메뉴 건너뛰기




Volumn 55, Issue 9, 1996, Pages 954-963

α-Calcium-Calmodulin-Dependent Kinase II is Associated with Paired Helical Filaments of Alzheimer's Disease

Author keywords

Alzheimer's disease; Kinases; Paired helical filaments; calmodulin dependent kinase II

Indexed keywords

CALMODULIN DEPENDENT PROTEIN KINASE II; CALMODULIN-DEPENDENT PROTEIN KINASE II; NEUROFILAMENT PROTEIN; PROTEIN KINASE (CALCIUM,CALMODULIN);

EID: 0030239827     PISSN: 00223069     EISSN: None     Source Type: Journal    
DOI: 10.1097/00005072-199609000-00002     Document Type: Article
Times cited : (46)

References (56)
  • 1
    • 0026231697 scopus 로고
    • Neurofibrillary tangles and β-amyloid deposits in Alzheimer's disease
    • Goedert M, Sisodia SS, Price DL. Neurofibrillary tangles and β-amyloid deposits in Alzheimer's disease. Cur Opin Neurobiol 1991;1:441-47
    • (1991) Cur Opin Neurobiol , vol.1 , pp. 441-447
    • Goedert, M.1    Sisodia, S.S.2    Price, D.L.3
  • 2
    • 0025753852 scopus 로고
    • The molecular pathology of Alzheimer's disease
    • Selkoe D. The molecular pathology of Alzheimer's disease. Neuron 1991;6:487-98
    • (1991) Neuron , vol.6 , pp. 487-498
    • Selkoe, D.1
  • 3
    • 0025904444 scopus 로고
    • A68: A major subunit of paired helical filaments and derivatized forms of normal tau
    • Lee VMY, Balin BJ, Otvos L, Trojanowski JQ. A68: A major subunit of paired helical filaments and derivatized forms of normal tau. Science 1991;251:675-78
    • (1991) Science , vol.251 , pp. 675-678
    • Lee, V.M.Y.1    Balin, B.J.2    Otvos, L.3    Trojanowski, J.Q.4
  • 4
    • 0025772021 scopus 로고
    • Molecular characterization of microtubule-associated proteins tau and MAP2
    • Goedert M, Crowther RA, Garner CC. Molecular characterization of microtubule-associated proteins tau and MAP2. TINS 1991;5:193-99
    • (1991) TINS , vol.5 , pp. 193-199
    • Goedert, M.1    Crowther, R.A.2    Garner, C.C.3
  • 5
    • 0027420369 scopus 로고
    • Tau and the neurofibrillary pathology of Alzheimer's disease
    • Goedert M. Tau and the neurofibrillary pathology of Alzheimer's disease. TINS 1993;16:460-66
    • (1993) TINS , vol.16 , pp. 460-466
    • Goedert, M.1
  • 6
    • 0026046950 scopus 로고
    • Tau protein binds to microtubules through a flexible array of distributed weak sites
    • Butner KA, Kirshner MW. Tau protein binds to microtubules through a flexible array of distributed weak sites. J Cell Biol 1991;115:717-30
    • (1991) J Cell Biol , vol.115 , pp. 717-730
    • Butner, K.A.1    Kirshner, M.W.2
  • 7
    • 0026595846 scopus 로고
    • Tau proteins of Alzheimer paired helical filaments: Abnormal phosphorylation of all six brain isoforms
    • Goedert M, Spillantini MG, Cairns NJ, Crowther RA. Tau proteins of Alzheimer paired helical filaments: Abnormal phosphorylation of all six brain isoforms. Neuron 1992;8:159-68
    • (1992) Neuron , vol.8 , pp. 159-168
    • Goedert, M.1    Spillantini, M.G.2    Cairns, N.J.3    Crowther, R.A.4
  • 8
    • 0028350740 scopus 로고
    • Dephosphorylation of microtubule-associated protein tau by protein phosphatase-1 and -2C and its implication in Alzheimer disease
    • Gong C-X, Grundke-Iqbal I, Damuni Z, Iqbal K. Dephosphorylation of microtubule-associated protein tau by protein phosphatase-1 and -2C and its implication in Alzheimer disease. FEBS Letts 1994;341:94-98
    • (1994) FEBS Letts , vol.341 , pp. 94-98
    • Gong, C.-X.1    Grundke-Iqbal, I.2    Damuni, Z.3    Iqbal, K.4
  • 9
    • 0027376632 scopus 로고
