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Volumn 151, Issue 4, 1997, Pages 1115-1122

Role of glycosaminoglycans in determining the helicity of paired helical filaments

Author keywords

[No Author keywords available]

Indexed keywords

GLYCOSAMINOGLYCAN; HEPARIN; TAU PROTEIN;

EID: 1842415999     PISSN: 00029440     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (70)

References (47)
  • 1
    • 0026740795 scopus 로고
    • Neurofibrillary tangles but not senile plaques parallel duration and severity of Alzheimer's disease
    • Arriagada PV, Growdon JH, Hedley-White T, Hyman BT: Neurofibrillary tangles but not senile plaques parallel duration and severity of Alzheimer's disease. Neurology 1992, 42:631-639
    • (1992) Neurology , vol.42 , pp. 631-639
    • Arriagada, P.V.1    Growdon, J.H.2    Hedley-White, T.3    Hyman, B.T.4
  • 2
    • 37049048544 scopus 로고
    • Paired helical filaments in electron microscopy of Alzheimer's disease
    • Kidd M: Paired helical filaments in electron microscopy of Alzheimer's disease. Nature 1963, 197:192-193
    • (1963) Nature , vol.197 , pp. 192-193
    • Kidd, M.1
  • 3
    • 0030049915 scopus 로고    scopus 로고
    • Filament heterogeneity within the dystrophic neurites of senile plaques suggests blockage of fast axonal transport in Alzheimer's disease
    • Praprotnik D, Smith MA, Richey PL, Vinters HV, Perry G: Filament heterogeneity within the dystrophic neurites of senile plaques suggests blockage of fast axonal transport in Alzheimer's disease. Acta Neuropathol 1996, 91:226-235
    • (1996) Acta Neuropathol , vol.91 , pp. 226-235
    • Praprotnik, D.1    Smith, M.A.2    Richey, P.L.3    Vinters, H.V.4    Perry, G.5
  • 4
    • 0028223431 scopus 로고
    • Twisted ribbon structure of paired helical filaments revealed by atomic force microscopy
    • Pollanen MS, Markiewicz P, Bergeron C, Goh MC: Twisted ribbon structure of paired helical filaments revealed by atomic force microscopy. Am J Pathol 1994, 144:869-873
    • (1994) Am J Pathol , vol.144 , pp. 869-873
    • Pollanen, M.S.1    Markiewicz, P.2    Bergeron, C.3    Goh, M.C.4
  • 5
    • 0027413656 scopus 로고
    • Tau protein and paired helical filaments of Alzheimer's disease
    • Crowther RA: Tau protein and paired helical filaments of Alzheimer's disease. Curr Opin Struct Biol 1993, 3:202-206
    • (1993) Curr Opin Struct Biol , vol.3 , pp. 202-206
    • Crowther, R.A.1
  • 6
    • 0022257253 scopus 로고
    • Mise en evidence immunologique de la proteine tau an niveau des lesions de degenerescence neurofibrillaire de la maladie d'Alzheimer
    • Brion J-P, Passareiro H, Nunez J, Flament-Durand J: Mise en evidence immunologique de la proteine tau an niveau des lesions de degenerescence neurofibrillaire de la maladie d'Alzheimer. Arch Biol 1985, 95:229-235
    • (1985) Arch Biol , vol.95 , pp. 229-235
    • Brion, J.-P.1    Passareiro, H.2    Nunez, J.3    Flament-Durand, J.4
  • 8
    • 0022724941 scopus 로고
    • Phosphorylated tau protein is integrated into paired helical filaments in Alzheimer's disease
    • Tokyo
    • Ihara Y, Nukina N, Miura R, Ogawara M: Phosphorylated tau protein is integrated into paired helical filaments in Alzheimer's disease. J Biochem (Tokyo) 1986, 99:1807-1810
    • (1986) J Biochem , vol.99 , pp. 1807-1810
    • Ihara, Y.1    Nukina, N.2    Miura, R.3    Ogawara, M.4
  • 9
    • 0009364134 scopus 로고
    • Microtubule-associated protein tau is a major antigenic component of paired helical filaments in Alzheimer disease
    • Kosik KS, Joachim CL, Selkoe DJ: Microtubule-associated protein tau is a major antigenic component of paired helical filaments in Alzheimer disease. Proc Natl Acad Sci USA 1986, 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
