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Volumn 73, Issue 5, 1999, Pages 1871-1880

Tau is modified by tissue transglutaminase in Situ: Possible functional and metabolic effects of polyamination

Author keywords

Alzheimer's disease; Calcium; Polyamines; SH SY5Y cells

Indexed keywords

CALCIUM ION; CALPAIN; MAITOTOXIN; POLYAMINE; PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE; TAU PROTEIN;

EID: 0032744527     PISSN: 00223042     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1471-4159.1999.01871.x     Document Type: Article
Times cited : (82)

References (69)
  • 1
    • 0027249085 scopus 로고
    • Rapid and transient alterations in transglutaminase activity in rat superior cervical ganglia following denervation or axotomy
    • Ando M., Kunii S., Tatematsu T., and Nagata Y. (1993) Rapid and transient alterations in transglutaminase activity in rat superior cervical ganglia following denervation or axotomy. Neurosci. Res. 17, 47-52.
    • (1993) Neurosci. Res. , vol.17 , pp. 47-52
    • Ando, M.1    Kunii, S.2    Tatematsu, T.3    Nagata, Y.4
  • 2
    • 3242861077 scopus 로고    scopus 로고
    • Localization of transglutaminase in hippocampal neurons: Implications for Alzheimer's disease
    • Appelt D. M., Kopen G. C., Boyne L. J., and Balin B. J. (1996) Localization of transglutaminase in hippocampal neurons: implications for Alzheimer's disease. J. Histochem. Cytochem. 44, 1421-1427.
    • (1996) J. Histochem. Cytochem. , vol.44 , pp. 1421-1427
    • Appelt, D.M.1    Kopen, G.C.2    Boyne, L.J.3    Balin, B.J.4
  • 3
    • 0024283029 scopus 로고
    • Covalent incorporation of polyamines as gamma-glutamyl derivatives into CHO cell protein
    • Beninati S., Piacentini M., Cocuzzi E. T., Autuori F., and Folk J. E. (1988) Covalent incorporation of polyamines as gamma-glutamyl derivatives into CHO cell protein. Biochim. Biophys. Acta 952, 325-333.
    • (1988) Biochim. Biophys. Acta , vol.952 , pp. 325-333
    • Beninati, S.1    Piacentini, M.2    Cocuzzi, E.T.3    Autuori, F.4    Folk, J.E.5
  • 5
    • 0029417023 scopus 로고
    • Apoptosis and increased generation of reactive oxygen species in Down's syndrome neurons in vitro
    • Busciglio J. and Yankner B. A. (1995) Apoptosis and increased generation of reactive oxygen species in Down's syndrome neurons in vitro. Nature 378, 776-779.
    • (1995) Nature , vol.378 , pp. 776-779
    • Busciglio, J.1    Yankner, B.A.2
  • 6
    • 0023664874 scopus 로고
    • Two types of transglutaminase in the PC12 pheochromocytoma cell line. Stimulation by sodium butyrate
    • Byrd J. C. and Lichti U. (1987) Two types of transglutaminase in the PC12 pheochromocytoma cell line. Stimulation by sodium butyrate. J. Biol. Chem. 262, 11699-11705.
    • (1987) J. Biol. Chem. , vol.262 , pp. 11699-11705
    • Byrd, J.C.A.1    Lichti, U.2
  • 7
    • 12644260802 scopus 로고    scopus 로고
    • The structural basis of monoclonal antibody Alz50's selectivity for Alzheimer's disease pathology
    • Carmel G., Mager E. M., Binder L. I., and Kuret J. (1996) The structural basis of monoclonal antibody Alz50's selectivity for Alzheimer's disease pathology. J. Biol. Chem. 271, 32789-32795.
    • (1996) J. Biol. Chem. , vol.271 , pp. 32789-32795
    • Carmel, G.1    Mager, E.M.2    Binder, L.I.3    Kuret, J.4
  • 8
    • 0031585857 scopus 로고    scopus 로고
    • Colocalization of tissue transglutaminase and stress fibers in human vascular smooth muscle cells and human umbilical vein endothelial cells
    • Chowdhury Z. A., Barsigian C., Chalupowicz G. D., Bach T. L., Garcia-Manero G., and Martinez J. (1997) Colocalization of tissue transglutaminase and stress fibers in human vascular smooth muscle cells and human umbilical vein endothelial cells. Exp. Cell Res. 231, 38-49.
