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Volumn 69, Issue 5, 1997, Pages 2026-2038

Degradation of tau by lysosomal enzyme cathepsin D: Implication for Alzheimer neurofibrillary degeneration

Author keywords

Alzheimer's disease; Cathepsin D; Degradation sites; Tau

Indexed keywords

CATHEPSIN D; LYSOSOME ENZYME; RECOMBINANT PROTEIN; TAU PROTEIN;

EID: 0030774852     PISSN: 00223042     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1471-4159.1997.69052026.x     Document Type: Article
Times cited : (159)

References (60)
  • 1
    • 0026689819 scopus 로고
    • The distribution of cathepsin D activity in adult and aging human brain regions
    • Banay-Schwartz M., DeGuzman T., Kenessey A., Palkovits M., and Lajtha A. (1992) The distribution of cathepsin D activity in adult and aging human brain regions. J. Neurochem. 58, 2207-2211.
    • (1992) J. Neurochem. , vol.58 , pp. 2207-2211
    • Banay-Schwartz, M.1    DeGuzman, T.2    Kenessey, A.3    Palkovits, M.4    Lajtha, A.5
  • 3
    • 0001310293 scopus 로고
    • Cathepsin D and other carboxyl proteinases
    • (Barrett A. J., ed), Elsevier North-Holland. Amsterdam
    • Barrett A. J. (1977) Cathepsin D and other carboxyl proteinases. in Proteinases in Mammalian Cells and Tissues (Barrett A. J., ed), pp. 209-248. Elsevier North-Holland. Amsterdam.
    • (1977) Proteinases in Mammalian Cells and Tissues , pp. 209-248
    • Barrett, A.J.1
  • 4
    • 0029845397 scopus 로고    scopus 로고
    • Cytosolic proteolysis of τ by cathepsin D in hippocampus following suppression of cathepsins B and L
    • Bednarski E. and Lynch G. (1996) Cytosolic proteolysis of τ by cathepsin D in hippocampus following suppression of cathepsins B and L. J. Neurochem. 67, 1846-1855.
    • (1996) J. Neurochem. , vol.67 , pp. 1846-1855
    • Bednarski, E.1    Lynch, G.2
  • 5
    • 0022220304 scopus 로고
    • Distribution of cathepsin D immunoreactivity in the central nervous system of rat and selected brain regions of man
    • Bernstein H.-G., Wiederanders B., Rinne A., and Dorn A. (1985) Distribution of cathepsin D immunoreactivity in the central nervous system of rat and selected brain regions of man. Acta Histochem. 77, 139-142.
    • (1985) Acta Histochem. , vol.77 , pp. 139-142
    • Bernstein, H.-G.1    Wiederanders, B.2    Rinne, A.3    Dorn, A.4
  • 6
    • 0022365608 scopus 로고
    • The distribution of tau in the mammalian central nervous system
    • Binder L. I., Frankfurter A., and Rebhun L. I. (1985) The distribution of tau in the mammalian central nervous system. J. Cell Biol. 101, 1371-1378.
    • (1985) J. Cell Biol. , vol.101 , pp. 1371-1378
    • Binder, L.I.1    Frankfurter, A.2    Rebhun, L.I.3
  • 7
    • 0024988546 scopus 로고
    • Molecular analysis of neurofibrillary degeneration in Alzheimer's disease
    • Bondareff W., Wischik C. M., Novak M., Amos W. B., Kluf A., and Roth M. (1990) Molecular analysis of neurofibrillary degeneration in Alzheimer's disease. Am. J. Pathol. 137, 711-723.
    • (1990) Am. J. Pathol. , vol.137 , pp. 711-723
    • Bondareff, W.1    Wischik, C.M.2    Novak, M.3    Amos, W.B.4    Kluf, A.5    Roth, M.6
  • 8
    • 0026097837 scopus 로고
    • Tau in Alzheimer neurofibrillary tangles: N- and C-terminal regions are differentially associated with paired helical filaments and the location of a putative abnormal phosphorylation site
    • Brion J. P., Hanger D. P., Bruce M. T., Couck A. M., Flament-Durand J., and Anderton B. H. (1991) Tau in Alzheimer neurofibrillary tangles: N- and C-terminal regions are differentially associated with paired helical filaments and the location of a putative abnormal phosphorylation site. Biochem. J. 273, 127-133.