  • 10
    • 0023690545 scopus 로고
    • Tau factor polymers are similar to paired helical filaments of Alzheimer's disease
    • Montejo de Garcini E, Carrascosa JL, Correas I, Nieto A, Avila J: Tau factor polymers are similar to paired helical filaments of Alzheimer's disease. FEBS Lett 1988, 236:150-154
    • (1988) FEBS Lett , vol.236 , pp. 150-154
    • Montejo De Garcini, E.1    Carrascosa, J.L.2    Correas, I.3    Nieto, A.4    Avila, J.5
  • 11
    • 0023687214 scopus 로고
    • A modified form of microtubule-associated tau protein is the main component of paired helical filaments
    • Nieto A, Correas I, Montejo de Garcini E, Avila J: A modified form of microtubule-associated tau protein is the main component of paired helical filaments. Biochem Biophys Res Commun 1988, 154:660-667
    • (1988) Biochem Biophys Res Commun , vol.154 , pp. 660-667
    • Nieto, A.1    Correas, I.2    Montejo De Garcini, E.3    Avila, J.4
  • 13
    • 1842685948 scopus 로고
    • Neurofibrillary tangles of Alzheimer disease share antigenic determinants with the axonal microtubule-associated protein tau
    • Wood JG, Mirra SS, Pollock NJ, Binder LI: Neurofibrillary tangles of Alzheimer disease share antigenic determinants with the axonal microtubule-associated protein tau. Proc Natl Acad Sci USA 1986, 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
  • 14
    • 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 Lett 1992, 309:199-202
    • (1992) FEBS Lett , vol.309 , pp. 199-202
    • Crowther, R.A.1    Olesen, O.F.2    Jakes, R.3    Goedert, M.4
  • 16
    • 0027184294 scopus 로고
    • Transglutaminase catalyzes the formation of sodium dodecyl sulphate-insoluble, Alz-50-reactive polymers of τ
    • Dudek S, Johnson GW: Transglutaminase catalyzes the formation of sodium dodecyl sulphate-insoluble, Alz-50-reactive polymers of τ. J Neurochem 1993, 61:1159-1162
    • (1993) J Neurochem , vol.61 , pp. 1159-1162
    • Dudek, S.1    Johnson, G.W.2
  • 17
    • 0022917474 scopus 로고
    • Self assembly of microtubule associated protein tau into filaments resembling those found in Alzheimer disease
    • Montejo de Garcini E, Serrano L, Avila J: Self assembly of microtubule associated protein tau into filaments resembling those found in Alzheimer disease. Biochem Biophys Res Commun 1986, 141:790-796
    • (1986) Biochem Biophys Res Commun , vol.141 , pp. 790-796
    • Montejo De Garcini, E.1    Serrano, L.2    Avila, J.3
  • 18
    • 0028850374 scopus 로고
    • Stable expression of apolipoprotein ApoE3 and ApoE4 in mouse neuroblastoma cells produces differential effects on neurite outgrowth
    • Bellosta S, Nathan BP, Orth M, Dong LM, Mahley RW, Pitas RE: Stable expression of apolipoprotein ApoE3 and ApoE4 in mouse neuroblastoma cells produces differential effects on neurite outgrowth. J Biol Chem 1995, 270:27063-27071
    • (1995) J Biol Chem , vol.270 , pp. 27063-27071
    • Bellosta, S.1    Nathan, B.P.2    Orth, M.3    Dong, L.M.4    Mahley, R.W.5    Pitas, R.E.6
  • 19
    • 0023465163 scopus 로고
    • In vitro conditions for the self polymerization of the microtubule associated protein tau factor
    • Tokyo
    • Montejo E, Avila J: In vitro conditions for the self polymerization of the microtubule associated protein tau factor. J Biochem (Tokyo) 1987, 102:1415-1421
    • (1987) J Biochem , vol.102 , pp. 1415-1421
    • Montejo, E.1    Avila, J.2
  • 21
    • 0028826633 scopus 로고
    • Polymerization of microtubule-associated protein tau under near-physiological conditions
    • Wilson DM, Binder LI: Polymerization of microtubule-associated protein tau under near-physiological conditions. J Biol Chem 1995, 270: 24306-24314
    • (1995) J Biol Chem , vol.270 , pp. 24306-24314
    • Wilson, D.M.1    Binder, L.I.2
  • 22
    • 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, Mandelkow E: Alzheimer-like paired helical filaments and antiparallel dimers formed from microtubule-associated protein tau in vitro. J Cell Biol 1992, 188:573-584
    • (1992) J Cell Biol , vol.188 , pp. 573-584
    • Wille, H.1    Drewes, G.2    Biernat, J.3    Mandelkow, E.-M.4    Mandelkow, E.5
  • 23
    • 0025852163 scopus 로고
    • Structural stability of paired helical filaments requires microtubule-binding domains of tau: A model for self association
    • Ksiezak-Reding H, Yen SH: Structural stability of paired helical filaments requires microtubule-binding domains of tau: a model for self association. Neuron 1991, 6:717-728
    • (1991) Neuron , vol.6 , pp. 717-728
    • Ksiezak-Reding, H.1    Yen, S.H.2
  • 24
    • 0029796168 scopus 로고    scopus 로고
    • Polymerization of τ into filaments in the presence of heparin: The minimal sequence required for τ-τ interaction
    • Pérez M, Valpuesta JM, Medina M, Montejo de Garcini E, Avila J: Polymerization of τ into filaments in the presence of heparin: the minimal sequence required for τ-τ interaction. J Neurochem 1996, 67:1183-1190
    • (1996) J Neurochem , vol.67 , pp. 1183-1190
    • Pérez, M.1    Valpuesta, J.M.2    Medina, M.3    Montejo De Garcini, E.4    Avila, J.5
  • 25
    • 0027209456 scopus 로고
    • Chondroitin sulfate proteoglycans are associated with the lesions of Alzheimer's Disease
    • DeWitt DA, Silver J, Canning DR, Perry G: Chondroitin sulfate proteoglycans are associated with the lesions of Alzheimer's Disease. Exp Neurol 1993, 121:149-152
    • (1993) Exp Neurol , vol.121 , pp. 149-152
    • DeWitt, D.A.1    Silver, J.2    Canning, D.R.3    Perry, G.4
  • 26
    • 0029907548 scopus 로고    scopus 로고
    • Assembly of microtubule-associated protein tau into Alzheimer-like filaments induced by sulphated glycosaminoglycans
    • Goedert M, Jakes R, Spillantini MG, Hasegawa M Smith MJ, Crowther RA: Assembly of microtubule-associated protein tau into Alzheimer-like filaments induced by sulphated glycosaminoglycans. Nature 1996, 383:550-553
    • (1996) Nature , vol.383 , pp. 550-553
    • Goedert, M.1    Jakes, R.2    Spillantini, M.G.3    Hasegawa, M.4    Smith, M.J.5    Crowther, R.A.6
  • 28
    • 1842407866 scopus 로고
    • Mapping of paired helical filament proteins at molecular resolution
    • Perry G, Siedlak SL: Mapping of paired helical filament proteins at molecular resolution. J Neuropathol Exp Neurol 1992, 151:318
    • (1992) J Neuropathol Exp Neurol , vol.151 , pp. 318
    • Perry, G.1    Siedlak, S.L.2
  • 29
    • 0026468915 scopus 로고
    • Localization of heparan sulphate glycosaminoglycan and proteoglycan core protein in aged brain and Alzheimer's disease
    • Su JH, Cummings BJ, Cotman W: Localization of heparan sulphate glycosaminoglycan and proteoglycan core protein in aged brain and Alzheimer's disease. Neuroscience 1992, 51:801-813
    • (1992) Neuroscience , vol.51 , pp. 801-813
    • Su, J.H.1    Cummings, B.J.2    Cotman, W.3
  • 30
    • 0025875756 scopus 로고
    • Proteoglycans structures and interactions
    • Kjiellen L, Lindahl U: Proteoglycans structures and interactions. Annu Rev Biochem 1991, 60:443-475
    • (1991) Annu Rev Biochem , vol.60 , pp. 443-475
    • Kjiellen, L.1    Lindahl, U.2
  • 31
    • 0028213567 scopus 로고
    • A heparin-binding domain in the amyloid protein precursor of Alzheimer's disease is involved in the regulation of neurite outgrowth
