady, S.T.3
  • 8
    • 0028261670 scopus 로고
    • Neurofilament-deficient axons and perikaryal aggregates in viable transgenic mice expressing a neurofilamentbeta-galactosidase fusion protein
    • Eyer J, Peterson A. Neurofilament-deficient axons and perikaryal aggregates in viable transgenic mice expressing a neurofilamentbeta- galactosidase fusion protein. Neuron 12: 389-405 (1994).
    • (1994) Neuron , vol.12 , pp. 389-405
    • Eyer, J.1    Peterson, A.2
  • 10
    • 0024237394 scopus 로고
    • Dephosphorylation of neurofilament proteins enhances their susceptibility to degradation by calpain
    • Pant HC. Dephosphorylation of neurofilament proteins enhances their susceptibility to degradation by calpain. Biochem J 256: 665-668 (1988).
    • (1988) Biochem J , vol.256 , pp. 665-668
    • Pant, H.C.1
  • 11
    • 0023931776 scopus 로고
    • Identification and quantification of calcium binding proteins in squid axoplasm
    • Krinks MH, Klee CB, Pant HC, Gainer H. Identification and quantification of calcium binding proteins in squid axoplasm. J Neurosci 8: 2172-2182 (1988).
    • (1988) J Neurosci , vol.8 , pp. 2172-2182
    • Krinks, M.H.1    Klee, C.B.2    Pant, H.C.3    Gainer, H.4
  • 15
    • 0033970533 scopus 로고    scopus 로고
    • Dual specificity phosphatases: A gene family for control of MAP kinase function
    • Camps M, Nichols A, Arkinstall S. Dual specificity phosphatases: a gene family for control of MAP kinase function. FASEB J 14: 6-16 (2000).
    • (2000) FASEB J , vol.14 , pp. 6-16
    • Camps, M.1    Nichols, A.2    Arkinstall, S.3
  • 17
    • 0030296869 scopus 로고    scopus 로고
    • Molecular mechanisms of the protein serine/threonine phosphatases
    • Barford D. Molecular mechanisms of the protein serine/threonine phosphatases. Trends Biochem Sci 21:407-412 (1996).
    • (1996) Trends Biochem Sci , vol.21 , pp. 407-412
    • Barford, D.1
  • 18
    • 15044348175 scopus 로고    scopus 로고
    • Protein serine/threonine phosphatases: Life, death, and sleeping
    • Gallego M, Virshup DM. Protein serine/threonine phosphatases: life, death, and sleeping. Curr Opin Cell Biol 17: 197-202 (2005).
    • (2005) Curr Opin Cell Biol , vol.17 , pp. 197-202
    • Gallego, M.1    Virshup, D.M.2
  • 19
    • 0031860103 scopus 로고    scopus 로고
    • The structure and mechanism of protein phosphatases: Insights into catalysis and regulation
    • Barford D, Das AK, Egloff MP. The structure and mechanism of protein phosphatases: Insights into catalysis and regulation. Ann Review Biophysics Biomolecular Structure 27: 133-164 (1998).
    • (1998) Ann Review Biophysics Biomolecular Structure , vol.27 , pp. 133-164
    • Barford, D.1    Das, A.K.2    Egloff, M.P.3
  • 20
    • 0030874269 scopus 로고    scopus 로고
    • Modulation of the enzymatic properties of protein phosphatase 2A catalytic subunit by the recombinant 65kDa regulatory subunit PR65-alpha
    • Turowski P, Favre B, Campbell KS, Lamb NJC, Hemmings BA. Modulation of the enzymatic properties of protein phosphatase 2A catalytic subunit by the recombinant 65kDa regulatory subunit PR65-alpha. Eur J Biochem 248: 200-208 (1997).
    • (1997) Eur J Biochem , vol.248 , pp. 200-208
    • Turowski, P.1    Favre, B.2    Campbell, K.S.3    Lamb, N.J.C.4    Hemmings, B.A.5
  • 21
    • 0028359957 scopus 로고
    • Protein phosphatase 2A is a "menage a trois "
    • Mayer-Jaekel RE, Hemmings BA. Protein phosphatase 2A is a "menage a trois ". Trends Cell Biol 4: 287-291 (1994).
    • (1994) Trends Cell Biol , vol.4 , pp. 287-291
    • Mayer-Jaekel, R.E.1    Hemmings, B.A.2
  • 22
    • 0024397415 scopus 로고
    • The structure and regulation of protein phosphatases
    • Cohen P. The structure and regulation of protein phosphatases. Annu Rev Biochem 58: 453-508 (1989).
    • (1989) Annu Rev Biochem , vol.58 , pp. 453-508
    • Cohen, P.1
  • 23
    • 33750006297 scopus 로고    scopus 로고
    • Structure of proteinphosphatase2A core enzyme bound to tumorinducing toxins
    • Xing YN, Xu YH, Chen Y, Jeffrey PD, Chao Y, Lin Z, et al. Structure of proteinphosphatase2A core enzyme bound to tumorinducing toxins. Cell 127: 341-353 (2006).
    • (2006) Cell , vol.127 , pp. 341-353
    • Xing, Y.N.1    Xu, Y.H.2    Chen, Y.3    Jeffrey, P.D.4    Chao, Y.5    Lin, Z.6
  • 24
    • 33846118688 scopus 로고    scopus 로고
    • Crystal structure of a protein phosphatase 2A heterotrimeric holoenzyme
    • Cho US, Xu WQ. Crystal structure of a protein phosphatase 2A heterotrimeric holoenzyme. Nature 445(1): 53-57 (2006).
    • (2006) Nature , vol.445 , Issue.1 , pp. 53-57
    • Cho, U.S.1    Xu, W.Q.2
  • 25
    • 0025313882 scopus 로고
    • Protein serine/ threonine phosphatases; an expanding family
    • Cohen PT, Brewis ND, Hughes V, Mann DJ. Protein serine/ threonine phosphatases; an expanding family. FEBS Lett 268(2): 355-359 (1990).
    • (1990) FEBS Lett , vol.268 , Issue.2 , pp. 355-359
    • Cohen, P.T.1    Brewis, N.D.2    Hughes, V.3    Mann, D.J.4
  • 26
    • 0035252894 scopus 로고    scopus 로고
    • Protein phosphatase 2A: A highly regulated family of serine/threonine phosphatases implicated in cell growth and signalling
    • Janssens V, Goris J. Protein phosphatase 2A: a highly regulated family of serine/threonine phosphatases implicated in cell growth and signalling. Biochem J 353: 417-439 (2001).
    • (2001) Biochem J , vol.353 , pp. 417-439
    • Janssens, V.1    Goris, J.2
  • 27
    • 0023748777 scopus 로고
    • Human liver phosphatase 2A: CDNA and amino acid sequence of two catalytic subunit isotypes
    • Arino J, Woon CW, Brautigan DL, Miller TB Jr, Johnson GL. Human liver phosphatase 2A: cDNA and amino acid sequence of two catalytic subunit isotypes. Proc Natl Acad Sci USA 85(12): 4252-4256 (1988).
    • (1988) Proc Natl Acad Sci USA , vol.85 , Issue.12 , pp. 4252-4256
    • Arino, J.1    Woon, C.W.2    Brautigan, D.L.3    Miller Jr., T.B.4    Johnson, G.L.5
  • 28
    • 0023372798 scopus 로고
    • Molecular cloning and sequence analysis of the catalytic subunit of bovine type 2A protein phosphatase
    • Green DD, Yang SI, Mumby MC. Molecular cloning and sequence analysis of the catalytic subunit of bovine type 2A protein phosphatase. Proc Natl Acad Sci USA 84(14): 4880-4 (1987).
