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Volumn 288, Issue 21, 2013, Pages 15154-15166

A lipoprotein receptor cluster IV mutant preferentially binds amyloid-β and regulates its clearance from the mouse brain

Author keywords

[No Author keywords available]

Indexed keywords

ASPARTIC ACID RESIDUES; EXPERIMENTAL STUDIES; HIPPOCAMPAL FUNCTIONS; LIPOPROTEIN RECEPTORS; LOW DENSITY LIPOPROTEINS; MATRIX METALLOPROTEINASE-9; MILD COGNITIVE IMPAIRMENTS; TISSUE PLASMINOGEN ACTIVATOR;

EID: 84878260940     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.439570     Document Type: Article
Times cited : (35)

References (71)
  • 2
    • 0035066332 scopus 로고    scopus 로고
    • Alzheimer's disease. Genes, proteins, and therapy
    • Selkoe, D. J. (2001) Alzheimer's disease. Genes, proteins, and therapy. Physiol. Rev. 81, 741-766
    • (2001) Physiol. Rev. , vol.81 , pp. 741-766
    • Selkoe, D.J.1
  • 3
    • 84857642949 scopus 로고    scopus 로고
    • The toxic Aβ oligomer and Alzheimer's disease. An emperor in need of clothes
    • Benilova, I., Karran, E., and De Strooper, B. (2012) The toxic Aβ oligomer and Alzheimer's disease. An emperor in need of clothes. Nat. Neurosci. 15, 349-357
    • (2012) Nat. Neurosci. , vol.15 , pp. 349-357
    • Benilova, I.1    Karran, E.2    De Strooper, B.3
  • 5
    • 78149255128 scopus 로고    scopus 로고
    • Low-density lipoprotein receptor-related protein-1. A serial clearance homeostatic mechanism controlling Alzheimer's amyloid β-peptide elimination from the brain
    • Zlokovic, B. V., Deane, R., Sagare, A. P., Bell, R. D., and Winkler, E. A. (2010) Low-density lipoprotein receptor-related protein-1. A serial clearance homeostatic mechanism controlling Alzheimer's amyloid β-peptide elimination from the brain. J. Neurochem. 115, 1077-1089
    • (2010) J. Neurochem. , vol.115 , pp. 1077-1089
    • Zlokovic, B.V.1    Deane, R.2    Sagare, A.P.3    Bell, R.D.4    Winkler, E.A.5
  • 9
    • 33750017850 scopus 로고    scopus 로고
    • Functional characterization of the brain-to-blood efflux clearance of human amyloid-β peptide (1-40) across the rat blood-brain barrier
    • DOI 10.1016/j.neures.2006.07.006, PII S0168010206001817
    • Ito, S., Ohtsuki, S., and Terasaki, T. (2006) Functional characterization of the brain-to-blood efflux clearance of human amyloid-β peptide (1-40) across the rat blood-brain barrier. Neurosci. Res. 56, 246-252 (Pubitemid 44572534)
    • (2006) Neuroscience Research , vol.56 , Issue.3 , pp. 246-252
    • Ito, S.1    Ohtsuki, S.2    Terasaki, T.3
  • 11
    • 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
    • (2011) Nat. Rev. Neurosci. , vol.12 , pp. 723-738
    • Zlokovic, B.V.1
  • 12
    • 0141867783 scopus 로고    scopus 로고
    • Efflux of human and mouse amyloid β proteins 1-40 and 1-42 from brain: Impairment in a mouse model of alzheimer's disease
    • DOI 10.1016/S0306-4522(03)00474-3
    • Banks, W. A., Robinson, S. M., Verma, S., and Morley, J. E. (2003) Efflux of human and mouse amyloid β proteins 1-40 and 1-42 from brain. Impairment in a mouse model of Alzheimer's disease. Neuroscience 121, 487-492 (Pubitemid 37176936)
    • (2003) Neuroscience , vol.121 , Issue.2 , pp. 487-492
    • Banks, W.A.1    Robinson, S.M.2    Verma, S.3    Morley, J.E.4
  • 13
    • 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
    • DOI 10.1038/sj.jcbfm.9600419, PII 9600419
    • 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 β-peptide and apolipoproteins E and J in the mouse central nervous system. J. Cereb. Blood Flow Metab. 27, 909-918 (Pubitemid 46659038)
    • (2007) Journal of Cerebral Blood Flow and Metabolism , vol.27 , Issue.5 , 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    Zlokovic, B.V.7
  • 19
    • 84865575547 scopus 로고    scopus 로고
    • Low-density lipoprotein receptor-related protein 1. A physiological Aβ homeostatic mechanism with multiple therapeutic opportunities
    • Sagare, A. P., Deane, R., and Zlokovic, B. V. (2012) Low-density lipoprotein receptor-related protein 1. A physiological Aβ homeostatic mechanism with multiple therapeutic opportunities. Pharmacol. Ther. 136, 94-105
    • (2012) Pharmacol. Ther. , vol.136 , pp. 94-105
    • Sagare, A.P.1    Deane, R.2    Zlokovic, B.V.3
  • 20
    • 84863895905 scopus 로고    scopus 로고
    • Enhanced brain amyloid-β clearance by rifampicin and caffeine as a possible protective mechanism against Alzheimer's disease
    • Qosa, H., Abuznait, A. H., Hill, R. A., and Kaddoumi, A. (2012) Enhanced brain amyloid-β clearance by rifampicin and caffeine as a possible protective mechanism against Alzheimer's disease. J. Alzheimers Dis. 31, 151-165
    • (2012) J. Alzheimers Dis. , vol.31 , pp. 151-165
    • Qosa, H.1    Abuznait, A.H.2    Hill, R.A.3    Kaddoumi, A.4
  • 21
    • 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
    • (2012) J. Neurosci. , vol.32 , pp. 16458-16465
    • Kanekiyo, T.1    Liu, C.C.2    Shinohara, M.3    Li, J.4    Bu, G.5
  • 22
    • 79955675470 scopus 로고    scopus 로고
    • Impaired lipoprotein receptor-mediated peripheral binding of plasma amyloid-β is an early biomarker for mild cognitive impairment preceding Alzheimer's disease
    • Sagare, A. P., Deane, R., Zetterberg, H., Wallin, A., Blennow, K., and Zlokovic, B. V. (2011) Impaired lipoprotein receptor-mediated peripheral binding of plasma amyloid-β is an early biomarker for mild cognitive impairment preceding Alzheimer's disease. J. Alzheimers Dis. 24, 25-34
    • (2011) J. Alzheimers Dis. , vol.24 , pp. 25-34
    • