메뉴 건너뛰기




Volumn 4, Issue 12, 2009, Pages

Real-time imaging and quantification of amyloid-β peptide aggregates by novel quantum-dot nanoprobes

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN ANTIBODY; AMYLOID BETA PROTEIN[1-42]; MONOMER; NANOCRYSTAL; OLIGOMER; QUANTUM DOT;

EID: 77954039898     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0008492     Document Type: Article
Times cited : (65)

References (40)
  • 1
    • 0033621165 scopus 로고    scopus 로고
    • Amyloid diseases: Abnormal protein aggregation in neurodegeneration
    • Koo EH, Lansbury PT Jr, Kelly JW (1999) Amyloid diseases: abnormal protein aggregation in neurodegeneration. Proc Natl Acad Sci U S A 96: 9989-9990.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 9989-9990
    • Koo, E.H.1    Lansbury Jr., P.T.2    Kelly, J.W.3
  • 3
    • 0024990330 scopus 로고
    • Neurotrophic and neurotoxic effects of amyloid beta protein: Reversal by tachykinin neuropeptides
    • Yankner BA, Duffy LK, Kirschner DA (1990) Neurotrophic and neurotoxic effects of amyloid beta protein: reversal by tachykinin neuropeptides. Science 250: 279-282.
    • (1990) Science , vol.250 , pp. 279-282
    • Yankner, B.A.1    Duffy, L.K.2    Kirschner, D.A.3
  • 4
    • 33645038471 scopus 로고    scopus 로고
    • A specific amyloid-beta protein assembly in the brain impairs memory
    • Lesne S, Koh MT, Kotilinek L, Kayed R, Glabe CG, et al. (2006) A specific amyloid-beta protein assembly in the brain impairs memory. Nature 440: 352-357.
    • (2006) Nature , vol.440 , pp. 352-357
    • Lesne, S.1    Koh, M.T.2    Kotilinek, L.3    Kayed, R.4    Glabe, C.G.5
  • 5
    • 41649107124 scopus 로고    scopus 로고
    • Stabilization of neurotoxic soluble beta-sheet-rich conformations of the Alzheimer's disease amyloid-beta peptide
    • Tew DJ, Bottomley SP, Smith DP, Ciccotosto GD, Babon J, et al. (2008) Stabilization of neurotoxic soluble beta-sheet-rich conformations of the Alzheimer's disease amyloid-beta peptide. Biophys J 94: 2752-2766.
    • (2008) Biophys J , vol.94 , pp. 2752-2766
    • Tew, D.J.1    Bottomley, S.P.2    Smith, D.P.3    Ciccotosto, G.D.4    Babon, J.5
  • 6
    • 49149124343 scopus 로고    scopus 로고
    • Amyloid-beta protein dimers isolated directly from Alzheimer's brains impair synaptic plasticity and memory
    • Shankar GM, Li S, Mehta TH, Garcia-Munoz A, Shepardson NE, et al. (2008) Amyloid-beta protein dimers isolated directly from Alzheimer's brains impair synaptic plasticity and memory. Nat Med 14: 837-842.
    • (2008) Nat Med , vol.14 , pp. 837-842
    • Shankar, G.M.1    Li, S.2    Mehta, T.H.3    Garcia-Munoz, A.4    Shepardson, N.E.5
  • 7
    • 0035066332 scopus 로고    scopus 로고
    • Alzheimer's disease: Genes, proteins, and therapy
    • Selkoe DJ (2001) Alzheimer's disease: genes, proteins, and therapy. Physiol Rev 81: 741-766.
    • (2001) Physiol Rev , vol.81 , pp. 741-766
    • Selkoe, D.J.1
  • 8
    • 0033527637 scopus 로고    scopus 로고
    • Uptake, degradation, and release of fibrillar and soluble forms of Alzheimer's amyloid beta-peptide by microglial cells
    • Chung H, Brazil MI, Soe TT, Maxfield FR (1999) Uptake, degradation, and release of fibrillar and soluble forms of Alzheimer's amyloid beta-peptide by microglial cells. J Biol Chem 274: 32301-32308.
