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Volumn 4, Issue 11, 2013, Pages 1417-1429

Alzheimer's disease: Pathophysiology and applications of magnetic nanoparticles as MRI theranostic agents

Author keywords

amyloid ; Magnetic resonance imaging; nanomedicine; nanotechnology; SPION

Indexed keywords

AMYLOID BETA PROTEIN; APOLIPOPROTEIN E; APOLIPOPROTEIN E4; NUCLEAR MAGNETIC RESONANCE IMAGING AGENT; PRESENILIN 1; PRESENILIN 2; SUPERPARAMAGNETIC IRON OXIDE NANOPARTICLE;

EID: 84888382800     PISSN: None     EISSN: 19487193     Source Type: Journal    
DOI: 10.1021/cn4001582     Document Type: Review
Times cited : (101)

References (163)
  • 2
    • 0001181116 scopus 로고    scopus 로고
    • Alzheimer's disease: Molecular understanding predicts amyloid-based therapeutics
    • - 584
    • Selkoe, D. J. and Schenk, D. (2003) Alzheimer's disease: molecular understanding predicts amyloid-based therapeutics Annu. Rev. Pharmacol. Toxicol. 43, 545-584
    • (2003) Annu. Rev. Pharmacol. Toxicol. , vol.43 , pp. 545
    • Selkoe, D.J.1    Schenk, D.2
  • 3
    • 84859114401 scopus 로고    scopus 로고
    • Multifunctional stable fluorescent magnetic nanoparticles
    • - 3959
    • Mahmoudi, M. and Shokrgozar, M. A. (2012) Multifunctional stable fluorescent magnetic nanoparticles Chem. Commun. 48, 3957-3959
    • (2012) Chem. Commun. , vol.48 , pp. 3957
    • Mahmoudi, M.1    Shokrgozar, M.A.2
  • 4
    • 84859152270 scopus 로고    scopus 로고
    • Silver-coated engineered magnetic nanoparticles are promising for the success in the fight against antibacterial resistance threat
    • - 2664
    • Mahmoudi, M. and Serpooshan, V. (2012) Silver-coated engineered magnetic nanoparticles are promising for the success in the fight against antibacterial resistance threat ACS Nano 6, 2656-2664
    • (2012) ACS Nano , vol.6 , pp. 2656
    • Mahmoudi, M.1    Serpooshan, V.2
  • 5
    • 56149092961 scopus 로고    scopus 로고
    • Survival in Alzheimer disease: A multiethnic, population-based study of incident cases
    • - 1495
    • Helzner, E. P., Scarmeas, N., Cosentino, S., Tang, M. X., Schupf, N., and Stern, Y. (2008) Survival in Alzheimer disease: a multiethnic, population-based study of incident cases Neurology 71, 1489-1495
    • (2008) Neurology , vol.71 , pp. 1489
    • Helzner, E.P.1    Scarmeas, N.2    Cosentino, S.3    Tang, M.X.4    Schupf, N.5    Stern, Y.6
  • 6
    • 39149114753 scopus 로고    scopus 로고
    • Survival times in people with dementia: Analysis from population based cohort study with 14 year follow-up
    • Medical Research Council Cognitive, F. and Ageing Study, c. () - 262
    • Xie, J., Brayne, C., Matthews, F. E., and Medical Research Council Cognitive, F., and Ageing Study, c. (2008) Survival times in people with dementia: analysis from population based cohort study with 14 year follow-up BMJ 336, 258-262
    • (2008) BMJ , vol.336 , pp. 258
    • Xie, J.1    Brayne, C.2    Matthews, F.E.3
  • 7
    • 0016823810 scopus 로고
    • Mini-mental state". A practical method for grading the cognitive state of patients for the clinician
    • - 198
    • Folstein, M. F., Folstein, S. E., and McHugh, P. R. (1975) "Mini-mental state". A practical method for grading the cognitive state of patients for the clinician J. Psychiatr. Res. 12, 189-198
    • (1975) J. Psychiatr. Res. , vol.12 , pp. 189
    • Folstein, M.F.1    Folstein, S.E.2    McHugh, P.R.3
  • 8
    • 55949101032 scopus 로고    scopus 로고
    • Diagnostic accuracy of the clock drawing test: The relevance of ″time setting'' in screening for dementia
    • - 260
    • Berger, G., Frolich, L., Weber, B., and Pantel, J. (2008) Diagnostic accuracy of the clock drawing test: the relevance of ″time setting'' in screening for dementia J. Geriatr. Psychiatry Neurol. 21, 250-260
    • (2008) J. Geriatr. Psychiatry Neurol. , vol.21 , pp. 250
    • Berger, G.1    Frolich, L.2    Weber, B.3    Pantel, J.4
  • 9
    • 32044434645 scopus 로고    scopus 로고
    • Odor identification and decline in different cognitive domains in old age
    • - 67
    • Wilson, R. S., Arnold, S. E., Tang, Y., and Bennett, D. A. (2006) Odor identification and decline in different cognitive domains in old age Neuroepidemiology 26, 61-67
    • (2006) Neuroepidemiology , vol.26 , pp. 61
    • Wilson, R.S.1    Arnold, S.E.2    Tang, Y.3    Bennett, D.A.4
  • 10
    • 84869117826 scopus 로고    scopus 로고
    • Protein fibrillation and the olfactory system: Speculations on their linkage
    • - 610
    • Mahmoudi, M. and Suslick, K. S. (2012) Protein fibrillation and the olfactory system: speculations on their linkage Trends Biotechnol. 30, 609-610
    • (2012) Trends Biotechnol. , vol.30 , pp. 609
    • Mahmoudi, M.1    Suslick, K.S.2
  • 11
    • 33750503415 scopus 로고    scopus 로고
    • Drug discovery in dementia: The role of rodent models
    • - 970
    • Van Dam, D. and De Deyn, P. P. (2006) Drug discovery in dementia: the role of rodent models Nat. Rev. Drug Discovery 5, 956-970
    • (2006) Nat. Rev. Drug Discovery , vol.5 , pp. 956
    • Van Dam, D.1    De Deyn, P.P.2
  • 12
    • 0242330374 scopus 로고    scopus 로고
    • ADAMs family members as amyloid precursor protein alpha-secretases
    • - 352
    • Allinson, T. M., Parkin, E. T., Turner, A. J., and Hooper, N. M. (2003) ADAMs family members as amyloid precursor protein alpha-secretases J. Neurosci. Res. 74, 342-352
    • (2003) J. Neurosci. Res. , vol.74 , pp. 342
    • Allinson, T.M.1    Parkin, E.T.2    Turner, A.J.3    Hooper, N.M.4
  • 13
    • 77956057086 scopus 로고    scopus 로고
    • Murine models of Alzheimer's disease and their use in developing immunotherapies
    • - 859
    • Wisniewski, T. and Sigurdsson, E. M. (2010) Murine models of Alzheimer's disease and their use in developing immunotherapies Biochim. Biophys. Acta, Mol. Basis Dis. 1802, 847-859
    • (2010) Biochim. Biophys. Acta, Mol. Basis Dis. , vol.1802 , pp. 847
    • Wisniewski, T.1    Sigurdsson, E.M.2
  • 14
    • 0042888860 scopus 로고    scopus 로고
    • Cerebral amyloid angiopathy: Pathogenesis and effects on the ageing and Alzheimer brain
    • - 616
    • Weller, R. O. and Nicoll, J. A. (2003) Cerebral amyloid angiopathy: pathogenesis and effects on the ageing and Alzheimer brain Neurol. Res. 25, 611-616
    • (2003) Neurol. Res. , vol.25 , pp. 611
    • Weller, R.O.1    Nicoll, J.A.2
  • 15
    • 33644819758 scopus 로고    scopus 로고
    • Hereditary cerebral hemorrhage with amyloidosis-Dutch type
    • - 297
    • Maat-Schieman, M., Roos, R., and van Duinen, S. (2005) Hereditary cerebral hemorrhage with amyloidosis-Dutch type Neuropathology 25, 288-297
    • (2005) Neuropathology , vol.25 , pp. 288
    • Maat-Schieman, M.1    Roos, R.2    Van Duinen, S.3
  • 16
    • 0032032969 scopus 로고    scopus 로고
    • Characteristics of the in vitro vasoactivity of beta-amyloid peptides
    • - 168
    • Crawford, F., Suo, Z., Fang, C., and Mullan, M. (1998) Characteristics of the in vitro vasoactivity of beta-amyloid peptides Exp. Neurol. 150, 159-168
