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Volumn 8, Issue SEP, 2016, Pages

In vivo differential brain clearance and catabolism of monomeric and oligomeric alzheimer's aβ protein

Author keywords

A brain efflux; A brain homeostasis; Cerebrospinal fluid; Local proteolytic degradation; Stereotaxic intra cerebral injection; Targeted mass spectrometric analysis

Indexed keywords

AMYLOID BETA PROTEIN[1-40]; MONOMER; OLIGOMER;

EID: 84992045356     PISSN: None     EISSN: 16634365     Source Type: Journal    
DOI: 10.3389/fnagi.2016.00223     Document Type: Article
Times cited : (37)

References (108)
  • 1
    • 0036319335 scopus 로고    scopus 로고
    • Astrocyte-endothelial interactions and blood-brain barrier permeability
    • Abbott, N. J. (2002). Astrocyte-endothelial interactions and blood-brain barrier permeability. J. Anat. 200, 629-638. doi: 10.1046/j.1469-7580.2002.00064.x.
    • (2002) J. Anat , vol.200 , pp. 629-638
    • Abbott, N.J.1
  • 3
    • 0035015517 scopus 로고    scopus 로고
    • Pericytes: cell biology and pathology
    • Allt, G., and Lawrenson, J. G. (2001). Pericytes: cell biology and pathology. Cells Tissues Organs 169, 1-11. doi: 10.1159/000047855.
    • (2001) Cells Tissues Organs , vol.169 , pp. 1-11
    • Allt, G.1    Lawrenson, J.G.2
  • 4
    • 25444463573 scopus 로고    scopus 로고
    • Endothelial/pericyte interactions
    • Armulik, A., Abramsson, A., and Betsholtz, C. (2005). Endothelial/pericyte interactions. Circ. Res. 97, 512-523. doi: 10.1161/01.RES.0000182903.16652.d7.
    • (2005) Circ. Res , vol.97 , pp. 512-523
    • Armulik, A.1    Abramsson, A.2    Betsholtz, C.3
  • 5
    • 84942469639 scopus 로고    scopus 로고
    • A dural lymphatic vascular system that drains brain interstitial fluid and macromolecules
    • Aspelund, A., Antila, S., Proulx, S. T., Karlsen, T. V., Karaman, S., Detmar, M., et al. (2015). A dural lymphatic vascular system that drains brain interstitial fluid and macromolecules. J. Exp. Med. 212, 991-999. doi: 10.1084/jem.20142290.
    • (2015) J. Exp. Med , vol.212 , pp. 991-999
    • Aspelund, A.1    Antila, S.2    Proulx, S.T.3    Karlsen, T.V.4    Karaman, S.5    Detmar, M.6
  • 6
    • 0035984815 scopus 로고    scopus 로고
    • Brain clearance of Alzheimer's amyloid-β40 in the squirrel monkey: a SPECT study in a primate model of cerebral amyloid angiopathy
    • Bading, J., Yamada, S., Mackic, J. B., Kirkman, L., Miller, C. A., Calero, M., et al. (2002). Brain clearance of Alzheimer's amyloid-β40 in the squirrel monkey: a SPECT study in a primate model of cerebral amyloid angiopathy. J. Drug Target 10, 359-368. doi: 10.1080/10611860290031831.
    • (2002) J. Drug Target , vol.10 , pp. 359-368
    • Bading, J.1    Yamada, S.2    Mackic, J.B.3    Kirkman, L.4    Miller, C.A.5    Calero, M.6
  • 8
    • 84961216596 scopus 로고    scopus 로고
    • Lymphatic clearance of the brain: perivascular, paravascular and significance for neurodegenerative diseases
    • Bakker, E. N., Bacskai, B. J., Arbel-Ornath, M., Aldea, R., Bedussi, B., Morris, A. W., et al. (2016). Lymphatic clearance of the brain: perivascular, paravascular and significance for neurodegenerative diseases. Cell. Mol. Neurobiol. 36, 181-194. doi: 10.1007/s10571-015-0273-8.
    • (2016) Cell. Mol. Neurobiol , vol.36 , pp. 181-194
    • Bakker, E.N.1    Bacskai, B.J.2    Arbel-Ornath, M.3    Aldea, R.4    Bedussi, B.5    Morris, A.W.6
  • 9
    • 70349229285 scopus 로고    scopus 로고
    • Increased b-amyloid levels in the choroid plexus followig lead exposure and the involvement of low-density lipoprotein receptor protein-1
    • Behl, M., Zhang, Y., Monnot, A. D., Jiang, W., and Zheng, W. (2009). Increased b-amyloid levels in the choroid plexus followig lead exposure and the involvement of low-density lipoprotein receptor protein-1. Toxicol. Appl. Pharmacol. 240, 245-254. doi: 10.1016/j.taap.2009.05.024.
    • (2009) Toxicol. Appl. Pharmacol , vol.240 , pp. 245-254
    • Behl, M.1    Zhang, Y.2    Monnot, A.D.3    Jiang, W.4    Zheng, W.5
  • 10
    • 34247506244 scopus 로고    scopus 로고
    • Transport pathways for clearance of human Alzheimer's amyloid β-peptide and apolipoproteins E and J in the mouse central nervous system
    • Bell, R. D., Sagare, A. P., Friedman, A. E., Bedi, G. S., Holtzman, D. M., Deane, R., et al. (2007). Transport pathways for clearance of human Alzheimer's amyloid β-peptide and apolipoproteins E and J in the mouse central nervous system. J. Cereb. Blood Flow Metab. 27, 909-918. doi: 10.1038/sj.jcbfm.9600419.
    • (2007) J. Cereb. Blood Flow Metab , vol.27 , pp. 909-918
    • Bell, R.D.1    Sagare, A.P.2    Friedman, A.E.3    Bedi, G.S.4    Holtzman, D.M.5    Deane, R.6
  • 11
    • 0028298886 scopus 로고
    • Expression and function of the low density lipoprotein receptor-related protein (LRP) in mammalian central neurons
    • Bu, G., Maksymovitch, E. A., Nerbonne, J. M., and Schwartz, A. L. (1994). Expression and function of the low density lipoprotein receptor-related protein (LRP) in mammalian central neurons. J. Biol. Chem. 269, 18521-18528.
    • (1994) J. Biol. Chem , vol.269 , pp. 18521-18528
    • Bu, G.1    Maksymovitch, E.A.2    Nerbonne, J.M.3    Schwartz, A.L.4
  • 12
    • 0037186074 scopus 로고    scopus 로고
    • Altered metabolism of the amyloid β precursor protein is associated with mitochondrial dysfunction in Down's syndrome
    • Busciglio, J., Pelsman, A., Wong, C., Pigino, G., Yuan, M., Mori, H., et al. (2002). Altered metabolism of the amyloid β precursor protein is associated with mitochondrial dysfunction in Down's syndrome. Neuron 33, 677-688. doi: 10.1016/S0896-6273(02)00604-9.
    • (2002) Neuron , vol.33 , pp. 677-688
    • Busciglio, J.1    Pelsman, A.2    Wong, C.3    Pigino, G.4    Yuan, M.5    Mori, H.6
  • 13
    • 22844452055 scopus 로고    scopus 로고
    • "Radioiodination of Aβ peptides,"
    • eds E. M. Sigurdsson (Totowa, NJ: Humana Press)
    • Calero, M., and Ghiso, J. (2005). "Radioiodination of Aβ peptides," in Amyloid Proteins: Methods and Protocols, eds E. M. Sigurdsson (Totowa, NJ: Humana Press), 325-348.
    • (2005) Amyloid Proteins: Methods and Protocols , pp. 325-348
    • Calero, M.1    Ghiso, J.2
  • 14
    • 78650659385 scopus 로고    scopus 로고
    • Apical-to-basolateral transport of amyloid-β peptides through blood-brain barrier cells is mediated by the receptor for advanced glycation end-products and is restricted by P-glycoprotein
    • Candela, P., Gosselet, F., Saint-Pol, J., Sevin, E., Boucau, M. C., Boulanger, E., et al. (2010). Apical-to-basolateral transport of amyloid-β peptides through blood-brain barrier cells is mediated by the receptor for advanced glycation end-products and is restricted by P-glycoprotein. J. Alzheimers. Dis. 22, 849-859. doi: 10.3233/JAD-2010-100462.
    • (2010) J. Alzheimers. Dis , vol.22 , pp. 849-859
    • Candela, P.1    Gosselet, F.2    Saint-Pol, J.3    Sevin, E.4    Boucau, M.C.5    Boulanger, E.6
  • 15
    • 0037551741 scopus 로고    scopus 로고
    • Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the inocent bystanders
    • Caughey, B., and Lansbury, P. T. (2003). Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the inocent bystanders. Annu. Rev. Neurosci. 26, 267-298. doi: 10.1146/annurev.neuro.26.010302.081142.
    • (2003) Annu. Rev. Neurosci , vol.26 , pp. 267-298
    • Caughey, B.1    Lansbury, P.T.2
  • 17
    • 84885352675 scopus 로고    scopus 로고
    • Tau clearance mechanisms and their possible role in the pathogenesis of Alzheimer disease
    • Chesser, A. S., Pritchard, S. M., and Johnson, G. V. (2013). Tau clearance mechanisms and their possible role in the pathogenesis of Alzheimer disease. Front. Neurol. 4:122. doi: 10.3389/fneur.2013.00122.
    • (2013) Front. Neurol , vol.4 , pp. 122
    • Chesser, A.S.1    Pritchard, S.M.2    Johnson, G.V.3
  • 18
    • 65649105035 scopus 로고    scopus 로고
    • Clearance of amyloid-β peptide across the blood-brain barrier: implication for therapies in Alzheimer's disease
    • Deane, R., Bell, R. D., Sagare, A., and Zlokovic, B. (2009). Clearance of amyloid-β peptide across the blood-brain barrier: implication for therapies in Alzheimer's disease. CNS Neurol. Dis. Drug Targets 8, 16-30. doi: 10.2174/187152709787601867.
    • (2009) CNS Neurol. Dis. Drug Targets , vol.8 , pp. 16-30
    • Deane, R.1    Bell, R.D.2    Sagare, A.3    Zlokovic, B.4
  • 19
    • 48949117577 scopus 로고    scopus 로고
    • The role of the cell surface LRP and soluble LRP in blood-brain barrier Ab clearance in Alzheimer's disease
    • Deane, R., Sagare, A., and Zlokovic, B. V. (2008). The role of the cell surface LRP and soluble LRP in blood-brain barrier Ab clearance in Alzheimer's disease. Curr. Pharmac. Des. 14, 1601-1605. doi: 10.2174/138161208784705487.
    • (2008) Curr. Pharmac. Des , vol.14 , pp. 1601-1605
    • Deane, R.1    Sagare, A.2    Zlokovic, B.V.3
  • 20
    • 7644225312 scopus 로고    scopus 로고
    • RAGE (Yin) versus LRP (yang) balance regulates Alzheimer Amyloid b-peptide clearance through transport across the blood-brain-barrier
    • Deane, R., Wu, Z., and Zlokovic, B. (2004). RAGE (Yin) versus LRP (yang) balance regulates Alzheimer Amyloid b-peptide clearance through transport across the blood-brain-barrier. Stroke 35, 2628-2631. doi: 10.1161/01.STR.0000143452.85382.d1.
    • (2004) Stroke , vol.35 , pp. 2628-2631
    • Deane, R.1    Wu, Z.2    Zlokovic, B.3
  • 21
    • 0037703255 scopus 로고    scopus 로고
    • RAGE mediates amyloid-β peptide transport across the blood-brain barrier and accumulation on the brain
    • Deane, R., Du Yan, S., Submamaryan, R. K., LaEue, B., Jovanovic, S., Hogg, E., et al. (2003). RAGE mediates amyloid-β peptide transport across the blood-brain barrier and accumulation on the brain. Nat. Med. 9, 907-913. doi: 10.1038/nm890.
    • (2003) Nat. Med , vol.9 , pp. 907-913
    • Deane, R.1    Du Yan, S.2    Submamaryan, R.K.3    LaEue, B.4    Jovanovic, S.5    Hogg, E.6
  • 22
    • 77951060145 scopus 로고    scopus 로고
    • Proteases and proteolysis in Alzheimer disease: a multifactorial view on the disease process
    • De Strooper, B. (2010). Proteases and proteolysis in Alzheimer disease: a multifactorial view on the disease process. Physiol. Rev. 90, 465-494. doi: 10.1152/physrev.00023.2009.
    • (2010) Physiol. Rev , vol.90 , pp. 465-494
    • De Strooper, B.1
  • 23
    • 81955164821 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and accumulation of the β-secretase-cleaved C-terminal fragment of APP in Alzheimer's disease transgenic mice
    • Devi, L., and Ohno, M. (2012). Mitochondrial dysfunction and accumulation of the β-secretase-cleaved C-terminal fragment of APP in Alzheimer's disease transgenic mice. Neurobiol. Dis. 45, 417-424. doi: 10.1016/j.nbd.2011.09.001.
    • (2012) Neurobiol. Dis , vol.45 , pp. 417-424
    • Devi, L.1    Ohno, M.2
  • 24
    • 42649145866 scopus 로고    scopus 로고
    • Megalin mediates the transport of leptin across the blood-CSF barrier
    • Dietrich, M. O., Spuch, C., Antequera, D., Rodal, I., de Yebenes, J. G., Molina, J. A., et al. (2008). Megalin mediates the transport of leptin across the blood-CSF barrier. Neurobiol. Aging 26, 902-912. doi: 10.1016/j.neurobiolaging.2007.01.008.
    • (2008) Neurobiol. Aging , vol.26 , pp. 902-912
    • Dietrich, M.O.1    Spuch, C.2    Antequera, D.3    Rodal, I.4    de Yebenes, J.G.5    Molina, J.A.6
  • 25
    • 84947046996 scopus 로고    scopus 로고
    • Vascular dysfunction in the pathogenesis of Alzheimer's disease-A review of endothelium-mediated mechanisms and ensuing vicious circles
    • Di Marco, L. Y., Venneri, A., Farkas, E., Evans, P. C., Marzo, A., and Frangi, A. F. (2015). Vascular dysfunction in the pathogenesis of Alzheimer's disease-A review of endothelium-mediated mechanisms and ensuing vicious circles. Neurobiol. Dis. 82, 593-606. doi: 10.1016/j.nbd.2015.08.014.
    • (2015) Neurobiol. Dis , vol.82 , pp. 593-606
    • Di Marco, L.Y.1    Venneri, A.2    Farkas, E.3    Evans, P.C.4    Marzo, A.5    Frangi, A.F.6
  • 26
    • 75149142245 scopus 로고    scopus 로고
    • Differential activation of mitochondrial apoptotic pathways by vasculotropic amyloid-β variants in cells composing the cerebral vessel walls
    • Fossati, S., Cam, J., Meyerson, J., Mezhericher, E., Romero, I. A., Couraud, P.-O., et al. (2010). Differential activation of mitochondrial apoptotic pathways by vasculotropic amyloid-β variants in cells composing the cerebral vessel walls. FASEB J. 24, 229-241. doi: 10.1096/fj.09-139584.
    • (2010) FASEB J , vol.24 , pp. 229-241
    • Fossati, S.1    Cam, J.2    Meyerson, J.3    Mezhericher, E.4    Romero, I.A.5    Couraud, P.-O.6
  • 27
    • 84952907682 scopus 로고    scopus 로고
    • The carbonic anhydrase inhibitor methazolamide prevents amyloid β-induced mitochondrial dysfunction and caspase activation protecting neuronal and glial cells in vitro and in the mouse brain
    • Fossati, S., Giannoni, P., Solesio, M. E., Cocklin, S. L., Cabrera, E., Ghiso, J., et al. (2016). The carbonic anhydrase inhibitor methazolamide prevents amyloid β-induced mitochondrial dysfunction and caspase activation protecting neuronal and glial cells in vitro and in the mouse brain. Neurobiol. Dis. 86 29-40. doi: 10.1016/j.nbd.2015.11.006.
    • (2016) Neurobiol. Dis , vol.86 , pp. 29-40
    • Fossati, S.1    Giannoni, P.2    Solesio, M.E.3    Cocklin, S.L.4    Cabrera, E.5    Ghiso, J.6
  • 28
    • 84950146977 scopus 로고    scopus 로고
    • Vascular mTOR-dependent mechanisms linking the control of aging to Alzheimer's disease
    • Galvan, V., and Hart, M. J. (2016). Vascular mTOR-dependent mechanisms linking the control of aging to Alzheimer's disease. Biochim. Biophys. Acta 1862, 992-1007. doi: 10.1016/j.bbadis.2015.11.010.