    • (1999) J Biol Chem , vol.274 , pp. 32301-32308
    • Chung, H.1    Brazil, M.I.2    Soe, T.T.3    Maxfield, F.R.4
  • 9
    • 56149091817 scopus 로고    scopus 로고
    • Cytokine mediated inhibition of fibrillar amyloid-beta peptide degradation by human mononuclear phagocytes
    • Yamamoto M, Kiyota T, Walsh SM, Liu J, Kipnis J, et al. (2008) Cytokine mediated inhibition of fibrillar amyloid-beta peptide degradation by human mononuclear phagocytes. J Immunol 181: 3877-3886.
    • (2008) J Immunol , vol.181 , pp. 3877-3886
    • Yamamoto, M.1    Kiyota, T.2    Walsh, S.M.3    Liu, J.4    Kipnis, J.5
  • 10
    • 51349110166 scopus 로고    scopus 로고
    • The amyloid beta-peptide is imported into mitochondria via the TOM import machinery and localized to mitochondrial cristae
    • Hansson Petersen CA, Alikhani N, Behbahani H, Wiehager B, Pavlov PF, et al. (2008) The amyloid beta-peptide is imported into mitochondria via the TOM import machinery and localized to mitochondrial cristae. Proc Natl Acad Sci U S A 105: 13145-13150.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 13145-13150
    • Hansson Petersen, C.A.1    Alikhani, N.2    Behbahani, H.3    Wiehager, B.4    Pavlov, P.F.5
  • 11
    • 33846633336 scopus 로고    scopus 로고
    • Abeta oligomer-induced aberrations in synapse composition, shape, and density provide a molecular basis for loss of connectivity in Alzheimer's disease
    • Lacor PN, Buniel MC, Furlow PW, Clemente AS, Velasco PT, et al. (2007) Abeta oligomer-induced aberrations in synapse composition, shape, and density provide a molecular basis for loss of connectivity in Alzheimer's disease. J Neurosci 27: 796-807.
    • (2007) J Neurosci , vol.27 , pp. 796-807
    • Lacor, P.N.1    Buniel, M.C.2    Furlow, P.W.3    Clemente, A.S.4    Velasco, P.T.5
  • 13
    • 0032566763 scopus 로고    scopus 로고
    • Quantum dot bioconjugates for ultrasensitive nonisotopic detection
    • Chan WC, Nie S (1998) Quantum dot bioconjugates for ultrasensitive nonisotopic detection. Science 281: 2016-2018.
    • (1998) Science , vol.281 , pp. 2016-2018
    • Chan, W.C.1    Nie, S.2
  • 14
    • 20144379798 scopus 로고    scopus 로고
    • Quantum dot bioconjugates for imaging, labelling and sensing
    • Medintz IL, Uyeda HT, Goldman ER, Mattoussi H (2005) Quantum dot bioconjugates for imaging, labelling and sensing. Nat Mater 4: 435-446.
    • (2005) Nat Mater , vol.4 , pp. 435-446
    • Medintz, I.L.1    Uyeda, H.T.2    Goldman, E.R.3    Mattoussi, H.4
  • 15
    • 2242495402 scopus 로고    scopus 로고
    • In vivo imaging of quantum dots encapsulated in phospholipid micelles
    • Dubertret B, Skourides P, Norris DJ, Noireaux V, Brivanlou AH, et al. (2002) In vivo imaging of quantum dots encapsulated in phospholipid micelles. Science 298: 1759-1762.
    • (2002) Science , vol.298 , pp. 1759-1762
    • Dubertret, B.1    Skourides, P.2    Norris, D.J.3    Noireaux, V.4    Brivanlou, A.H.5
  • 16
    • 3543022686 scopus 로고    scopus 로고
    • In vivo cancer targeting and imaging with semiconductor quantum dots
    • Gao X, Cui Y, Levenson RM, Chung LW, Nie S (2004) In vivo cancer targeting and imaging with semiconductor quantum dots. Nat Biotechnol 22: 969-976.
    • (2004) Nat Biotechnol , vol.22 , pp. 969-976
    • Gao, X.1    Cui, Y.2    Levenson, R.M.3    Chung, L.W.4    Nie, S.5
  • 17
    • 0142116238 scopus 로고    scopus 로고
    • Diffusion dynamics of glycine receptors revealed by single-quantum dot tracking
    • Dahan M, Levi S, Luccardini C, Rostaing P, Riveau B, et al. (2003) Diffusion dynamics of glycine receptors revealed by single-quantum dot tracking. Science 302: 442-445.