    • (1997) Exp. Cell Res. , vol.231 , pp. 38-49
    • Chowdhury, Z.A.1    Barsigian, C.2    Chalupowicz, G.D.3    Bach, T.L.4    Garcia-Manero, G.5    Martinez, J.6
  • 9
    • 0017649032 scopus 로고
    • Purification of tau, a microtubule-associated protein that induces assembly of microtubules from purified tubulin
    • Cleveland D. W., Hwo S. Y., and Kirschner M. W. (1977) Purification of tau, a microtubule-associated protein that induces assembly of microtubules from purified tubulin. J. Mol. Biol. 116, 207-225.
    • (1977) J. Mol. Biol. , vol.116 , pp. 207-225
    • Cleveland, D.W.1    Hwo, S.Y.2    Kirschner, M.W.3
  • 11
    • 0022896901 scopus 로고
    • Tau protein function in living cells
    • Drubin D. G. and Kirschner M. W. (1986) Tau protein function in living cells. J. Cell Biol. 103, 2739-2746.
    • (1986) J. Cell Biol. , vol.103 , pp. 2739-2746
    • Drubin, D.G.1    Kirschner, M.W.2
  • 12
    • 0027184294 scopus 로고
    • Transglutaminase catalyzes the formation of sodium dodecyl sulfate-insoluble, Alz-50-reactive polymers of tau
    • Dudek S. M. and Johnson G. V. W. (1993) Transglutaminase catalyzes the formation of sodium dodecyl sulfate-insoluble, Alz-50-reactive polymers of tau. J. Neurochem. 61, 1159-1162.
    • (1993) J. Neurochem. , vol.61 , pp. 1159-1162
    • Dudek, S.M.1    Johnson, G.V.W.2
  • 13
    • 0028455060 scopus 로고
    • Recovery of visual response of injured adult rat optic nerves treated with transglutaminase
    • Eitan S., Solomon A., Lavie V., Yoles E., Hirschberg D. L., Belkin M., and Schwartz M. (1994) Recovery of visual response of injured adult rat optic nerves treated with transglutaminase. Science 264, 1764-1768.
    • (1994) Science , vol.264 , pp. 1764-1768
    • Eitan, S.1    Solomon, A.2    Lavie, V.3    Yoles, E.4    Hirschberg, D.L.5    Belkin, M.6    Schwartz, M.7
  • 14
    • 0018816617 scopus 로고
    • Transglutaminases
    • Folk J. E. (1980) Transglutaminases. Annu. Rev. Biochem. 49, 517-531.
    • (1980) Annu. Rev. Biochem. , vol.49 , pp. 517-531
    • Folk, J.E.1
  • 15
    • 0025822888 scopus 로고
    • Protein cross-linking by transglutaminase induced in long-term potentiation in the Ca1 region of hippocampal slices
    • Friedrich P., Fesus L., Tarcsa E., and Czeh G. (1991) Protein cross-linking by transglutaminase induced in long-term potentiation in the Ca1 region of hippocampal slices. Neuroscience 43, 331 -334.
    • (1991) Neuroscience , vol.43 , pp. 331-334
    • Friedrich, P.1    Fesus, L.2    Tarcsa, E.3    Czeh, G.4
  • 16
    • 0026018479 scopus 로고
    • Isolation and characterization of cDNA clones to mouse macrophage and human endothelial cell tissue transglutaminases
    • Gentile V., Saydak M., Chiocca E. A., Akande O., Birckbichler P. J., Lee K. N., Stein J. P., and Davies P. J. (1991) Isolation and characterization of cDNA clones to mouse macrophage and human endothelial cell tissue transglutaminases. J. Biol. Chem. 266, 478-483.
    • (1991) J. Biol. Chem. , vol.266 , pp. 478-483
    • Gentile, V.1    Saydak, M.2    Chiocca, E.A.3    Akande, O.4    Birckbichler, P.J.5    Lee, K.N.6    Stein, J.P.7    Davies, P.J.8
  • 17
    • 0022203159 scopus 로고
    • Transglutaminase activity in rat brain: Characterization, distribution, and changes with age
    • Gilad G. M. and Varon L. E. (1985) Transglutaminase activity in rat brain: characterization, distribution, and changes with age. J. Neurochem. 45, 1522-1526.