    • (2016) Biochim. Biophys. Acta , vol.1862 , pp. 992-1007
    • Galvan, V.1    Hart, M.J.2
  • 29
    • 0030035294 scopus 로고    scopus 로고
    • Fate of cerebrospinal fluid-borne amyloid b-peptide: rapid clearence into blood and appreciable accumulation by cerebral arteries
    • Ghersi-Egea, J. F., Gorevic, P., Ghiso, J., Frangione, B., Patlak, C. S., and Fenstermacher, J. (1996). Fate of cerebrospinal fluid-borne amyloid b-peptide: rapid clearence into blood and appreciable accumulation by cerebral arteries. J. Neurochem. 67, 880-883. doi: 10.1046/j.1471-4159.1996.67020880.x.
    • (1996) J. Neurochem , vol.67 , pp. 880-883
    • Ghersi-Egea, J.F.1    Gorevic, P.2    Ghiso, J.3    Frangione, B.4    Patlak, C.S.5    Fenstermacher, J.6
  • 30
    • 0037038813 scopus 로고    scopus 로고
    • Amyloidosis and Alzheimer's disease
    • Ghiso, J., and Frangione, B. (2002). Amyloidosis and Alzheimer's disease. Adv. Drug Delivery Rev. 54, 1539-1551. doi: 10.1016/S0169-409X(02)00149-7.
    • (2002) Adv. Drug Delivery Rev , vol.54 , pp. 1539-1551
    • Ghiso, J.1    Frangione, B.2
  • 31
    • 0035941310 scopus 로고    scopus 로고
    • Systemic amyloid deposits in Familial British Dementia
    • Ghiso, J., Holton, J., Miravalle, L., Calero, M., Lashley, T., Vidal, R., et al. (2001). Systemic amyloid deposits in Familial British Dementia. J. Biol. Chem. 276, 43909-43914. doi: 10.1074/jbc.M105956200.
    • (2001) J. Biol. Chem , vol.276 , pp. 43909-43914
    • Ghiso, J.1    Holton, J.2    Miravalle, L.3    Calero, M.4    Lashley, T.5    Vidal, R.6
  • 32
    • 8544240891 scopus 로고    scopus 로고
    • Systemic catabolism of Alzheimer's Aβ40 and Aβ42
    • Ghiso, J., Shayo, M., Calero, M., Ng, D., Tomidokoro, Y., Gandy, S. E., et al. (2004). Systemic catabolism of Alzheimer's Aβ40 and Aβ42. J. Biol. Chem. 279, 45897-45908. doi: 10.1074/jbc.M407668200.
    • (2004) J. Biol. Chem , vol.279 , pp. 45897-45908
    • Ghiso, J.1    Shayo, M.2    Calero, M.3    Ng, D.4    Tomidokoro, Y.5    Gandy, S.E.6
  • 33
    • 33847662852 scopus 로고    scopus 로고
    • Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid β-peptide
    • Haass, C., and Selkoe, D. J. (2007). Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid β-peptide. Nat. Rev. Mol. Cell Biol. 8, 101-112. doi: 10.1038/nrm2101.
    • (2007) Nat. Rev. Mol. Cell Biol , vol.8 , pp. 101-112
    • Haass, C.1    Selkoe, D.J.2
  • 34
    • 70349558522 scopus 로고    scopus 로고
    • Genome-wide association study identifies variants at CLU and PICALM associated with Alzheimer's disease
    • Harold, D., Abraham, R., Hollingworth, P., Sims, R., Gerrish, A., Hamshere, M. L., et al. (2009). Genome-wide association study identifies variants at CLU and PICALM associated with Alzheimer's disease. Nat. Genet. 41, 1088-1093. doi: 10.1038/ng.440.
    • (2009) Nat. Genet , vol.41 , pp. 1088-1093
    • Harold, D.1    Abraham, R.2    Hollingworth, P.3    Sims, R.4    Gerrish, A.5    Hamshere, M.L.6
  • 35
    • 79954623282 scopus 로고    scopus 로고
    • Perivascular drainage of solutes is impaired in the ageing mouse brain and in the presence of cerebral amyloid angiopathy
    • Hawkes, C. A., Härtig, W., Kacza, J., Schliebs, R., Weller, R. O., Nicoll, J. A., et al. (2011). Perivascular drainage of solutes is impaired in the ageing mouse brain and in the presence of cerebral amyloid angiopathy. Acta Neuropathol. 121, 431-443. doi: 10.1007/s00401-011-0801-7.
    • (2011) Acta Neuropathol , vol.121 , pp. 431-443
    • Hawkes, C.A.1    Härtig, W.2    Kacza, J.3    Schliebs, R.4    Weller, R.O.5    Nicoll, J.A.6
  • 36
    • 84931291962 scopus 로고    scopus 로고
    • Sequential amyloid-β degradation by the matrix metalloproteases MMP-2 and MMP-9
    • Hernandez-Guillamon, M., Mawhirt, S., Blais, S., Montaner, J., Neubert, T. A., Rostagno, A., et al. (2015). Sequential amyloid-β degradation by the matrix metalloproteases MMP-2 and MMP-9. J. Biol. Chem. 290, 15078-15091. doi: 10.1074/jbc.M114.610931.
    • (2015) J. Biol. Chem , vol.290 , pp. 15078-15091
    • Hernandez-Guillamon, M.1    Mawhirt, S.2    Blais, S.3    Montaner, J.4    Neubert, T.A.5    Rostagno, A.6
  • 37
    • 79953854897 scopus 로고    scopus 로고
    • Alzheimer's disease: the challenge of the second century
    • Holtzman, D. M., Morris, J. C., and Goate, A. M. (2011). Alzheimer's disease: the challenge of the second century. Sci. Transl. Med. 3:77sr1. doi: 10.1126/scitranslmed.3002369.
    • (2011) Sci. Transl. Med , vol.3
    • Holtzman, D.M.1    Morris, J.C.2    Goate, A.M.3
  • 38
    • 84914691722 scopus 로고    scopus 로고
    • Impairment of glymphatic pathway function promotes tau pathology after traumatic brain injury
    • Iliff, J. J., Chen, M. J., Plog, B. A., Zeppenfeld, D. M., Soltero, M., Yang, L., et al. (2014). Impairment of glymphatic pathway function promotes tau pathology after traumatic brain injury. J. Neurosci. 34, 16180-16193. doi: 10.1523/JNEUROSCI.3020-14.2014.
    • (2014) J. Neurosci , vol.34 , pp. 16180-16193
    • Iliff, J.J.1    Chen, M.J.2    Plog, B.A.3    Zeppenfeld, D.M.4    Soltero, M.5    Yang, L.6
  • 39
    • 84865123660 scopus 로고    scopus 로고
    • A paravascular pathway facilitates CSF flow through the brain parenchyma and the clearance of interstitial solutes, including amyloid β
    • Iliff, J. J., Wang, M., Liao, Y., Plogg, B. A., Peng, W., Gundersen, G. A., et al. (2012). A paravascular pathway facilitates CSF flow through the brain parenchyma and the clearance of interstitial solutes, including amyloid β. Sci. Transl. Med. 4:147ra111. doi: 10.1126/scitranslmed.3003748.
    • (2012) Sci. Transl. Med , vol.4
    • Iliff, J.J.1    Wang, M.2    Liao, Y.3    Plogg, B.A.4    Peng, W.5    Gundersen, G.A.6
  • 40
    • 79955044494 scopus 로고    scopus 로고
    • Soluble amyloid β-protein dimers isolated from Alzheimer cortex directly induce Tau hyperphosphorylation and neuritic degeneration
    • Jin, M., Shepardson, N., Yang, T., Chen, G., Walsh, D., and Selkoe, D. J. (2011). Soluble amyloid β-protein dimers isolated from Alzheimer cortex directly induce Tau hyperphosphorylation and neuritic degeneration. Proc. Natl. Acad. Sci. U.S.A. 108, 5819-5824. doi: 10.1073/pnas.1017033108.
    • (2011) Proc. Natl. Acad. Sci. U.S.A , vol.108 , pp. 5819-5824
    • Jin, M.1    Shepardson, N.2    Yang, T.3    Chen, G.4    Walsh, D.5    Selkoe, D.J.6
  • 42
    • 68949163262 scopus 로고    scopus 로고
    • Preparation of fluorescently-labeled amyloid-β peptide assemblies: the effect of fluorophore conjugation on structure and function
    • Jungbauera, L. M., Yua, C., Laxtona, K. J., and LaDu, M. J. (2009). Preparation of fluorescently-labeled amyloid-β peptide assemblies: the effect of fluorophore conjugation on structure and function. J. Mol. Recognit. 22, 403-413. doi: 10.1002/jmr.948.
    • (2009) J. Mol. Recognit , vol.22 , pp. 403-413
    • Jungbauera, L.M.1    Yua, C.2    Laxtona, K.J.3    LaDu, M.J.4
  • 43
    • 0034657130 scopus 로고    scopus 로고
    • Evidence for seeding of β-amyloid by intracerebral infusion of Alzheimer brain extracts in β-amyloid precursor protein-transgenic mice
    • Kane, M. D., Lipinski, W. J., Callahan, M. J., Bian, F., Durham, R. A., Schwarz, R. D., et al. (2000). Evidence for seeding of β-amyloid by intracerebral infusion of Alzheimer brain extracts in β-amyloid precursor protein-transgenic mice. J. Neurosci. 20, 3606-3611.
    • (2000) J. Neurosci , vol.20 , pp. 3606-3611
    • Kane, M.D.1    Lipinski, W.J.2    Callahan, M.J.3    Bian, F.4    Durham, R.A.5    Schwarz, R.D.6
  • 44
    • 84889041948 scopus 로고    scopus 로고
    • Neuronal clearance of amyloid-β by endocytic receptor LRP1
    • Kanekiyo, T., Cirrito, J. R., Liu, C. C., Shinohara, M., Li, J., Schuler, D. R., et al. (2013). Neuronal clearance of amyloid-β by endocytic receptor LRP1. J. Neurosci. 33, 19276-19283. doi: 10.1523/JNEUROSCI.3487-13.2013.
    • (2013) J. Neurosci , vol.33 , pp. 19276-19283
    • Kanekiyo, T.1    Cirrito, J.R.2    Liu, C.C.3    Shinohara, M.4    Li, J.5    Schuler, D.R.6
  • 45
    • 84869037441 scopus 로고    scopus 로고
    • LRP1 in brain vascular smooth muscle cells mediates local clearance of Alzheimer's amyloid-β
    • Kanekiyo, T., Liu, C. C., Shinohara, M., Li, J., and Bu, G. (2012). LRP1 in brain vascular smooth muscle cells mediates local clearance of Alzheimer's amyloid-β. J. Neurosci. 32, 16458-16465. doi: 10.1523/JNEUROSCI.3987-12.2012.
    • (2012) J. Neurosci , vol.32 , pp. 16458-16465
    • Kanekiyo, T.1    Liu, C.C.2    Shinohara, M.3    Li, J.4    Bu, G.5
  • 46
    • 0023105114 scopus 로고
    • The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor
    • Kang, J., Lemaire, H. G., Unterbeck, A., Salbaum, J. M., Masters, C. L., Grzeschik, K. H., et al. (1987). The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor. Nature 325, 733-736. doi: 10.1038/325733a0.
    • (1987) Nature , vol.325 , pp. 733-736
    • Kang, J.1    Lemaire, H.G.2    Unterbeck, A.3    Salbaum, J.M.4    Masters, C.L.5    Grzeschik, K.H.6
  • 47
    • 33746781304 scopus 로고    scopus 로고
    • Structural differences in Abeta amyloid protofibrils and fibrils mapped by hydrogen exchange-Mass spectrometry with on-line proteolytic fragmentation
    • Kheterpal, I., Chen, M., Cook, K. D., and Wetzel, R. (2006). Structural differences in Abeta amyloid protofibrils and fibrils mapped by hydrogen exchange-Mass spectrometry with on-line proteolytic fragmentation. J. Mol. Biol. 361, 785-795. doi: 10.1016/j.jmb.2006.06.066.
    • (2006) J. Mol. Biol , vol.361 , pp. 785-795
    • Kheterpal, I.1    Chen, M.2    Cook, K.D.3    Wetzel, R.4
  • 48
    • 3142781310 scopus 로고    scopus 로고
    • Apolipoprotein E promotes astrocyte colocalization and degradation of deposited amyloid-β peptides
    • Koistinaho, M., Lin, S., Wu, X., Esterman, M., Koger, D., Hanson, J., et al. (2004). Apolipoprotein E promotes astrocyte colocalization and degradation of deposited amyloid-β peptides. Nat. Med. 10, 719-726. doi: 10.1038/nm1058.
    • (2004) Nat. Med , vol.10 , pp. 719-726
    • Koistinaho, M.1    Lin, S.2    Wu, X.3    Esterman, M.4    Koger, D.5    Hanson, J.6
  • 49
    • 0029671451 scopus 로고    scopus 로고
    • Water-soluble Abeta (N-40, N-42) oligomers in normal and Alzheimer disease brains
    • Kuo, Y. M., Emmerling, M. R., Vigo-Pelfrey, C., Kasunic, T. C., Kirkpatrick, J. B., Murdoch, G. H., et al. (1996). Water-soluble Abeta (N-40, N-42) oligomers in normal and Alzheimer disease brains. J. Biol. Chem. 271, 4077-4081. doi: 10.1074/jbc.271.8.4077.
    • (1996) J. Biol. Chem , vol.271 , pp. 4077-4081
    • Kuo, Y.M.1    Emmerling, M.R.2    Vigo-Pelfrey, C.3    Kasunic, T.C.4    Kirkpatrick, J.B.5    Murdoch, G.H.6
  • 50
    • 84888317489 scopus 로고    scopus 로고
    • Meta-analysis of 74,046 individuals identifies 11 new susceptibility loci for Alzheimer's disease
    • Lambert, J. C., Ibrahim-Verbaas, C. A., Harold, D., Naj, A. C., Sims, R., Bellenguez, C., et al. (2013). Meta-analysis of 74,046 individuals identifies 11 new susceptibility loci for Alzheimer's disease. Nat. Genet. 45, 1452-1458. doi: 10.1038/ng.2802.
    • (2013) Nat. Genet , vol.45 , pp. 1452-1458
    • Lambert, J.C.1    Ibrahim-Verbaas, C.A.2    Harold, D.3    Naj, A.C.4    Sims, R.5    Bellenguez, C.6
  • 51
    • 67249087641 scopus 로고    scopus 로고
    • Soluble oligomers of amyloid β protein facilitate hippocampal long-term depression by disrupting neuronal glutamate uptake
    • Li, S., Hong, S., Shepardson, N. E., Walsh, D. M., Shankar, G. M., and Selkoe, D. (2009). Soluble oligomers of amyloid β protein facilitate hippocampal long-term depression by disrupting neuronal glutamate uptake. Neuron 62, 788-801. doi: 10.1016/j.neuron.2009.05.012.
    • (2009) Neuron , vol.62 , pp. 788-801
    • Li, S.1    Hong, S.2    Shepardson, N.E.3    Walsh, D.M.4    Shankar, G.M.5    Selkoe, D.6
  • 52
    • 80055104131 scopus 로고    scopus 로고
    • A technique for serial collection of cerebrospinal fluid from the Cisterna Magna in Mouse
    • Liu, L., and Duff, K. (2008). A technique for serial collection of cerebrospinal fluid from the Cisterna Magna in Mouse. J. Vis. Exp. pii:960. doi: 10.3791/960.
    • (2008) J. Vis. Exp , pp. 960
    • Liu, L.1    Duff, K.2
  • 53
    • 84936871460 scopus 로고    scopus 로고
    • Structural and functional features of central nervous system lymphatic vessels
    • Louveau, A., Smirnov, I., Keyes, T. J., Eccles, J. D., Rouhani, S. J., Peske, J. D., et al. (2015). Structural and functional features of central nervous system lymphatic vessels. Nature 523, 337-341. doi: 10.1038/nature14432.
    • (2015) Nature , vol.523 , pp. 337-341
    • Louveau, A.1    Smirnov, I.2    Keyes, T.J.3    Eccles, J.D.4    Rouhani, S.J.5    Peske, J.D.6
  • 54
    • 0032888131 scopus 로고    scopus 로고
    • Soluble amyloid β concentration is a predictor of synaptic change in Alzheimer's disease
    • Lue, L. F., Kuo, Y. M., Roher, A. E., Brachova, L., Shen, Y., Sue, L., et al. (1999). Soluble amyloid β concentration is a predictor of synaptic change in Alzheimer's disease. Am. J. Pathol. 155, 853-862. doi: 10.1016/S0002-9440(10)65184-X.
    • (1999) Am. J. Pathol , vol.155 , pp. 853-862
    • Lue, L.F.1    Kuo, Y.M.2    Roher, A.E.3    Brachova, L.4    Shen, Y.5    Sue, L.6
  • 55
    • 11144353586 scopus 로고    scopus 로고
    • ABAD directly links Abeta to mitochondrial toxicity in Alzheimer's disease
    • Lustbader, J. W., Cirilli, M., Lin, C., Xu, H. W., Takuma, K., Wang, N., et al. (2004). ABAD directly links Abeta to mitochondrial toxicity in Alzheimer's disease. Science 304, 448-452. doi: 10.1126/science.1091230.
    • (2004) Science , vol.304 , pp. 448-452
    • Lustbader, J.W.1    Cirilli, M.2    Lin, C.3    Xu, H.W.4    Takuma, K.5    Wang, N.6
  • 56
    • 84891762244 scopus 로고    scopus 로고
    • Molecular links between endothelial dysfunction and neurodegeneration in Alzheimer's disease
    • Lyros, E., Bakogiannis, C., Liu, Y., and Fassbender, K. (2014). Molecular links between endothelial dysfunction and neurodegeneration in Alzheimer's disease. Curr. Alzheimer Res. 11, 18-26. doi: 10.2174/1567205010666131119235254.
    • (2014) Curr. Alzheimer Res , vol.11 , pp. 18-26
    • Lyros, E.1    Bakogiannis, C.2    Liu, Y.3    Fassbender, K.4
  • 57
    • 0032529151 scopus 로고    scopus 로고
    • Human blood-brain barrier receptors for Alzheimer's amyloid-β 1-40. Asymmetrical binding, endocytosis, and transcytosis at the apical side of brain microvascular endothelial cell monolayer
    • Mackic, J. B., Stins, M., McComb, J. G., Calero, M., Ghiso, J., Kim, K. S., et al. (1998). Human blood-brain barrier receptors for Alzheimer's amyloid-β 1-40. Asymmetrical binding, endocytosis, and transcytosis at the apical side of brain microvascular endothelial cell monolayer. J. Clin. Invest. 102, 734-743. doi: 10.1172/JCI2029.
    • (1998) J. Clin. Invest , vol.102 , pp. 734-743
    • Mackic, J.B.1    Stins, M.2    McComb, J.G.3    Calero, M.4    Ghiso, J.5    Kim, K.S.6
  • 58
    • 65249170245 scopus 로고    scopus 로고
    • Microglia mediate the clearance of soluble Abeta through fluid phase macropinocytosis
    • Mandrekar, S., Jiang, Q., Lee, C. Y., Koenigsknecht-Talboo, J., Holtzman, D. M., and Landreth, G. E. (2009). Microglia mediate the clearance of soluble Abeta through fluid phase macropinocytosis. J. Neurosci. 29, 4252-4262. doi: 10.1523/JNEUROSCI.5572-08.2009.
    • (2009) J. Neurosci , vol.29 , pp. 4252-4262
    • Mandrekar, S.1    Jiang, Q.2    Lee, C.Y.3    Koenigsknecht-Talboo, J.4    Holtzman, D.M.5    Landreth, G.E.6
  • 59
    • 0030779128 scopus 로고    scopus 로고
    • Isoform-specific effects of apolipoproteins E2, E3, and E4 on cerebral capillary sequestration and blood-brain barrier transport of circulating Alzheimer's amyloid β
    • Martel, C., Mackic, J. B., Matsubara, E., Governale, S., Miguel, C., Miao, W., et al. (1997). Isoform-specific effects of apolipoproteins E2, E3, and E4 on cerebral capillary sequestration and blood-brain barrier transport of circulating Alzheimer's amyloid β. J. Neurochem. 69, 1995-2004. doi: 10.1046/j.1471-4159.1997.69051995.x.
    • (1997) J. Neurochem , vol.69 , pp. 1995-2004
    • Martel, C.1    Mackic, J.B.2    Matsubara, E.3    Governale, S.4    Miguel, C.5    Miao, W.6
  • 60
    • 0022156464 scopus 로고
    • Neuronal origin of cerebral amyloid: neurofibrillary tangles of Alzheimer's disease contain the same protein as the amyloid of plaque cores and blood vessels
    • Masters, C. L., Multhaup, G., Sims, G., Pottigiesser, J., Martins, R. N., and Beyreuther, K. (1985a). Neuronal origin of cerebral amyloid: neurofibrillary tangles of Alzheimer's disease contain the same protein as the amyloid of plaque cores and blood vessels. EMBO J. 4, 2757-2763.
    • (1985) EMBO J , vol.4 , pp. 2757-2763
    • Masters, C.L.1    Multhaup, G.2    Sims, G.3    Pottigiesser, J.4    Martins, R.N.5    Beyreuther, K.6
  • 62
    • 3943092621 scopus 로고    scopus 로고
    • Pathways towards and away from Alzheimer's disease
    • Mattson, M. P. (2004). Pathways towards and away from Alzheimer's disease. Nature 430, 631-639. doi: 10.1038/nature02621.
    • (2004) Nature , vol.430 , pp. 631-639
    • Mattson, M.P.1
  • 63
    • 78650678688 scopus 로고    scopus 로고
    • Decreased clearance of CNS β-amyloid in Alzheimer's disease
    • Mawuenyega, K. G., Sigurdson, W., Ovod, V., Munsell, L., Kasten, T., Morris, J. C., et al. (2010). Decreased clearance of CNS β-amyloid in Alzheimer's disease. Science 330, 1774. doi: 10.1126/science.1197623.
    • (2010) Science , vol.330 , pp. 1774
    • Mawuenyega, K.G.1    Sigurdson, W.2    Ovod, V.3    Munsell, L.4    Kasten, T.5    Morris, J.C.6
  • 64
    • 4744352010 scopus 로고    scopus 로고
    • Neuronal LRP1 functionally associates with postsynaptic proteins and is required for normal motor function in mice
    • May, P., Rohlmann, A., Bock, H. H., Zurhove, K., Marth, J. D., Schomburg, E. D., et al. (2004). Neuronal LRP1 functionally associates with postsynaptic proteins and is required for normal motor function in mice. Mol. Cell Biol. 24, 8872-8883. doi: 10.1128/MCB.24.20.8872-8883.2004.
    • (2004) Mol. Cell Biol , vol.24 , pp. 8872-8883
    • May, P.1    Rohlmann, A.2    Bock, H.H.3    Zurhove, K.4    Marth, J.D.5    Schomburg, E.D.6
  • 65
    • 0032590054 scopus 로고    scopus 로고
    • Soluble pool of Abeta amyloid as a determinant of severity of neurodegeneration in Alzheimer's disease
    • McLean, C. A., Cherny, R. A., Fraser, F. W., Fuller, S. J., Smith, M. J., Beyreuther, K., et al. (1999). Soluble pool of Abeta amyloid as a determinant of severity of neurodegeneration in Alzheimer's disease. Ann. Neurol. 46, 860-866.
    • (1999) Ann. Neurol , vol.46 , pp. 860-866
    • McLean, C.A.1    Cherny, R.A.2    Fraser, F.W.3    Fuller, S.J.4    Smith, M.J.5    Beyreuther, K.6
  • 66
    • 33749020837 scopus 로고    scopus 로고
    • Exogenous induction of cerebral β-amyloidogenesis is governed by agent and host
    • Meyer-Luehmann, M., Coomaraswamy, J., Bolmont, T., Kaeser, P. S., Schaefer, C., Kilger, E., et al. (2006). Exogenous induction of cerebral β-amyloidogenesis is governed by agent and host. Science 313, 1781-1784. doi: 10.1126/science.1131864.
    • (2006) Science , vol.313 , pp. 1781-1784
    • Meyer-Luehmann, M.1    Coomaraswamy, J.2    Bolmont, T.3    Kaeser, P.S.4    Schaefer, C.5    Kilger, E.6
  • 67
  • 68
    • 0037931536 scopus 로고    scopus 로고
    • Differential degradation of Aβ genetic variants associated with hereditary dementia or stroke by Insulin-degraded enzyme (IDE)
    • Morelli, L., Llovera, R., Gonzalez, S. A., Affranchino, J. L., Prelli, F., Frangione, B., et al. (2003). Differential degradation of Aβ genetic variants associated with hereditary dementia or stroke by Insulin-degraded enzyme (IDE). J. Biol. Chem. 278, 23221-23226. doi: 10.1074/jbc.M300276200.