    • (2003) Science , vol.302 , pp. 442-445
    • Dahan, M.1    Levi, S.2    Luccardini, C.3    Rostaing, P.4    Riveau, B.5
  • 18
    • 31444437864 scopus 로고    scopus 로고
    • Processive movement of single kinesins on crowded microtubules visualized using quantum dots
    • Seitz A, Surrey T (2006) Processive movement of single kinesins on crowded microtubules visualized using quantum dots. Embo J 25: 267-277.
    • (2006) Embo J , vol.25 , pp. 267-277
    • Seitz, A.1    Surrey, T.2
  • 19
    • 0038780625 scopus 로고    scopus 로고
    • Water-soluble quantum dots for multiphoton fluorescence imaging in vivo
    • Larson DR, Zipfel WR, Williams RM, Clark SW, Bruchez MP, et al. (2003) Water-soluble quantum dots for multiphoton fluorescence imaging in vivo. Science 300: 1434-1436.
    • (2003) Science , vol.300 , pp. 1434-1436
    • Larson, D.R.1    Zipfel, W.R.2    Williams, R.M.3    Clark, S.W.4    Bruchez, M.P.5
  • 20
    • 33745430441 scopus 로고    scopus 로고
    • An alternative approach to amyloid fibrils morphology: CdSe/ZnS quantum dots labelled beta-amyloid peptide fragments Abeta (31-35), Abeta (1-40) and Abeta (1-42)
    • Ji X, Naistat D, Li C, Orbulesco J, Leblanc RM (2006) An alternative approach to amyloid fibrils morphology: CdSe/ZnS quantum dots labelled beta-amyloid peptide fragments Abeta (31-35), Abeta (1-40) and Abeta (1-42). Colloids Surf B Biointerfaces 50: 104-111.
    • (2006) Colloids Surf B Biointerfaces , vol.50 , pp. 104-111
    • Ji, X.1    Naistat, D.2    Li, C.3    Orbulesco, J.4    Leblanc, R.M.5
  • 21
    • 55549108666 scopus 로고    scopus 로고
    • Detection of Alzheimer's amyloid beta aggregation by capturing molecular trails of individual assemblies
    • Vestergaard M, Hamada T, Saito M, Yajima Y, Kudou M, et al. (2008) Detection of Alzheimer's amyloid beta aggregation by capturing molecular trails of individual assemblies. Biochem Biophys Res Commun 377: 725-728.
    • (2008) Biochem Biophys Res Commun , vol.377 , pp. 725-728
    • Vestergaard, M.1    Hamada, T.2    Saito, M.3    Yajima, Y.4    Kudou, M.5
  • 22
    • 84935851672 scopus 로고    scopus 로고
    • Mechanism of neuronal versus endothelial cell uptake of Alzheimer's disease amyloid beta protein
    • Kandimalla KK, Scott OG, Fulzele S, Davidson MW, Poduslo JF (2009) Mechanism of neuronal versus endothelial cell uptake of Alzheimer's disease amyloid beta protein. PLoS ONE 4: e4627.
    • (2009) PLoS ONE , vol.e4627 , pp. 4
    • Kandimalla, K.K.1    Scott, O.G.2    Fulzele, S.3    Davidson, M.W.4    Poduslo, J.F.5
  • 23
    • 40649128835 scopus 로고    scopus 로고
    • Imaging proteins in live mammalian cells with biotin ligase and monovalent streptavidin
    • Howarth M, Ting AY (2008) Imaging proteins in live mammalian cells with biotin ligase and monovalent streptavidin. Nat Protoc 3: 534-545.
    • (2008) Nat Protoc , vol.3 , pp. 534-545
    • Howarth, M.1    Ting, A.Y.2
  • 24
    • 27744531964 scopus 로고    scopus 로고
    • New light on quantum dot cytotoxicity
    • Tsay JM, Michalet X (2005) New light on quantum dot cytotoxicity. Chem Biol 12: 1159-1161.