    • (1987) Proc Natl Acad Sci USA , vol.84 , Issue.14 , pp. 4880-4884
    • Green, D.D.1    Yang, S.I.2    Mumby, M.C.3
  • 29
    • 0025275038 scopus 로고
    • Alpha- and beta-forms of the 65-kDa subunit of protein phosphatase 2A have a similar 39 amino acid repeating structure
    • Hemmings BA, Adams-Pearson C, Maurer F, Müller P, Goris J, Merlevede W, et al. alpha- and beta-forms of the 65-kDa subunit of protein phosphatase 2A have a similar 39 amino acid repeating structure. Biochemistry 29(13): 3166-3173. (1990)
    • (1990) Biochemistry , vol.29 , Issue.13 , pp. 3166-3173
    • Hemmings, B.A.1    Adams-Pearson, C.2    Maurer, F.3    Müller, P.4    Goris, J.5    Merlevede, W.6
  • 30
    • 33750006297 scopus 로고    scopus 로고
    • Structure of protein phosphatase 2A core enzyme bound to tumor-inducing toxins
    • Xing Y, Xu Y, Chen Y, Jeffrey PD, Chao Y, Lin Z, et al. Structure of protein phosphatase 2A core enzyme bound to tumor-inducing toxins. Cell 127(2): 341-353 (2006).
    • (2006) Cell , vol.127 , Issue.2 , pp. 341-353
    • Xing, Y.1    Xu, Y.2    Chen, Y.3    Jeffrey, P.D.4    Chao, Y.5    Lin, Z.6
  • 31
    • 0025635610 scopus 로고
    • Tautomycin from the bacterium Streptomyces verticillatus. Another potent and specific inhibitor of protein phosphatases 1 and 2A
    • MacKintosh C, Klumpp S. Tautomycin from the bacterium Streptomyces verticillatus. Another potent and specific inhibitor of protein phosphatases 1 and 2A. FEBS Lett 277: 137-140 (1990)
    • (1990) FEBS Lett , vol.277 , pp. 137-140
    • Mackintosh, C.1    Klumpp, S.2
  • 33
    • 0025201229 scopus 로고
    • Characterization of microcystin-LR, a potent inhibitor of type 1 and type 2A protein phosphatases
    • Honkanen RE, Zwiller J, Moore RE, Daily SL, Khatra BS, Dukelow M, et al. Characterization of microcystin-LR, a potent inhibitor of type 1 and type 2A protein phosphatases. J Biol Chem 265: 19401-19404 (1990).
    • (1990) J Biol Chem , vol.265 , pp. 19401-19404
    • Honkanen, R.E.1    Zwiller, J.2    Moore, R.E.3    Daily, S.L.4    Khatra, B.S.5    Dukelow, M.6
  • 35
    • 0027096275 scopus 로고
    • Cantharidin binding protein: Identification as protein phosphatase 2A
    • Li YM, Casida JE. Cantharidin binding protein: identification as protein phosphatase 2A. Proc Natl Acad Sci USA 89: 11867-11870 (1992).
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 11867-11870
    • Li, Y.M.1    Casida, J.E.2
  • 36
    • 0028931302 scopus 로고
    • Urification and characterization of two potent heat-stable protein inhibitors of protein phosphatase 2A from bovine kidney
    • Li M, Guo H, Damuni Z. Urification and characterization of two potent heat-stable protein inhibitors of protein phosphatase 2A from bovine kidney. Biochemistry 34: 1988-1996 (1995).
    • (1995) Biochemistry , vol.34 , pp. 1988-1996
    • Li, M.1    Guo, H.2    Damuni, Z.3
  • 37
    • 0029665228 scopus 로고    scopus 로고
    • Molecular identification of I1PP2A, a novel potent heat-stable inhibitor protein of protein phosphatase 2A
    • Li M, Makkinje A, Damuni Z. Molecular identification of I1PP2A, a novel potent heat-stable inhibitor protein of protein phosphatase 2A. Biochemistry 35: 6998-7002 (1996).
    • (1996) Biochemistry , vol.35 , pp. 6998-7002
    • Li, M.1    Makkinje, A.2    Damuni, Z.3
  • 38
    • 11844273281 scopus 로고    scopus 로고
    • Grundke-Iqbal, Iqbal K. Inhibitors of protein phosphatase-2A from human brain structures, immunocytological localization and activities towards dephosphorylation of the Alzheimer type hyperphosphorylated Tau
    • Tsujio I, Zaidi T, Xu J, Kotula L, Grundke-Iqbal, Iqbal K. Inhibitors of protein phosphatase-2A from human brain structures, immunocytological localization and activities towards dephosphorylation of the Alzheimer type hyperphosphorylated Tau. FEBS Lett 579: 363-372. (2005)
    • (2005) FEBS Lett , vol.579 , pp. 363-372
    • Tsujio, I.1    Zaidi, T.2    Xu, J.3    Kotula, L.4
  • 39
    • 0030813618 scopus 로고    scopus 로고
    • Biochemical characterization of mapmodulin, a protein that binds microtubule-associated proteins
    • Ulitzur N, Rancano C, Pfeffer SR. Biochemical characterization of mapmodulin, a protein that binds microtubule-associated proteins. J Biol Chem 272: 30577-30582 (1997).
    • (1997) J Biol Chem , vol.272 , pp. 30577-30582
    • Ulitzur, N.1    Rancano, C.2    Pfeffer, S.R.3
  • 40
    • 0026693436 scopus 로고
    • Can, a putative oncogene associated with myeloid leukemogenesis, may be activated by fusion of its 3' half to different genes: Characterization of the set gene
    • von Lindern M, van Baal S, Wiegant J, Raap A, Hagemeijer A, Grosvela G. Can, a putative oncogene associated with myeloid leukemogenesis, may be activated by fusion of its 3' half to different genes: characterization of the set gene. Mol Cell Biol 12: 3346-3355 (1992).
    • (1992) Mol Cell Biol , vol.12 , pp. 3346-3355
    • von Lindern, M.1    van Baal, S.2    Wiegant, J.3    Raap, A.4    Hagemeijer, A.5    Grosvela, G.6
  • 41
    • 19544362550 scopus 로고    scopus 로고
    • Up-regulation of inhibitors of protein phosphatase-2A in Alzheimer's disease
    • Tanimukai H, Grundke-Iqbal I, Iqbal K. Up-regulation of inhibitors of protein phosphatase-2A in Alzheimer's disease. Am J Pathol 166: 1761-1771 (2005).
    • (2005) Am J Pathol , vol.166 , pp. 1761-1771
    • Tanimukai, H.1    Grundke-Iqbal, I.2    Iqbal, K.3
  • 42
    • 41149176740 scopus 로고    scopus 로고
    • I1 PP2A and I2 PP2A affect Tau phosphorylation via association with the catalytic subunit of protein phosphatase 2A
    • Chen S, Grundke-Iqbal I, Iqbal K. I1 PP2A and I2 PP2A affect Tau phosphorylation via association with the catalytic subunit of protein phosphatase 2A. Alzheimers Dement 2: S471(2006).
    • (2006) Alzheimers Dement , vol.2
    • Chen, S.1    Grundke-Iqbal, I.2    Iqbal, K.3
  • 43
    • 44849144122 scopus 로고    scopus 로고
    • I1PP2A affects Tau phosphorylation via association with the catalytic subunit of protein phosphatase 2A
    • Chen S, Li B, Grundke-Iqbal I, Iqbal K. I1PP2A affects Tau phosphorylation via association with the catalytic subunit of protein phosphatase 2A. J Biol Chem 283:10513-10521 (2008).