    • (2003) J. Biol. Chem , vol.278 , pp. 23221-23226
    • Morelli, L.1    Llovera, R.2    Gonzalez, S.A.3    Affranchino, J.L.4    Prelli, F.5    Frangione, B.6
  • 69
    • 0036866553 scopus 로고    scopus 로고
    • The degradation of amyloid β as a therapeutic strategy in Alzheimer's disease and cerebrovascular amyloidosis
    • Morelli, L., Llovera, R., Ibemdahl, S., and Castaño, E. M. (2002). The degradation of amyloid β as a therapeutic strategy in Alzheimer's disease and cerebrovascular amyloidosis. Neurochem. Res. 27, 1387-1399. doi: 10.1023/A:1021679817756.
    • (2002) Neurochem. Res , vol.27 , pp. 1387-1399
    • Morelli, L.1    Llovera, R.2    Ibemdahl, S.3    Castaño, E.M.4
  • 70
    • 84907222721 scopus 로고    scopus 로고
    • The cerebrovascular basement membrane: role in the clearance of β-amyloid and cerebral amyloid angiopathy
    • Morris, A. W., Carare, R. O., Schreiber, S., and Hawkes, C. A. (2014). The cerebrovascular basement membrane: role in the clearance of β-amyloid and cerebral amyloid angiopathy. Front. Aging Neurosci. 6:251. doi: 10.3389/fnagi.2014.00251.
    • (2014) Front. Aging Neurosci , vol.6 , pp. 251
    • Morris, A.W.1    Carare, R.O.2    Schreiber, S.3    Hawkes, C.A.4
  • 71
    • 84961167095 scopus 로고    scopus 로고
    • Vascular basement membranes as pathways for the passage of fluid into and out of the brain
    • Morris, A. W., Sharp, M. M., Albargothy, N. J., Fernandes, R., Hawkes, C. A., Verma, A., et al. (2016). Vascular basement membranes as pathways for the passage of fluid into and out of the brain. Acta Neuropathol. 131, 725-736. doi: 10.1007/s00401-016-1555-z.
    • (2016) Acta Neuropathol , vol.131 , pp. 725-736
    • Morris, A.W.1    Sharp, M.M.2    Albargothy, N.J.3    Fernandes, R.4    Hawkes, C.A.5    Verma, A.6
  • 72
    • 41549157232 scopus 로고    scopus 로고
    • Transgenic mice lacking NMDAR-dependent LTD exhibit deficits in behavioral flexibility
    • Nicholls, R. E., Alarcon, J. M., Malleret, G., Carroll, R. C., Grody, M., Vronskaya, S., et al. (2008). Transgenic mice lacking NMDAR-dependent LTD exhibit deficits in behavioral flexibility. Neuron 58, 104-117. doi: 10.1016/j.neuron.2008.01.039.
    • (2008) Neuron , vol.58 , pp. 104-117
    • Nicholls, R.E.1    Alarcon, J.M.2    Malleret, G.3    Carroll, R.C.4    Grody, M.5    Vronskaya, S.6
  • 73
    • 77954375412 scopus 로고    scopus 로고
    • Astrocytic A β 1-42 uptake is determined by A β-aggregation state and the presence of amyloid-associated proteins
    • Nielsen, H. M., Mulder, S. D., Beliën, J. A., Musters, R. J., Eikelenboom, P., and Veerhuis, R. (2010). Astrocytic A β 1-42 uptake is determined by A β-aggregation state and the presence of amyloid-associated proteins. Glia 58, 1235-1246. doi: 10.1002/glia.21004.
    • (2010) Glia , vol.58 , pp. 1235-1246
    • Nielsen, H.M.1    Mulder, S.D.2    Beliën, J.A.3    Musters, R.J.4    Eikelenboom, P.5    Veerhuis, R.6
  • 74
    • 19744380563 scopus 로고    scopus 로고
    • Resting microglial cells are highly dynamic surveillants of brain parenchyma in vivo
    • Nimmerjahn, A., Kirchhoff, F., and Helmchen, F. (2005). Resting microglial cells are highly dynamic surveillants of brain parenchyma in vivo. Science 308, 1314-1318. doi: 10.1126/science.1110647.
    • (2005) Science , vol.308 , pp. 1314-1318
    • Nimmerjahn, A.1    Kirchhoff, F.2    Helmchen, F.3
  • 75
    • 84897562702 scopus 로고    scopus 로고
    • Genetics of PICALM expression and Alzheimer's disease
    • Parikh, I., Fardo, D. W., and Estus, S. (2014). Genetics of PICALM expression and Alzheimer's disease. PLoS ONE 9:e91242. doi: 10.1371/journal.pone.0091242.
    • (2014) PLoS ONE , vol.9
    • Parikh, I.1    Fardo, D.W.2    Estus, S.3
  • 76
    • 0032995727 scopus 로고    scopus 로고
    • Receptor-mediated transport of human amyloid-β1-40 and 1-42 at the blood-brain barrier
    • Poduslo, J. F., Curran, G. L., Sanyal, B., and Selkoe, D. (1999). Receptor-mediated transport of human amyloid-β1-40 and 1-42 at the blood-brain barrier. Neurobiol. Dis. 6, 190-199. doi: 10.1006/nbdi.1999.0238.
    • (1999) Neurobiol. Dis , vol.6 , pp. 190-199
    • Poduslo, J.F.1    Curran, G.L.2    Sanyal, B.3    Selkoe, D.4
  • 77
    • 33645775230 scopus 로고    scopus 로고
    • Determination of β-amyloid peptide signatures in cerebrospinal fluid using immunoprecipitation-mass spectrometry
    • Portelius, E., Westman-Brinkmalm, A., Zetterberg, H., and Blennow, K. (2006). Determination of β-amyloid peptide signatures in cerebrospinal fluid using immunoprecipitation-mass spectrometry. J. Proteome Res. 5, 1010-1016. doi: 10.1021/pr050475v.
    • (2006) J. Proteome Res , vol.5 , pp. 1010-1016
    • Portelius, E.1    Westman-Brinkmalm, A.2    Zetterberg, H.3    Blennow, K.4
  • 78
    • 75449102536 scopus 로고    scopus 로고
    • Alzheimer's disease
    • Querfurth, H. W., and LaFerla, F. M. (2010). Alzheimer's disease. N. Engl. J. Med. 362, 329-344. doi: 10.1056/NEJMra0909142.
    • (2010) N. Engl. J. Med , vol.362 , pp. 329-344
    • Querfurth, H.W.1    LaFerla, F.M.2
  • 81
    • 9444245809 scopus 로고    scopus 로고
    • Morphology and toxicity of Abeta-(1-42) dimer derived from neuritic and vascular amyloid deposits of Alzheimer's disease
    • Roher, A. E., Chaney, M. O., Kuo, Y. M., Webster, S. D., Stine, W. B., Haverkamp, L. J., et al. (1996). Morphology and toxicity of Abeta-(1-42) dimer derived from neuritic and vascular amyloid deposits of Alzheimer's disease. J. Biol. Chem. 271, 20631-20635. doi: 10.1074/jbc.271.34.20631.
    • (1996) J. Biol. Chem , vol.271 , pp. 20631-20635
    • Roher, A.E.1    Chaney, M.O.2    Kuo, Y.M.3    Webster, S.D.4    Stine, W.B.5    Haverkamp, L.J.6
  • 82
    • 75649127668 scopus 로고    scopus 로고
    • Cerebral amyloidosis: amyloid subunits, mutants and phenotypes
    • Rostagno, A., Holton, J. L., Lashley, T., Revesz, T., and Ghiso, J. (2010). Cerebral amyloidosis: amyloid subunits, mutants and phenotypes. Cell Mol. Life Sci. 67, 581-600. doi: 10.1007/s00018-009-0182-4.