    • (1985) J. Neurochem. , vol.45 , pp. 1522-1526
    • Gilad, G.M.1    Varon, L.E.2
  • 18
    • 0021811514 scopus 로고
    • Calcium-dependent transglutaminase of rat sympathetic ganglion in development and after nerve injury
    • Gilad G. M., Varon L. E., and Gilad V. H. (1985) Calcium-dependent transglutaminase of rat sympathetic ganglion in development and after nerve injury. J. Neurochem. 44, 1385-1390.
    • (1985) J. Neurochem. , vol.44 , pp. 1385-1390
    • Gilad, G.M.1    Varon, L.E.2    Gilad, V.H.3
  • 19
    • 0024745894 scopus 로고
    • Multiple isoforms of human microtubule-associated protein tau: Sequences and localization in neurofibrillary tangles of Alzheimer's disease
    • Goedert M., Spillantini M. G., Jakes R., Rutherford D., and Crowther R. A. (1989) Multiple isoforms of human microtubule-associated protein tau: sequences and localization in neurofibrillary tangles of Alzheimer's disease. Neuron 3, 519-526.
    • (1989) Neuron , vol.3 , pp. 519-526
    • Goedert, M.1    Spillantini, M.G.2    Jakes, R.3    Rutherford, D.4    Crowther, R.A.5
  • 21
    • 0029161154 scopus 로고
    • Localization and in situ phosphorylation state of nuclear tau
    • Greenwood J. A. and Johnson G. V. W. (1995) Localization and in situ phosphorylation state of nuclear tau. Exp. Cell Res. 220, 332-337.
    • (1995) Exp. Cell Res. , vol.220 , pp. 332-337
    • Greenwood, J.A.1    Johnson, G.V.W.2
  • 22
  • 23
    • 0029843684 scopus 로고    scopus 로고
    • τ is widely expressed in rat tissues
    • Gu Y., Oyama F., and Ihara Y. (1996) τ is widely expressed in rat tissues. J. Neurochem. 67, 1235-1244.
    • (1996) J. Neurochem. , vol.67 , pp. 1235-1244
    • Gu, Y.1    Oyama, F.2    Ihara, Y.3
  • 24
    • 0004588617 scopus 로고    scopus 로고
    • Calpain-mediated proteolysis of neuronal structural proteins
    • Wang K. K. W. and Yuen P.-W., eds, Taylor and Francis, Philadelphia
    • Guttmann R. P. and Johnson G. V. W. (1999) Calpain-mediated proteolysis of neuronal structural proteins, in Pharmacology and Toxicology of Calcium-Dependent Proteases (Wang K. K. W. and Yuen P.-W., eds), pp. 229-249. Taylor and Francis, Philadelphia.
    • (1999) Pharmacology and Toxicology of Calcium-dependent Proteases , pp. 229-249
    • Guttmann, R.P.1    Johnson, G.V.W.2
  • 25
    • 0028985066 scopus 로고
    • τ self-association: Stabilization with a chemical cross-linker and modulation by phosphorylation and oxidation state
    • Guttmann R. P., Erickson A. C., and Johnson G. V. W. (1995) τ self-association: stabilization with a chemical cross-linker and modulation by phosphorylation and oxidation state. J. Neurochem. 64, 1209-1215.
    • (1995) J. Neurochem. , vol.64 , pp. 1209-1215
    • Guttmann, R.P.1    Erickson, A.C.2    Johnson, G.V.W.3
  • 26
    • 0032549637 scopus 로고    scopus 로고
    • The cell adhesion molecule C-CAM is a substrate for tissue transglutaminase
    • Hunter I., Sigmundsson K., Beauchemin N., and Obrink B. (1998) The cell adhesion molecule C-CAM is a substrate for tissue transglutaminase. FEBS Lett. 425, 141-144.
    • (1998) FEBS Lett. , vol.425 , pp. 141-144
    • Hunter, I.1    Sigmundsson, K.2    Beauchemin, N.3    Obrink, B.4
  • 27
    • 0032529396 scopus 로고    scopus 로고
    • Identification of amine acceptor protein substrates of transglutaminase in liver extracts: Use of 5-(biotinamido)pentylamine as a probe
    • Ikura K., Kita K., Fujita I., Hashimoto H., and Kawabata N. (1998) Identification of amine acceptor protein substrates of transglutaminase in liver extracts: use of 5-(biotinamido)pentylamine as a probe. Arch. Biochem. Biophys. 356, 280-286.