    • (1998) Exp. Neurol. , vol.150 , pp. 159
    • Crawford, F.1    Suo, Z.2    Fang, C.3    Mullan, M.4
  • 18
    • 0034603552 scopus 로고    scopus 로고
    • Critically attained threshold of cerebral hypoperfusion: The CATCH hypothesis of Alzheimer's pathogenesis
    • - 342
    • de la Torre, J. C. (2000) Critically attained threshold of cerebral hypoperfusion: the CATCH hypothesis of Alzheimer's pathogenesis Neurobiol. Aging 21, 331-342
    • (2000) Neurobiol. Aging , vol.21 , pp. 331
    • De La Torre, J.C.1
  • 19
    • 0031728139 scopus 로고    scopus 로고
    • Alzheimer's beta-amyloid vasoactivity: Identification of a novel beta-amyloid conformational intermediate
    • - 448
    • Crawford, F., Soto, C., Suo, Z., Fang, C., Parker, T., Sawar, A., Frangione, B., and Mullan, M. (1998) Alzheimer's beta-amyloid vasoactivity: identification of a novel beta-amyloid conformational intermediate FEBS Lett. 436, 445-448
    • (1998) FEBS Lett. , vol.436 , pp. 445
    • Crawford, F.1    Soto, C.2    Suo, Z.3    Fang, C.4    Parker, T.5    Sawar, A.6    Frangione, B.7    Mullan, M.8
  • 20
    • 0030724476 scopus 로고    scopus 로고
    • Beta-amyloid-induced coronary artery vasoactivity and endothelial damage
    • - 522
    • Thomas, T., Sutton, E. T., Hellermann, A., and Price, J. M. (1997) Beta-amyloid-induced coronary artery vasoactivity and endothelial damage J. Cardiovasc. Pharmacol. 30, 517-522
    • (1997) J. Cardiovasc. Pharmacol. , vol.30 , pp. 517
    • Thomas, T.1    Sutton, E.T.2    Hellermann, A.3    Price, J.M.4
  • 21
    • 74949090244 scopus 로고    scopus 로고
    • Olfactory dysfunction correlates with amyloid-beta burden in an Alzheimer's disease mouse model
    • - 514
    • Wesson, D. W., Levy, E., Nixon, R. A., and Wilson, D. A. (2010) Olfactory dysfunction correlates with amyloid-beta burden in an Alzheimer's disease mouse model J. Neurosci. 30, 505-514
    • (2010) J. Neurosci. , vol.30 , pp. 505
    • Wesson, D.W.1    Levy, E.2    Nixon, R.A.3    Wilson, D.A.4
  • 22
    • 79955044494 scopus 로고    scopus 로고
    • Soluble amyloid beta-protein dimers isolated from Alzheimer cortex directly induce Tau hyperphosphorylation and neuritic degeneration
    • - 5824
    • Jin, M., Shepardson, N., Yang, T., Chen, G., Walsh, D., and Selkoe, D. J. (2011) Soluble amyloid beta-protein dimers isolated from Alzheimer cortex directly induce Tau hyperphosphorylation and neuritic degeneration Proc. Natl. Acad. Sci. U.S.A. 108, 5819-5824
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 5819
    • Jin, M.1    Shepardson, N.2    Yang, T.3    Chen, G.4    Walsh, D.5    Selkoe, D.J.6
  • 24
    • 33847662852 scopus 로고    scopus 로고
    • Soluble protein oligomers in neurodegeneration: Lessons from the Alzheimer's amyloid beta-peptide
    • - 112
    • Haass, C. and Selkoe, D. J. (2007) Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid beta-peptide Nat. Rev. Mol. Cell Biol. 8, 101-112
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 101
    • Haass, C.1    Selkoe, D.J.2
  • 25
    • 77649305060 scopus 로고    scopus 로고
    • Senescent synapses and hippocampal circuit dynamics
    • - 161
    • Burke, S. N. and Barnes, C. A. (2010) Senescent synapses and hippocampal circuit dynamics Trends Neurosci. 33, 153-161
    • (2010) Trends Neurosci. , vol.33 , pp. 153
    • Burke, S.N.1    Barnes, C.A.2
  • 26
    • 0027973771 scopus 로고
    • Hippocampal connectivity and Alzheimer's dementia: Effects of synapse loss and tangle frequency in a two-component model
    • - 2088
    • Samuel, W., Masliah, E., Hill, L. R., Butters, N., and Terry, R. (1994) Hippocampal connectivity and Alzheimer's dementia: effects of synapse loss and tangle frequency in a two-component model Neurology 44, 2081-2088
    • (1994) Neurology , vol.44 , pp. 2081
    • Samuel, W.1    Masliah, E.2    Hill, L.R.3    Butters, N.4    Terry, R.5
  • 27
    • 0029821150 scopus 로고    scopus 로고
    • Preserved neuron number in the hippocampus of aged rats with spatial learning deficits
    • - 9930
    • Rapp, P. R. and Gallagher, M. (1996) Preserved neuron number in the hippocampus of aged rats with spatial learning deficits Proc. Natl. Acad. Sci. U.S.A. 93, 9926-9930
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 9926
    • Rapp, P.R.1    Gallagher, M.2
  • 28
    • 79251554354 scopus 로고    scopus 로고
    • Selective vulnerability of neurons in layer II of the entorhinal cortex during aging and Alzheimer's disease
    • Stranahan, A. M. and Mattson, M. P. (2010) Selective vulnerability of neurons in layer II of the entorhinal cortex during aging and Alzheimer's disease Neural Plast. 2010, 108190
    • (2010) Neural Plast. , vol.2010 , pp. 108190
    • Stranahan, A.M.1    Mattson, M.P.2
  • 29
    • 0034213718 scopus 로고    scopus 로고
    • High-level neuronal expression of abeta 1-42 in wild-type human amyloid protein precursor transgenic mice: Synaptotoxicity without plaque formation
    • - 4058
    • Mucke, L., Masliah, E., Yu, G. Q., Mallory, M., Rockenstein, E. M., Tatsuno, G., Hu, K., Kholodenko, D., Johnson-Wood, K., and McConlogue, L. (2000) High-level neuronal expression of abeta 1-42 in wild-type human amyloid protein precursor transgenic mice: synaptotoxicity without plaque formation J. Neurosci. 20, 4050-4058
    • (2000) J. Neurosci. , vol.20 , pp. 4050
    • Mucke, L.1    Masliah, E.2    Yu, G.Q.3    Mallory, M.4    Rockenstein, E.M.5    Tatsuno, G.6    Hu, K.7    Kholodenko, D.8    Johnson-Wood, K.9    McConlogue, L.10
  • 31
    • 33845565678 scopus 로고    scopus 로고
    • Spatial relationship between synapse loss and beta-amyloid deposition in Tg2576 mice
    • - 321
    • Dong, H., Martin, M. V., Chambers, S., and Csernansky, J. G. (2007) Spatial relationship between synapse loss and beta-amyloid deposition in Tg2576 mice J. Comp. Neurol. 500, 311-321
    • (2007) J. Comp. Neurol. , vol.500 , pp. 311
    • Dong, H.1    Martin, M.V.2    Chambers, S.3    Csernansky, J.G.4
  • 33
    • 0035950188 scopus 로고    scopus 로고
    • New frontiers in Alzheimer's disease genetics
    • - 184
    • Tanzi, R. E. and Bertram, L. (2001) New frontiers in Alzheimer's disease genetics Neuron 32, 181-184
    • (2001) Neuron , vol.32 , pp. 181
    • Tanzi, R.E.1    Bertram, L.2
  • 34
    • 0041856595 scopus 로고    scopus 로고
    • Epidemiology of Neurodegeneration
    • - 104
    • Mayeux. (2003) Epidemiology of Neurodegeneration Annu. Rev. Neurosci. 26, 81-104
    • (2003) Annu. Rev. Neurosci. , vol.26 , pp. 81
    • Mayeux1
  • 35
    • 0028598502 scopus 로고
    • Interaction between genetic and environmental risk factors for Alzheimer's disease: A reanalysis of case-control studies. EURODEM Risk Factors Research Group
    • - 551
    • Van Duijn, C. M., Clayton, D. G., Chandra, V., Fratiglioni, L., Graves, A. B., Heyman, A., Jorm, A. F., Kokmen, E., Kondo, K., and Mortimer, J. A. 1994, Interaction between genetic and environmental risk factors for Alzheimer's disease: a reanalysis of case-control studies. EURODEM Risk Factors Research Group Genet. Epidemiol. 11, 539-551
