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Volumn 329, Issue 2, 2004, Pages 238-246

Electron microscopy as a quantitative method for investigating tau fibrillization

Author keywords

Adsorption; Amyloid; Fibrillization; Interfacial concentration; Microscopy; Tau

Indexed keywords

ADSORPTION; ELECTRON MICROSCOPES; ELECTRON MICROSCOPY; HYPERBOLIC FUNCTIONS; MICROSCOPIC EXAMINATION; NEURODEGENERATIVE DISEASES;

EID: 2542436215     PISSN: 00032697     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ab.2004.02.023     Document Type: Article
Times cited : (33)

References (47)
  • 2
    • 0034843039 scopus 로고    scopus 로고
    • Sequence of neurofibrillary changes in aging and Alzheimer's disease: A confocal study with phospho-tau antibody, AD2
    • Galvan M., David J.P., Delacourte A., Luna J., Mena R. Sequence of neurofibrillary changes in aging and Alzheimer's disease: a confocal study with phospho-tau antibody, AD2. J. Alzheimers Dis. 3:2001;417-425
    • (2001) J. Alzheimers Dis. , vol.3 , pp. 417-425
    • Galvan, M.1    David, J.P.2    Delacourte, A.3    Luna, J.4    Mena, R.5
  • 4
    • 0342368728 scopus 로고    scopus 로고
    • The extent of neurofibrillary pathology in perforant pathway neurons is the key determinant of dementia in the very old
    • Garcia-Sierra F., Hauw J.J., Duyckaerts C., Wischik C.M., Luna-Munoz J., Mena R. The extent of neurofibrillary pathology in perforant pathway neurons is the key determinant of dementia in the very old. Acta Neuropathol. (Berl.). 100:2000;29-35
    • (2000) Acta Neuropathol. (Berl.) , vol.100 , pp. 29-35
    • Garcia-Sierra, F.1    Hauw, J.J.2    Duyckaerts, C.3    Wischik, C.M.4    Luna-Munoz, J.5    Mena, R.6
  • 5
    • 0027502784 scopus 로고
    • Thioflavine T interaction with synthetic Alzheimer's disease beta-amyloid peptides: Detection of amyloid aggregation in solution
    • LeVine 3rd H. Thioflavine T interaction with synthetic Alzheimer's disease beta-amyloid peptides: detection of amyloid aggregation in solution. Protein Sci. 2:1993;404-410
    • (1993) Protein Sci. , vol.2 , pp. 404-410
    • Levine III, H.1
  • 6
    • 0032516493 scopus 로고    scopus 로고
    • Rapid assembly of Alzheimer-like paired helical filaments from microtubule-associated protein tau monitored by fluorescence in solution
    • Friedhoff P., Schneider A., Mandelkow E.M., Mandelkow E. Rapid assembly of Alzheimer-like paired helical filaments from microtubule-associated protein tau monitored by fluorescence in solution. Biochemistry. 37:1998;10223-10230
    • (1998) Biochemistry , vol.37 , pp. 10223-10230
    • Friedhoff, P.1    Schneider, A.2    Mandelkow, E.M.3    Mandelkow, E.4
  • 7
    • 9044229145 scopus 로고    scopus 로고
    • On the nucleation and growth of amyloid beta-protein fibrils: Detection of nuclei and quantitation of rate constants
    • Lomakin A., Chung D.S., Benedek G.B., Kirschner D.A., Teplow D.B. On the nucleation and growth of amyloid beta-protein fibrils: detection of nuclei and quantitation of rate constants. Proc. Natl. Acad. Sci. USA. 93:1996;1125-1129
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 1125-1129
    • Lomakin, A.1    Chung, D.S.2    Benedek, G.B.3    Kirschner, D.A.4    Teplow, D.B.5
  • 8
  • 9
    • 0038152836 scopus 로고    scopus 로고
    • Anionic micelles and vesicles induce tau fibrillization in vitro
    • Chirita C.N., Necula M., Kuret J. Anionic micelles and vesicles induce tau fibrillization in vitro. J. Biol. Chem. 278:2003;25644-25650
    • (2003) J. Biol. Chem. , vol.278 , pp. 25644-25650