    • (1991) Biochem. J. , vol.273 , pp. 127-133
    • Brion, J.P.1    Hanger, D.P.2    Bruce, M.T.3    Couck, A.M.4    Flament-Durand, J.5    Anderton, B.H.6
  • 9
    • 0029975425 scopus 로고    scopus 로고
    • Evaluation of cathepsin D and G and EC 3.4.24.15 as candidate β-secretase proteases using peptide and amyloid precursor protein substrates
    • Brown A. M., Tummolo D. M., Spruyt M. A., Jacobsen J. S., and Sonnenberg-Reines J. (1996) Evaluation of cathepsin D and G and EC 3.4.24.15 as candidate β-secretase proteases using peptide and amyloid precursor protein substrates. J. Neurochem. 66, 2436-2445.
    • (1996) J. Neurochem. , vol.66 , pp. 2436-2445
    • Brown, A.M.1    Tummolo, D.M.2    Spruyt, M.A.3    Jacobsen, J.S.4    Sonnenberg-Reines, J.5
  • 10
    • 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
  • 11
    • 0025195944 scopus 로고
    • Enzymatically active lysosomal proteases are associated with amyloid deposits in Alzheimer brain
    • Cataldo A. M. and Nixon R. A. (1990) Enzymatically active lysosomal proteases are associated with amyloid deposits in Alzheimer brain. Proc. Natl. Acad. Sci. USA 87, 3861-3865.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 3861-3865
    • Cataldo, A.M.1    Nixon, R.A.2
  • 12
    • 0025355591 scopus 로고
    • Lysosomal proteinase antigens are prominently localized within senile plaques of Alzheimer's disease: Evidence for a neuronal origin
    • Cataldo A. M., Thayer C. Y., Bird E. D., Wheelock T. R., and Nixon R. A. (1990) Lysosomal proteinase antigens are prominently localized within senile plaques of Alzheimer's disease: evidence for a neuronal origin. Brain Res. 513, 181-192.
    • (1990) Brain Res. , vol.513 , pp. 181-192
    • Cataldo, A.M.1    Thayer, C.Y.2    Bird, E.D.3    Wheelock, T.R.4    Nixon, R.A.5
  • 13
    • 0017649032 scopus 로고
    • Purification of tau, a microtubule associated protein that induces assembly of microtubules from purified tubulin
    • Cleveland D. W., Hwo H.-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, H.-Y.2    Kirschner, M.W.3
  • 14
    • 0026342276 scopus 로고
    • The N terminal region of human tau is present in Alzheimer's disease protein A68 and is incorporated into paired helical filaments
    • Crowe A., Ksiezak-Reding H., Liu W.-K., Dickson D. W., and Yen S.-H. (1991) The N terminal region of human tau is present in Alzheimer's disease protein A68 and is incorporated into paired helical filaments. Am. J. Pathol. 139, 1463-1470.
    • (1991) Am. J. Pathol. , vol.139 , pp. 1463-1470
    • Crowe, A.1    Ksiezak-Reding, H.2    Liu, W.-K.3    Dickson, D.W.4    Yen, S.-H.5
  • 15
    • 0026451030 scopus 로고
    • Immunocytochemistry of neurofibrillary tangles with antibodies to subregions of tau protein: Identification of hidden and cleaved tau epitopes and a new phosphorylation site
    • Dickson D. W., Ksiezak-Reding H., Liu W.-K., Davies P., Crowe A., and Yen S.-H. (1992) Immunocytochemistry of neurofibrillary tangles with antibodies to subregions of tau protein: identification of hidden and cleaved tau epitopes and a new phosphorylation site. Acta Neuropathol. (Berl.) 84, 596-605.