    • (2005) Chem Biol , vol.12 , pp. 1159-1161
    • Tsay, J.M.1    Michalet, X.2
  • 25
    • 33646398886 scopus 로고    scopus 로고
    • Cellulareffect of high doses of silica-coated quantum dot profiled with high throughput gene expression analysis and high content cellomics measurements
    • Zhang T, Stilwell JL, Gerion D, Ding L, Elboudwarej O, et al. (2006) Cellulareffect of high doses of silica-coated quantum dot profiled with high throughput gene expression analysis and high content cellomics measurements. Nano Lett 6: 800-808.
    • (2006) Nano Lett , vol.6 , pp. 800-808
    • Zhang, T.1    Stilwell, J.L.2    Gerion, D.3    Ding, L.4    Elboudwarej, O.5
  • 26
    • 0027258525 scopus 로고
    • The carboxy terminus of the beta amyloid protein is critical for the seeding of amyloid formation: Implications for the pathogenesis of Alzheimer's disease
    • Jarrett JT, Berger EP, Lansbury PT Jr (1993) The carboxy terminus of the beta amyloid protein is critical for the seeding of amyloid formation: implications for the pathogenesis of Alzheimer's disease. Biochemistry 32: 4693-4697.
    • (1993) Biochemistry , vol.32 , pp. 4693-4697
    • Jarrett, J.T.1    Berger, E.P.2    Lansbury Jr., P.T.3
  • 27
    • 30744433878 scopus 로고    scopus 로고
    • Experimental constraints on quaternary structure in Alzheimer's beta-amyloid fibrils
    • Petkova AT, Yau WM, Tycko R (2006) Experimental constraints on quaternary structure in Alzheimer's beta-amyloid fibrils. Biochemistry 45: 498-512.
    • (2006) Biochemistry , vol.45 , pp. 498-512
    • Petkova, A.T.1    Yau, W.M.2    Tycko, R.3
  • 28
    • 34948874211 scopus 로고    scopus 로고
    • Polyfluorinated bis-styrylbenzene beta-amyloid plaque binding ligands
    • Flaherty DP, Walsh SM, Kiyota T, Dong Y, Ikezu T, et al. (2007) Polyfluorinated bis-styrylbenzene beta-amyloid plaque binding ligands. J Med Chem 50: 4986-4992.
    • (2007) J Med Chem , vol.50 , pp. 4986-4992
    • Flaherty, D.P.1    Walsh, S.M.2    Kiyota, T.3    Dong, Y.4    Ikezu, T.5
  • 29
    • 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 JD, Lansbury PT Jr (1997) 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: 385-407.
    • (1997) Annu Rev Biochem , vol.66 , pp. 385-407
    • Harper, J.D.1    Lansbury Jr., P.T.2
  • 30
    • 0037422540 scopus 로고    scopus 로고
    • Amyloid beta -protein (Abeta) assembly: Abeta 40 and Abeta 42 oligomerize through distinct pathways
    • Bitan G, Kirkitadze MD, Lomakin A, Vollers SS, Benedek GB, et al. (2003) Amyloid beta -protein (Abeta) assembly: Abeta 40 and Abeta 42 oligomerize through distinct pathways. Proc Natl Acad Sci U S A 100: 330-335.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 330-335
    • Bitan, G.1    Kirkitadze, M.D.2    Lomakin, A.3    Vollers, S.S.4    Benedek, G.B.5
  • 31
    • 0037168655 scopus 로고    scopus 로고
    • A structural model for Alzheimer's beta -amyloid fibrils based on experimental constraints from solid state NMR
    • Petkova AT, Ishii Y, Balbach JJ, Antzutkin ON, Leapman RD, et al. (2002) A structural model for Alzheimer's beta -amyloid fibrils based on experimental constraints from solid state NMR. Proc Natl Acad Sci U S A 99: 16742-16747.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 16742-16747
    • Petkova, A.T.1    Ishii, Y.2    Balbach, J.J.3    Antzutkin, O.N.4    Leapman, R.D.5
  • 32
    • 51149120624 scopus 로고    scopus 로고
    • Microglial dysfunction and defective beta-amyloid clearance pathways in aging Alzheimer's disease mice
    • Hickman SE, Allison EK, El Khoury J (2008) Microglial dysfunction and defective beta-amyloid clearance pathways in aging Alzheimer's disease mice. J Neurosci 28: 8354-8360.