    • Small DV, Nurcombe V, Reed G, Clarris H, Moir R, Beyreuther K, Masters CL: A heparin-binding domain in the amyloid protein precursor of Alzheimer's disease is involved in the regulation of neurite outgrowth. J Neurosci 1994, 14:2117-2127
    • (1994) J Neurosci , vol.14 , pp. 2117-2127
    • Small, D.V.1    Nurcombe, V.2    Reed, G.3    Clarris, H.4    Moir, R.5    Beyreuther, K.6    Masters, C.L.7
  • 32
    • 0024273721 scopus 로고
    • The presence of heparin sulfate proteoglycans in the neurite plaques and Congophilic angiopathy in Alzheimer's disease
    • Snow AD, Mar H, Nochlin D, Kimatak K, Suzuk S, Hassel J, Wight TN: The presence of heparin sulfate proteoglycans in the neurite plaques and Congophilic angiopathy in Alzheimer's disease. Am J Pathol 1988, 133:456-463
    • (1988) Am J Pathol , vol.133 , pp. 456-463
    • Snow, A.D.1    Mar, H.2    Nochlin, D.3    Kimatak, K.4    Suzuk, S.5    Hassel, J.6    Wight, T.N.7
  • 33
    • 0028082136 scopus 로고
    • An important role of heparan sulphate proteglycan (perlecan) in a model system of the deposition and persistence of fibrillar Aβ-amyloid in rat brain
    • Snow AD, Sekiguchi R, Nochlin D, Fraser P, Kimata K, Mizutani A, Aral M, Shreier WA, Morgan DG: An important role of heparan sulphate proteglycan (perlecan) in a model system of the deposition and persistence of fibrillar Aβ-amyloid in rat brain. Neuron 1994, 12:219-234
    • (1994) Neuron , vol.12 , pp. 219-234
    • Snow, A.D.1    Sekiguchi, R.2    Nochlin, D.3    Fraser, P.4    Kimata, K.5    Mizutani, A.6    Aral, M.7    Shreier, W.A.8    Morgan, D.G.9
  • 34
    • 0025292866 scopus 로고
    • A preparation of Alzheimer paired helical filaments that displays distinct tau proteins by polyacrylamide gel electrophoresis
    • Greenberg SC, Davies P: A preparation of Alzheimer paired helical filaments that displays distinct tau proteins by polyacrylamide gel electrophoresis. Proc Natl Acad Sci USA 1990, 87:5827-5831
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 5827-5831
    • Greenberg, S.C.1    Davies, P.2
  • 35
    • 0029018840 scopus 로고
    • The role of tau phosphorylation in transfected COS-1 cells
    • Medina M, Montejo de Garcini E, Avila J: The role of tau phosphorylation in transfected COS-1 cells. Mol Cell Biochem 1995, 148:79-88
    • (1995) Mol Cell Biochem , vol.148 , pp. 79-88
    • Medina, M.1    Montejo De Garcini, E.2    Avila, J.3
  • 36
    • 0029122946 scopus 로고
    • The macromolecular structure of type VI-collagen: Formation and stability of filaments
    • Kuo HJ, Knee DR, Glanville RW: The macromolecular structure of type VI-collagen: formation and stability of filaments. Eur J Biochem 1995, 232:364-372
    • (1995) Eur J Biochem , vol.232 , pp. 364-372
    • Kuo, H.J.1    Knee, D.R.2    Glanville, R.W.3
  • 38
    • 0029815467 scopus 로고    scopus 로고
    • Glycosylation of microtubule associated protein tau: An abnormal posttranslational modification in Alzheimer's disease
    • Wang J-Z, Grundke-Iqbal I, Iqbal K: Glycosylation of microtubule associated protein tau: an abnormal posttranslational modification in Alzheimer's disease. Nature Med 1996, 2:871-875
    • (1996) Nature Med , vol.2 , pp. 871-875
    • Wang, J.-Z.1    Grundke-Iqbal, I.2    Iqbal, K.3
  • 39
    • 0029999787 scopus 로고    scopus 로고
    • Alzheimer's disease hyperphosphorylated tau sequesters normal tau into tangles of filaments and disassembles microtubules
    • Alonso A, Grundke-Iqbal I, Iqbal K: Alzheimer's disease hyperphosphorylated tau sequesters normal tau into tangles of filaments and disassembles microtubules. Nature Med 1996, 2:783-789
    • (1996) Nature Med , vol.2 , pp. 783-789
    • Alonso, A.1    Grundke-Iqbal, I.2    Iqbal, K.3
  • 40