    • (1998) Arch. Biochem. Biophys. , vol.356 , pp. 280-286
    • Ikura, K.1    Kita, K.2    Fujita, I.3    Hashimoto, H.4    Kawabata, N.5
  • 28
    • 0026445630 scopus 로고
    • Affinity purification of histidine-tagged proteins transiently produced in HeLa cells
    • Janknecht R. and Nordheim A. (1992) Affinity purification of histidine-tagged proteins transiently produced in HeLa cells. Gene 121, 321-324.
    • (1992) Gene , vol.121 , pp. 321-324
    • Janknecht, R.1    Nordheim, A.2
  • 30
    • 0026563915 scopus 로고
    • 2+/calmodulin-dependent protein kinase II: Metabolic and functional consequences
    • 2+/calmodulin-dependent protein kinase II: metabolic and functional consequences. J. Neurochem. 59, 2056-2062.
    • (1992) J. Neurochem. , vol.59 , pp. 2056-2062
    • Johnson, G.V.W.1
  • 32
    • 0031025396 scopus 로고    scopus 로고
    • The tau protein in human cerebrospinal fluid in Alzheimer's disease consists of proteolytically derived fragments
    • Johnson G. V. W., Seubert P., Cox T. M., Motter R., Brown J. P., and Galasko D. (1997b) The tau protein in human cerebrospinal fluid in Alzheimer's disease consists of proteolytically derived fragments. J. Neurochem. 68, 430-433.
    • (1997) J. Neurochem. , vol.68 , pp. 430-433
    • Johnson, G.V.W.1    Seubert, P.2    Cox, T.M.3    Motter, R.4    Brown, J.P.5    Galasko, D.6
  • 34
    • 0009364134 scopus 로고
    • Microtubule-associated protein tau (tau) is a major antigenic component of paired helical filaments in Alzheimer disease
    • Kosik K. S., Joachim C. L., and Selkoe D. J. (1986) Microtubule-associated protein tau (tau) is a major antigenic component of paired helical filaments in Alzheimer disease. Proc. Natl. Acad. Sci. USA 83, 4044-4048.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 4044-4048
    • Kosik, K.S.1    Joachim, C.L.2    Selkoe, D.J.3
  • 35
    • 0027165996 scopus 로고
    • Site-directed mutagenesis of human tissue transglutaminase: Cys-277 is essential for transglutaminase activity but not for GTPase activity
    • Lee K. N., Arnold S. A., Birckbichler P. J., Patterson M. K. Jr., Fraij B. M., Takeuchi Y., and Carter H. A. (1993) Site-directed mutagenesis of human tissue transglutaminase: Cys-277 is essential for transglutaminase activity but not for GTPase activity. Biochim. Biophys. Acta 1202, 1-6.
    • (1993) Biochim. Biophys. Acta , vol.1202 , pp. 1-6
    • Lee, K.N.1    Arnold, S.A.2    Birckbichler, P.J.3    Patterson M.K., Jr.4    Fraij, B.M.5    Takeuchi, Y.6    Carter, H.A.7
  • 36
    • 0032524312 scopus 로고    scopus 로고
    • Distinct nuclear localization and activity of tissue transglutaminase
    • Lesort M., Attanavanich K., Zhang J., and Johnson G. V. W. (1998) Distinct nuclear localization and activity of tissue transglutaminase. J. Biol. Chem. 273, 11991-11994.
    • (1998) J. Biol. Chem. , vol.273 , pp. 11991-11994
    • Lesort, M.1    Attanavanich, K.2    Zhang, J.3    Johnson, G.V.W.4
  • 37
    • 0026597280 scopus 로고
    • Phosphorylation by cAMP-dependent protein kinase inhibits the degradation of tau by calpain
    • Litersky J. M. and Johnson G. V. W. (1992) Phosphorylation by cAMP-dependent protein kinase inhibits the degradation of tau by calpain. J. Biol. Chem. 267, 1563-1568.
    • (1992) J. Biol. Chem. , vol.267 , pp. 1563-1568
    • Litersky, J.M.1    Johnson, G.V.W.2
  • 38
    • 0029081290 scopus 로고
    • Phosphorylation of τ in situ: Inhibition of calcium-dependent proteolysis
    • Litersky J. M. and Johnson G. V. W. (1995) Phosphorylation of τ in situ: inhibition of calcium-dependent proteolysis. J. Neurochem. 65, 903-911.