    • Tau as a marker for Alzheimer's disease
    • Mandelkow EM, Mandelkow E. Tau as a marker for Alzheimer's disease. TIBS 1993;18:480-83
    • (1993) TIBS , vol.18 , pp. 480-483
    • Mandelkow, E.M.1    Mandelkow, E.2
  • 10
    • 0026941497 scopus 로고
    • The disordered neuronal cytoskeleton in Alzheimer's disease
    • Lee VMY, Trojanowski JQ. The disordered neuronal cytoskeleton in Alzheimer's disease. Curr Opin Neurobiol 1992;2:653-56
    • (1992) Curr Opin Neurobiol , vol.2 , pp. 653-656
    • Lee, V.M.Y.1    Trojanowski, J.Q.2
  • 11
    • 0027361281 scopus 로고
    • Microtubule-associated protein tau: Abnormal phosphorylation of a non-paired helical filament pool in Alzheimer disease
    • Kopke E, Tung Y-C, Shaikh S, Alonso AC, Iqbal K, Grundke-Iqbal I. Microtubule-associated protein tau: Abnormal phosphorylation of a non-paired helical filament pool in Alzheimer disease. J Biol Chem 1993;268:24374-78
    • (1993) J Biol Chem , vol.268 , pp. 24374-24378
    • Kopke, E.1    Tung, Y.-C.2    Shaikh, S.3    Alonso, A.C.4    Iqbal, K.5    Grundke-Iqbal, I.6
  • 13
    • 0027217679 scopus 로고
    • The abnormal phosphorylation of tau protein at ser-202 in Alzheimer's disease recapitulates phosphorylation during development
    • Goedert M, Jakes R, Crowther RA, et al. The abnormal phosphorylation of tau protein at ser-202 in Alzheimer's disease recapitulates phosphorylation during development. Proc Natl Acad Sci 1993;90:5066-70
    • (1993) Proc Natl Acad Sci , vol.90 , pp. 5066-5070
    • Goedert, M.1    Jakes, R.2    Crowther, R.A.3
  • 14
    • 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 ES, Shin RW, Billingsley ML, et al. Biopsy-derived adult human brain tau is phosphorylated at many of the same sites as Alzheimer's disease paired helical filament tau. Neuron 1994;13:989-102
    • (1994) Neuron , vol.13 , pp. 989-1102
    • Matsuo, E.S.1    Shin, R.W.2    Billingsley, M.L.3
  • 15
    • 0021338217 scopus 로고
    • Phosphorylation affects the ability of tau protein to promote microtubule assembly
    • Lindwall G, Cole RD. Phosphorylation affects the ability of tau protein to promote microtubule assembly. J Biol Chem 1984;259:5301-5
    • (1984) J Biol Chem , vol.259 , pp. 5301-5305
    • Lindwall, G.1    Cole, R.D.2
  • 16
    • 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, Jakes R. Expression of separate isoforms of human tau protein: Correlation with the tau pattern in brain and effects on tubulin polymerization. EMBO J 1990;9:4225-30
    • (1990) EMBO J , vol.9 , pp. 4225-4230
    • Goedert, M.1    Jakes, R.2
  • 17
    • 0028227962 scopus 로고
    • Role of abnormally phosphorylated tau in the breakdown of microtubules in Alzheimer disease
    • Alonso A, Zaidi T, Grundke-Iqbal I, Iqbal K. Role of abnormally phosphorylated tau in the breakdown of microtubules in Alzheimer disease. Proc Natl Acad Sci 1994;91:5562-66
    • (1994) Proc Natl Acad Sci , vol.91 , pp. 5562-5566
    • Alonso, A.1    Zaidi, T.2    Grundke-Iqbal, I.3    Iqbal, K.4
  • 18
    • 0027308924 scopus 로고
    • Abnormal tau phosphorylation at ser396 in Alzheimer's disease recapitulates development and contributes to reduced microtubule binding
    • Bramblett GT, Goedert M, Jakes R, Merrick SE, Trojanowski JQ, Lee VMY. Abnormal tau phosphorylation at ser396 in Alzheimer's disease recapitulates development and contributes to reduced microtubule binding. Neuron 1993;10:1089-99
    • (1993) Neuron , vol.10 , pp. 1089-1099