    • (1992) Acta Neuropathol. (Berl.) , vol.84 , pp. 596-605
    • Dickson, D.W.1    Ksiezak-Reding, H.2    Liu, W.-K.3    Davies, P.4    Crowe, A.5    Yen, S.-H.6
  • 17
    • 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
  • 18
    • 0027534862 scopus 로고
    • Lack of the carboxyl terminal sequence of tau in ghost tangles of Alzheimer's disease
    • Endoh R., Ogawara M., Iwatsubo T., Nakano I., and Mori H. (1993) Lack of the carboxyl terminal sequence of tau in ghost tangles of Alzheimer's disease. Brain Res. 601, 164-172.
    • (1993) Brain Res. , vol.601 , pp. 164-172
    • Endoh, R.1    Ogawara, M.2    Iwatsubo, T.3    Nakano, I.4    Mori, H.5
  • 19
    • 0025600995 scopus 로고
    • Expression of separate isoforms of human tau protein: Correlation with the tau pattern in brain and effects on tubulin polymerization
    • Goedert M. and Jakes R. (1990) Expression of separate isoforms of human tau protein: correlation with the tau pattern in brain and effects on tubulin polymerization. EMBO J. 9, 4225-4230.
    • (1990) EMBO J. , vol.9 , pp. 4225-4230
    • Goedert, M.1    Jakes, R.2
  • 20
    • 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. (1989a) 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
    • 0024387161 scopus 로고
    • Cloning and sequencing of the cDNA encoding an isoform of microtubule-associated protein tau containing four tandem repeats: Differential expression of tau protein mRNAs in human brain
    • Goedert M., Spillantini M. G., Potier M. C., Ulrich J., and Crowther R. A. (1989b) Cloning and sequencing of the cDNA encoding an isoform of microtubule-associated protein tau containing four tandem repeats: differential expression of tau protein mRNAs in human brain. EMBO J. 8, 393-399.
    • (1989) EMBO J. , vol.8 , pp. 393-399
    • Goedert, M.1    Spillantini, M.G.2    Potier, M.C.3    Ulrich, J.4    Crowther, R.A.5
  • 22
    • 0025853691 scopus 로고
    • Localization of the Alz-50 epitope in recombinant human microtubule-associated protein tau
    • Goedert M., Spillantini M. G., and Jakes R. (1991) Localization of the Alz-50 epitope in recombinant human microtubule-associated protein tau. Neurosci. Lett. 126, 149-154.
    • (1991) Neurosci. Lett. , vol.126 , pp. 149-154
    • Goedert, M.1    Spillantini, M.G.2    Jakes, R.3
  • 23
    • 0025292866 scopus 로고
    • A preparation of Alzheimer paired helical filaments that displays distinct tau proteins by polyacrylamide gel electrophoresis
    • Greenberg S. G. and Davies P. (1990) A preparation of Alzheimer paired helical filaments that displays distinct tau proteins by polyacrylamide gel electrophoresis. Proc. Natl. Acad. Sci. USA 87, 5827-5831.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 5827-5831
    • Greenberg, S.G.1    Davies, P.2
  • 24
    • 0024461007 scopus 로고
    • Tau protein becomes long and stiff upon phosphorylation: Correlation between paracrystalline structure and degree of phosphorylation
    • Hagestedt T., Lichtenberg B., Wille H., Mandelkow E.-M. and Mandelkow E. (1989) Tau protein becomes long and stiff upon phosphorylation: correlation between paracrystalline structure and degree of phosphorylation. J. Cell Biol. 109, 1643-1651.
    • (1989) J. Cell Biol. , vol.109 , pp. 1643-1651
    • Hagestedt, T.1    Lichtenberg, B.2    Wille, H.3    Mandelkow, E.-M.4    Mandelkow, E.5
  • 25
    • 0024498630 scopus 로고
    • Structure of the bovine tau gene: Alternatively spliced transcripts generate a protein family
    • Himmler A. (1989) Structure of the bovine tau gene: alternatively spliced transcripts generate a protein family. Mol. Cell Biol. 9, 1389-1396.
    • (1989) Mol. Cell Biol. , vol.9 , pp. 1389-1396
    • Himmler, A.1
  • 26
    • 0024438227 scopus 로고
    • Expression of multiple tau isoforms and microtubule bundle formation in fibroblasts transfected with a single tau cDNA
    • Kanai Y., Takemura R., Oshima T., Mori H.. Ihara Y., Yanagisawa M., Masaki T., and Hirokawa N. (1989) Expression of multiple tau isoforms and microtubule bundle formation in fibroblasts transfected with a single tau cDNA. J. Cell Biol. 109, 1173-1184.