    • (2008) J Biol Chem , vol.283 , pp. 10513-10521
    • Chen, S.1    Li, B.2    Grundke-Iqbal, I.3    Iqbal, K.4
  • 44
    • 0025994387 scopus 로고
    • Protein phosphorylation and neuronal function
    • Walaas SI, Greengard P. Protein phosphorylation and neuronal function. Pharmacol Rev 43: 299-349 (1991).
    • (1991) Pharmacol Rev , vol.43 , pp. 299-349
    • Walaas, S.I.1    Greengard, P.2
  • 45
    • 0033010457 scopus 로고    scopus 로고
    • Role of calcineurin and protein phosphatase-2A in the regulation of DARPP-32 dephosphorylation in neostriatal neurons
    • Nishi A, Snyder GL, Nairn AC, Greengard P. Role of calcineurin and protein phosphatase-2A in the regulation of DARPP-32 dephosphorylation in neostriatal neurons. J Neurochem 72: 2015-2021 (1999).
    • (1999) J Neurochem , vol.72 , pp. 2015-2021
    • Nishi, A.1    Snyder, G.L.2    Nairn, A.C.3    Greengard, P.4
  • 46
    • 0021112202 scopus 로고
    • Characterization of a phosphotyrosyl protein phosphatase activity associated with a phosphoseryl protein phosphatase of Mr = 95,000 from bovine heart
    • Chernoff J, Li HC, Cheng YSE, Chen LB. Characterization of a phosphotyrosyl protein phosphatase activity associated with a phosphoseryl protein phosphatase of Mr = 95,000 from bovine heart. J Biol Chem 258: 7852-7857 (1983).
    • (1983) J Biol Chem , vol.258 , pp. 7852-7857
    • Chernoff, J.1    Li, H.C.2    Cheng, Y.S.E.3    Chen, L.B.4
  • 47
    • 0021154718 scopus 로고
    • Isolation and characterization of rabbit skeletal muscle protein phosphatases C-I and C-II
    • Silberman SR, Speth M, Nemani R, Ganapathi MK, Dombradi V, Paris H, et al. Isolation and characterization of rabbit skeletal muscle protein phosphatases C-I and C-II. J Biol Chem 259: 2913-2922 (1984).
    • (1984) J Biol Chem , vol.259 , pp. 2913-2922
    • Silberman, S.R.1    Speth, M.2    Nemani, R.3    Ganapathi, M.K.4    Dombradi, V.5    Paris, H.6
  • 48
    • 0024278373 scopus 로고
    • Polycationstimulated (PCSL) protein phosphatase from Xenopus laevis oocytes. ATP-mediated regulation of alkaline phosphatase activity
    • Hermann J, Cayla X, Dumortier K, Goris J, Ozon R, Merlevede W. Polycationstimulated (PCSL) protein phosphatase from Xenopus laevis oocytes. ATP-mediated regulation of alkaline phosphatase activity. Eur J Biochem 173: 17-25 (1988).
    • (1988) Eur J Biochem , vol.173 , pp. 17-25
    • Hermann, J.1    Cayla, X.2    Dumortier, K.3    Goris, J.4    Ozon, R.5    Merlevede, W.6
  • 50
    • 0024521319 scopus 로고
    • Tubulin and MAP2 regulate the PCSL phosphatase activity. A possible new role for microtubular proteins
    • Jessus C, Goris J, Cayla X, Hermann J, Hendrix P, Ozon R, et al. Tubulin and MAP2 regulate the PCSL phosphatase activity. A possible new role for microtubular proteins. Eur J Biochem 180: 15-22 (1989).
    • (1989) Eur J Biochem , vol.180 , pp. 15-22
    • Jessus, C.1    Goris, J.2    Cayla, X.3    Hermann, J.4    Hendrix, P.5    Ozon, R.6
  • 51
    • 0025169811 scopus 로고
    • Isolation and characterization of a tyrosyl phosphatase activator from rabbit skeletal muscle and Xenopus laevis oocytes
    • Cayla X, Goris J, Hermann J, Hendrix P, Ozon R, Merlevede W. Isolation and characterization of a tyrosyl phosphatase activator from rabbit skeletal muscle and Xenopus laevis oocytes. Biochemistry 29: 658-667 (1990).
    • (1990) Biochemistry , vol.29 , pp. 658-667
    • Cayla, X.1    Goris, J.2    Hermann, J.3    Hendrix, P.4    Ozon, R.5    Merlevede, W.6
  • 52
    • 0028575812 scopus 로고
    • The phosphotyrosyl phosphatase activator of protein phosphatase 2A. A novel purification method, immunological and enzymic characterization
    • Van Hoof C, Cayla X, Bosch M, Merlevede W, Goris J. The phosphotyrosyl phosphatase activator of protein phosphatase 2A. A novel purification method, immunological and enzymic characterization. Eur J Biochem 226: 899-907 (1994).
    • (1994) Eur J Biochem , vol.226 , pp. 899-907
    • van Hoof, C.1    Cayla, X.2    Bosch, M.3    Merlevede, W.4    Goris, J.5
  • 53
    • 0032530960 scopus 로고    scopus 로고
    • Functional analysis of conserved domains in the phosphotyrosyl phosphatase activator. Molecular cloning of the homologues from Drosophila melanogaster and Saccharomyces cerevisiae
    • Van Hoof C, Janssens V, Dinishiotu A, Merlevede W, Goris J. Functional analysis of conserved domains in the phosphotyrosyl phosphatase activator. Molecular cloning of the homologues from Drosophila melanogaster and Saccharomyces cerevisiae. Biochemistry 37: 12899-12908 (1998).
    • (1998) Biochemistry , vol.37 , pp. 12899-12908
    • van Hoof, C.1    Janssens, V.2    Dinishiotu, A.3    Merlevede, W.4    Goris, J.5
  • 55
    • 0028358381 scopus 로고
    • Molecular cloning, expression, and characterization of PTPA, a protein that activates the tyrosyl phosphatase activity of protein phosphatase 2A
    • Cayla X, Van Hoof C, Bosch M, Waelkens E, Vandekerckhove J, Peeters B, et al. Molecular cloning, expression, and characterization of PTPA, a protein that activates the tyrosyl phosphatase activity of protein phosphatase 2A. J Biol Chem 269: 15668-15675 (1994).
    • (1994) J Biol Chem , vol.269 , pp. 15668-15675
    • Cayla, X.1    van Hoof, C.2    Bosch, M.3    Waelkens, E.4    Vandekerckhove, J.5    Peeters, B.6
  • 56
    • 33746408988 scopus 로고    scopus 로고
    • Crystal structure of the PP2A phosphatase activator: Implications for its PP2A-specific PPIase activity
    • Leulliot N, Vicentini G, Jordens J, Quevillon-Cheruel S, Schiltz M, Barford D, et al. Crystal structure of the PP2A phosphatase activator: implications for its PP2A-specific PPIase activity. Mol Cell 23: 413-424. (2006).
    • (2006) Mol Cell , vol.23 , pp. 413-424
    • Leulliot, N.1    Vicentini, G.2    Jordens, J.3    Quevillon-Cheruel, S.4    Schiltz, M.5    Barford, D.6
  • 57
    • 27644478606 scopus 로고    scopus 로고
    • Contributions of protein phosphatases PP1, PP2A, PP2B and PP5 to the regulation of tau phosphorylation
    • Liu F, Grundke-Iqbal I, Iqbal K, Gong CX. Contributions of protein phosphatases PP1, PP2A, PP2B and PP5 to the regulation of tau phosphorylation. Eur J Neurosci 22: 1942 (2005).