    • Bramblett, G.T.1    Goedert, M.2    Jakes, R.3    Merrick, S.E.4    Trojanowski, J.Q.5    Lee, V.M.Y.6
  • 19
    • 0026683725 scopus 로고
    • The Alzheimer-like phosphorylation of tau protein reduces microtubule binding and involves Ser-Pro and Thr-Pro motifs
    • Gustke A, Steiner B, Mandelkow EM, et al. The Alzheimer-like phosphorylation of tau protein reduces microtubule binding and involves Ser-Pro and Thr-Pro motifs. FEBS Letts 1992;307:199-205
    • (1992) FEBS Letts , vol.307 , pp. 199-205
    • Gustke, A.1    Steiner, B.2    Mandelkow, E.M.3
  • 20
    • 0023630392 scopus 로고
    • Phosphorylation of tau proteins to a state like that in Alzheimer's brain is catalyzed by a calcium/calmodulin-dependent kinase and modulated by phospholipids
    • Baudier J, Cole DR. Phosphorylation of tau proteins to a state like that in Alzheimer's brain is catalyzed by a calcium/calmodulin-dependent kinase and modulated by phospholipids. J Biol Chem 1987;262:17577-83
    • (1987) J Biol Chem , vol.262 , pp. 17577-17583
    • Baudier, J.1    Cole, D.R.2
  • 21
    • 0025013270 scopus 로고
    • Phosphorylation of microtubule-associated protein tau: Identification of the site for Ca2+-calmodulin dependent kinase and relationship with tau phosphorylation in Alzheimer's tangles
    • Steiner B, Mandelkow EM, Biernat J, et al. Phosphorylation of microtubule-associated protein tau: Identification of the site for Ca2+-calmodulin dependent kinase and relationship with tau phosphorylation in Alzheimer's tangles. EMBO J 1990;9:3539-44
    • (1990) EMBO J , vol.9 , pp. 3539-3544
    • Steiner, B.1    Mandelkow, E.M.2    Biernat, J.3
  • 22
    • 0028897322 scopus 로고
    • Modulation of GSK-3-catalyzed phosphorylation of microtubule-associated protein tau by non-proline-dependent protein kinases
    • Singh TJ, Zaidi T, Grundke-Iqbal I, Iqbal K. Modulation of GSK-3-catalyzed phosphorylation of microtubule-associated protein tau by non-proline-dependent protein kinases. FEBS Letts 1995;358:4-8
    • (1995) FEBS Letts , vol.358 , pp. 4-8
    • Singh, T.J.1    Zaidi, T.2    Grundke-Iqbal, I.3    Iqbal, K.4
  • 23
    • 0028967378 scopus 로고
    • Rapid Alzheimer-like phosphorylation of tau by the synergistic actions of nonproline-dependent protein kinases and GSK-3
    • Singh TJ, Haque N, Grundke-Iqbal I, Iqbal K. Rapid Alzheimer-like phosphorylation of tau by the synergistic actions of nonproline-dependent protein kinases and GSK-3. FEBS Letts 1995;358:267-72
    • (1995) FEBS Letts , vol.358 , pp. 267-272
    • Singh, T.J.1    Haque, N.2    Grundke-Iqbal, I.3    Iqbal, K.4
  • 24
    • 0026549985 scopus 로고
    • Mitogen activated protein (MAP) kinase transforms tau protein into an Alzheimer-like state
    • Drews G, Lichtenberg-Kraag B, Doring F, et al. Mitogen activated protein (MAP) kinase transforms tau protein into an Alzheimer-like state. EMBO J 1992;11:2131-38
    • (1992) EMBO J , vol.11 , pp. 2131-2138
    • Drews, G.1    Lichtenberg-Kraag, B.2    Doring, F.3
  • 25
    • 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 Comm 1993;193:639-47
    • (1993) Biochem Biophys Res Comm , vol.193 , pp. 639-647
    • Roder, H.M.1    Eden, P.A.2    Ingram, V.M.3
  • 26
    • 0026784416 scopus 로고
    • P42 MAP kinase phosphorylation sites in microtubule-associated protein tau are dephosphorylated by protein phosphatase 2A1. Implications for Alzheimer's disease
    • Goedert M, Cohen ES, Jakes R, Cohen P. p42 MAP kinase phosphorylation sites in microtubule-associated protein tau are dephosphorylated by protein phosphatase 2A1. Implications for Alzheimer's disease. FEBS Letts 1992;312:95-99