    • (2008) J Neurosci , vol.28 , pp. 8354-8360
    • Hickman, S.E.1    Allison, E.K.2    El Khoury, J.3
  • 33
    • 45849130218 scopus 로고    scopus 로고
    • Bioconjugated quantum rods as targeted probes for efficient transmigration across an in vitro blood-brain barrier
    • Xu G, Yong KT, Roy I, Mahajan SD, Ding H, et al. (2008) Bioconjugated quantum rods as targeted probes for efficient transmigration across an in vitro blood-brain barrier. Bioconjug Chem 19: 1179-1185.
    • (2008) Bioconjug Chem , vol.19 , pp. 1179-1185
    • Xu, G.1    Yong, K.T.2    Roy, I.3    Mahajan, S.D.4    Ding, H.5
  • 34
    • 34248679167 scopus 로고    scopus 로고
    • Tricine-SDS-PAGE
    • Schagger H (2006) Tricine-SDS-PAGE. Nat Protoc 1: 16-22.
    • (2006) Nat Protoc , vol.1 , pp. 16-22
    • Schagger, H.1
  • 35
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK (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
  • 36
    • 33947512432 scopus 로고    scopus 로고
    • Interferon-gamma and tumor necrosis factor-alpha regulate amyloid-beta plaque deposition and beta-secretase expression in Swedish mutant APP transgenic mice
    • Yamamoto M, Kiyota T, Horiba M, Buescher JL, Walsh SM, et al. (2007) Interferon-gamma and tumor necrosis factor-alpha regulate amyloid-beta plaque deposition and beta-secretase expression in Swedish mutant APP transgenic mice. Am J Pathol 170: 680-692.
    • (2007) Am J Pathol , vol.170 , pp. 680-692
    • Yamamoto, M.1    Kiyota, T.2    Horiba, M.3    Buescher, J.L.4    Walsh, S.M.5
  • 37
    • 14944385354 scopus 로고    scopus 로고
    • Beta-amyloid-stimulated microglia induce neuron death via synergistic stimulation of tumor necrosis factor alpha and NMDA receptors
    • Floden AM, Li S, Combs CK (2005) Beta-amyloid-stimulated microglia induce neuron death via synergistic stimulation of tumor necrosis factor alpha and NMDA receptors. J Neurosci 25: 2566-2575.
    • (2005) J Neurosci , vol.25 , pp. 2566-2575
    • Floden, A.M.1    Li, S.2    Combs, C.K.3
  • 38
    • 0037841390 scopus 로고    scopus 로고
    • Silatrane-based surface chemistry for immobilization of DNA, protein-DNA complexes and other biological materials
    • Shlyakhtenko LS, Gall AA, Filonov A, Cerovac Z, Lushnikov A, et al. (2003) Silatrane-based surface chemistry for immobilization of DNA, protein-DNA complexes and other biological materials. Ultramicroscopy 97: 279-287.
    • (2003) Ultramicroscopy , vol.97 , pp. 279-287
    • Shlyakhtenko, L.S.1    Gall, A.A.2    Filonov, A.3    Cerovac, Z.4    Lushnikov, A.5
  • 39
    • 59749090938 scopus 로고    scopus 로고
    • AFM for analysis of structure and dynamics of DNA and protein-DNA complexes
    • Lyubchenko YL, Shlyakhtenko LS (2009) AFM for analysis of structure and dynamics of DNA and protein-DNA complexes. Methods 47: 206-213.
    • (2009) Methods , vol.47 , pp. 206-213
    • Lyubchenko, Y.L.1    Shlyakhtenko, L.S.2
  • 40
    • 0033598697 scopus 로고    scopus 로고
    • Interaction between A beta(1-42) and A beta(1-40) in Alzheimer's beta-amyloid fibril formation in vitro
    • Hasegawa K, Yamaguchi I, Omata S, Gejyo F, Naiki H (1999) Interaction between A beta(1-42) and A beta(1-40) in Alzheimer's beta-amyloid fibril formation in vitro. Biochemistry 38: 15514-15521.
    • (1999) Biochemistry , vol.38 , pp. 15514-15521
    • Hasegawa, K.1    Yamaguchi, I.2    Omata, S.3    Gejyo, F.4    Naiki, H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.