    • (2010) Cell Mol. Life Sci , vol.67 , pp. 581-600
    • Rostagno, A.1    Holton, J.L.2    Lashley, T.3    Revesz, T.4    Ghiso, J.5
  • 83
    • 67349123049 scopus 로고    scopus 로고
    • "Protein misfolding, aggregation, and fibril formation: common features of cerebral and non-cerebral amyloid diseases,"
    • eds D. Dawbarn S. and Allen (Oxford: Oxford University Press)
    • Rostagno, A., Lal, R., and Ghiso, J. (2007). "Protein misfolding, aggregation, and fibril formation: common features of cerebral and non-cerebral amyloid diseases," in The Neurobiology of Alzheimer's Disease, eds D. Dawbarn S. and Allen (Oxford: Oxford University Press), 133-160.
    • (2007) The Neurobiology of Alzheimer's Disease , pp. 133-160
    • Rostagno, A.1    Lal, R.2    Ghiso, J.3
  • 84
    • 84864755408 scopus 로고    scopus 로고
    • Proteolytic degradation of amyloid β-protein
    • Saido, T., and Leissring, M. A. (2012). Proteolytic degradation of amyloid β-protein. Cold Spring Harb. Perspect. Biol. 2:a006379. doi: 10.1101/cshperspect.a006379.
    • (2012) Cold Spring Harb. Perspect. Biol , vol.2
    • Saido, T.1    Leissring, M.A.2
  • 85
    • 0035950225 scopus 로고    scopus 로고
    • Clearing the brain's amyloid cobwebs
    • Selkoe, D. J. (2001). Clearing the brain's amyloid cobwebs. Neuron 32, 177-180. doi: 10.1016/S0896-6273(01)00475-5.
    • (2001) Neuron , vol.32 , pp. 177-180
    • Selkoe, D.J.1
  • 86
    • 84934441666 scopus 로고    scopus 로고
    • Isolation of low-n amyloid β-protein oligomers from cultured cells, CSF, and brain
    • Shankar, G. M., Welzel, A. T., McDonald, J. M., Selkoe, D. J., and Walsh, D. M. (2011). Isolation of low-n amyloid β-protein oligomers from cultured cells, CSF, and brain. Methods Mol. Biol. 670, 33-44. doi: 10.1007/978-1-60761-744-0_3.
    • (2011) Methods Mol. Biol , vol.670 , pp. 33-44
    • Shankar, G.M.1    Welzel, A.T.2    McDonald, J.M.3    Selkoe, D.J.4    Walsh, D.M.5
  • 87
    • 0034521392 scopus 로고    scopus 로고
    • Clearance of Alzheimer's amyloid-aβ(1-40) peptide from brain by LDL receptor-related protein-1 at the blood-brain barrier
    • Shibata, M., Yamada, S., Kumar, S. R., Calero, M., Bading, J., Frangione, B., et al. (2000). Clearance of Alzheimer's amyloid-aβ(1-40) peptide from brain by LDL receptor-related protein-1 at the blood-brain barrier. J. Clin. Invest. 106, 1489-1499. doi: 10.1172/JCI10498.
    • (2000) J. Clin. Invest , vol.106 , pp. 1489-1499
    • Shibata, M.1    Yamada, S.2    Kumar, S.R.3    Calero, M.4    Bading, J.5    Frangione, B.6
  • 88
    • 58149520137 scopus 로고    scopus 로고
    • Dutch and Arctic mutant peptides of β amyloid(1-40) differentially affect the FGF-2 pathway in brain endothelium
    • Solito, R., Corti, F., Fossati, S., Mezhericher, E., Donnini, S., Ghiso, J., et al. (2009). Dutch and Arctic mutant peptides of β amyloid(1-40) differentially affect the FGF-2 pathway in brain endothelium. Exp. Cell Res. 315, 385-395. doi: 10.1016/j.yexcr.2008.11.002.
    • (2009) Exp. Cell Res , vol.315 , pp. 385-395
    • Solito, R.1    Corti, F.2    Fossati, S.3    Mezhericher, E.4    Donnini, S.5    Ghiso, J.6
  • 89
    • 0038176528 scopus 로고    scopus 로고
    • In vitro characterization of conditions for amyloid-β peptide oligomerization and fibrillogenesis
    • Stine, W. B. Jr., Dahlgren, K. N., Krafft, G. A., and LaDu, M. J. (2003). In vitro characterization of conditions for amyloid-β peptide oligomerization and fibrillogenesis. J. Biol. Chem. 278, 11612-11622. doi: 10.1074/jbc.M210207200.
    • (2003) J. Biol. Chem , vol.278 , pp. 11612-11622
    • Stine, W.B.1    Dahlgren, K.N.2    Krafft, G.A.3    LaDu, M.J.4
  • 90
    • 0033973997 scopus 로고    scopus 로고
    • In vitro evidence that b-amyloid peptide 1-40 diffuses accross the blood-brain barrier and affects its permeability
    • Strazielle, N., Ghersi-Egea, J.-F., Ghiso, J., Dehouck, M.-P., Frangione, B., Patlak, C. S., et al. (2000). In vitro evidence that b-amyloid peptide 1-40 diffuses accross the blood-brain barrier and affects its permeability. J. Neuropathol. Exp. Neurol. 59, 29-38. doi: 10.1093/jnen/59.1.29.
    • (2000) J. Neuropathol. Exp. Neurol , vol.59 , pp. 29-38
    • Strazielle, N.1    Ghersi-Egea, J.-F.2    Ghiso, J.3    Dehouck, M.-P.4    Frangione, B.5    Patlak, C.S.6
  • 91
    • 84867608942 scopus 로고    scopus 로고
    • The genetics of Alzheimer disease
    • Tanzi, R. E. (2012). The genetics of Alzheimer disease. Cold Spring Harbor Perspect. Med. 2:a006296. doi: 10.1101/cshperspect.a006296.
    • (2012) Cold Spring Harbor Perspect. Med , vol.2
    • Tanzi, R.E.1
  • 92
    • 27744442655 scopus 로고    scopus 로고
    • Familial danish dementia: co-existence of ADan and Aβ amyloid subunits in the absence of compact plaques
    • Tomidokoro, Y., Lashley, T., Rostagno, A., Neubert, T. A., Bojsen-Moller, M., Braendgaard, H., et al. (2005). Familial danish dementia: co-existence of ADan and Aβ amyloid subunits in the absence of compact plaques. J. Biol. Chem. 280, 36883-36894. doi: 10.1074/jbc.M504038200.
    • (2005) J. Biol. Chem , vol.280 , pp. 36883-36894
    • Tomidokoro, Y.1    Lashley, T.2    Rostagno, A.3    Neubert, T.A.4    Bojsen-Moller, M.5    Braendgaard, H.6
  • 93
    • 77950569777 scopus 로고    scopus 로고
    • Iowa variant of familial Alzheimer's disease: accumulation of posttranslationally modified AβD23N in parenchymal and cerebrovascular amyloid deposits
    • Tomidokoro, Y., Rostagno, A., Neubert, T. A., Lu, Y., Rebeck, G. W., Frangione, B., et al. (2010). Iowa variant of familial Alzheimer's disease: accumulation of posttranslationally modified AβD23N in parenchymal and cerebrovascular amyloid deposits. Am. J. Pathol. 176, 1841-1854. doi: 10.2353/ajpath.2010.090636.
    • (2010) Am. J. Pathol , vol.176 , pp. 1841-1854
    • Tomidokoro, Y.1    Rostagno, A.2    Neubert, T.A.3    Lu, Y.4    Rebeck, G.W.5    Frangione, B.6
  • 94
    • 84962311360 scopus 로고    scopus 로고
    • Blood-brain barrier and blood-cerebrospinal fluid barrier in normal and pathological conditions
    • Ueno, M., Chiba, Y., Murakami, R., Matsumoto, K., Kawauchi, M., and Fujihara, R. (2016). Blood-brain barrier and blood-cerebrospinal fluid barrier in normal and pathological conditions. Brain Tumor Pathol. 33, 89-96. doi: 10.1007/s10014-016-0255-7.
    • (2016) Brain Tumor Pathol , vol.33 , pp. 89-96
    • Ueno, M.1    Chiba, Y.2    Murakami, R.3    Matsumoto, K.4    Kawauchi, M.5    Fujihara, R.6
  • 95
    • 26244462301 scopus 로고    scopus 로고
    • Proteolytic mechanisms in amyloid-β metabolism: therapeutic implications for Alzheimer's disease
    • Vardy, E. R., Catto, A. J., and Hooper, N. M. (2005). Proteolytic mechanisms in amyloid-β metabolism: therapeutic implications for Alzheimer's disease. Trends Mol. Med. 11, 464-472. doi: 10.1016/j.molmed.2005.08.004.