    • (1992) FEBS Letts , vol.312 , pp. 95-99
    • Goedert, M.1    Cohen, E.S.2    Jakes, R.3    Cohen, P.4
  • 28
    • 0026619584 scopus 로고
    • Gylcogen synthase kinase-3 and the Alzheimer-like state of microtubule-associated protein tau
    • Mandelkow EM, Drews G, Biernat J, et al. Gylcogen synthase kinase-3 and the Alzheimer-like state of microtubule-associated protein tau. FEBS Letts 1992;314:315-21
    • (1992) FEBS Letts , vol.314 , pp. 315-321
    • Mandelkow, E.M.1    Drews, G.2    Biernat, J.3
  • 29
    • 0026487365 scopus 로고
    • Glycogen synthase kinase-3 induces Alzheimer's disease-like phosphorylation of tau: Generation of paired helical filament epitopes and neuronal localization of the kinase
    • Hanger DP, Hughes K, Woodgett JR, Brion JP, Anderton BH. Glycogen synthase kinase-3 induces Alzheimer's disease-like phosphorylation of tau: Generation of paired helical filament epitopes and neuronal localization of the kinase. Neurosci Letts 1992;147:58-62
    • (1992) Neurosci Letts , vol.147 , pp. 58-62
    • Hanger, D.P.1    Hughes, K.2    Woodgett, J.R.3    Brion, J.P.4    Anderton, B.H.5
  • 30
    • 0026731425 scopus 로고
    • Tau protein kinase I converts normal tau protein into A68-like component of paired helical filaments
    • Ishiguro K, Takamatsu M, Tomizawa K, et al. Tau protein kinase I converts normal tau protein into A68-like component of paired helical filaments. J Biol Chem 1992;267:10897-10901
    • (1992) J Biol Chem , vol.267 , pp. 10897-10901
    • Ishiguro, K.1    Takamatsu, M.2    Tomizawa, K.3
  • 31
    • 0027338266 scopus 로고
    • Phosphorylation of ser262 strongly reduces binding of tau to microtubules: Distinction between PHF-like immunoreactivity and microtubule binding
    • Biernat J, Gustke N, Drews G, Mandelkow EM, Mandelkow E. Phosphorylation of ser262 strongly reduces binding of tau to microtubules: Distinction between PHF-like immunoreactivity and microtubule binding. Neuron 1993;11:153-63
    • (1993) Neuron , vol.11 , pp. 153-163
    • Biernat, J.1    Gustke, N.2    Drews, G.3    Mandelkow, E.M.4    Mandelkow, E.5
  • 32
    • 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 EM, Mandelkow E. Alzheimer-like paired helical filaments and antiparallel dimers formed from microtubule-associated protein tau in vitro. J Cell Biol 1992;118:573-84
    • (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
  • 33
    • 0026799198 scopus 로고
    • The microtubule binding repeats of tau protein assemble into filaments like those found in Alzheimer's disease
    • Crowther RA, Olesen OF, Jakes R, Goedert M. The microtubule binding repeats of tau protein assemble into filaments like those found in Alzheimer's disease. FEBS Letts 1992;309:199-202
    • (1992) FEBS Letts , vol.309 , pp. 199-202
    • Crowther, R.A.1    Olesen, O.F.2    Jakes, R.3    Goedert, M.4
  • 34
    • 0026521716 scopus 로고
    • A protein kinase associated with paired helical filaments in Alzheimer's disease
    • Vincent IJ, Davies P. A protein kinase associated with paired helical filaments in Alzheimer's disease. Proc Natl Acad Sci 1992;89:2878-82
    • (1992) Proc Natl Acad Sci , vol.89 , pp. 2878-2882
    • Vincent, I.J.1    Davies, P.2
  • 35
    • 0028878537 scopus 로고
    • Detection of a cdc2-related kinase associated with Alzheimer paired helical filaments
    • Liu WK, Williams RT, Hall FL, Dickson DW, Yen SH. Detection of a cdc2-related kinase associated with Alzheimer paired helical filaments. Amer J Pathol 1995;146:228-38