    • (2005) Eur J Neurosci , vol.22 , pp. 1942
    • Liu, F.1    Grundke-Iqbal, I.2    Iqbal, K.3    Gong, C.X.4
  • 58
    • 0034680902 scopus 로고    scopus 로고
    • 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 CX, Grundke-Iqbal I, Iqbal K. Role of protein phosphatase-2A and -1 in the regulation of GSK-3, cdk5 and cdc2 and the phosphorylation of Tau in rat forebrain. FEBS Lett 485: 87-93 (2000).
    • (2000) FEBS Lett , vol.485 , pp. 87-93
    • Bennecib, M.1    Gong, C.X.2    Grundke-Iqbal, I.3    Iqbal, K.4
  • 59
    • 0033986391 scopus 로고    scopus 로고
    • Regulation of phosphorylation of neuronal microtubuleassociated proteins MAP1b and MAP2 by protein phosphatase-2A and -2B in rat brain
    • Gong CX, Wegiel J, Lidsky T, Zuck L, Avila J, Wisniewski HM, et al. Regulation of phosphorylation of neuronal microtubuleassociated proteins MAP1b and MAP2 by protein phosphatase-2A and -2B in rat brain. Brain Res 853: 299-309 (2000).
    • (2000) Brain Res , vol.853 , pp. 299-309
    • Gong, C.X.1    Wegiel, J.2    Lidsky, T.3    Zuck, L.4    Avila, J.5    Wisniewski, H.M.6
  • 60
    • 0035851175 scopus 로고    scopus 로고
    • Reduced protein phosphatase 2A activity induces hyperphosphorylation and altered compartmentalization of Tau in transgenic mice
    • Kins S, Crameri A, Evans DR, Hemmings BA, Nitsch RM, Gotz J. Reduced protein phosphatase 2A activity induces hyperphosphorylation and altered compartmentalization of Tau in transgenic mice. J Biol Chem 276: 38193-38200 (2001).
    • (2001) J Biol Chem , vol.276 , pp. 38193-38200
    • Kins, S.1    Crameri, A.2    Evans, D.R.3    Hemmings, B.A.4    Nitsch, R.M.5    Gotz, J.6
  • 61
    • 0029925968 scopus 로고    scopus 로고
    • Site-specific regulation of alzheimer-like Tau phosphorylation in living neurons
    • Burack MA, Halpain S. Site-specific regulation of alzheimer-like Tau phosphorylation in living neurons. Neuroscience 72 167-184 (1996).
    • (1996) Neuroscience , vol.72 , pp. 167-184
    • Burack, M.A.1    Halpain, S.2
  • 62
    • 33747401659 scopus 로고    scopus 로고
    • Tau phosphorylation and proteolysis: Insights and perspectives
    • Johnson GV. Tau phosphorylation and proteolysis: insights and perspectives. J Alzheimers Dis 9: 243-250 (2006).
    • (2006) J Alzheimers Dis , vol.9 , pp. 243-250
    • Johnson, G.V.1
  • 64
    • 0031741247 scopus 로고    scopus 로고
    • New phosphorylation sites identified in hyperphosphorylated Tau (paired helical filament-Tau) from Alzheimer's disease brain using nanoelectrospray mass spectrometry
    • Hanger DP, Betts JC, Loviny TL, Blackstock WP, Anderton BH. New phosphorylation sites identified in hyperphosphorylated Tau (paired helical filament-Tau) from Alzheimer's disease brain using nanoelectrospray mass spectrometry. J Neurochem 71: 2465-2476 (1998).
    • (1998) J Neurochem , vol.71 , pp. 2465-2476
    • Hanger, D.P.1    Betts, J.C.2    Loviny, T.L.3    Blackstock, W.P.4    Anderton, B.H.5
  • 65
    • 0033302735 scopus 로고    scopus 로고
    • Tau protein in normal and Alzheimer's disease brain: An update
    • Johnson GV, Hartigan JA. Tau protein in normal and Alzheimer's disease brain: an update. J Alzheimers Dis 1: 329-351(1999).
    • (1999) J Alzheimers Dis , vol.1 , pp. 329-351
    • Johnson, G.V.1    Hartigan, J.A.2
  • 66
    • 0028220180 scopus 로고
    • Comparison of the phosphorylation of microtubule-associated protein Tau by nonproline dependent protein kinases
    • Singh TJ, Grundke-Iqbal I, McDonald B, Iqbal K. Comparison of the phosphorylation of microtubule-associated protein Tau by nonproline dependent protein kinases. Mol Cell Biochem 131:181-189 (1994).
    • (1994) Mol Cell Biochem , vol.131 , pp. 181-189
    • Singh, T.J.1    Grundke-Iqbal, I.2    McDonald, B.3    Iqbal, K.4
  • 67
    • 0035863188 scopus 로고    scopus 로고
    • Decreased nuclear beta-catenin, Tau hyperphosphorylation and neurodegeneration in GSK-3beta conditional transgenic mice
    • Lucas JJ, Hernandez F, Gomez-Ramos P, Moran MA, Hen R, Avila J. Decreased nuclear beta-catenin, Tau hyperphosphorylation and neurodegeneration in GSK-3beta conditional transgenic mice. EMBO J. 20:27-39 (2001).
    • (2001) EMBO J , vol.20 , pp. 27-39
    • Lucas, J.J.1    Hernandez, F.2    Gomez-Ramos, P.3    Moran, M.A.4    Hen, R.5    Avila, J.6
  • 69
    • 0032850599 scopus 로고    scopus 로고
    • Distribution of active glycogen synthase kinase 3beta (GSK-3beta) in brains staged for Alzheimer disease neurofibrillary changes
    • Pei JJ, Braak E, Braak H, Grunke-Iqbal I, Iqbal K, Winblad B et al. Distribution of active glycogen synthase kinase 3beta (GSK-3beta) in brains staged for Alzheimer disease neurofibrillary changes. J Neuropathol Exp Neurol. 58:1010-1019 (1999).
    • (1999) J Neuropathol Exp Neurol , vol.58 , pp. 1010-1019
    • Pei, J.J.1    Braak, E.2    Braak, H.3    Grunke-Iqbal, I.4    Iqbal, K.5    Winblad, B.6
  • 70
    • 0032578024 scopus 로고    scopus 로고
    • Accumulation of cyclin-dependent kinase 5 (cdk5) in neurons with early stages of Alzheimer's disease neurofibrillary degeneration
    • Pei JJ, Grundke-Iqbal I, Iqbal K, Boqdanovic N, Winblad B, Cowburn RF. Accumulation of cyclin-dependent kinase 5 (cdk5) in neurons with early stages of Alzheimer's disease neurofibrillary degeneration. Brain Res. 797:267-277 (1998).
    • (1998) Brain Res , vol.797 , pp. 267-277
    • Pei, J.J.1    Grundke-Iqbal, I.2    Iqbal, K.3    Boqdanovic, N.4    Winblad, B.5    Cowburn, R.F.6
  • 71
    • 0038689162 scopus 로고    scopus 로고
    • Cdk5 is a key factor in Tau aggregation and tangle formation in vivo
    • Noble W, Olm V, Takata K, Casey E, Marry O, Meyerson J, et al. Cdk5 is a key factor in Tau aggregation and tangle formation in vivo. Neuron 38:555-565 (2003).
    • (2003) Neuron , vol.38 , pp. 555-565
    • Noble, W.1    Olm, V.2    Takata, K.3    Casey, E.4    Marry, O.5    Meyerson, J.6
  • 72
    • 0034595834 scopus 로고    scopus 로고
    • Calpain-dependent proteolytic cleavage of the p35 cyclindependent kinase 5 activator to p25
    • Kusakawa G, Saito T, Onuki R, Ishiquro K, Kishimoto T, Hisanage S. Calpain-dependent proteolytic cleavage of the p35 cyclindependent kinase 5 activator to p25. J Biol Chem. 275:17166-17172 (2000).