    • (2005) Trends Mol. Med , vol.11 , pp. 464-472
    • Vardy, E.R.1    Catto, A.J.2    Hooper, N.M.3
  • 96
    • 62349110126 scopus 로고    scopus 로고
    • Tauroursodeoxycholic acid prevents E22Q Alzheimer's Abeta toxicity in human cerebral endothelial cells
    • Viana, R. J., Nunes, A. F., Castro, R. E., Ramalho, R. M., Meyerson, J., Fossati, S., et al. (2009). Tauroursodeoxycholic acid prevents E22Q Alzheimer's Abeta toxicity in human cerebral endothelial cells. Cell. Mol. Life Sci. 66, 1094-1104. doi: 10.1007/s00018-009-8746-x.
    • (2009) Cell. Mol. Life Sci , vol.66 , pp. 1094-1104
    • Viana, R.J.1    Nunes, A.F.2    Castro, R.E.3    Ramalho, R.M.4    Meyerson, J.5    Fossati, S.6
  • 97
    • 0037041426 scopus 로고    scopus 로고
    • Naturally secreted oligomers of amyloid β protein potently inhibit hippocampal long-term potentiation in vivo
    • Walsh, D. M., Klyubin, I., Fadeeva, J. V., Cullen, W. K., Anwyl, R., Wolfe, M. S., et al. (2002). Naturally secreted oligomers of amyloid β protein potently inhibit hippocampal long-term potentiation in vivo. Nature 416, 535-539. doi: 10.1038/416535a.
    • (2002) Nature , vol.416 , pp. 535-539
    • Walsh, D.M.1    Klyubin, I.2    Fadeeva, J.V.3    Cullen, W.K.4    Anwyl, R.5    Wolfe, M.S.6
  • 98
    • 34248190279 scopus 로고    scopus 로고
    • A β oligomers-a decade of discovery
    • Walsh, D. M., and Selkoe, D. J. (2007). A β oligomers-a decade of discovery. J. Neurochem. 101, 1172-1184. doi: 10.1111/j.1471-4159.2006.04426.x.
    • (2007) J. Neurochem , vol.101 , pp. 1172-1184
    • Walsh, D.M.1    Selkoe, D.J.2
  • 99
    • 33748753481 scopus 로고    scopus 로고
    • Clearance of amyloid-β in Alzheimer's disease: progress, problems and perspectives
    • Wang, Y. J., Zhou, H. D., and Zhou, X. F. (2006). Clearance of amyloid-β in Alzheimer's disease: progress, problems and perspectives. Drug Disc. Today 11, 931-938. doi: 10.1016/j.drudis.2006.08.004.
    • (2006) Drug Disc. Today , vol.11 , pp. 931-938
    • Wang, Y.J.1    Zhou, H.D.2    Zhou, X.F.3
  • 100
    • 41149157623 scopus 로고    scopus 로고
    • Perivascular drainage of amyloid-β peptides from the brain and its failure in cerebral amyloid angiopathy and Alzheimer's disease
    • Weller, R. O., Subash, M., Preston, S. D., Mazanti, I., and Carare, R. O. (2008). Perivascular drainage of amyloid-β peptides from the brain and its failure in cerebral amyloid angiopathy and Alzheimer's disease. Brain Pathol. 18, 253-266. doi: 10.1111/j.1750-3639.2008.00133.x.
    • (2008) Brain Pathol , vol.18 , pp. 253-266
    • Weller, R.O.1    Subash, M.2    Preston, S.D.3    Mazanti, I.4    Carare, R.O.5
  • 101
    • 26944437967 scopus 로고    scopus 로고
    • Small non-fibrillar assemblies of amyloid B-protein bearing the Arctic mutation induce rapid neuritic degeneration
    • Whalen, B. M., Selkoe, D. J., and Hartley, D. M. (2005). Small non-fibrillar assemblies of amyloid B-protein bearing the Arctic mutation induce rapid neuritic degeneration. Neurobiol. Dis. 20, 254-266. doi: 10.1016/j.nbd.2005.03.007.
    • (2005) Neurobiol. Dis , vol.20 , pp. 254-266
    • Whalen, B.M.1    Selkoe, D.J.2    Hartley, D.M.3
  • 102
    • 0029569085 scopus 로고
    • Matrix-Assisted Laser Desorption/lonization of noncovalently bound compounds
    • Woods, A. S., Buchsbaum, J. C., Worrall, T. S., Berg, J. M., and Cotter, R. J. (1995). Matrix-Assisted Laser Desorption/lonization of noncovalently bound compounds. Anal. Chem. 67, 4462-4465. doi: 10.1021/ac00120a005.
    • (1995) Anal. Chem , vol.67 , pp. 4462-4465
    • Woods, A.S.1    Buchsbaum, J.C.2    Worrall, T.S.3    Berg, J.M.4    Cotter, R.J.5
  • 103
    • 0034744296 scopus 로고    scopus 로고
    • TGF-β1 promotes microglial amyloid-β clearance and reduces plaque burden in transgenic mice
    • Wyss-Coray, T., Lin, C., Yan, F., Yu, G. Q., Rohde, M., McConlogue, L., et al. (2001). TGF-β1 promotes microglial amyloid-β clearance and reduces plaque burden in transgenic mice. Nat. Med. 7, 612-618. doi: 10.1038/87945.
    • (2001) Nat. Med , vol.7 , pp. 612-618
    • Wyss-Coray, T.1    Lin, C.2    Yan, F.3    Yu, G.Q.4    Rohde, M.5    McConlogue, L.6
  • 104
    • 0037394788 scopus 로고    scopus 로고
    • Adult mouse astrocytes degrade amyloid-β in vitro and in situ
    • Wyss-Coray, T., Loike, J. D., Brionne, T. C., Lu, E., Anankov, R., Yan, F., et al. (2003). Adult mouse astrocytes degrade amyloid-β in vitro and in situ. Nat. Med. 9, 453-457. doi: 10.1038/nm838.
    • (2003) Nat. Med , vol.9 , pp. 453-457
    • Wyss-Coray, T.1    Loike, J.D.2    Brionne, T.C.3    Lu, E.4    Anankov, R.5    Yan, F.6
  • 105
    • 84863331844 scopus 로고    scopus 로고
    • Abcg2 deficiency augments oxidative stress and cognitive deficits in Tg-SwDI transgenic mice
    • Zeng, Y., Callaghan, D., Xiong, H., Yang, Z., Huang, P., and Zhang, W. (2012). Abcg2 deficiency augments oxidative stress and cognitive deficits in Tg-SwDI transgenic mice. J. Neurochem. 122, 456-469. doi: 10.1111/j.1471-4159.2012.07783.x.
    • (2012) J. Neurochem , vol.122 , pp. 456-469
    • Zeng, Y.1    Callaghan, D.2    Xiong, H.3    Yang, Z.4    Huang, P.5    Zhang, W.6
  • 107
    • 0029920929 scopus 로고    scopus 로고
    • Gp330/megalin: probable role in receptor-mediated transport of apolipoprotein J alone and in a complex with Alzheimer's Amyloid b at the blood-brain and blood-cerebrospinal fluid barriers
    • Zlokovic, B., Martel, C., Matsubara, E., McCombo, J. G., Zheng, G., McCluskey, R. T., et al. (1996). Gp330/megalin: probable role in receptor-mediated transport of apolipoprotein J alone and in a complex with Alzheimer's Amyloid b at the blood-brain and blood-cerebrospinal fluid barriers. Proc. Natl. Acad. Sci. U.S.A. 93, 4229-4234. doi: 10.1073/pnas.93.9.4229.
    • (1996) Proc. Natl. Acad. Sci. U.S.A , vol.93 , pp. 4229-4234
    • Zlokovic, B.1    Martel, C.2    Matsubara, E.3    McCombo, J.G.4    Zheng, G.5    McCluskey, R.T.6
  • 108
    • 81555200043 scopus 로고    scopus 로고
    • Neurovascular pathways to neurodegeneration in Alzheimer's disease and other disorders
    • Zlokovic, B. V. (2011). Neurovascular pathways to neurodegeneration in Alzheimer's disease and other disorders. Nat. Rev. Neurosci. 12, 723-738. doi: 10.1038/nrn3114.
    • (2011) Nat. Rev. Neurosci , vol.12 , pp. 723-738
    • Zlokovic, B.V.1


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