    • (1995) Amer J Pathol , vol.146 , pp. 228-238
    • Liu, W.K.1    Williams, R.T.2    Hall, F.L.3    Dickson, D.W.4    Yen, S.H.5
  • 36
    • 0026742451 scopus 로고
    • Impaired spatial learning in α-calcium-calmodulin kinase II mutant mice
    • Silva A, Paylor R, Wehner JM, Tonegawa S. Impaired spatial learning in α-calcium-calmodulin kinase II mutant mice. Science 1992;257:206-11
    • (1992) Science , vol.257 , pp. 206-211
    • Silva, A.1    Paylor, R.2    Wehner, J.M.3    Tonegawa, S.4
  • 37
    • 0026637195 scopus 로고
    • Deficient hippocampal long-term potentiation in α-calcium-calmodulin kinase II mutant mice
    • Silva AJ, Stevens CF, Tonegawa S, Wang Y. Deficient hippocampal long-term potentiation in α-calcium-calmodulin kinase II mutant mice. Science 1992;257:201-6
    • (1992) Science , vol.257 , pp. 201-206
    • Silva, A.J.1    Stevens, C.F.2    Tonegawa, S.3    Wang, Y.4
  • 38
    • 0025292866 scopus 로고
    • A preparation of Alzheimer paired helical filaments that displays distinct T proteins by polyacrylamide gel electrophoresis
    • Greenberg SG, Davies P. A preparation of Alzheimer paired helical filaments that displays distinct T proteins by polyacrylamide gel electrophoresis. Proc Natl Acad Sci 1990;87:5827-31
    • (1990) Proc Natl Acad Sci , vol.87 , pp. 5827-5831
    • Greenberg, S.G.1    Davies, P.2
  • 39
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (Lond) 1970;227:680-85
    • (1970) Nature (Lond) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 40
    • 0028208253 scopus 로고
    • Identification and characterization of a novel (115 kDa) neurofilament-associated kinase
    • Xiao J, Monteiro MJ. Identification and characterization of a novel (115 kDa) neurofilament-associated kinase. J Neuroscience 1994;14:1820-33
    • (1994) J Neuroscience , vol.14 , pp. 1820-1833
    • Xiao, J.1    Monteiro, M.J.2
  • 41
    • 0019800463 scopus 로고
    • Silver stain for proteins in polyacrylamide gels: A modified procedure with enhanced uniform sensitivity
    • Morrissey JH. Silver stain for proteins in polyacrylamide gels: A modified procedure with enhanced uniform sensitivity. Anal Biochem 1981;117:307-10
    • (1981) Anal Biochem , vol.117 , pp. 307-310
    • Morrissey, J.H.1
  • 42
    • 0027984739 scopus 로고
    • Epitope mapping of monoclonal antibodies to the paired helical filaments of Alzheimer's disease: Identification of phosphorylation sites in tau protein
    • Goedert M, Jakes R, Crowther A, Cohen P, Vanmechelen E, Vandermeeren M, Crass P. Epitope mapping of monoclonal antibodies to the paired helical filaments of Alzheimer's disease: Identification of phosphorylation sites in tau protein. Biochem J 1994;301:871-77
    • (1994) Biochem J , vol.301 , pp. 871-877
    • Goedert, M.1    Jakes, R.2    Crowther, A.3    Cohen, P.4    Vanmechelen, E.5    Vandermeeren, M.6    Crass, P.7
  • 44
    • 0028361291 scopus 로고
    • A new kinesinlike protein (Klp1) localizes to a single microtubule of the Chlamydomonas flagellum
    • Bernstein M, Beech PL, Katz SG, Rosenbaum JL. A new kinesinlike protein (Klp1) localizes to a single microtubule of the Chlamydomonas flagellum. J Cell Biol 1994;125:1313-26
    • (1994) J Cell Biol , vol.125 , pp. 1313-1326
    • Bernstein, M.1    Beech, P.L.2    Katz, S.G.3    Rosenbaum, J.L.4
  • 46
    • 0029913235 scopus 로고    scopus 로고
    • Resolution of kinase activities during the HeLa cell cycle: Identification of kinases with cyclic activities