    • (2000) J Biol Chem , vol.275 , pp. 17166-17172
    • Kusakawa, G.1    Saito, T.2    Onuki, R.3    Ishiquro, K.4    Kishimoto, T.5    Hisanage, S.6
  • 73
    • 0345405447 scopus 로고    scopus 로고
    • Aberrant Cdk5 activation by p25 triggers pathological events leading to neurodegeneration and neurofibrillary tangles
    • Cruz JC, Tseng HC, Goldman JA, Shih H, Tsai LH. Aberrant Cdk5 activation by p25 triggers pathological events leading to neurodegeneration and neurofibrillary tangles. Neuron 40: 471-483 (2003).
    • (2003) Neuron , vol.40 , pp. 471-483
    • Cruz, J.C.1    Tseng, H.C.2    Goldman, J.A.3    Shih, H.4    Tsai, L.H.5
  • 74
    • 0026694067 scopus 로고
    • Implication of brain cdc2 and MAP2 kinases in the phosphorylation of Tau protein in Alzheimer's disease
    • Ledesma MD, Correas I, Avila J, Diaz-Nido J. Implication of brain cdc2 and MAP2 kinases in the phosphorylation of Tau protein in Alzheimer's disease. FEBS Lett 308: 218-224 (1992).
    • (1992) FEBS Lett , vol.308 , pp. 218-224
    • Ledesma, M.D.1    Correas, I.2    Avila, J.3    Diaz-Nido, J.4
  • 75
    • 0027181221 scopus 로고
    • Brain protein kinase PK40erk converts TAU into a PHF-like form as found in Alzheimer's disease
    • Roder HM, Eden PA, Ingram VM. Brain protein kinase PK40erk converts TAU into a PHF-like form as found in Alzheimer's disease. Biochem Biophys Res Commun 193: 639-647 (1993).
    • (1993) Biochem Biophys Res Commun , vol.193 , pp. 639-647
    • Roder, H.M.1    Eden, P.A.2    Ingram, V.M.3
  • 76
    • 0042679509 scopus 로고    scopus 로고
    • Okadaic-acid-induced inhibition of protein phosphatase 2A produces activation of mitogen-activated protein kinases ERK1/2, MEK1/2, and p70 S6, similar to that in Alzheimer's disease
    • Pei JJ, Gong CX, An WL, Winblad B, Cowburn RF, Grundke-Iqbal I, et al. Okadaic-acid-induced inhibition of protein phosphatase 2A produces activation of mitogen-activated protein kinases ERK1/2, MEK1/2, and p70 S6, similar to that in Alzheimer's disease. Am J Pathol. 163:845-858 (2003).
    • (2003) Am J Pathol , vol.163 , pp. 845-858
    • Pei, J.J.1    Gong, C.X.2    An, W.L.3    Winblad, B.4    Cowburn, R.F.5    Grundke-Iqbal, I.6
  • 77
    • 0026549985 scopus 로고
    • Mitogen activated protein (MAP) kinase transforms Tau protein into an Alzheimer-like state
    • Drewes G, Lichtenberg-Kraag B, Doring F, et al. Mitogen activated protein (MAP) kinase transforms Tau protein into an Alzheimer- like state. EMBO J. 11:2131-2138 (1992).
    • (1992) EMBO J , vol.11 , pp. 2131-2138
    • Drewes, G.1    Lichtenberg-Kraag, B.2    Doring, F.3
  • 78
    • 0041343303 scopus 로고    scopus 로고
    • Up-regulation of phosphorylated/activated p70 S6 kinase and its relationship to neurofibrillary pathology in Alzheimer's disease
    • An WL, Cowburn RF, Li L, Alafuzzoff I, Iqbal K, Iqbal IG, et al. Up-regulation of phosphorylated/activated p70 S6 kinase and its relationship to neurofibrillary pathology in Alzheimer's disease. Am J Pathol. 163:591-607 (2003).
    • (2003) Am J Pathol , vol.163 , pp. 591-607
    • An, W.L.1    Cowburn, R.F.2    Li, L.3    Alafuzzoff, I.4    Iqbal, K.5    Iqbal, I.G.6
  • 79
    • 0029888525 scopus 로고    scopus 로고
    • Calcium/calmodulin-dependent protein kinase II phosphorylates Tau at Ser-262 but only partially inhibits its binding to microtubules
    • Singh TJ, Wang JZ, Novak M, Kontzekova E, Grunde-Iqbal I, Iqbal K. Calcium/calmodulin-dependent protein kinase II phosphorylates Tau at Ser-262 but only partially inhibits its binding to microtubules. FEBS Lett. 387:145-148 (1996).
    • (1996) FEBS Lett , vol.387 , pp. 145-148
    • Singh, T.J.1    Wang, J.Z.2    Novak, M.3    Kontzekova, E.4    Grunde-Iqbal, I.5    Iqbal, K.6
  • 80
    • 0027508998 scopus 로고
    • Phosphorylation of recombinant Tau by cAMPdependent protein kinase Identification of phosphorylation sites and effect on microtubule assembly
    • Scott CW, Spreen RC, Herman JL, Chow FP, Davison MD, Young J, et al. Phosphorylation of recombinant Tau by cAMPdependent protein kinase Identification of phosphorylation sites and effect on microtubule assembly. J Biol Chem. 268:1166-1173 (1993).
    • (1993) J Biol Chem , vol.268 , pp. 1166-1173
    • Scott, C.W.1    Spreen, R.C.2    Herman, J.L.3    Chow, F.P.4    Davison, M.D.5    Young, J.6
  • 81
    • 0032159462 scopus 로고    scopus 로고
    • Physiologic importance of protein phosphatase inhibitors
    • Oliver CJ, Shenolikar S. Physiologic importance of protein phosphatase inhibitors, Front Biosci 3: 961-972 (1998).
    • (1998) Front Biosci , vol.3 , pp. 961-972
    • Oliver, C.J.1    Shenolikar, S.2
  • 82
    • 0033520355 scopus 로고    scopus 로고
    • Molecular interactions among protein phosphatase 2A, tau, and microtubules: Implications for the regulation of tau phosphorylation and the development of tauopathies
    • Sontag E, Nunbhakdi-Craig V, Lee G, Brandt R, Kamibayashi C, Kuret J, et al. Molecular interactions among protein phosphatase 2A, tau, and microtubules: Implications for the regulation of tau phosphorylation and the development of tauopathies. J Biol Chem 274: 25490-25498 (1999).
    • (1999) J Biol Chem , vol.274 , pp. 25490-25498
    • Sontag, E.1    Nunbhakdi-Craig, V.2    Lee, G.3    Brandt, R.4    Kamibayashi, C.5    Kuret, J.6
  • 83
    • 0035823496 scopus 로고    scopus 로고
    • Inhibition of protein phosphatase 2A overrides Tau protein kinase I/glycogen synthase kinase 3β and cyclindependent kinase 5 inhibition and results in tau hyperphosphorylation in the hippocampus of starved mouse
    • Planel E, Yasutake K, Fujita SC, Ishiguro K. Inhibition of protein phosphatase 2A overrides Tau protein kinase I/glycogen synthase kinase 3β and cyclindependent kinase 5 inhibition and results in tau hyperphosphorylation in the hippocampus of starved mouse. J Biol Chem 276: 34298-34306 (2001).
    • (2001) J Biol Chem , vol.276 , pp. 34298-34306
    • Planel, E.1    Yasutake, K.2    Fujita, S.C.3    Ishiguro, K.4
  • 84
    • 2442465965 scopus 로고    scopus 로고
    • Memantine inhibits and reverses the Alzheimer type abnormal hyperphosphorylation of Tau and associated neurodegeneration
    • Li L, Sengupta A, Haque N, Grundke-Iqbal I, Iqbal K. Memantine inhibits and reverses the Alzheimer type abnormal hyperphosphorylation of Tau and associated neurodegeneration. FEBS Lett 566: 261-269 (2004).