    • Chirita, C.N.1    Necula, M.2    Kuret, J.3
  • 10
    • 0030908095 scopus 로고    scopus 로고
    • Models of amyloid seeding in Alzheimer's disease and scrapie: Mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins
    • Harper J.D., Lansbury P.T. Jr. Models of amyloid seeding in Alzheimer's disease and scrapie: mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins. Annu. Rev. Biochem. 66:1997;385-407
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 385-407
    • Harper, J.D.1    Lansbury Jr., P.T.2
  • 11
    • 0033539689 scopus 로고    scopus 로고
    • Ligand-dependent tau filament formation: Implications for Alzheimer's disease progression
    • King M.E., Ahuja V., Binder L.I., Kuret J. Ligand-dependent tau filament formation: implications for Alzheimer's disease progression. Biochemistry. 38:1999;14851-14859
    • (1999) Biochemistry , vol.38 , pp. 14851-14859
    • King, M.E.1    Ahuja, V.2    Binder, L.I.3    Kuret, J.4
  • 12
    • 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 A.C., Iqbal K., Grundke-Iqbal I. Microtubule-associated protein tau. Abnormal phosphorylation of a non-paired helical filament pool in Alzheimer disease. J. Biol. Chem. 268:1993;24374-24384
    • (1993) J. Biol. Chem. , vol.268 , pp. 24374-24384
    • Kopke, E.1    Tung, Y.C.2    Shaikh, S.3    Alonso, A.C.4    Iqbal, K.5    Grundke-Iqbal, I.6
  • 13
    • 0036830506 scopus 로고    scopus 로고
    • Structure, stability, and aggregation of paired helical filaments from tau protein and FTDP-17 mutants probed by tryptophan scanning mutagenesis
    • Li L., von Bergen M., Mandelkow E.M., Mandelkow E. Structure, stability, and aggregation of paired helical filaments from tau protein and FTDP-17 mutants probed by tryptophan scanning mutagenesis. J. Biol. Chem. 277:2002;41390-41400
    • (2002) J. Biol. Chem. , vol.277 , pp. 41390-41400
    • Li, L.1    Von Bergen, M.2    Mandelkow, E.M.3    Mandelkow, E.4
  • 14
    • 0037126688 scopus 로고    scopus 로고
    • Toward a unified scheme for the aggregation of tau into Alzheimer paired helical filaments
    • Barghorn S., Mandelkow E. Toward a unified scheme for the aggregation of tau into Alzheimer paired helical filaments. Biochemistry. 41:2002;14885-14896
    • (2002) Biochemistry , vol.41 , pp. 14885-14896
    • Barghorn, S.1    Mandelkow, E.2
  • 15
    • 0000376757 scopus 로고
    • Competitive adsorption of high-molecular-weight kininogen and fibrinogen from binary-mixtures to glass-surface
    • Dejardin P., Tenhove P., Yu X.J., Brash J.L. Competitive adsorption of high-molecular-weight kininogen and fibrinogen from binary-mixtures to glass-surface. Langmuir. 11:1995;4001-4007
    • (1995) Langmuir , vol.11 , pp. 4001-4007
    • Dejardin, P.1    Tenhove, P.2    Yu, X.J.3    Brash, J.L.4
  • 17
    • 0033324013 scopus 로고    scopus 로고
    • Electrochemical studies of the adsorption behavior of bovine serum albumin on stainless steel
    • Omanovic S., Roscoe S.G. Electrochemical studies of the adsorption behavior of bovine serum albumin on stainless steel. Langmuir. 15:1999;8315-8321
    • (1999) Langmuir , vol.15 , pp. 8315-8321
    • Omanovic, S.1    Roscoe, S.G.2
  • 18
    • 0000998141 scopus 로고
    • Interfacial behavior of globular-proteins at a platinum-electrode
    • Roscoe S.G., Fuller K.L. Interfacial behavior of globular-proteins at a platinum-electrode. J. Colloid Interface Sci. 152:1992;429-441
    • (1992) J. Colloid Interface Sci. , vol.152 , pp. 429-441
    • Roscoe, S.G.1    Fuller, K.L.2
  • 19
    • 0030602282 scopus 로고    scopus 로고