    • (1989) J. Cell Biol. , vol.109 , pp. 1173-1184
    • Kanai, Y.1    Takemura, R.2    Oshima, T.3    Mori, H.4    Ihara, Y.5    Yanagisawa, M.6    Masaki, T.7    Hirokawa, N.8
  • 27
    • 0026711059 scopus 로고
    • Fetal-type phosphorylation of the τ in paired helical filaments
    • Kanemaru K., Takio K., Miura R., Titani K., and Ihara Y. (1992) Fetal-type phosphorylation of the τ in paired helical filaments. J. Neurochem. 58, 1667-1675.
    • (1992) J. Neurochem. , vol.58 , pp. 1667-1675
    • Kanemaru, K.1    Takio, K.2    Miura, R.3    Titani, K.4    Ihara, Y.5
  • 28
    • 0027372016 scopus 로고
    • The extent of phosphorylation of F-tau is comparable to that of PHF-tau from Alzheimer paired helical filaments
    • Kenessey A. and Yen S.-H. (1993) The extent of phosphorylation of F-tau is comparable to that of PHF-tau from Alzheimer paired helical filaments. Brain Res. 629, 40-46.
    • (1993) Brain Res. , vol.629 , pp. 40-46
    • Kenessey, A.1    Yen, S.-H.2
  • 31
    • 0025852163 scopus 로고
    • Structural stability of paired helical filaments requires microtubule-binding domains of tau: A model for self-association
    • Ksiezak-Reding H. and Yen S.-H. (1991) Structural stability of paired helical filaments requires microtubule-binding domains of tau: a model for self-association. Neuron 6, 717-728.
    • (1991) Neuron , vol.6 , pp. 717-728
    • Ksiezak-Reding, H.1    Yen, S.-H.2
  • 33
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 34
    • 0028065142 scopus 로고
    • Analysis of microtubule-associated protein tau glycation in paired helical filaments
    • Ledesma M. D., Bonay P., Colaco C., and Avila J. (1994) Analysis of microtubule-associated protein tau glycation in paired helical filaments. J. Biol. Chem. 269, 21614-21619.
    • (1994) J. Biol. Chem. , vol.269 , pp. 21614-21619
    • Ledesma, M.D.1    Bonay, P.2    Colaco, C.3    Avila, J.4
  • 35
    • 0025904444 scopus 로고
    • A68: A major subunit of paired helical filaments and derivatized forms of normal tau
    • Lee V. M.-Y.,Balin B. J., Otvos L. Jr., and Trojanowski J. Q. (1991) A68: a major subunit of paired helical filaments and derivatized forms of normal tau. Science 251, 675-678.
    • (1991) Science , vol.251 , pp. 675-678
    • Lee, V.M.-Y.1    Balin, B.J.2    Otvos Jr., L.3    Trojanowski, J.Q.4
  • 36
    • 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
  • 37
    • 0027534625 scopus 로고
    • Application of synthetic phospho- and unphospho-peptides to identify phosphorylation sites in a subregion of tau molecule, which is modified in Alzheimer's disease
    • Liu W.-K., Moore W. T., Williams R. T., Hall F. L., and Yen S.-H. (1993a) Application of synthetic phospho- and unphospho-peptides to identify phosphorylation sites in a subregion of tau molecule, which is modified in Alzheimer's disease. J. Neurosci. Res. 34, 371-376.
    • (1993) J. Neurosci. Res. , vol.34 , pp. 371-376
    • Liu, W.-K.1    Moore, W.T.2    Williams, R.T.3    Hall, F.L.4    Yen, S.-H.5
  • 38
    • 0027402861 scopus 로고
    • Heterogeneity of tau proteins in Alzheimer's disease: Evidence for increased expression of an isoform and preferential distribution of a phosphorylated isoform in neuntes
    • Liu W.-K., Dickson D. W., and Yen S.-H. (1993b) Heterogeneity of tau proteins in Alzheimer's disease: evidence for increased expression of an isoform and preferential distribution of a phosphorylated isoform in neuntes. Am. J. Pathol. 142, 387-394.