    • (2004) FEBS Lett , vol.566 , pp. 261-269
    • Li, L.1    Sengupta, A.2    Haque, N.3    Grundke-Iqbal, I.4    Iqbal, K.5
  • 85
    • 0025514319 scopus 로고
    • Transfected rat high-molecular-weight neurofilament (NF-H) coassembles with vimentin in a predominantly nonphosphorylated form
    • Chin SS, Liem RK. Transfected rat high-molecular-weight neurofilament (NF-H) coassembles with vimentin in a predominantly nonphosphorylated form. J Neurosci 10: 3714-3726 (1990).
    • (1990) J Neurosci , vol.10 , pp. 3714-3726
    • Chin, S.S.1    Liem, R.K.2
  • 86
    • 0025943790 scopus 로고
    • Neurofilament phosphorylation: A new look at regulation and function
    • Nixon RA, Sihag RK. Neurofilament phosphorylation: a new look at regulation and function. Trends Neurosci 14: 501-506 (1991).
    • (1991) Trends Neurosci , vol.14 , pp. 501-506
    • Nixon, R.A.1    Sihag, R.K.2
  • 87
    • 85044014129 scopus 로고    scopus 로고
    • Grant. Regulation of axonal neurofilament phosphorylation
    • HC Pant, Veeranna, P Grant. Regulation of axonal neurofilament phosphorylation, Curr. Top. Cell Regul 36133-150 (2000).
    • (2000) Curr. Top. Cell Regul , pp. 36133-150
    • Pant, H.C.1    Veeranna, P.2
  • 88
    • 34249714850 scopus 로고    scopus 로고
    • Role of phosphorylation on the structural dynamics and function of types III and IV intermediate filaments
    • Sihag RK, M Inagaki, T Yamaguchi, TB Shea, HC Pant. Role of phosphorylation on the structural dynamics and function of types III and IV intermediate filaments. Exp Cell Res 313: 2098-2109 (2007).
    • (2007) Exp Cell Res , vol.313 , pp. 2098-2109
    • Sihag, R.K.1    Inagaki, M.2    Yamaguchi, T.3    Shea, T.B.4    Pant, H.C.5
  • 89
    • 0035075793 scopus 로고    scopus 로고
    • PP2A mRNA expression is quantitatively decreased in Alzheimer's disease hippocampus
    • Vogelsberg-Ragaglia VT, Schuck JQ, Trojanowski, VM Lee. PP2A mRNA expression is quantitatively decreased in Alzheimer's disease hippocampus. Exp Neurol 168: 402-412 (2001).
    • (2001) Exp Neurol , vol.168 , pp. 402-412
    • Vogelsberg-Ragaglia, V.T.1    Schuck, J.Q.2    Trojanowski, V.M.3    Lee4
  • 90
    • 1842510667 scopus 로고    scopus 로고
    • Altered expression levels of the protein phosphatase 2A ABalphaC enzyme are associated with Alzheimer disease pathology
    • Sontag EA, Luangpirom C, Hladik I, Mudrak E, Ogris S, Speciale, et al. Altered expression levels of the protein phosphatase 2A ABalphaC enzyme are associated with Alzheimer disease pathology. J Neuropathol Exp Neurol 63: 287-301 (2004).
    • (2004) J Neuropathol Exp Neurol , vol.63 , pp. 287-301
    • Sontag, E.A.1    Luangpirom, C.2    Hladik, I.3    Mudrak, E.4    Speciale, O.S.5
  • 91
    • 0027214404 scopus 로고
    • Phosphoprotein phosphatase activities in Alzheimer disease brain
    • Gong X, TJ Singh, I Grundke-Iqbal, K Iqbal. Phosphoprotein phosphatase activities in Alzheimer disease brain. J Neurochem 61: 921-927 (1993).
    • (1993) J Neurochem , vol.61 , pp. 921-927
    • Gong, X.1    Singh, T.J.2    Grundke-Iqbal, I.3    Iqbal, K.4
  • 92
    • 0029113874 scopus 로고
    • Phosphatase activity toward abnormally phosphorylated Tau: Decrease in Alzheimer disease brain
    • Gong CX, Shaikh S, Wang JZ, Zaidi T, Grundke-Iqbal I, Iqbal. Phosphatase activity toward abnormally phosphorylated Tau: decrease in Alzheimer disease brain. J Neurochem 65: 732-738 (1995).
    • (1995) J Neurochem , vol.65 , pp. 732-738
    • Gong, C.X.1    Shaikh, S.2    Wang, J.Z.3    Zaidi, T.4    Grundke-Iqbal, I.5
  • 93
    • 0034088846 scopus 로고    scopus 로고
    • Phosphorylation of microtubule-associated protein Tau is regulated by protein phosphatase 2A in mammalian brain. Implications for neurofibrillary degeneration in Alzheimer's disease
    • Gong CX, T Lidsky, J Wegiel, L Zuck, I Grundke-Iqbal, K Iqbal. Phosphorylation of microtubule-associated protein Tau is regulated by protein phosphatase 2A in mammalian brain. Implications for neurofibrillary degeneration in Alzheimer's disease. J Biol Chem 275: 5535-5544 (2000).
    • (2000) J Biol Chem , vol.275 , pp. 5535-5544
    • Gong, C.X.1    Lidsky, T.2    Wegiel, J.3    Zuck, L.4    Grundke-Iqbal, I.5    Iqbal, K.6
  • 94
    • 0026276683 scopus 로고
    • The regulation and function of protein phosphatases in the brain
    • Sim ATR. The regulation and function of protein phosphatases in the brain. Mol Neurobiol 5: 229-246 (1991).
    • (1991) Mol Neurobiol , vol.5 , pp. 229-246
    • Sim, A.T.R.1
  • 95
    • 0026056514 scopus 로고
    • Effect of chronic ethanol ingestion on phosphate content of NF proteins and NF associated protein phosphatase in rat spinal cord
    • Guru SC, Shetty KT, Shankar SK. Effect of chronic ethanol ingestion on phosphate content of NF proteins and NF associated protein phosphatase in rat spinal cord. Neurochem Res 16: 1193-1197 (1991).
    • (1991) Neurochem Res , vol.16 , pp. 1193-1197
    • Guru, S.C.1    Shetty, K.T.2    Shankar, S.K.3
  • 96
    • 0026529602 scopus 로고
    • Effect of chronic ethanol ingestion on phosphate content of neurofilament proteins and neurofilament associated protein phosphatase in rat spinal cord
    • Shetty KT, Veeranna, Guru SC. Effect of chronic ethanol ingestion on phosphate content of neurofilament proteins and neurofilament associated protein phosphatase in rat spinal cord. Neurosci Lett 137: 83-86 (1992).
    • (1992) Neurosci Lett , vol.137 , pp. 83-86
    • Shetty, K.T.1    Veeranna, G.S.C.2
  • 97
    • 0023148301 scopus 로고
    • Posttranslational modification of neurofilament proteins by phosphate during axoplasmic transport in retinal ganglion cell neurons
    • Nixon RA, Lewis SE, Marotta CA. Posttranslational modification of neurofilament proteins by phosphate during axoplasmic transport in retinal ganglion cell neurons. J Neurosci 7: 1145-1158 (1987).