    • Electrochemical studies of the interfacial behavior of insulin
    • MacDonald S.M., Roscoe S.G. Electrochemical studies of the interfacial behavior of insulin. J. Colloid Interface Sci. 184:1996;449-455
    • (1996) J. Colloid Interface Sci. , vol.184 , pp. 449-455
    • MacDonald, S.M.1    Roscoe, S.G.2
  • 20
    • 0001293174 scopus 로고
    • An electrochemical study of the effect of temperature on the adsorption behavior of beta-lactoglobulin
    • Roscoe S.G., Fuller K.L., Robitaille G. An electrochemical study of the effect of temperature on the adsorption behavior of beta-lactoglobulin. J. Colloid Interface Sci. 160:1993;243-251
    • (1993) J. Colloid Interface Sci. , vol.160 , pp. 243-251
    • Roscoe, S.G.1    Fuller, K.L.2    Robitaille, G.3
  • 21
    • 0021357664 scopus 로고
    • Mass-action effects on competitive adsorption of fibrinogen from hemoglobin-solutions and from plasma
    • Horbett T.A. Mass-action effects on competitive adsorption of fibrinogen from hemoglobin-solutions and from plasma. Thromb. Haemost. 51:1984;174-181
    • (1984) Thromb. Haemost. , vol.51 , pp. 174-181
    • Horbett, T.A.1
  • 22
    • 0026146327 scopus 로고
    • Protein adsorption at solid-liquid interfaces. 2. Adsorption from binary protein mixture
    • Hajra S., Chattoraj D.K. Protein adsorption at solid-liquid interfaces. 2. Adsorption from binary protein mixture. Indian J. Biochem. Biophys. 28:1991;124-132
    • (1991) Indian J. Biochem. Biophys. , vol.28 , pp. 124-132
    • Hajra, S.1    Chattoraj, D.K.2
  • 23
    • 0027912153 scopus 로고
    • Temperature-dependence of bovine serum-albumin adsorption onto a poly(ethylene oxide)-grafted surface
    • Kiss E. Temperature-dependence of bovine serum-albumin adsorption onto a poly(ethylene oxide)-grafted surface. Colloid Surface A. 76:1993;135-140
    • (1993) Colloid Surface a , vol.76 , pp. 135-140
    • Kiss, E.1
  • 24
    • 0026167162 scopus 로고
    • Protein adsorption at solid-liquid interfaces. 3. Adsorption from ternary protein mixture
    • Hajra S., Chattoraj D.K. Protein adsorption at solid-liquid interfaces. 3. Adsorption from ternary protein mixture. Indian J. Biochem. Biophys. 28:1991;184-192
    • (1991) Indian J. Biochem. Biophys. , vol.28 , pp. 184-192
    • Hajra, S.1    Chattoraj, D.K.2
  • 26
    • 0021233461 scopus 로고
    • Effect of plasma dilution on adsorption of fibrinogen to solid-surfaces
    • Brash J.L., Tenhove P. Effect of plasma dilution on adsorption of fibrinogen to solid-surfaces. Thromb. Haemost. 51:1984;326-330
    • (1984) Thromb. Haemost. , vol.51 , pp. 326-330
    • Brash, J.L.1    Tenhove, P.2
  • 27
    • 0018917567 scopus 로고
    • Interaction of high molecular weight kininogen, factor XII, and fibrinogen in plasma at interfaces
    • Vroman L., Adams A.L., Fischer G.C., Munoz P.C. Interaction of high molecular weight kininogen, factor XII, and fibrinogen in plasma at interfaces. Blood. 55:1980;156-159
    • (1980) Blood , vol.55 , pp. 156-159
    • Vroman, L.1    Adams, A.L.2    Fischer, G.C.3    Munoz, P.C.4
  • 28
    • 0001545635 scopus 로고
    • Changes in the strength of fibrinogen attachment to solid surfaces: An explanation of the influence of surface chemistry on the Vroman effect
    • Slack S.M., Horbett T.A. Changes in the strength of fibrinogen attachment to solid surfaces: an explanation of the influence of surface chemistry on the Vroman effect. J. Colloid Interface Sci. 133:1989;148-165
    • (1989) J. Colloid Interface Sci. , vol.133 , pp. 148-165
    • Slack, S.M.1    Horbett, T.A.2
  • 29
    • 0022079435 scopus 로고
