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Volumn 581, Issue 4, 2007, Pages 617-622

A novel monoclonal antibody DC63 reveals that inhibitor 1 of protein phosphatase 2A is preferentially nuclearly localised in human brain

Author keywords

Alzheimer's disease; Inhibitor 1 of protein phosphatase 2A; Leucine rich acidic phosphoprotein; Tau protein hyperphosphorylation

Indexed keywords

INHIBITOR 1 OF PROTEIN PHOSPHATASE 2A; INHIBITOR PROTEIN; MONOCLONAL ANTIBODY; MONOCLONAL ANTIBODY DC63; UNCLASSIFIED DRUG;

EID: 33846820241     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2007.01.015     Document Type: Article
Times cited : (10)

References (31)
  • 2
    • 0024814559 scopus 로고
    • Characterisation of the first monoclonal antibody against the pronase resistant core of the Alzheimer PHF
    • Novak M., Wischik C.M., Edwards P., Pannell R., and Milstein C. Characterisation of the first monoclonal antibody against the pronase resistant core of the Alzheimer PHF. Prog. Clin. Biol. Res. 317 (1989) 755-761
    • (1989) Prog. Clin. Biol. Res. , vol.317 , pp. 755-761
    • Novak, M.1    Wischik, C.M.2    Edwards, P.3    Pannell, R.4    Milstein, C.5
  • 3
    • 0027398169 scopus 로고
    • Molecular characterization of the minimal protease resistant tau unit of the Alzheimer's disease paired helical filament
    • Novak M., Kabat J., and Wischik C.M. Molecular characterization of the minimal protease resistant tau unit of the Alzheimer's disease paired helical filament. Embo J. 12 (1993) 365-370
    • (1993) Embo J. , vol.12 , pp. 365-370
    • Novak, M.1    Kabat, J.2    Wischik, C.M.3
  • 4
    • 14244253319 scopus 로고    scopus 로고
    • Metabolic/signal transduction hypothesis of Alzheimer's disease and other tauopathies
    • Iqbal K., and Grundke-Iqbal I. Metabolic/signal transduction hypothesis of Alzheimer's disease and other tauopathies. Acta Neuropathol. (Berl.) 109 (2005) 25-31
    • (2005) Acta Neuropathol. (Berl.) , vol.109 , pp. 25-31
    • Iqbal, K.1    Grundke-Iqbal, I.2
  • 5
    • 33745152289 scopus 로고    scopus 로고
    • Truncated tau from sporadic Alzheimer's disease suffices to drive neurofibrillary degeneration in vivo
    • Zilka N., et al. Truncated tau from sporadic Alzheimer's disease suffices to drive neurofibrillary degeneration in vivo. FEBS Lett. 580 (2006) 3582-3588
    • (2006) FEBS Lett. , vol.580 , pp. 3582-3588
    • Zilka, N.1
  • 6
    • 2942594301 scopus 로고    scopus 로고
    • Folding of Alzheimer's core PHF subunit revealed by monoclonal antibody 423
    • Skrabana R., Kontsek P., Mederlyova A., Iqbal K., and Novak M. Folding of Alzheimer's core PHF subunit revealed by monoclonal antibody 423. FEBS Lett. 568 (2004) 178-182
    • (2004) FEBS Lett. , vol.568 , pp. 178-182
    • Skrabana, R.1    Kontsek, P.2    Mederlyova, A.3    Iqbal, K.4    Novak, M.5
  • 7
    • 0037454475 scopus 로고    scopus 로고
    • DC11: a novel monoclonal antibody revealing Alzheimer's disease-specific tau epitope
    • Vechterova L., Kontsekova E., Zilka N., Ferencik M., Ravid R., and Novak M. DC11: a novel monoclonal antibody revealing Alzheimer's disease-specific tau epitope. Neuroreport 14 (2003) 87-91
    • (2003) Neuroreport , vol.14 , pp. 87-91
    • Vechterova, L.1    Kontsekova, E.2    Zilka, N.3    Ferencik, M.4    Ravid, R.5    Novak, M.6
  • 8
    • 33745140951 scopus 로고    scopus 로고
    • Tau phosphorylation and aggregation in Alzheimer's disease pathology
    • Avila J. Tau phosphorylation and aggregation in Alzheimer's disease pathology. FEBS Lett. 580 (2006) 2922-2927
    • (2006) FEBS Lett. , vol.580 , pp. 2922-2927
    • Avila, J.1
  • 9
    • 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., and Gong C.X. Contributions of protein phosphatases PP1, PP2A, PP2B and PP5 to the regulation of tau phosphorylation. Eur. J. Neurosci. 22 (2005) 1942-1950
    • (2005) Eur. J. Neurosci. , vol.22 , pp. 1942-1950
    • Liu, F.1    Grundke-Iqbal, I.2    Iqbal, K.3    Gong, C.X.4