    • 0031012497 scopus 로고    scopus 로고
    • Abnormal phosphorylation of tau and the mechanism of Alzheimer neurofibrillary degeneration: Sequestration of microtubule-associated proteins 1 and 2 and the disassembly of microtubules by the abnormal tau
    • Alonso A, Grundke-Iqbal I, Barra HS, Iqbal K: Abnormal phosphorylation of tau and the mechanism of Alzheimer neurofibrillary degeneration: sequestration of microtubule-associated proteins 1 and 2 and the disassembly of microtubules by the abnormal tau. Proc Natl Acad Sci USA 1997, 94:298-303
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 298-303
    • Alonso, A.1    Grundke-Iqbal, I.2    Barra, H.S.3    Iqbal, K.4
  • 41
    • 0024584913 scopus 로고
    • Molecular modelling of protein glycosaminoglycans interactions
    • Cardin AD, Weintraub HJR: Molecular modelling of protein glycosaminoglycans interactions. Arteriosclerosis 1989, 9:38-32
    • (1989) Arteriosclerosis , vol.9 , pp. 38-132
    • Cardin, A.D.1    Weintraub, H.J.R.2
  • 42
    • 0024745894 scopus 로고
    • Multiple isoforms of human microtubule associated protein tau: Sequences and localization in neurofibrillary tangles of Alzheimer's disease
    • Goedert M, Spillantini MG, Jakes R, Rutherford D, Crowther RA: Multiple isoforms of human microtubule associated protein tau: sequences and localization in neurofibrillary tangles of Alzheimer's disease. Neuron 1989, 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
  • 43
    • 0028173897 scopus 로고
    • Structures and functions of multiligand lipoprotein receptors: Macrophage scavenger receptors and LDL receptor-related protein (LRP)
    • Krieger M, Herz J: Structures and functions of multiligand lipoprotein receptors: macrophage scavenger receptors and LDL receptor-related protein (LRP). Annu Rev Biochem 1994, 63:601-637
    • (1994) Annu Rev Biochem , vol.63 , pp. 601-637
    • Krieger, M.1    Herz, J.2
  • 44
    • 0029989760 scopus 로고    scopus 로고
    • The intracellular fate of apolipoprotein is tau dependent and apoE allele specific
    • Lovestone S, Anderton BH, Hartley K, Jensen TG, Jorgensen AL: The intracellular fate of apolipoprotein is tau dependent and apoE allele specific. Neuroreport 1996, 7:1005-1008
    • (1996) Neuroreport , vol.7 , pp. 1005-1008
    • Lovestone, S.1    Anderton, B.H.2    Hartley, K.3    Jensen, T.G.4    Jorgensen, A.L.5
  • 45
    • 0028822219 scopus 로고
    • Low density lipoprotein receptor-related protein mediates apolipoprotein E-dependent neurite outgrowth in a central nervous system-derived neural cell line
    • Holtzman DM, Pitas RE, Kilbridge J, Nathan B, Mahley RW, Bu G, Schwartz AL: Low density lipoprotein receptor-related protein mediates apolipoprotein E-dependent neurite outgrowth in a central nervous system-derived neural cell line. Proc Natl Acad Sci USA 1995, 92:9480-9484
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 9480-9484
    • Holtzman, D.M.1    Pitas, R.E.2    Kilbridge, J.3    Nathan, B.4    Mahley, R.W.5    Bu, G.6    Schwartz, A.L.7
  • 46
    • 0029128232 scopus 로고
    • LDL-receptor related protein, a multifunctional ApoE receptor, binds secreted β-amyloid precursor protein and mediates its degradation
    • Kounnas MZ, Moir RD, Rebeck GW, Bush AI, Argraves WS, Tanzi RE, Hyman BT, Strickland DK: LDL-receptor related protein, a multifunctional ApoE receptor, binds secreted β-amyloid precursor protein and mediates its degradation. Cell 1995, 82:331-340
    • (1995) Cell , vol.82 , pp. 331-340
    • Kounnas, M.Z.1    Moir, R.D.2    Rebeck, G.W.3    Bush, A.I.4    Argraves, W.S.5    Tanzi, R.E.6    Hyman, B.T.7    Strickland, D.K.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.