    • (1994) Genet. Epidemiol. , vol.11 , pp. 539
    • Van Duijn, C.M.1    Clayton, D.G.2    Chandra, V.3    Fratiglioni, L.4    Graves, A.B.5    Heyman, A.6    Jorm, A.F.7    Kokmen, E.8    Kondo, K.9    Mortimer, J.A.10
  • 39
    • 0035115847 scopus 로고    scopus 로고
    • Two distal downstream enhancers direct expression of the human apolipoprotein e gene to astrocytes in the brain
    • - 822
    • Grehan, S., Tse, E., and Taylor, J. M. (2001) Two distal downstream enhancers direct expression of the human apolipoprotein E gene to astrocytes in the brain J. Neurosci. 21, 812-822
    • (2001) J. Neurosci. , vol.21 , pp. 812
    • Grehan, S.1    Tse, E.2    Taylor, J.M.3
  • 40
    • 84888346046 scopus 로고
    • Lipoproteins and their receptors in the central nervous system. Characterization of the lipoproteins in cerebrospinal fluid and identification of apolipoprotein B,E(LDL) receptors in the brain
    • - 75
    • Pitas, R. E., B., J., Lee, S. H., Hui, D., and Weisgraber, K. H. (1987) Lipoproteins and their receptors in the central nervous system. Characterization of the lipoproteins in cerebrospinal fluid and identification of apolipoprotein B,E(LDL) receptors in the brain J. Biol. Chem. 6, 63-75
    • (1987) J. Biol. Chem. , vol.6 , pp. 63
    • Pitas, R.E.1    Lee, S.H.2    Hui, D.3    Weisgraber, K.H.4
  • 42
    • 33646911081 scopus 로고    scopus 로고
    • Profile and regulation of apolipoprotein e (ApoE) expression in the CNS in mice with targeting of green fluorescent protein gene to the ApoE locus
    • - 4994
    • Xu, Q., Bernardo, A., Walker, D., Kanegawa, T., Mahley, R. W., and Huang, Y. (2006) Profile and regulation of apolipoprotein E (ApoE) expression in the CNS in mice with targeting of green fluorescent protein gene to the ApoE locus J. Neurosci. 26, 4985-4994
    • (2006) J. Neurosci. , vol.26 , pp. 4985
    • Xu, Q.1    Bernardo, A.2    Walker, D.3    Kanegawa, T.4    Mahley, R.W.5    Huang, Y.6
  • 43
    • 0034575124 scopus 로고    scopus 로고
    • Apolipoprotein E: Far more than a lipid transport protein
    • - 537
    • Mahley, R. W. and Rall, S. C., Jr. (2000) Apolipoprotein E: far more than a lipid transport protein Annu. Rev. Genomics Hum. Genet. 1, 507-537
    • (2000) Annu. Rev. Genomics Hum. Genet. , vol.1 , pp. 507
    • Mahley, R.W.1    Rall, Jr.S.C.2
  • 45
    • 0029931412 scopus 로고    scopus 로고
    • A prospective study of the clinical utility of ApoE genotype in the prediction of outcome in patients with memory impairment
    • - 154
    • Tierney, M. C., Szalai, J. P., Snow, W. G., Fisher, R. H., Tsuda, T., Chi, H., McLachlan, D. R., and St George-Hyslop, P. H. (1996) A prospective study of the clinical utility of ApoE genotype in the prediction of outcome in patients with memory impairment Neurology 46, 149-154
    • (1996) Neurology , vol.46 , pp. 149
    • Tierney, M.C.1    Szalai, J.P.2    Snow, W.G.3    Fisher, R.H.4    Tsuda, T.5    Chi, H.6    McLachlan, D.R.7    St George-Hyslop, P.H.8
  • 47
    • 33645808672 scopus 로고    scopus 로고
    • Apolipoprotein E4: A causative factor and therapeutic target in neuropathology, including Alzheimer's disease
    • - 5651
    • Mahley, R. W., Weisgraber, K. H., and Huang, Y. (2006) Apolipoprotein E4: a causative factor and therapeutic target in neuropathology, including Alzheimer's disease Proc. Natl. Acad. Sci. U.S.A. 103, 5644-5651
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 5644
    • Mahley, R.W.1    Weisgraber, K.H.2    Huang, Y.3
  • 50
    • 34247506244 scopus 로고    scopus 로고
    • Transport pathways for clearance of human Alzheimer's amyloid beta-peptide and apolipoproteins e and J in the mouse central nervous system
    • - 918
    • Bell, R. D., Sagare, A. P., Friedman, A. E., Bedi, G. S., Holtzman, D. M., Deane, R., and Zlokovic, B. V. (2007) Transport pathways for clearance of human Alzheimer's amyloid beta-peptide and apolipoproteins E and J in the mouse central nervous system J. Cereb. Blood Flow Metab. 27, 909-918
    • (2007) J. Cereb. Blood Flow Metab. , vol.27 , pp. 909
    • Bell, R.D.1    Sagare, A.P.2    Friedman, A.E.3    Bedi, G.S.4    Holtzman, D.M.5    Deane, R.6    Zlokovic, B.V.7
  • 51
    • 36448976927 scopus 로고    scopus 로고
    • Cerebral clearance of human amyloid-beta peptide (1-40) across the blood-brain barrier is reduced by self-aggregation and formation of low-density lipoprotein receptor-related protein-1 ligand complexes
    • - 2490
    • Ito, S., Ohtsuki, S., Kamiie, J., Nezu, Y., and Terasaki, T. (2007) Cerebral clearance of human amyloid-beta peptide (1-40) across the blood-brain barrier is reduced by self-aggregation and formation of low-density lipoprotein receptor-related protein-1 ligand complexes J. Neurochem. 103, 2482-2490
    • (2007) J. Neurochem. , vol.103 , pp. 2482
    • Ito, S.1    Ohtsuki, S.2    Kamiie, J.3    Nezu, Y.4    Terasaki, T.5
  • 55
    • 0030007964 scopus 로고    scopus 로고
    • Sequence of deposition of heterogeneous amyloid beta-peptides and APO e in Down syndrome: Implications for initial events in amyloid plaque formation
    • - 32
    • Lemere, C. A., Blusztajn, J. K., Yamaguchi, H., Wisniewski, T., Saido, T. C., and Selkoe, D. J. (1996) Sequence of deposition of heterogeneous amyloid beta-peptides and APO E in Down syndrome: implications for initial events in amyloid plaque formation Neurobiol. Dis. 3, 16-32
    • (1996) Neurobiol. Dis. , vol.3 , pp. 16
    • Lemere, C.A.1    Blusztajn, J.K.2    Yamaguchi, H.3    Wisniewski, T.4    Saido, T.C.5    Selkoe, D.J.6
  • 56
    • 0025899041 scopus 로고
    • Amyloid deposition as the central event in the aetiology of Alzheimer's disease
    • - 388
    • Hardy, J. and Allsop, D. (1991) Amyloid deposition as the central event in the aetiology of Alzheimer's disease Trends Pharmacol. Sci. 12, 383-388
    • (1991) Trends Pharmacol. Sci. , vol.12 , pp. 383
    • Hardy, J.1    Allsop, D.2
  • 57
    • 0025987048 scopus 로고
    • Physical basis of cognitive alterations in Alzheimer's disease: Synapse loss is the major correlate of cognitive impairment
    • - 580
    • Terry, R. D., Masliah, E., Salmon, D. P., Butters, N., DeTeresa, R., Hill, R., Hansen, L. A., and Katzman, R. (1991) Physical basis of cognitive alterations in Alzheimer's disease: synapse loss is the major correlate of cognitive impairment Ann. Neurol. 30, 572-580
    • (1991) Ann. Neurol. , vol.30 , pp. 572
    • Terry, R.D.1    Masliah, E.2    Salmon, D.P.3    Butters, N.4    Deteresa, R.5    Hill, R.6    Hansen, L.A.7    Katzman, R.8
  • 58
    • 0029078972 scopus 로고
    • Correlations of synaptic and pathological markers with cognition of the elderly
    • discussion 298-304. - 298
    • Dickson, D. W., Crystal, H. A., Bevona, C., Honer, W., Vincent, I., and Davies, P. (1995) Correlations of synaptic and pathological markers with cognition of the elderly Neurobiol. Aging 16, 285-298 discussion 298-304.
    • (1995) Neurobiol. Aging , vol.16 , pp. 285
    • Dickson, D.W.1    Crystal, H.A.2    Bevona, C.3    Honer, W.4    Vincent, I.5    Davies, P.6
  • 61
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics
    • - 356
    • Hardy, J. and Selkoe, D. J. (2002) The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics Science 297, 353-356
    • (2002) Science , vol.297 , pp. 353
    • Hardy, J.1    Selkoe, D.J.2
  • 62
    • 34248190279 scopus 로고    scopus 로고
    • A beta oligomers - A decade of discovery
    • - 1184
    • Walsh, D. M. and Selkoe, D. J. (2007) A beta oligomers-a decade of discovery J. Neurochem. 101, 1172-1184
    • (2007) J. Neurochem. , vol.101 , pp. 1172
    • Walsh, D.M.1    Selkoe, D.J.2
  • 63
    • 33947314641 scopus 로고    scopus 로고
    • Natural oligomers of the Alzheimer amyloid-beta protein induce reversible synapse loss by modulating an NMDA-type glutamate receptor-dependent signaling pathway
    • - 2875
    • Shankar, G. M., Bloodgood, B. L., Townsend, M., Walsh, D. M., Selkoe, D. J., and Sabatini, B. L. (2007) Natural oligomers of the Alzheimer amyloid-beta protein induce reversible synapse loss by modulating an NMDA-type glutamate receptor-dependent signaling pathway J. Neurosci. 27, 2866-2875
    • (2007) J. Neurosci. , vol.27 , pp. 2866
    • Shankar, G.M.1    Bloodgood, B.L.2    Townsend, M.3    Walsh, D.M.4    Selkoe, D.J.5    Sabatini, B.L.6
  • 64
    • 67249087641 scopus 로고    scopus 로고
    • Soluble oligomers of amyloid Beta protein facilitate hippocampal long-term depression by disrupting neuronal glutamate uptake
    • - 801
    • Li, S., Hong, S., Shepardson, N. E., Walsh, D. M., Shankar, G. M., and Selkoe, D. (2009) Soluble oligomers of amyloid Beta protein facilitate hippocampal long-term depression by disrupting neuronal glutamate uptake Neuron 62, 788-801
    • (2009) Neuron , vol.62 , pp. 788
    • Li, S.1    Hong, S.2    Shepardson, N.E.3    Walsh, D.M.4    Shankar, G.M.5    Selkoe, D.6
  • 65
    • 0021256895 scopus 로고
    • Alzheimer's disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid protein
    • - 890
    • Glenner, G. G. and Wong, C. W. (1984) Alzheimer's disease: initial report of the purification and characterization of a novel cerebrovascular amyloid protein Biochem. Biophys. Res. Commun. 120, 885-890
    • (1984) Biochem. Biophys. Res. Commun. , vol.120 , pp. 885
    • Glenner, G.G.1    Wong, C.W.2
  • 66
    • 0024808798 scopus 로고
    • Amyloid beta protein and the basis for Alzheimer's disease
    • - 868
    • Glenner, G. G. (1989) Amyloid beta protein and the basis for Alzheimer's disease Prog. Clin. Biol. Res. 317, 857-868
    • (1989) Prog. Clin. Biol. Res. , vol.317 , pp. 857
    • Glenner, G.G.1
  • 67
    • 0024535310 scopus 로고
    • Morphology and distribution of plaque and related deposits in the brains of Alzheimer's disease and control cases. An immunohistochemical study using amyloid beta-protein antibody
    • - 122
    • Ikeda, S., Allsop, D., and Glenner, G. G. (1989) Morphology and distribution of plaque and related deposits in the brains of Alzheimer's disease and control cases. An immunohistochemical study using amyloid beta-protein antibody Lab. Invest. 60, 113-122
    • (1989) Lab. Invest. , vol.60 , pp. 113
    • Ikeda, S.1    Allsop, D.2    Glenner, G.G.3
  • 68
    • 0023132387 scopus 로고
    • Characterization and chromosomal localization of a cDNA encoding brain amyloid of Alzheimer's disease
    • - 880
    • Goldgaber, D., Lerman, M. I., McBride, O. W., Saffiotti, U., and Gajdusek, D. C. (1987) Characterization and chromosomal localization of a cDNA encoding brain amyloid of Alzheimer's disease Science 235, 877-880
    • (1987) Science , vol.235 , pp. 877
    • Goldgaber, D.1    Lerman, M.I.2    McBride, O.W.3    Saffiotti, U.4    Gajdusek, D.C.5
  • 73
    • 0032211830 scopus 로고    scopus 로고
    • The cell biology of beta-amyloid precursor protein and presenilin in Alzheimer's disease
    • - 453
    • Selkoe, D. J. (1998) The cell biology of beta-amyloid precursor protein and presenilin in Alzheimer's disease Trends Cell Biol. 8, 447-453
    • (1998) Trends Cell Biol. , vol.8 , pp. 447
    • Selkoe, D.J.1
  • 74
    • 0038795645 scopus 로고    scopus 로고
    • Signals for sorting of transmembrane proteins to endosomes and lysosomes
    • - 447
    • Bonifacino, J. S. and Traub, L. M. (2003) Signals for sorting of transmembrane proteins to endosomes and lysosomes Annu. Rev. Biochem. 72, 395-447
    • (2003) Annu. Rev. Biochem. , vol.72 , pp. 395
    • Bonifacino, J.S.1    Traub, L.M.2
  • 75
    • 0029934134 scopus 로고    scopus 로고
    • Trafficking of cell-surface amyloid beta-protein precursor. II. Endocytosis, recycling and lysosomal targeting detected by immunolocalization
    • - 1008
    • Yamazaki, T., Koo, E. H., and Selkoe, D. J. (1996) Trafficking of cell-surface amyloid beta-protein precursor. II. Endocytosis, recycling and lysosomal targeting detected by immunolocalization J. Cell Sci. 109 (Pt 5) 999-1008
    • (1996) J. Cell Sci. , vol.109 , Issue.PART 5 , pp. 999
    • Yamazaki, T.1    Koo, E.H.2    Selkoe, D.J.3
  • 76
    • 0029950149 scopus 로고    scopus 로고
    • Trafficking of cell-surface amyloid beta-protein precursor. I. Secretion, endocytosis and recycling as detected by labeled monoclonal antibody
    • - 998
    • Koo, E. H., Squazzo, S. L., Selkoe, D. J., and Koo, C. H. (1996) Trafficking of cell-surface amyloid beta-protein precursor. I. Secretion, endocytosis and recycling as detected by labeled monoclonal antibody J. Cell Sci. 109 (Pt 5) 991-998
    • (1996) J. Cell Sci. , vol.109 , Issue.PART 5 , pp. 991
    • Koo, E.H.1    Squazzo, S.L.2    Selkoe, D.J.3    Koo, C.H.4
  • 78
    • 79959886270 scopus 로고    scopus 로고
    • Amyloid precursor protein processing and Alzheimer's disease
    • - 204
    • O'Brien, R. J. and Wong, P. C. (2011) Amyloid precursor protein processing and Alzheimer's disease Annu. Rev. Neurosci. 34, 185-204
    • (2011) Annu. Rev. Neurosci. , vol.34 , pp. 185
    • O'Brien, R.J.1    Wong, P.C.2
  • 79
    • 33746355958 scopus 로고    scopus 로고
    • Axonal transport and Alzheimer's disease
    • - 627
    • Stokin, G. B. and Goldstein, L. S. (2006) Axonal transport and Alzheimer's disease Annu. Rev. Biochem. 75, 607-627
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 607
    • Stokin, G.B.1    Goldstein, L.S.2
  • 80
    • 10144263284 scopus 로고    scopus 로고
    • The beta-amyloid domain is essential for axonal sorting of amyloid precursor protein
    • Tienari, P., D. S., B., Ikonen, E., Simons, M., Weidemann, A., and Czech, C., (1996) The beta-amyloid domain is essential for axonal sorting of amyloid precursor protein., EMBO J. 15.