    • Monteiro MJ, Mical T. Resolution of kinase activities during the HeLa cell cycle: Identification of kinases with cyclic activities. Exp Cell Res 1996;223:443-51
    • (1996) Exp Cell Res , vol.223 , pp. 443-451
    • Monteiro, M.J.1    Mical, T.2
  • 47
    • 0025014874 scopus 로고
    • Hippocampal neurons predisposed to neuroflbrillary tangle formation are enriched in type II calcium/calmodulin-dependent protein kinase
    • McKee A, Kosik KS, Kennedy MB, Kowall NW. Hippocampal neurons predisposed to neuroflbrillary tangle formation are enriched in type II calcium/calmodulin-dependent protein kinase. J Neuropath Exp Neurol 1990;49:49-63
    • (1990) J Neuropath Exp Neurol , vol.49 , pp. 49-63
    • McKee, A.1    Kosik, K.S.2    Kennedy, M.B.3    Kowall, N.W.4
  • 48
    • 0028142015 scopus 로고
    • Calcium/calmodulin-dependent protein kinase II immunostaining is preserved in Alzheimer's disease hippocampal neurons
    • Simonian NA, Elvhage T, Czernik AJ, Greengard P, Hyman BT. Calcium/calmodulin-dependent protein kinase II immunostaining is preserved in Alzheimer's disease hippocampal neurons. Brain Research 1994;657:294-99
    • (1994) Brain Research , vol.657 , pp. 294-299
    • Simonian, N.A.1    Elvhage, T.2    Czernik, A.J.3    Greengard, P.4    Hyman, B.T.5
  • 49
    • 0028785525 scopus 로고
    • Interaction of tau with the neural plasma membrane mediated by tau's amino-terminal projection domain
    • Brandt R, Leger J, Lee, G. Interaction of tau with the neural plasma membrane mediated by tau's amino-terminal projection domain. J Cell Biol 1995;131:1327-40
    • (1995) J Cell Biol , vol.131 , pp. 1327-1340
    • Brandt, R.1    Leger, J.2    Lee, G.3
  • 50
    • 0027586519 scopus 로고
    • 2+/calmodulin-dependent protein kinases
    • 2+/calmodulin-dependent protein kinases. Curr Opin Cell Biol 1993;5:247-53
    • (1993) Curr Opin Cell Biol , vol.5 , pp. 247-253
    • Schulman, H.1
  • 52
    • 0028579743 scopus 로고
    • Potentiated transmission and prevention of further LTP by increased CaMKII activity in postsynaptic hippocampal slice neurons
    • Pettit DL, Perlman S, Malinow R. Potentiated transmission and prevention of further LTP by increased CaMKII activity in postsynaptic hippocampal slice neurons. Science 1994;266:1881-85
    • (1994) Science , vol.266 , pp. 1881-1885
    • Pettit, D.L.1    Perlman, S.2    Malinow, R.3
  • 53
    • 0028031221 scopus 로고
    • The CaM kinase II hypothesis for the storage of synaptic memory
    • Lisman J. The CaM kinase II hypothesis for the storage of synaptic memory. Trends Neurosci 1994;17:406-12
    • (1994) Trends Neurosci , vol.17 , pp. 406-412
    • Lisman, J.1
  • 54
    • 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 EM, Mandelkow E. Tau protein becomes long and stiff upon phosphorylation: Correlation between paracrystalline structure and degree of phosphorylation. J Cell Biol 1989;109:1643-51
    • (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
  • 56
    • 0024358172 scopus 로고
    • A sensitive method for detection of calmodulin-dependent protein kinase II activity in sodium dodecyl sulfate-polyacrylamide gel
    • Kameshita I, Fujisawa H. A sensitive method for detection of calmodulin-dependent protein kinase II activity in sodium dodecyl sulfate-polyacrylamide gel. Anal Biochem 1989;183:139-43
    • (1989) Anal Biochem , vol.183 , pp. 139-143
    • Kameshita, I.1    Fujisawa, H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.