    • (1995) J. Neurochem. , vol.65 , pp. 903-911
    • Litersky, J.M.1    Johnson, G.V.W.2
  • 40
    • 0022575415 scopus 로고
    • Transglutaminase and neuronal differentiation
    • Maccioni R. B. and Seeds N. W. (1986) Transglutaminase and neuronal differentiation. Mol. Cell. Biochem. 69, 161-168.
    • (1986) Mol. Cell. Biochem. , vol.69 , pp. 161-168
    • Maccioni, R.B.1    Seeds, N.W.2
  • 42
    • 0026636023 scopus 로고
    • Calcium as sculptor and destroyer of neural circuitry
    • Mattson M. P. (1992) Calcium as sculptor and destroyer of neural circuitry. Exp. Gerontol. 27, 29-49.
    • (1992) Exp. Gerontol. , vol.27 , pp. 29-49
    • Mattson, M.P.1
  • 44
    • 0029096258 scopus 로고
    • Transglutaminase cross-linking of the τ protein
    • Miller M. L. and Johnson G. V. W. (1995) Transglutaminase cross-linking of the τ protein. J. Neurochem. 65, 1760-1770.
    • (1995) J. Neurochem. , vol.65 , pp. 1760-1770
    • Miller, M.L.1    Johnson, G.V.W.2
  • 46
    • 0029159811 scopus 로고
    • Polyamines in human brain: Regional distribution and influence of aging
    • Morrison L. D., Becker L., Ang L. C., and Kish S. J. (1995) Polyamines in human brain: regional distribution and influence of aging. J. Neurochem. 65, 636-642.
    • (1995) J. Neurochem. , vol.65 , pp. 636-642
    • Morrison, L.D.1    Becker, L.2    Ang, L.C.3    Kish, S.J.4
  • 47
    • 0040041521 scopus 로고    scopus 로고
    • Cross-linking sites of the human tau protein, probed by reactions with human transglutaminase
    • Murthy S. N., Wilson J. H., Lukas T. J., Kuret J., and Lorand L. (1998) Cross-linking sites of the human tau protein, probed by reactions with human transglutaminase. J. Neurochem. 71, 2607-2614.
    • (1998) J. Neurochem. , vol.71 , pp. 2607-2614
    • Murthy, S.N.1    Wilson, J.H.2    Lukas, T.J.3    Kuret, J.4    Lorand, L.5
  • 48
    • 0028176166 scopus 로고
    • Gh: A GTP-binding protein with transglutaminase activity and receptor signaling function
    • Nakaoka H., Perez D. M., Baek K. J., Das T., Husain A., Misono K., Im M. J., and Graham R. M. (1994) Gh: a GTP-binding protein with transglutaminase activity and receptor signaling function. Science 264, 1593-1596.
    • (1994) Science , vol.264 , pp. 1593-1596
    • Nakaoka, H.1    Perez, D.M.2    Baek, K.J.3    Das, T.4    Husain, A.5    Misono, K.6    Im, M.J.7    Graham, R.M.8
  • 49
    • 1842332757 scopus 로고    scopus 로고
    • Identification of cytoplasmic actin as an abundant glutaminyl substrate for tissue transglutaminase in HL-60 and U937 cells undergoing apoptosis
    • Nemes Z. Jr., Adany R., Balazs M., Boross P., and Fesus L. (1997) Identification of cytoplasmic actin as an abundant glutaminyl substrate for tissue transglutaminase in HL-60 and U937 cells undergoing apoptosis. J. Biol. Chem. 272, 20577-20583.
    • (1997) J. Biol. Chem. , vol.272 , pp. 20577-20583
    • Nemes Z., Jr.1    Adany, R.2    Balazs, M.3    Boross, P.4    Fesus, L.5
  • 50
    • 0029614688 scopus 로고
    • Purification and characterization of rat brain transglutaminase
    • Ohashi H., Itoh Y., Birckbichler P. J., and Takeuchi Y. (1995) Purification and characterization of rat brain transglutaminase. J. Biochem. (Tokyo) 118, 1271-1278.