    • (1993) Am. J. Pathol. , vol.142 , pp. 387-394
    • Liu, W.-K.1    Dickson, D.W.2    Yen, S.-H.3
  • 39
    • 1842381828 scopus 로고
    • Separation of acid and neutral proteinases of brain
    • Marks N. and Lajtha A. (1965) Separation of acid and neutral proteinases of brain. Biochem. J. 97, 74-83.
    • (1965) Biochem. J. , vol.97 , pp. 74-83
    • Marks, N.1    Lajtha, A.2
  • 40
    • 0027945346 scopus 로고
    • Biopsy-derived adult human brain tau is phosphorylated at many of the same sites as Alzheimer's disease paired helical filament tau
    • Matsuo E. S., Shin R.-W., Billingsley M. L., Van de Voorde A., O'Connor M., Trojanowski J. Q., and Lee V. M.-Y. (1994) Biopsy-derived adult human brain tau is phosphorylated at many of the same sites as Alzheimer's disease paired helical filament tau. Neuron 13, 989-1002.
    • (1994) Neuron , vol.13 , pp. 989-1002
    • Matsuo, E.S.1    Shin, R.-W.2    Billingsley, M.L.3    Van De Voorde, A.4    O'Connor, M.5    Trojanowski, J.Q.6    Lee, V.M.-Y.7
  • 41
    • 0029039987 scopus 로고
    • Differential sensitivity to proteolysis by brain calpain of adult human tau, fetal human tau and PHF-tau
    • Mercken M., Grynspan F., and Nixon R. A. (1995) Differential sensitivity to proteolysis by brain calpain of adult human tau, fetal human tau and PHF-tau. FEBS Lett. 368, 10-14.
    • (1995) FEBS Lett. , vol.368 , pp. 10-14
    • Mercken, M.1    Grynspan, F.2    Nixon, R.A.3
  • 42
    • 0027193036 scopus 로고
    • Ubiquitin is conjugated with amino-terminally processed tau in paired helical filaments
    • Morishima-Kawashima M., Hasegawa M., Takio K., Suzuki M., Titani K., and Ihara Y. (1993) Ubiquitin is conjugated with amino-terminally processed tau in paired helical filaments. Neuron 10, 1151-1160.
    • (1993) Neuron , vol.10 , pp. 1151-1160
    • Morishima-Kawashima, M.1    Hasegawa, M.2    Takio, K.3    Suzuki, M.4    Titani, K.5    Ihara, Y.6
  • 46
    • 0028323067 scopus 로고
    • Age-related changes in activities and localizations of cathepsins D, E, B, and L in the rat brain tissues
    • Nakanishi H., Tominaga K., Amano T., Hirotsu I., Inoue T. and Yamamato K. (1994) Age-related changes in activities and localizations of cathepsins D, E, B, and L in the rat brain tissues. Exp. Neurol. 126, 119-128.
    • (1994) Exp. Neurol. , vol.126 , pp. 119-128
    • Nakanishi, H.1    Tominaga, K.2    Amano, T.3    Hirotsu, I.4    Inoue, T.5    Yamamato, K.6
  • 48
    • 0028458037 scopus 로고
    • Truncated tau protein as a new marker for Alzheimer's disease
    • Praha
    • Novak M. (1994) Truncated tau protein as a new marker for Alzheimer's disease. Acta Virol. (Praha) 38, 173-189.
    • (1994) Acta Virol. , vol.38 , pp. 173-189
    • Novak, M.1
  • 49
    • 0028237079 scopus 로고
    • Proteolytic degradation of microtubule associated protein tau by thrombin
    • Olesen O. F. (1994) Proteolytic degradation of microtubule associated protein tau by thrombin. Biochem. Biophys. Res. Commun. 201, 716-721.
    • (1994) Biochem. Biophys. Res. Commun. , vol.201 , pp. 716-721
    • Olesen, O.F.1
  • 50
    • 0028593606 scopus 로고
    • Monoclonal antibody PHF-1 recognizes tau protein phosphorylated at serine residues 396 and 404
    • Otvos L. Jr., Feiner L., Lang E., Szendrei G. I., Goedert M., and Lee V. M.-Y. (1994) Monoclonal antibody PHF-1 recognizes tau protein phosphorylated at serine residues 396 and 404. J. Neurosci. Res. 39, 669-673.