  • 10
    • 0029113874 scopus 로고
    • Phosphatase activity toward abnormally phosphorylated tau: decrease in Alzheimer disease brain
    • Gong C.X., Shaikh S., Wang J.Z., Zaidi T., Grundke-Iqbal I., and Iqbal K. Phosphatase activity toward abnormally phosphorylated tau: decrease in Alzheimer disease brain. J. Neurochem. 65 (1995) 732-738
    • (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    Iqbal, K.6
  • 11
    • 0027214404 scopus 로고
    • Phosphoprotein phosphatase activities in Alzheimer disease brain
    • Gong C.X., Singh T.J., Grundke-Iqbal I., and Iqbal K. Phosphoprotein phosphatase activities in Alzheimer disease brain. J. Neurochem. 61 (1993) 921-927
    • (1993) J. Neurochem. , vol.61 , pp. 921-927
    • Gong, C.X.1    Singh, T.J.2    Grundke-Iqbal, I.3    Iqbal, K.4
  • 12
    • 0035075793 scopus 로고    scopus 로고
    • PP2A mRNA expression is quantitatively decreased in Alzheimer's disease hippocampus
    • Vogelsberg-Ragaglia V., Schuck T., Trojanowski J.Q., and Lee V.M. PP2A mRNA expression is quantitatively decreased in Alzheimer's disease hippocampus. Exp. Neurol. 168 (2001) 402-412
    • (2001) Exp. Neurol. , vol.168 , pp. 402-412
    • Vogelsberg-Ragaglia, V.1    Schuck, T.2    Trojanowski, J.Q.3    Lee, V.M.4
  • 13
    • 0035155854 scopus 로고    scopus 로고
    • Selective changes of calcineurin (protein phosphatase 2B) activity in Alzheimer's disease cerebral cortex
    • Lian Q., Ladner C.J., Magnuson D., and Lee J.M. Selective changes of calcineurin (protein phosphatase 2B) activity in Alzheimer's disease cerebral cortex. Exp. Neurol. 167 (2001) 158-165
    • (2001) Exp. Neurol. , vol.167 , pp. 158-165
    • Lian, Q.1    Ladner, C.J.2    Magnuson, D.3    Lee, J.M.4
  • 14
    • 0028931302 scopus 로고
    • Purification and characterization of two potent heat-stable protein inhibitors of protein phosphatase 2A from bovine kidney
    • Li M., Guo H., and Damuni Z. Purification and characterization of two potent heat-stable protein inhibitors of protein phosphatase 2A from bovine kidney. Biochemistry 34 (1995) 1988-1996
    • (1995) Biochemistry , vol.34 , pp. 1988-1996
    • Li, M.1    Guo, H.2    Damuni, Z.3
  • 15
    • 0029665228 scopus 로고    scopus 로고
    • Molecular identification of I1PP2A, a novel potent heat-stable inhibitor protein of protein phosphatase 2A
    • Li M., Makkinje A., and Damuni Z. Molecular identification of I1PP2A, a novel potent heat-stable inhibitor protein of protein phosphatase 2A. Biochemistry 35 (1996) 6998-7002
    • (1996) Biochemistry , vol.35 , pp. 6998-7002
    • Li, M.1    Makkinje, A.2    Damuni, Z.3
  • 16
    • 19544362550 scopus 로고    scopus 로고
    • Up-regulation of inhibitors of protein phosphatase-2A in Alzheimer's disease
    • Tanimukai H., Grundke-Iqbal I., and Iqbal K. Up-regulation of inhibitors of protein phosphatase-2A in Alzheimer's disease. Am. J. Pathol. 166 (2005) 1761-1771
    • (2005) Am. J. Pathol. , vol.166 , pp. 1761-1771
    • Tanimukai, H.1    Grundke-Iqbal, I.2    Iqbal, K.3
  • 17
    • 11844273281 scopus 로고    scopus 로고
    • 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 I., and 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 (2005) 363-372
    • (2005) FEBS Lett. , vol.579 , pp. 363-372
    • Tsujio, I.1    Zaidi, T.2    Xu, J.3    Kotula, L.4    Grundke-Iqbal, I.5    Iqbal, K.6
  • 19
    • 0033575254 scopus 로고    scopus 로고
    • Identification of sequences required for inhibition of oncogene-mediated transformation by pp32
    • Brody J.R., Kadkol S.S., Mahmoud M.A., Rebel J.M., and Pasternack G.R. Identification of sequences required for inhibition of oncogene-mediated transformation by pp32. J. Biol. Chem. 274 (1999) 20053-20055
    • (1999) J. Biol. Chem. , vol.274 , pp. 20053-20055
    • Brody, J.R.1    Kadkol, S.S.2    Mahmoud, M.A.3    Rebel, J.M.4    Pasternack, G.R.5
  • 20
    • 0035912064 scopus 로고    scopus 로고