    • (1996) EMBO J. , vol.15
    • Tienari, P.1    Ikonen, E.2    Simons, M.3    Weidemann, A.4    Czech, C.5
  • 81
    • 0347357617 scopus 로고    scopus 로고
    • Protein folding and misfolding
    • - 890
    • Dobson, C. M. (2003) Protein folding and misfolding Nature 426, 884-890
    • (2003) Nature , vol.426 , pp. 884
    • Dobson, C.M.1
  • 82
    • 63849197629 scopus 로고    scopus 로고
    • Amyloid beta-protein assembly and Alzheimer disease
    • - 4753
    • Roychaudhuri, R., Yang, M., Hoshi, M. M., and Teplow, D. B. (2009) Amyloid beta-protein assembly and Alzheimer disease J. Biol. Chem. 284, 4749-4753
    • (2009) J. Biol. Chem. , vol.284 , pp. 4749
    • Roychaudhuri, R.1    Yang, M.2    Hoshi, M.M.3    Teplow, D.B.4
  • 85
    • 80052501210 scopus 로고    scopus 로고
    • Resolving controversies on the path to Alzheimer's therapeutics
    • - 1065
    • Selkoe, D. J. (2011) Resolving controversies on the path to Alzheimer's therapeutics Nat. Med. 17, 1060-1065
    • (2011) Nat. Med. , vol.17 , pp. 1060
    • Selkoe, D.J.1
  • 86
    • 45249102680 scopus 로고    scopus 로고
    • Structure-function relationships of pre-fibrillar protein assemblies in Alzheimer's disease and related disorders
    • - 341
    • Rahimi, F., Shanmugam, A., and Bitan, G. (2008) Structure-function relationships of pre-fibrillar protein assemblies in Alzheimer's disease and related disorders Curr. Alzheimer Res. 5, 319-341
    • (2008) Curr. Alzheimer Res. , vol.5 , pp. 319
    • Rahimi, F.1    Shanmugam, A.2    Bitan, G.3
  • 87
    • 77749308402 scopus 로고    scopus 로고
    • Amyloid oligomers: Formation and toxicity of Abeta oligomers
    • - 1358
    • Sakono, M. and Zako, T. (2010) Amyloid oligomers: formation and toxicity of Abeta oligomers FEBS J. 277, 1348-1358
    • (2010) FEBS J. , vol.277 , pp. 1348
    • Sakono, M.1    Zako, T.2
  • 88
    • 77954132249 scopus 로고    scopus 로고
    • Amyloid-beta-induced neuronal dysfunction in Alzheimer's disease: From synapses toward neural networks
    • - 818
    • Palop, J. J. and Mucke, L. (2010) Amyloid-beta-induced neuronal dysfunction in Alzheimer's disease: from synapses toward neural networks Nat. Neurosci. 13, 812-818
    • (2010) Nat. Neurosci. , vol.13 , pp. 812
    • Palop, J.J.1    Mucke, L.2
  • 89
    • 84880759156 scopus 로고    scopus 로고
    • Neurotoxicity of Amyloid beta-Protein: Synaptic and Network Dysfunction
    • Mucke, L. and Selkoe, D. J. (2012) Neurotoxicity of Amyloid beta-Protein: Synaptic and Network Dysfunction Cold Spring Harbor Perspect. Med. 2, a006338
    • (2012) Cold Spring Harbor Perspect. Med. , vol.2 , pp. 006338
    • Mucke, L.1    Selkoe, D.J.2
  • 90
    • 79959351077 scopus 로고    scopus 로고
    • Amyloid-beta annular protofibrils evade fibrillar fate in Alzheimer disease brain
    • - 22130
    • Lasagna-Reeves, C. A., Glabe, C. G., and Kayed, R. (2011) Amyloid-beta annular protofibrils evade fibrillar fate in Alzheimer disease brain J. Biol. Chem. 286, 22122-22130
    • (2011) J. Biol. Chem. , vol.286 , pp. 22122
    • Lasagna-Reeves, C.A.1    Glabe, C.G.2    Kayed, R.3
  • 91
    • 84857642949 scopus 로고    scopus 로고
    • The toxic Abeta oligomer and Alzheimer's disease: An emperor in need of clothes
    • - 357
    • Benilova, I., Karran, E., and De Strooper, B. (2012) The toxic Abeta oligomer and Alzheimer's disease: an emperor in need of clothes Nat. Neurosci. 15, 349-357
    • (2012) Nat. Neurosci. , vol.15 , pp. 349
    • Benilova, I.1    Karran, E.2    De Strooper, B.3
  • 92
    • 0037551741 scopus 로고    scopus 로고
    • Protofibrils, pores, fibrils, and neurodegeneration: Separating the responsible protein aggregates from the innocent bystanders
    • - 298
    • Caughey, B. and Lansbury, P. T. (2003) Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders Annu. Rev. Neurosci. 26, 267-298
    • (2003) Annu. Rev. Neurosci. , vol.26 , pp. 267
    • Caughey, B.1    Lansbury, P.T.2
  • 93
    • 33644861975 scopus 로고    scopus 로고
    • Common structure and toxic function of amyloid oligomers implies a common mechanism of pathogenesis
    • - 78
    • Glabe, C. G. and Kayed, R. (2006) Common structure and toxic function of amyloid oligomers implies a common mechanism of pathogenesis Neurology 66, S74-78
    • (2006) Neurology , vol.66 , pp. 74
    • Glabe, C.G.1    Kayed, R.2
  • 94
    • 0034951646 scopus 로고    scopus 로고
    • Chemical selection of elements by cells
    • - 595
    • Williams, R. (2001) Chemical selection of elements by cells Coord. Chem. Rev. 216, 583-595
    • (2001) Coord. Chem. Rev. , vol.216 , pp. 583
    • Williams, R.1
  • 95
    • 84865155590 scopus 로고    scopus 로고
    • Interdisciplinary challenges and promising theranostic effects of nanoscience in Alzheimer's disease
    • - 5033
    • Laurent, S., Ejtehadi, M. R., Rezaei, M., Kehoe, P. G., and Mahmoudi, M. (2012) Interdisciplinary challenges and promising theranostic effects of nanoscience in Alzheimer's disease RSC Adv. 2, 5008-5033
    • (2012) RSC Adv. , vol.2 , pp. 5008
    • Laurent, S.1    Ejtehadi, M.R.2    Rezaei, M.3    Kehoe, P.G.4    Mahmoudi, M.5
  • 96
    • 84944174559 scopus 로고    scopus 로고
    • Serum Multivalent Cationic Pattern: Speculation on the reliable Approach for Detection of Alzheimer's Disease
    • 10.1038/srep02782
    • Azhdarzadeh, M. 2013, Serum Multivalent Cationic Pattern: Speculation on the reliable Approach for Detection of Alzheimer's Disease Sci. Rep. 3, 2783 10.1038/srep02782
    • (2013) Sci. Rep. , vol.3 , pp. 2783
    • Azhdarzadeh, M.1
  • 98
    • 66149153889 scopus 로고    scopus 로고
    • Comparison of amyloid plaque contrast generated by T2-weighted, T2-weighted, and susceptibility-weighted imaging methods in transgenic mouse models of Alzheimer's disease
    • - 1164
    • Chamberlain, R., Reyes, D., Curran, G. L., Marjanska, M., Wengenack, T. M., Poduslo, J. F., Garwood, M., and Jack, C. R., Jr. (2009) Comparison of amyloid plaque contrast generated by T2-weighted, T2*-weighted, and susceptibility-weighted imaging methods in transgenic mouse models of Alzheimer's disease Magn. Reson. Med. 61, 1158-1164
    • (2009) Magn. Reson. Med. , vol.61 , pp. 1158
    • Chamberlain, R.1    Reyes, D.2    Curran, G.L.3    Marjanska, M.4    Wengenack, T.M.5    Poduslo, J.F.6    Garwood, M.7    Jack, Jr.C.R.8
  • 99
    • 84883151906 scopus 로고    scopus 로고
    • Microvascular cerebral blood volume changes in aging APP(swe)/PS1 (dE9) AD mouse model: A voxel-wise approach
    • - 1898
    • Zerbi, V., Jansen, D., Dederen, P. J., Veltien, A., Hamans, B., Liu, Y., Heerschap, A., and Kiliaan, A. J. (2012) Microvascular cerebral blood volume changes in aging APP(swe)/PS1 (dE9) AD mouse model: a voxel-wise approach Brain Struc. Funct. 218, 1805-1898
    • (2012) Brain Struc. Funct. , vol.218 , pp. 1805
    • Zerbi, V.1    Jansen, D.2    Dederen, P.J.3    Veltien, A.4    Hamans, B.5    Liu, Y.6    Heerschap, A.7    Kiliaan, A.J.8
  • 100
    • 84855688858 scopus 로고    scopus 로고
    • Nanotherapeutics for Alzheimer's disease (AD): Past, present and future
    • - 113
    • Fazil, M., Shadab, Baboota, S., Sahni, J. K., and Ali, J. (2012) Nanotherapeutics for Alzheimer's disease (AD): Past, present and future J. Drug Targeting 20, 97-113
    • (2012) J. Drug Targeting , vol.20 , pp. 97
    • Fazil, M.1    Shadab Baboota, S.2    Sahni, J.K.3    Ali, J.4
  • 101
    • 6944255523 scopus 로고    scopus 로고
    • Delivery of therapeutic agents to the central nervous system: The problems and the possibilities
    • - 45
    • Begley, D. J. (2004) Delivery of therapeutic agents to the central nervous system: the problems and the possibilities Pharmacol. Ther. 104, 29-45
    • (2004) Pharmacol. Ther. , vol.104 , pp. 29
    • Begley, D.J.1
  • 102
    • 70449529637 scopus 로고    scopus 로고
    • Approaches to transport therapeutic drugs across the blood-brain barrier to treat brain diseases
    • - 57
    • Gabathuler, R. (2010) Approaches to transport therapeutic drugs across the blood-brain barrier to treat brain diseases Neurobiol. Dis. 37, 48-57
    • (2010) Neurobiol. Dis. , vol.37 , pp. 48
    • Gabathuler, R.1
  • 103
    • 27744599588 scopus 로고    scopus 로고
    • Targeted nanoparticles for drug delivery through the blood-brain barrier for Alzheimer's disease
    • - 214
    • Roney, C., Kulkarni, P., Arora, V., Antich, P., Bonte, F., and Wu, A. 2005, Targeted nanoparticles for drug delivery through the blood-brain barrier for Alzheimer's disease J. Controlled Release 108, 193-214
    • (2005) J. Controlled Release , vol.108 , pp. 193
    • Roney, C.1    Kulkarni, P.2    Arora, V.3    Antich, P.4    Bonte, F.5    Wu, A.6
  • 105
    • 79952670561 scopus 로고    scopus 로고
    • Detection of amyloid plaques targeted by USPIO-Abeta1-42 in Alzheimer's disease transgenic mice using magnetic resonance microimaging
    • - 1609
    • Yang, J., Wadghiri, Y. Z., Hoang, D. M., Tsui, W., Sun, Y., Chung, E., Li, Y., Wang, A., de Leon, M., and Wisniewski, T. (2011) Detection of amyloid plaques targeted by USPIO-Abeta1-42 in Alzheimer's disease transgenic mice using magnetic resonance microimaging NeuroImage 55, 1600-1609
    • (2011) NeuroImage , vol.55 , pp. 1600
    • Yang, J.1    Wadghiri, Y.Z.2    Hoang, D.M.3    Tsui, W.4    Sun, Y.5    Chung, E.6    Li, Y.7    Wang, A.8    De Leon, M.9    Wisniewski, T.10
  • 106
    • 78751501329 scopus 로고    scopus 로고
    • Noninvasive magnetic resonance imaging detection of cerebral amyloid angiopathy-related microvascular alterations using superparamagnetic iron oxide particles in APP transgenic mouse models of Alzheimer's disease: Application to passive Abeta immunotherapy
    • - 1031
    • Beckmann, N., Gerard, C., Abramowski, D., Cannet, C., and Staufenbiel, M. (2011) Noninvasive magnetic resonance imaging detection of cerebral amyloid angiopathy-related microvascular alterations using superparamagnetic iron oxide particles in APP transgenic mouse models of Alzheimer's disease: application to passive Abeta immunotherapy J. Neurosci. 31, 1023-1031
    • (2011) J. Neurosci. , vol.31 , pp. 1023
    • Beckmann, N.1    Gerard, C.2    Abramowski, D.3    Cannet, C.4    Staufenbiel, M.5
  • 110
    • 36048993546 scopus 로고    scopus 로고
    • Nanoplatforms for targeted molecular imaging in living subjects
    • - 1854
    • Cai, W. and Chen, X. (2007) Nanoplatforms for targeted molecular imaging in living subjects Small 3, 1840-1854
    • (2007) Small , vol.3 , pp. 1840
    • Cai, W.1    Chen, X.2
  • 111
    • 84872719911 scopus 로고    scopus 로고
    • Controlled intracellular self-assembly of gadolinium nanoparticles as smart molecular MR contrast agents
    • Cao, C. Y., Shen, Y. Y., Wang, J. D., Li, L., and Liang, G. L. (2013) Controlled intracellular self-assembly of gadolinium nanoparticles as smart molecular MR contrast agents Sci. Rep. 3, 1024
    • (2013) Sci. Rep. , vol.3 , pp. 1024
    • Cao, C.Y.1    Shen, Y.Y.2    Wang, J.D.3    Li, L.4    Liang, G.L.5
  • 112
    • 84867891642 scopus 로고    scopus 로고
    • Gadolinium-based magnetic resonance contrast agents for neuroradiology: An overview
    • - 631
    • Kanal, E. (2012) Gadolinium-based magnetic resonance contrast agents for neuroradiology: an overview Magn. Reson. Imaging Clin. North Am. 20, 625-631
    • (2012) Magn. Reson. Imaging Clin. North Am. , vol.20 , pp. 625
    • Kanal, E.1
  • 114
    • 0842285216 scopus 로고    scopus 로고
    • Synthesis and physicochemical characterization of Gd-DTPA-B(sLex)A, a new MRI contrast agent targeted to inflammation
    • - 103
    • Laurent, S., Vander Elst, L., Fu, Y., and Muller, R. N. (2004) Synthesis and physicochemical characterization of Gd-DTPA-B(sLex)A, a new MRI contrast agent targeted to inflammation Bioconjugate Chem. 15, 99-103
    • (2004) Bioconjugate Chem. , vol.15 , pp. 99
    • Laurent, S.1    Vander Elst, L.2    Fu, Y.3    Muller, R.N.4
  • 116
    • 79952685419 scopus 로고    scopus 로고
    • Superparamagnetic colloidal nanocrystal clusters coated with polyethylene glycol fumarate: A possible novel theranostic agent
    • - 1030
    • Amiri, H., Mahmoudi, M., and Lascialfari, A. (2011) Superparamagnetic colloidal nanocrystal clusters coated with polyethylene glycol fumarate: a possible novel theranostic agent Nanoscale 3, 1022-1030
    • (2011) Nanoscale , vol.3 , pp. 1022
    • Amiri, H.1    Mahmoudi, M.2    Lascialfari, A.3
  • 117
    • 84873703911 scopus 로고    scopus 로고
    • Synthesis of pseudopolyrotaxanes-coated Superparamagnetic Iron Oxide Nanoparticles as new MRI contrast agent
    • - 657
    • Hosseini, F., P., A., Adeli, M., Amiri, H., Lascialfari, A., Orsini, F., Doschak, M. R., and Mahmoudi, M. (2013) Synthesis of pseudopolyrotaxanes-coated Superparamagnetic Iron Oxide Nanoparticles as new MRI contrast agent Colloids Surf., B 652-657
    • (2013) Colloids Surf., B , pp. 652
    • Hosseini, F.1    Adeli, M.2    Amiri, H.3    Lascialfari, A.4    Orsini, F.5    Doschak, M.R.6    Mahmoudi, M.7
  • 118
    • 84857619411 scopus 로고    scopus 로고
    • Superparamagnetic iron oxide based MRI contrast agents: Current status of clinical application
    • - 40
    • Wang, Y. X. (2011) Superparamagnetic iron oxide based MRI contrast agents: Current status of clinical application Quant. Imaging Med. Surg. 1, 35-40
    • (2011) Quant. Imaging Med. Surg. , vol.1 , pp. 35
    • Wang, Y.X.1
  • 120
    • 79955991824 scopus 로고    scopus 로고
    • In vivo detection of amyloid beta deposition using (1)(9)F magnetic resonance imaging with a (1)(9)F-containing curcumin derivative in a mouse model of Alzheimer's disease
    • - 127
    • Yanagisawa, D., Amatsubo, T., Morikawa, S., Taguchi, H., Urushitani, M., Shirai, N., Hirao, K., Shiino, A., Inubushi, T., and Tooyama, I. (2011) In vivo detection of amyloid beta deposition using (1)(9)F magnetic resonance imaging with a (1)(9)F-containing curcumin derivative in a mouse model of Alzheimer's disease Neuroscience 184, 120-127
    • (2011) Neuroscience , vol.184 , pp. 120
    • Yanagisawa, D.1    Amatsubo, T.2    Morikawa, S.3    Taguchi, H.4    Urushitani, M.5    Shirai, N.6    Hirao, K.7    Shiino, A.8    Inubushi, T.9    Tooyama, I.10
  • 122
    • 84875154058 scopus 로고    scopus 로고
    • Therapeutic benefits from nanoparticles: The potential significance of nanoscience in diseases with compromise to the blood brain barrier
    • - 1903
    • Krol, S., Macrez, R., Docagne, F., Defer, G., Laurent, S., Rahman, M., Hajipour, M. J., Kehoe, P. G., and Mahmoudi, M. (2013) Therapeutic benefits from nanoparticles: the potential significance of nanoscience in diseases with compromise to the blood brain barrier Chem. Rev. 113, 1877-1903