    • (1994) J. Neurosci. Res. , vol.39 , pp. 669-673
    • Otvos Jr., L.1    Feiner, L.2    Lang, E.3    Szendrei, G.I.4    Goedert, M.5    Lee, V.M.-Y.6
  • 51
    • 0023931692 scopus 로고
    • Intraneuronal and extraneuronal neurofibrillary tangles exhibit mutually exclusive cytoskeletal antigens
    • Schmidt M. L., Gur R. E., Gur R. C., and Trojanowski J. Q. (1988) Intraneuronal and extraneuronal neurofibrillary tangles exhibit mutually exclusive cytoskeletal antigens. Ann. Neurol. 23, 184-189.
    • (1988) Ann. Neurol. , vol.23 , pp. 184-189
    • Schmidt, M.L.1    Gur, R.E.2    Gur, R.C.3    Trojanowski, J.Q.4
  • 52
    • 0026584008 scopus 로고
    • Autophagy and other vacuolar protein degradation mechanisms
    • Seglen P. O. and Bohley P. (1992) Autophagy and other vacuolar protein degradation mechanisms. Experientia 48, 158-172.
    • (1992) Experientia , vol.48 , pp. 158-172
    • Seglen, P.O.1    Bohley, P.2
  • 54
    • 0028157916 scopus 로고
    • Increased production of paired helical filament epitopes in a cell culture system reduces the turnover of τ
    • Vincent I., Rosado M., Kim E., and Davies P. (1994) Increased production of paired helical filament epitopes in a cell culture system reduces the turnover of τ. J. Neurochem. 62, 715-723.
    • (1994) J. Neurochem. , vol.62 , pp. 715-723
    • Vincent, I.1    Rosado, M.2    Kim, E.3    Davies, P.4
  • 55
    • 0029874767 scopus 로고    scopus 로고
    • Specific processing of native and phosphorylated τ protein by proteases
    • Wang X., An S., and Wu J. M. (1996) Specific processing of native and phosphorylated τ protein by proteases. Biochem. Biophys. Res. Commun. 219, 591-597.
    • (1996) Biochem. Biophys. Res. Commun. , vol.219 , pp. 591-597
    • Wang, X.1    An, S.2    Wu, J.M.3
  • 56
    • 0019462155 scopus 로고
    • Immunocytochemical localization of cathepsin D in rat neural tissue
    • Whitaker J. N., Terry L. C., and Whetsell W. O. Jr. (1981) Immunocytochemical localization of cathepsin D in rat neural tissue. Brain Res. 216, 109-124.
    • (1981) Brain Res. , vol.216 , pp. 109-124
    • Whitaker, J.N.1    Terry, L.C.2    Whetsell Jr., W.O.3
  • 57
    • 0026755755 scopus 로고
    • Alzheimer-like paired helical filaments and antiparallel dimers formed from microtubule-associated protein tau in vitro
    • Wille H., Drewes G., Biernat J., Mandelkow E.-M., and Mandelkow E. (1992) Alzheimer-like paired helical filaments and antiparallel dimers formed from microtubule-associated protein tau in vitro. J. Cell Biol. 118, 573-584.
    • (1992) J. Cell Biol. , vol.118 , pp. 573-584
    • Wille, H.1    Drewes, G.2    Biernat, J.3    Mandelkow, E.-M.4    Mandelkow, E.5
  • 59
    • 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
  • 60
    • 0027237861 scopus 로고
    • τ in paired helical filaments is functionally distinct from fetal τ: Assembly incompetence of paired helical filament-τ
    • Yoshida H. and Ihara Y. (1993) τ in paired helical filaments is functionally distinct from fetal τ: assembly incompetence of paired helical filament-τ. J. Neurochem. 61, 1183-1186.
    • (1993) J. Neurochem. , vol.61 , pp. 1183-1186
    • Yoshida, H.1    Ihara, Y.2


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