    • Tumor suppression and potentiation by manipulation of pp32 expression
    • Bai J., Brody J.R., Kadkol S.S., and Pasternack G.R. Tumor suppression and potentiation by manipulation of pp32 expression. Oncogene 20 (2001) 2153-2160
    • (2001) Oncogene , vol.20 , pp. 2153-2160
    • Bai, J.1    Brody, J.R.2    Kadkol, S.S.3    Pasternack, G.R.4
  • 21
    • 0030787867 scopus 로고    scopus 로고
    • Recombinant human granzyme A binds to two putative HLA-associated proteins and cleaves one of them
    • Beresford P.J., Kam C.M., Powers J.C., and Lieberman J. Recombinant human granzyme A binds to two putative HLA-associated proteins and cleaves one of them. Proc. Natl. Acad. Sci. USA 94 (1997) 9285-9290
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 9285-9290
    • Beresford, P.J.1    Kam, C.M.2    Powers, J.C.3    Lieberman, J.4
  • 23
    • 0030925589 scopus 로고    scopus 로고
    • Mapmodulin: a possible modulator of the interaction of microtubule-associated proteins with microtubules
    • Ulitzur N., Humbert M., and Pfeffer S.R. Mapmodulin: a possible modulator of the interaction of microtubule-associated proteins with microtubules. Proc. Natl. Acad. Sci. USA 94 (1997) 5084-5089
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 5084-5089
    • Ulitzur, N.1    Humbert, M.2    Pfeffer, S.R.3
  • 24
    • 0030813618 scopus 로고    scopus 로고
    • Biochemical characterization of mapmodulin, a protein that binds microtubule-associated proteins
    • Ulitzur N., Rancano C., and Pfeffer S.R. Biochemical characterization of mapmodulin, a protein that binds microtubule-associated proteins. J. Biol. Chem. 272 (1997) 30577-30582
    • (1997) J. Biol. Chem. , vol.272 , pp. 30577-30582
    • Ulitzur, N.1    Rancano, C.2    Pfeffer, S.R.3
  • 25
    • 0032816013 scopus 로고    scopus 로고
    • Mapmodulin, cytoplasmic dynein, and microtubules enhance the transport of mannose 6-phosphate receptors from endosomes to the trans-golgi network
    • Itin C., Ulitzur N., Muhlbauer B., and Pfeffer S.R. Mapmodulin, cytoplasmic dynein, and microtubules enhance the transport of mannose 6-phosphate receptors from endosomes to the trans-golgi network. Mol. Biol. Cell 10 (1999) 2191-2197
    • (1999) Mol. Biol. Cell , vol.10 , pp. 2191-2197
    • Itin, C.1    Ulitzur, N.2    Muhlbauer, B.3    Pfeffer, S.R.4
  • 26
    • 17844367134 scopus 로고    scopus 로고
    • The Anp32 family of proteins containing leucine-rich repeats
    • Matilla A., and Radrizzani M. The Anp32 family of proteins containing leucine-rich repeats. Cerebellum 4 (2005) 7-18
    • (2005) Cerebellum , vol.4 , pp. 7-18
    • Matilla, A.1    Radrizzani, M.2
  • 27
    • 2642562952 scopus 로고    scopus 로고
    • Rapid purification of truncated tau proteins: model approach to purification of functionally active fragments of disordered proteins, implication for neurodegenerative diseases
    • Csokova N., Skrabana R., Liebig H.D., Mederlyova A., Kontsek P., and Novak M. Rapid purification of truncated tau proteins: model approach to purification of functionally active fragments of disordered proteins, implication for neurodegenerative diseases. Protein Expr. Purif. 35 (2004) 366-372
    • (2004) Protein Expr. Purif. , vol.35 , pp. 366-372
    • Csokova, N.1    Skrabana, R.2    Liebig, H.D.3    Mederlyova, A.4    Kontsek, P.5    Novak, M.6
  • 29
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 30
    • 19944375450 scopus 로고    scopus 로고
    • Tau pathology in Alzheimer disease and other tauopathies
    • Iqbal K., et al. Tau pathology in Alzheimer disease and other tauopathies. Biochim. Biophys. Acta 1739 (2005) 198-210
    • (2005) Biochim. Biophys. Acta , vol.1739 , pp. 198-210
    • Iqbal, K.1
  • 31
    • 0027968068 scopus 로고
    • CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson J.D., Higgins D.G., and Gibson T.J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22 (1994) 4673-4680
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.