    • Phenomenology and mechanism of the transient adsorption of fibrinogen from plasma (Vroman effect)
    • Wojciechowski P., Tenhove P., Brash J.L. Phenomenology and mechanism of the transient adsorption of fibrinogen from plasma (Vroman effect). J. Colloid Interface Sci. 111:1986;455-465
    • (1986) J. Colloid Interface Sci. , vol.111 , pp. 455-465
    • Wojciechowski, P.1    Tenhove, P.2    Brash, J.L.3
  • 30
    • 0034023751 scopus 로고    scopus 로고
    • Differential assembly of human tau isoforms in the presence of arachidonic acid
    • King M.E., Gamblin T.C., Kuret J., Binder L.I. Differential assembly of human tau isoforms in the presence of arachidonic acid. J. Neurochem. 74:2000;1749-1757
    • (2000) J. Neurochem. , vol.74 , pp. 1749-1757
    • King, M.E.1    Gamblin, T.C.2    Kuret, J.3    Binder, L.I.4
  • 31
    • 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., Kuret J. The structural basis of monoclonal antibody Alz50's selectivity for Alzheimer's disease pathology. J. Biol. Chem. 271:1996;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
  • 33
    • 49549158674 scopus 로고
    • A general treatment and classification of the solute adsorption isotherm. I: Theoretical
    • Giles C.H., Smith D., Huitson A. A general treatment and classification of the solute adsorption isotherm. I: Theoretical. J. Colloid Interface Sci. 47:1974;755-765
    • (1974) J. Colloid Interface Sci. , vol.47 , pp. 755-765
    • Giles, C.H.1    Smith, D.2    Huitson, A.3
  • 34
    • 0035140929 scopus 로고    scopus 로고
    • Description of sorption data with isoform equations
    • Hinz C. Description of sorption data with isoform equations. Geoderma. 99:2001;225-243
    • (2001) Geoderma , vol.99 , pp. 225-243
    • Hinz, C.1
  • 35
    • 0035075693 scopus 로고    scopus 로고
    • Structural analysis of Pick's disease-derived and in vitro-assembled tau filaments
    • King M.E., Ghoshal N., Wall J.S., Binder L.I., Ksiezak-Reding H. Structural analysis of Pick's disease-derived and in vitro-assembled tau filaments. Am. J. Pathol. 158:2001;1481-1490
    • (2001) Am. J. Pathol. , vol.158 , pp. 1481-1490
    • King, M.E.1    Ghoshal, N.2    Wall, J.S.3    Binder, L.I.4    Ksiezak-Reding, H.5
  • 36
    • 0035060814 scopus 로고    scopus 로고
    • On the adsorption of proteins on solid surfaces, a common but very complicated phenomenon
    • Nakanishi K., Sakiyama T., Imamura K. On the adsorption of proteins on solid surfaces, a common but very complicated phenomenon. J. Biosci. Bioeng. 91:2001;233-244
    • (2001) J. Biosci. Bioeng. , vol.91 , pp. 233-244
    • Nakanishi, K.1    Sakiyama, T.2    Imamura, K.3
  • 37
    • 0023306682 scopus 로고
    • Simultaneous adsorption of gelatin and long-chain amphiphiles at solid-water interface
    • Samanta A., Chattoraj D.K. Simultaneous adsorption of gelatin and long-chain amphiphiles at solid-water interface. J. Colloid Interface Sci. 116:1987;168-176
    • (1987) J. Colloid Interface Sci. , vol.116 , pp. 168-176
    • Samanta, A.1    Chattoraj, D.K.2
  • 38
    • 1542327644 scopus 로고    scopus 로고
    • Ligand-dependent inhibition and reversal of tau filament formation
    • Chirita C.N., Necula M., Kuret J. Ligand-dependent inhibition and reversal of tau filament formation. Biochemistry. 43:2004;2879-2887
    • (2004) Biochemistry , vol.43 , pp. 2879-2887
    • Chirita, C.N.1    Necula, M.2    Kuret, J.3
  • 39
    • 0024352110 scopus 로고
    • Quantitative evaluation of Congo red binding to amyloid-like proteins with a beta-pleated sheet conformation