    • (1995) J. Biochem. (Tokyo) , vol.118 , pp. 1271-1278
    • Ohashi, H.1    Itoh, Y.2    Birckbichler, P.J.3    Takeuchi, Y.4
  • 51
    • 0030863635 scopus 로고    scopus 로고
    • Tissue transglutaminase-dependent posttranslational modification of the retinoblastoma gene product in promonocytic cells undergoing apoptosis
    • Oliverio S., Amendola A., Di Sano F., Farrace M. G., Fesus L., Nemes Z., Piredda L., Spinedi A., and Piacentini M. (1997) Tissue transglutaminase-dependent posttranslational modification of the retinoblastoma gene product in promonocytic cells undergoing apoptosis. Mol. Cell. Biol. 17, 6040-6048.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 6040-6048
    • Oliverio, S.1    Amendola, A.2    Di Sano, F.3    Farrace, M.G.4    Fesus, L.5    Nemes, Z.6    Piredda, L.7    Spinedi, A.8    Piacentini, M.9
  • 52
    • 0022586820 scopus 로고
    • A role for transglutaminase in neurotransmitter release by rat brain synaptosomes
    • Pastuszko A., Wilson D. F., and Erecińska M. (1986) A role for transglutaminase in neurotransmitter release by rat brain synaptosomes. J. Neurochem. 46, 499-508.
    • (1986) J. Neurochem. , vol.46 , pp. 499-508
    • Pastuszko, A.1    Wilson, D.F.2    Erecińska, M.3
  • 53
    • 0028927182 scopus 로고
    • Transglutaminase C in cerebellar granule neurons: Regulation and localization of substrate cross-linking
    • Perry M. J., Mahoney S. A., and Haynes L. W. (1995) Transglutaminase C in cerebellar granule neurons: regulation and localization of substrate cross-linking. Neuroscience 65, 1063-1076.
    • (1995) Neuroscience , vol.65 , pp. 1063-1076
    • Perry, M.J.1    Mahoney, S.A.2    Haynes, L.W.3
  • 54
    • 0023751017 scopus 로고
    • Posttranslational modifications of cellular proteins by polyamines and polyamine-derivatives
    • Piacentini M., Cerù-Argento M. P., Farrace M. G., and Autuori F. (1988a) Posttranslational modifications of cellular proteins by polyamines and polyamine-derivatives. Adv. Exp. Med. Biol. 231, 185-198.
    • (1988) Adv. Exp. Med. Biol. , vol.231 , pp. 185-198
    • Piacentini, M.1    Cerù-Argento M, P.2    Farrace, M.G.3    Autuori, F.4
  • 55
    • 0023838641 scopus 로고
    • Free and protein-conjugated polyamines in mouse epidermal cells. Effect of high calcium and retinoic acid
    • Piacentini M., Martinet N., Beninati S., and Folk J. E. (1988b) Free and protein-conjugated polyamines in mouse epidermal cells. Effect of high calcium and retinoic acid. J. Biol. Chem. 263, 3790-3794.
    • (1988) J. Biol. Chem. , vol.263 , pp. 3790-3794
    • Piacentini, M.1    Martinet, N.2    Beninati, S.3    Folk, J.E.4
  • 57
    • 0019891027 scopus 로고
    • Posttranslational modification of ornithine decarboxylase by its product putrescine
    • Russell D. H. (1981) Posttranslational modification of ornithine decarboxylase by its product putrescine. Biochem. Biophys. Res. Commun. 99, 1167-1172.
    • (1981) Biochem. Biophys. Res. Commun. , vol.99 , pp. 1167-1172
    • Russell, D.H.1
  • 58
    • 0000831917 scopus 로고
    • Brain transglutaminase: In vitro crosslinking of human neurofilament proteins into insoluble polymers
    • Selkoe D. J., Abraham C, and Ihara Y. (1982a) Brain transglutaminase: in vitro crosslinking of human neurofilament proteins into insoluble polymers. Proc. Natl. Acad. Sci. USA 79, 6070-6074.
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 6070-6074
    • Selkoe, D.J.1    Abraham, C.2    Ihara, Y.3
  • 59
    • 0020034866 scopus 로고
    • Alzheimer's disease: Insolubility of partially purified paired helical filaments in sodium dodecyl sulfate and urea
    • Selkoe D. J., Ihara Y., and Salazar F. J. (1982b) Alzheimer's disease: insolubility of partially purified paired helical filaments in sodium dodecyl sulfate and urea. Science 215, 1243-1245.
    • (1982) Science , vol.215 , pp. 1243-1245
    • Selkoe, D.J.1    Ihara, Y.2    Salazar, F.J.3
  • 60
    • 0028879127 scopus 로고
    • Tau isoforms expression and phosphorylation state during differentiation of cultured neuronal cells
    • Smith C. J., Anderton B. H., Davis D. R., and Gallo J. M. (1995) Tau isoforms expression and phosphorylation state during differentiation of cultured neuronal cells. FEBS Lett. 375, 243-248.