    • (1987) J Neurosci , vol.7 , pp. 1145-1158
    • Nixon, R.A.1    Lewis, S.E.2    Marotta, C.A.3
  • 98
    • 0026580004 scopus 로고
    • Local modulation of neurofilament phosphorylation, axonal caliber and slow axonal transport by mylenating Schwann cells
    • De Waegh SM, Lee VM, Brady ST. Local modulation of neurofilament phosphorylation, axonal caliber and slow axonal transport by mylenating Schwann cells. Cell 68: 451-463 (1992).
    • (1992) Cell , vol.68 , pp. 451-463
    • de Waegh, S.M.1    Lee, V.M.2    Brady, S.T.3
  • 99
    • 0026529403 scopus 로고
    • Phosphorylation dependent neurofilament epitopes are reduced at the node of Ranvier
    • Mata M, Kupina N, Fink DJ. Phosphorylation dependent neurofilament epitopes are reduced at the node of Ranvier. J Neurocytol 21: 199-210 (1992).
    • (1992) J Neurocytol , vol.21 , pp. 199-210
    • Mata, M.1    Kupina, N.2    Fink, D.J.3
  • 100
    • 0029022205 scopus 로고
    • Neuronal cyclin-dependent kinase-5 phosphorylation sites in neurofilament protein (NF-H) are dephosphorylated by protein phosphatase 2A
    • Veeranna, Shetty KT, Link WT, Jaffe H, Wang J, Pant HC. Neuronal cyclin-dependent kinase-5 phosphorylation sites in neurofilament protein (NF-H) are dephosphorylated by protein phosphatase 2A. J Neurochem 64: 2681-2690 (1995).
    • (1995) J Neurochem , vol.64 , pp. 2681-2690
    • Veeranna, S.K.T.1    Link, W.T.2    Jaffe, H.3    Wang, J.4    Pant, H.C.5
  • 101
    • 0036316279 scopus 로고    scopus 로고
    • Myelin-associated glycoprotein modulates expression and phosphorylation of neuronal cytoskeletal elements and their associated kinases
    • Dashiell SM, Tanner SL, Pant HC, Quarles RH. Myelin-associated glycoprotein modulates expression and phosphorylation of neuronal cytoskeletal elements and their associated kinases. J Neurochem 81: 1263-1272 (2002).
    • (2002) J Neurochem , vol.81 , pp. 1263-1272
    • Dashiell, S.M.1    Tanner, S.L.2    Pant, H.C.3    Quarles, R.H.4
  • 102
    • 0035075793 scopus 로고    scopus 로고
    • PP2A mRNA expression is quantitatively decreased in Alzheimer's disease hippocampus
    • Vogelsberg-Ragaglia V, Schuck T, Trojanowski JQ, Lee VM. PP2A mRNA expression is quantitatively decreased in Alzheimer's disease hippocampus. Exp Neurol 168: 402-412 (2001).
    • (2001) Exp Neurol , vol.168 , pp. 402-412
    • Vogelsberg-Ragaglia, V.1    Schuck, T.2    Trojanowski, J.Q.3    Lee, V.M.4
  • 104
    • 0023931776 scopus 로고
    • Identification and quantification of calcium-binding proteins in squid axoplasm
    • Krinks MH, Klee CB, Pant HC, Gainer H. Identification and quantification of calcium-binding proteins in squid axoplasm. J Neurosci 8: 2172-2182 (1988).
    • (1988) J Neurosci , vol.8 , pp. 2172-2182
    • Krinks, M.H.1    Klee, C.B.2    Pant, H.C.3    Gainer, H.4
  • 105
    • 27644478606 scopus 로고    scopus 로고
    • Contributions of protein phosphatases PP1, PP2A, PP2B and PP5 to the regulation of Tau phosphorylation
    • Liu F, Grundke-Iqbal I, Iqbal K, Gong CX. Contributions of protein phosphatases PP1, PP2A, PP2B and PP5 to the regulation of Tau phosphorylation. Eur J Neurosci 22: 1942-1950 (2005).
    • (2005) Eur J Neurosci , vol.22 , pp. 1942-1950
    • Liu, F.1    Grundke-Iqbal, I.2    Iqbal, K.3    Gong, C.X.4
  • 106
    • 79958815089 scopus 로고    scopus 로고
    • Declining phosphatases underlie aging-related hyperphosphorylation of neurofilaments
    • ] Veeranna, Yang DS, Lee JH, Vinod KY, Stavrides P, Amin ND, et al. Declining phosphatases underlie aging-related hyperphosphorylation of neurofilaments. Neurobiol Aging 109 (2009).
    • (2009) Neurobiol Aging , pp. 109
    • Veeranna, Y.D.S.1    Lee, J.H.2    Vinod, K.Y.3    Stavrides, P.4    Amin, N.D.5
  • 107
    • 19544362550 scopus 로고    scopus 로고
    • Up-regulation of inhibitors of protein phosphatase-2A in Alzheimer's disease
    • Tanimukai H, Grundke-Iqbal I, Iqbal, K. Up-regulation of inhibitors of protein phosphatase-2A in Alzheimer's disease. Am J Pathol 166: 1761-1771 (2005).
    • (2005) Am J Pathol , vol.166 , pp. 1761-1771
    • Tanimukai, H.1    Grundke-Iqbal, I.2    Iqbal, K.3
  • 108
    • 80051706942 scopus 로고    scopus 로고
    • Novel mechanism where ApoE mimetics activate PP2A activity and reduce Alzheimer's pathology in three different transgenic models
    • Vitek MP, Christensen DJ, Wilcock D, Oddo J, Gharkholonarehe N, Ohkubo, et al. Novel mechanism where ApoE mimetics activate PP2A activity and reduce Alzheimer's pathology in three different transgenic models. Alzheimer's Demen.: J Alzheimer's Assoc 5 P111 (2009).
    • (2009) Alzheimer's Demen.: J Alzheimer's Assoc , vol.5
    • Vitek, M.P.1    Christensen, D.J.2    Wilcock, D.3    Oddo, J.4    Ohkubo, G.N.5
  • 109
    • 35448945269 scopus 로고    scopus 로고
    • The prolyl isomerase PIN1: A pivotal new twist in phosphorylation signaling and disease
    • Lu KP, Zhou XZ. The prolyl isomerase PIN1: a pivotal new twist in phosphorylation signaling and disease. Nat Rev Mol Cell Biol 8: 904-916 (2007).
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 904-916
    • Lu, K.P.1    Zhou, X.Z.2
  • 110
    • 0031438929 scopus 로고    scopus 로고
    • Sequence-specific and phosphorylationdependent proline isomerization: A potential mitotic regulatory mechanism
    • Yaffe MB, Schutkowski M, Shen M, Zhou XZ, Stukenberg PT, Rahfeld JU, et al. Sequence-specific and phosphorylationdependent proline isomerization: a potential mitotic regulatory mechanism. Science 278: 1957-1960 (1997).
    • (1997) Science , vol.278 , pp. 1957-1960
    • Yaffe, M.B.1    Schutkowski, M.2    Shen, M.3    Zhou, X.Z.4    Stukenberg, P.T.5    Rahfeld, J.U.6
  • 111
    • 55549124552 scopus 로고    scopus 로고
    • Pin1dependent prolyl isomerization modulates the stressinduced phosphorylation of high molecular weight neurofilament protein
    • Rudrabhatla P, Zheng YL, Amin ND, Kesavapany S, Albers W, Pant HC. Pin1dependent prolyl isomerization modulates the stressinduced phosphorylation of high molecular weight neurofilament protein. J Biol Chem 283: 26737-26747 (2008).