    • Klunk W.E., Pettegrew J.W., Abraham D.J. Quantitative evaluation of Congo red binding to amyloid-like proteins with a beta-pleated sheet conformation. J. Histochem. Cytochem. 37:1989;1273-1281
    • (1989) J. Histochem. Cytochem. , vol.37 , pp. 1273-1281
    • Klunk, W.E.1    Pettegrew, J.W.2    Abraham, D.J.3
  • 40
    • 0342931315 scopus 로고
    • Ratio of final interfacial concentrations in exchange processes
    • Dejardin P., Le M.T. Ratio of final interfacial concentrations in exchange processes. Langmuir. 11:1995;4008-4012
    • (1995) Langmuir , vol.11 , pp. 4008-4012
    • Dejardin, P.1    Le M., T.2
  • 41
    • 0343772550 scopus 로고
    • A general treatment and classification of the solute adsorption isotherm. II: Experimental interpretation
    • Giles C.H., D'Silva A.P., Easton I.A. A general treatment and classification of the solute adsorption isotherm. II: Experimental interpretation. J. Colloid Interface Sci. 47:1974;766-778
    • (1974) J. Colloid Interface Sci. , vol.47 , pp. 766-778
    • Giles, C.H.1    D'Silva, A.P.2    Easton, I.A.3
  • 42
    • 0030072180 scopus 로고    scopus 로고
    • Competitive diffusion-adsorption of polymers of differing chain lengths on solid surfaces
    • Devotta I., Mashelkar R.A. Competitive diffusion-adsorption of polymers of differing chain lengths on solid surfaces. Chem. Eng. Sci. 51:1996;561-569
    • (1996) Chem. Eng. Sci. , vol.51 , pp. 561-569
    • Devotta, I.1    Mashelkar, R.A.2
  • 43
    • 0028766615 scopus 로고
    • Surface exchange kinetics of chemically different polymers
    • Dijt J.C., Stuart M.A.C., Fleer G.J. Surface exchange kinetics of chemically different polymers. Macromolecules. 27:1994;3229-3237
    • (1994) Macromolecules , vol.27 , pp. 3229-3237
    • Dijt, J.C.1    Stuart, M.A.C.2    Fleer, G.J.3
  • 44
    • 0032000515 scopus 로고    scopus 로고
    • Sequential adsorption of polymers. Displacement or trapping?
    • Krabi A., Stuart M.A.C. Sequential adsorption of polymers. Displacement or trapping? Macromolecules. 31:1998;1285-1291
    • (1998) Macromolecules , vol.31 , pp. 1285-1291
    • Krabi, A.1    Stuart, M.A.C.2
  • 45
    • 0022781496 scopus 로고
    • Adsorption of proteins from solution at the solid-liquid interface
    • Norde W. Adsorption of proteins from solution at the solid-liquid interface. Adv. Colloid Interface Sci. 25:1986;267-340
    • (1986) Adv. Colloid Interface Sci. , vol.25 , pp. 267-340
    • Norde, W.1
  • 46
    • 0026595559 scopus 로고
    • Effect of sulfonation of segmented polyurethanes on the transient adsorption of fibrinogen from plasma - Possible correlation with anticoagulant behavior
    • Santerre J.P., Tenhove P., Vanderkamp N.H., Brash J.L. Effect of sulfonation of segmented polyurethanes on the transient adsorption of fibrinogen from plasma - possible correlation with anticoagulant behavior. J. Biomed. Mater. Res. 26:1992;39-57
    • (1992) J. Biomed. Mater. Res. , vol.26 , pp. 39-57
    • Santerre, J.P.1    Tenhove, P.2    Vanderkamp, N.H.3    Brash, J.L.4
  • 47
    • 0028170411 scopus 로고
    • Structural studies of tau protein and Alzheimer paired helical filaments show no evidence for beta-structure
    • Schweers O., Schonbrunn-Hanebeck E., Marx A., Mandelkow E. Structural studies of tau protein and Alzheimer paired helical filaments show no evidence for beta-structure. J. Biol. Chem. 269:1994;24290-24297
    • (1994) J. Biol. Chem. , vol.269 , pp. 24290-24297
    • Schweers, O.1    Schonbrunn-Hanebeck, E.2    Marx, A.3    Mandelkow, E.4


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