    • (1995) FEBS Lett. , vol.375 , pp. 243-248
    • Smith, C.J.1    Anderton, B.H.2    Davis, D.R.3    Gallo, J.M.4
  • 62
    • 0027388775 scopus 로고
    • Recognition of the minimal epitope of monoclonal antibody Tau-1 depends upon the presence of a phosphate group but not its location
    • Szendrei G. I., Lee V. M., and Otvos L. Jr. (1993) Recognition of the minimal epitope of monoclonal antibody Tau-1 depends upon the presence of a phosphate group but not its location. J. Neurosci. Res. 34, 243-249.
    • (1993) J. Neurosci. Res. , vol.34 , pp. 243-249
    • Szendrei, G.I.1    Lee, V.M.2    Otvos L., Jr.3
  • 63
    • 0032078612 scopus 로고    scopus 로고
    • Nuclear translocation of tissue type transglutaminase during sphingosine-induced cell death: A novel aspect of the enzyme with DNA hydrolytic activity
    • Takeuchi Y., Ohashi H., Birckbichler P. J., and Ikejima T. (1998) Nuclear translocation of tissue type transglutaminase during sphingosine-induced cell death: a novel aspect of the enzyme with DNA hydrolytic activity. Z. Naturforsch. [C] 53, 352-358.
    • (1998) Z. Naturforsch. [C] , vol.53 , pp. 352-358
    • Takeuchi, Y.1    Ohashi, H.2    Birckbichler, P.J.3    Ikejima, T.4
  • 65
    • 1842685948 scopus 로고
    • Neurofibrillary tangles of Alzheimer disease share antigenic determinants with the axonal microtubule-associated protein tau
    • Wood J. G., Mirra S. S., Pollock N. J., and Binder L. I. (1986) Neurofibrillary tangles of Alzheimer disease share antigenic determinants with the axonal microtubule-associated protein tau. Proc. Natl. Acad. Sci. USA 83, 4040-4043.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 4040-4043
    • Wood, J.G.1    Mirra, S.S.2    Pollock, N.J.3    Binder, L.I.4
  • 66
    • 0032528162 scopus 로고    scopus 로고
    • Calcineurin inhibition prevents calpain-mediated proteolysis of tau in differentiated PC12 cells
    • Xie H. and Johnson G. V. W. (1998) Calcineurin inhibition prevents calpain-mediated proteolysis of tau in differentiated PC12 cells. J. Neurosci. Res. 53, 153-164.
    • (1998) J. Neurosci. Res. , vol.53 , pp. 153-164
    • Xie, H.1    Johnson, G.V.W.2
  • 67
    • 0032490652 scopus 로고    scopus 로고
    • The interrelationship between selective tau phosphorylation and microtubule association
    • Xie H., Litersky J. M., Hartigan J. A., Jope R. S., and Johnson G. V. W. (1998) The interrelationship between selective tau phosphorylation and microtubule association. Brain Res. 798, 173-183.
    • (1998) Brain Res. , vol.798 , pp. 173-183
    • Xie, H.1    Litersky, J.M.2    Hartigan, J.A.3    Jope, R.S.4    Johnson, G.V.W.5
  • 68
    • 0028785672 scopus 로고
    • Calpain-induced proteolysis of normal human tau and tau associated with paired helical filaments
    • Yang L. S. and Ksiezak-Reding H. (1995) Calpain-induced proteolysis of normal human tau and tau associated with paired helical filaments. Eur. J. Biochem. 233, 9-17.
    • (1995) Eur. J. Biochem. , vol.233 , pp. 9-17
    • Yang, L.S.1    Ksiezak-Reding, H.2
  • 69
    • 0031893826 scopus 로고    scopus 로고
    • Modulation of the in situ activity of tissue transglutaminase by calcium and GTP
    • Zhang J., Lesort M., Guttmann R. P., and Johnson G. V. W. (1998) Modulation of the in situ activity of tissue transglutaminase by calcium and GTP. J. Biol. Chem. 273, 2288-2295.
    • (1998) J. Biol. Chem. , vol.273 , pp. 2288-2295
    • Zhang, J.1    Lesort, M.2    Guttmann, R.P.3    Johnson, G.V.W.4


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