    • (2008) J Biol Chem , vol.283 , pp. 26737-26747
    • Rudrabhatla, P.1    Zheng, Y.L.2    Amin, N.D.3    Kesavapany, S.4    Albers, W.5    Pant, H.C.6
  • 112
    • 34548490722 scopus 로고    scopus 로고
    • Inhibition of Pin1 reduces glutamate-induced perikaryal accumulation of phosphorylated neurofilament-H in neurons
    • Kesavapany S, Patel V, Zheng YL, Pareek TK, Bjelogrlic M, Albers W, et al. Inhibition of Pin1 reduces glutamate-induced perikaryal accumulation of phosphorylated neurofilament-H in neurons. Mol Biol Cell 18: 3645-3655 (2007).
    • (2007) Mol Biol Cell , vol.18 , pp. 3645-3655
    • Kesavapany, S.1    Patel, V.2    Zheng, Y.L.3    Pareek, T.K.4    Bjelogrlic, M.5    Albers, W.6
  • 113
    • 80051722674 scopus 로고    scopus 로고
    • Pin1: A new outlook in Alzheimer Disease. Current Alzheimeŕs Research. Special thematic Issue Tau protein and Alzheimeŕs disease. New paradigms and future challenges
    • (2011)
    • Lonati E, Masserini M, Bulbarelli A. (2011) Pin1: a new outlook in Alzheimer Disease. Current Alzheimeŕs Research. Special thematic Issue Tau protein and Alzheimeŕs disease. New paradigms and future challenges Curr Alzheimers Res 8(6): 615-622 (2011).
    • (2011) Curr Alzheimers Res , vol.8 , Issue.6 , pp. 615-622
    • Lonati, E.1    Masserini, M.2    Bulbarelli, A.3
  • 114
    • 33645238274 scopus 로고    scopus 로고
    • The prolyl-isomerase Pin1 accumulates in the Lewy bodies of Parkinson's disease and facilitates the formation of alpha-synuclein inclusions
    • Ryo A, Togo T, Nakai T, Hirai A, Nishi M, Yamaguchi A, et al. The prolyl-isomerase Pin1 accumulates in the Lewy bodies of Parkinson's disease and facilitates the formation of alpha-synuclein inclusions. J Biol Chem 281: 4117-4125 (2006).
    • (2006) J Biol Chem , vol.281 , pp. 4117-4125
    • Ryo, A.1    Togo, T.2    Nakai, T.3    Hirai, A.4    Nishi, M.5    Yamaguchi, A.6
  • 115
    • 0033600242 scopus 로고    scopus 로고
    • The prolyl isomerase Pin1 restores the function of Alzheimer-associated phosphorylated Tau protein
    • Lu PJ, Wulf G, Zhou XZ, Davies P, Lu KP. The prolyl isomerase Pin1 restores the function of Alzheimer-associated phosphorylated Tau protein. Nature 399: 784-788 (1999).
    • (1999) Nature , vol.399 , pp. 784-788
    • Lu, P.J.1    Wulf, G.2    Zhou, X.Z.3    Davies, P.4    Lu, K.P.5
  • 116
    • 0037022355 scopus 로고    scopus 로고
    • Role of the prolyl isomerase Pin1 in protecting against agedependent neurodegeneration
    • Liou YC, Ryo A, Huang HK, Lu PJ, Bronson R, Fujimori F, et al. Role of the prolyl isomerase Pin1 in protecting against agedependent neurodegeneration. Proc Natl Acad Sci USA 99: 1335-1340 (2002).
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 1335-1340
    • Liou, Y.C.1    Ryo, A.2    Huang, H.K.3    Lu, P.J.4    Bronson, R.5    Fujimori, F.6
  • 117
    • 43049143027 scopus 로고    scopus 로고
    • Pin1 has opposite effects on wild-type and P301L Tau stability and Tauopathy
    • Lim J, Balastik M, Lee TH, Nakamura K, Liou YC, Sun A, et al. Pin1 has opposite effects on wild-type and P301L Tau stability and Tauopathy. J Clin Invest 118: 1877-1889 (2008).
    • (2008) J Clin Invest , vol.118 , pp. 1877-1889
    • Lim, J.1    Balastik, M.2    Lee, T.H.3    Nakamura, K.4    Liou, Y.C.5    Sun, A.6
  • 118
    • 0034426011 scopus 로고    scopus 로고
    • Neurofibrillary tangles, amyotrophy and progressive motor disturbance in mice expressing mutant (P301L) Tau protein
    • Lewis J, McGowan E, Rockwood J, Melrose H, Nacharaju P, Slegtenhorst MV, et al. Neurofibrillary tangles, amyotrophy and progressive motor disturbance in mice expressing mutant (P301L) Tau protein. Nat Genet 25: 402-405 (2000).
    • (2000) Nat Genet , vol.25 , pp. 402-405
    • Lewis, J.1    McGowan, E.2    Rockwood, J.3    Melrose, H.4    Nacharaju, P.5    Slegtenhorst, M.V.6
  • 119
    • 17944382037 scopus 로고    scopus 로고
    • Enhanced neurofibrillary degeneration in transgenic mice expressing mutant Tau and APP
    • Lewis J, Dickson DW, Lin WL, Chisholm L, Corral A, Jones G, et al. Enhanced neurofibrillary degeneration in transgenic mice expressing mutant Tau and APP. Science 293: 1487-1491 (2001).
    • (2001) Science , vol.293 , pp. 1487-1491
    • Lewis, J.1    Dickson, D.W.2    Lin, W.L.3    Chisholm, L.4    Corral, A.5    Jones, G.6
  • 120
    • 0344011538 scopus 로고    scopus 로고
    • Pin1 modulates the structure and function of human RNA polymerase II
    • Xu YX, Hirose Y, Zhou XZ, Lu KP, Manley JL. Pin1 modulates the structure and function of human RNA polymerase II. Genes Dev 17: 2765-2776 (2003).
    • (2003) Genes Dev , vol.17 , pp. 2765-2776
    • Xu, Y.X.1    Hirose, Y.2    Zhou, X.Z.3    Lu, K.P.4    Manley, J.L.5
  • 121
    • 0037146905 scopus 로고    scopus 로고
    • Neuroprotection by memantine against neurodegeneration induced by betaamyloid(1-40)
    • Miguel-Hidalgo JJ, Alvarez XA, Cacabelos R, Quack G. Neuroprotection by memantine against neurodegeneration induced by betaamyloid(1-40). Brain Res 958: 210-221 (2002).
    • (2002) Brain Res , vol.958 , pp. 210-221
    • Miguel-Hidalgo, J.J.1    Alvarez, X.A.2    Cacabelos, R.3    Quack, G.4
  • 122
    • 33745370049 scopus 로고    scopus 로고
    • Involvement of I2PP2A in the abnormal hyperphosphorylation of tau and its reversal by Memantine
    • Chohan MO, Khatoon S, Grundke-Iqbal I, Iqbal K. Involvement of I2PP2A in the abnormal hyperphosphorylation of tau and its reversal by Memantine. FEBS Lett 580: 3973-3979 (2006).
    • (2006) FEBS Lett , vol.580 , pp. 3973-3979
    • Chohan, M.O.1    Khatoon, S.2    Grundke-Iqbal, I.3    Iqbal, K.4
  • 123
    • 2442465965 scopus 로고    scopus 로고
    • Memantine inhibits and reverses the Alzheimer type abnormal hyperphosphorylation of tau and associated neurodegeneration
    • Li L, Sengupta A, Haque N, Grundke-Iqbal I, Iqbal K. Memantine inhibits and reverses the Alzheimer type abnormal hyperphosphorylation of tau and associated neurodegeneration. FEBS Lett 566: 261-269 (2004).
    • (2004) FEBS Lett , vol.566 , pp. 261-269
    • Li, L.1    Sengupta, A.2    Haque, N.3    Grundke-Iqbal, I.4    Iqbal, K.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.