    • (2013) Chem. Rev. , vol.113 , pp. 1877
    • Krol, S.1    MacRez, R.2    Docagne, F.3    Defer, G.4    Laurent, S.5    Rahman, M.6    Hajipour, M.J.7    Kehoe, P.G.8    Mahmoudi, M.9
  • 123
    • 84875545405 scopus 로고    scopus 로고
    • Influence of the physiochemical properties of superparamagnetic iron oxide nanoparticles on amyloid beta protein fibrillation in solution
    • - 485
    • Mahmoudi, M., Quinlan-Pluck, F., Monopoli, M. P., Sheibani, S., Vali, H., Dawson, K. A., and Lynch, I. (2013) Influence of the physiochemical properties of superparamagnetic iron oxide nanoparticles on amyloid beta protein fibrillation in solution ACS Chem. Neurosci. 4, 475-485
    • (2013) ACS Chem. Neurosci. , vol.4 , pp. 475
    • Mahmoudi, M.1    Quinlan-Pluck, F.2    Monopoli, M.P.3    Sheibani, S.4    Vali, H.5    Dawson, K.A.6    Lynch, I.7
  • 124
    • 77951681963 scopus 로고    scopus 로고
    • Dual effect of amino modified polystyrene nanoparticles on amyloid beta protein fibrillation
    • - 287
    • Cabaleiro-Lago, C., Quinlan-Pluck, F., Lynch, I., Dawson, K. A., and Linse, S. (2010) Dual effect of amino modified polystyrene nanoparticles on amyloid beta protein fibrillation ACS Chem. Neurosci. 1, 279-287
    • (2010) ACS Chem. Neurosci. , vol.1 , pp. 279
    • Cabaleiro-Lago, C.1    Quinlan-Pluck, F.2    Lynch, I.3    Dawson, K.A.4    Linse, S.5
  • 127
    • 79952302512 scopus 로고    scopus 로고
    • Physical-chemical aspects of protein corona: Relevance to in vitro and in vivo biological impacts of nanoparticles
    • - 2534
    • Monopoli, M. P., Walczyk, D., Campbell, A., Elia, G., Lynch, I., Bombelli, F. B., and Dawson, K. A. (2011) Physical-chemical aspects of protein corona: relevance to in vitro and in vivo biological impacts of nanoparticles J. Am. Chem. Soc. 133, 2525-2534
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 2525
    • Monopoli, M.P.1    Walczyk, D.2    Campbell, A.3    Elia, G.4    Lynch, I.5    Bombelli, F.B.6    Dawson, K.A.7
  • 129
    • 84864241697 scopus 로고    scopus 로고
    • Effects of the presence or absence of a protein corona on silica nanoparticle uptake and impact on cells
    • - 5857
    • Lesniak, A., Fenaroli, F., Monopoli, M. P., Aberg, C., Dawson, K. A., and Salvati, A. (2012) Effects of the presence or absence of a protein corona on silica nanoparticle uptake and impact on cells ACS Nano 6, 5845-5857
    • (2012) ACS Nano , vol.6 , pp. 5845
    • Lesniak, A.1    Fenaroli, F.2    Monopoli, M.P.3    Aberg, C.4    Dawson, K.A.5    Salvati, A.6
  • 130
  • 131
    • 84870950366 scopus 로고    scopus 로고
    • Graphene oxide strongly inhibits amyloid beta fibrillation
    • - 7325
    • Mahmoudi, M., Akhavan, O., Ghavami, M., Rezaee, F., and Ghiasi, S. M. (2012) Graphene oxide strongly inhibits amyloid beta fibrillation Nanoscale 4, 7322-7325
    • (2012) Nanoscale , vol.4 , pp. 7322
    • Mahmoudi, M.1    Akhavan, O.2    Ghavami, M.3    Rezaee, F.4    Ghiasi, S.M.5
  • 133
    • 84875516187 scopus 로고    scopus 로고
    • Physiological temperature has a crucial role in amyloid beta in the absence and presence of hydrophobic and hydrophilic nanoparticles
    • - 378
    • Ghavami, M., Rezaei, M., Ejtehadi, R., Lotfi, M., Shokrgozar, M. A., Abd Emamy, B., Raush, J., and Mahmoudi, M. (2013) Physiological temperature has a crucial role in amyloid beta in the absence and presence of hydrophobic and hydrophilic nanoparticles ACS Chem. Neurosci. 4, 375-378
    • (2013) ACS Chem. Neurosci. , vol.4 , pp. 375
    • Ghavami, M.1    Rezaei, M.2    Ejtehadi, R.3    Lotfi, M.4    Shokrgozar, M.A.5    Abd Emamy, B.6    Raush, J.7    Mahmoudi, M.8
  • 134
    • 80053333203 scopus 로고    scopus 로고
    • Toxicity evaluations of superparamagnetic iron oxide nanoparticles: Cell "vision" versus physicochemical properties of nanoparticles
    • - 7276
    • Mahmoudi, M., Laurent, S., Shokrgozar, M. A., and Hosseinkhani, M. (2011) Toxicity evaluations of superparamagnetic iron oxide nanoparticles: cell "vision" versus physicochemical properties of nanoparticles ACS Nano 5, 7263-7276
    • (2011) ACS Nano , vol.5 , pp. 7263
    • Mahmoudi, M.1    Laurent, S.2    Shokrgozar, M.A.3    Hosseinkhani, M.4
  • 136
    • 84870818714 scopus 로고    scopus 로고
    • Cell type-specific activation of AKT and ERK signaling pathways by small negatively-charged magnetic nanoparticles
    • Rauch, J., Kolch, W., and Mahmoudi, M. (2012) Cell type-specific activation of AKT and ERK signaling pathways by small negatively-charged magnetic nanoparticles Sci. Rep. 2, 868
    • (2012) Sci. Rep. , vol.2 , pp. 868
    • Rauch, J.1    Kolch, W.2    Mahmoudi, M.3
  • 138
    • 84855611478 scopus 로고    scopus 로고
    • Crucial ignored parameters on nanotoxicology: The importance of toxicity assay modifications and "cell vision"
    • Laurent, S., Burtea, C., Thirifays, C., Hafeli, U. O., and Mahmoudi, M. (2012) Crucial ignored parameters on nanotoxicology: the importance of toxicity assay modifications and "cell vision" PloS one 7, e29997
    • (2012) PloS One , vol.7 , pp. 29997
    • Laurent, S.1    Burtea, C.2    Thirifays, C.3    Hafeli, U.O.4    Mahmoudi, M.5
  • 139
    • 79951614619 scopus 로고    scopus 로고
    • Magnetic resonance imaging tracking of stem cells in vivo using iron oxide nanoparticles as a tool for the advancement of clinical regenerative medicine
    • - 280
    • Mahmoudi, M., Hosseinkhani, H., Hosseinkhani, M., Boutry, S., Simchi, A., Journeay, W. S., Subramani, K., and Laurent, S. (2011) Magnetic resonance imaging tracking of stem cells in vivo using iron oxide nanoparticles as a tool for the advancement of clinical regenerative medicine Chem. Rev. 111, 253-280
    • (2011) Chem. Rev. , vol.111 , pp. 253
    • Mahmoudi, M.1    Hosseinkhani, H.2    Hosseinkhani, M.3    Boutry, S.4    Simchi, A.5    Journeay, W.S.6    Subramani, K.7    Laurent, S.8
  • 140
    • 79951588828 scopus 로고    scopus 로고
    • Surface Architecture of Superparamagnetic Iron Oxide Nanoparticles for Application in Drug Delivery and Their Biological Response: A Review
    • - 201
    • Mahmoudi, M., M., A., and Stroeve, P. (2010) Surface Architecture of Superparamagnetic Iron Oxide Nanoparticles for Application in Drug Delivery and Their Biological Response: A Review Int. J. Biomed. Nanosci. Nanotechnol. 164-201
    • (2010) Int. J. Biomed. Nanosci. Nanotechnol. , pp. 164
    • Mahmoudi, M.1    Stroeve, P.2
  • 141
    • 79952668032 scopus 로고    scopus 로고
    • Irreversible changes in protein conformation due to interaction with superparamagnetic iron oxide nanoparticles
    • - 1138
    • Mahmoudi, M., Shokrgozar, M. A., Sardari, S., Moghadam, M. K., Vali, H., Laurent, S., and Stroeve, P. (2011) Irreversible changes in protein conformation due to interaction with superparamagnetic iron oxide nanoparticles Nanoscale 3, 1127-1138
    • (2011) Nanoscale , vol.3 , pp. 1127
    • Mahmoudi, M.1    Shokrgozar, M.A.2    Sardari, S.3    Moghadam, M.K.4    Vali, H.5    Laurent, S.6    Stroeve, P.7
  • 142
    • 77956861022 scopus 로고    scopus 로고
    • Recent Advances in Surface Engineering of Superparamagnetic Iron Oxide Nanoparticles for Biomedical Applications
    • - S27
    • Mahmoudi, M., S., A., and Imani, M. (2010) Recent Advances in Surface Engineering of Superparamagnetic Iron Oxide Nanoparticles for Biomedical Applications J. Iran. Chem. Soc. 7, S1-S27
    • (2010) J. Iran. Chem. Soc. , vol.7 , pp. 1
    • Mahmoudi, M.1    Imani, M.2
  • 144
    • 34848828298 scopus 로고    scopus 로고
    • Iron oxide particle-enhanced MRI suggests variability of brain inflammation at early stages after ischemic stroke
    • - 2737
    • Saleh, A., Schroeter, M., Ringelstein, A., Hartung, H. P., Siebler, M., Modder, U., and Jander, S. (2007) Iron oxide particle-enhanced MRI suggests variability of brain inflammation at early stages after ischemic stroke Stroke 38, 2733-2737
    • (2007) Stroke , vol.38 , pp. 2733
    • Saleh, A.1    Schroeter, M.2    Ringelstein, A.3    Hartung, H.P.4    Siebler, M.5    Modder, U.6    Jander, S.7
  • 145
    • 33750597937 scopus 로고    scopus 로고
    • MR imaging of relapsing multiple sclerosis patients using ultra-small-particle iron oxide and compared with gadolinium
    • - 1005
    • Dousset, V., Brochet, B., Deloire, M. S., Lagoarde, L., Barroso, B., Caille, J. M., and Petry, K. G. (2006) MR imaging of relapsing multiple sclerosis patients using ultra-small-particle iron oxide and compared with gadolinium AJNR Am. J. Neuroradiol. 27, 1000-1005
    • (2006) AJNR Am. J. Neuroradiol. , vol.27 , pp. 1000
    • Dousset, V.1    Brochet, B.2    Deloire, M.S.3    Lagoarde, L.4    Barroso, B.5    Caille, J.M.6    Petry, K.G.7
  • 147
    • 79952809883 scopus 로고    scopus 로고
    • Superparamagnetic iron oxide nanoparticles: Promises for diagnosis and treatment of multiple sclerosis
    • - 140
    • Mahmoudi, M., Sahraian, M. A., Shokrgozar, M. A., and Laurent, S. (2011) Superparamagnetic iron oxide nanoparticles: promises for diagnosis and treatment of multiple sclerosis ACS Chem. Neurosci. 2, 118-140
    • (2011) ACS Chem. Neurosci. , vol.2 , pp. 118
    • Mahmoudi, M.1    Sahraian, M.A.2    Shokrgozar, M.A.3    Laurent, S.4
  • 148
    • 78649522496 scopus 로고    scopus 로고
    • Superparamagnetic iron oxide nanoparticles (SPIONs): Development, surface modification and applications in chemotherapy
    • - 46
    • Mahmoudi, M., Sant, S., Wang, B., Laurent, S., and Sen, T. (2011) Superparamagnetic iron oxide nanoparticles (SPIONs): development, surface modification and applications in chemotherapy Adv. Drug Delivery Rev. 63, 24-46
    • (2011) Adv. Drug Delivery Rev. , vol.63 , pp. 24
    • Mahmoudi, M.1    Sant, S.2    Wang, B.3    Laurent, S.4    Sen, T.5
  • 151
    • 67649148203 scopus 로고    scopus 로고
    • Synthesis and characterization of fluorinated magnetic core-shell nanoparticles for inhibition of insulin amyloid fibril formation
    • Skaat, H., Belfort, G., and Margel, S. (2009) Synthesis and characterization of fluorinated magnetic core-shell nanoparticles for inhibition of insulin amyloid fibril formation Nanotechnology 20, 225106
    • (2009) Nanotechnology , vol.20 , pp. 225106
    • Skaat, H.1    Belfort, G.2    Margel, S.3
  • 152
    • 67650492226 scopus 로고    scopus 로고
    • Synthesis of fluorescent-maghemite nanoparticles as multimodal imaging
    • - 649
    • Skaat, H. and Margel, S. (2009) Synthesis of fluorescent-maghemite nanoparticles as multimodal imaging agents for amyloid-beta fibrils detection and removal by a magnetic field Biochem. Biophys. Res. Commun. 386, 645-649
    • (2009) Biochem. Biophys. Res. Commun. , vol.386 , pp. 645
    • Skaat, H.1    Margel, S.2
  • 153
    • 70349466557 scopus 로고    scopus 로고
    • Effect of maghemite nanoparticles on insulin amyloid fibril formation: Selective labeling, kinetics, and fibril removal by a magnetic field
    • - 351
    • Skaat, H., Sorci, M., Belfort, G., and Margel, S. (2009) Effect of maghemite nanoparticles on insulin amyloid fibril formation: selective labeling, kinetics, and fibril removal by a magnetic field J. Biomed. Mater. Res., Part A 91, 342-351
    • (2009) J. Biomed. Mater. Res., Part A , vol.91 , pp. 342
    • Skaat, H.1    Sorci, M.2    Belfort, G.3    Margel, S.4
  • 154
    • 84858745162 scopus 로고    scopus 로고
    • Preparation of amyloid-like fibrils containing magnetic iron oxide nanoparticles: Effect of protein aggregation on proton relaxivity
    • - 686
    • Andersson, B. V., Skoglund, C., Uvdal, K., and Solin, N. (2012) Preparation of amyloid-like fibrils containing magnetic iron oxide nanoparticles: effect of protein aggregation on proton relaxivity Biochem. Biophys. Res. Commun. 419, 682-686
    • (2012) Biochem. Biophys. Res. Commun. , vol.419 , pp. 682
    • Andersson, B.V.1    Skoglund, C.2    Uvdal, K.3    Solin, N.4
  • 156
    • 84859706269 scopus 로고    scopus 로고
    • Assessing the in vitro and in vivo toxicity of superparamagnetic iron oxide nanoparticles
    • - 2338
    • Mahmoudi, M., Hofmann, H., Rothen-Rutishauser, B., and Petri-Fink, A. (2012) Assessing the in vitro and in vivo toxicity of superparamagnetic iron oxide nanoparticles Chem. Rev. 112, 2323-2338
    • (2012) Chem. Rev. , vol.112 , pp. 2323
    • Mahmoudi, M.1    Hofmann, H.2    Rothen-Rutishauser, B.3    Petri-Fink, A.4
  • 157
    • 84874023865 scopus 로고    scopus 로고
    • A cool way to live long
    • - 672
    • Conti, B. and Hansen, M. (2013) A cool way to live long Cell 152, 671-672
    • (2013) Cell , vol.152 , pp. 671
    • Conti, B.1    Hansen, M.2
  • 158
    • 84874065131 scopus 로고    scopus 로고
    • A Genetic Program Promotes C elegans Longevity at Cold Temperatures via a Thermosensitive TRP Channel
    • - 817
    • Xiao, R., Zhang, B., Dong, Y., Gong, J., Xu, T., Liu, J., and Xu, X. Z. (2013) A Genetic Program Promotes C. elegans Longevity at Cold Temperatures via a Thermosensitive TRP Channel Cell 152, 806-817
    • (2013) Cell , vol.152 , pp. 806
    • Xiao, R.1    Zhang, B.2    Dong, Y.3    Gong, J.4    Xu, T.5    Liu, J.6    Xu, X.Z.7
  • 160
    • 34147115541 scopus 로고    scopus 로고
    • Ccr2 deficiency impairs microglial accumulation and accelerates progression of Alzheimer-like disease
    • - 438
    • El Khoury, J., Toft, M., Hickman, S. E., Means, T. K., Terada, K., Geula, C., and Luster, A. D. (2007) Ccr2 deficiency impairs microglial accumulation and accelerates progression of Alzheimer-like disease Nat. Med. 13, 432-438
    • (2007) Nat. Med. , vol.13 , pp. 432
    • El Khoury, J.1    Toft, M.2    Hickman, S.E.3    Means, T.K.4    Terada, K.5    Geula, C.6    Luster, A.D.7
  • 161
    • 77949890133 scopus 로고    scopus 로고
    • Mechanisms of mononuclear phagocyte recruitment in Alzheimer's disease
    • - 173
    • Hickman, S. E. and El Khoury, J. (2010) Mechanisms of mononuclear phagocyte recruitment in Alzheimer's disease CNS Neurol. Disord.: Drug Targets 9, 168-173
    • (2010) CNS Neurol. Disord.: Drug Targets , vol.9 , pp. 168
    • Hickman, S.E.1    El Khoury, J.2
  • 162
    • 78650606928 scopus 로고    scopus 로고
    • Nanoparticle-induced unfolding of fibrinogen promotes Mac-1 receptor activation and inflammation
    • - 44
    • Deng, Z. J., Liang, M., Monteiro, M., Toth, I., and Minchin, R. F. (2011) Nanoparticle-induced unfolding of fibrinogen promotes Mac-1 receptor activation and inflammation Nature Nanotechnol. 6, 39-44
    • (2011) Nature Nanotechnol. , vol.6 , pp. 39
    • Deng, Z.J.1    Liang, M.2    Monteiro, M.3    Toth, I.4    Minchin, R.F.5


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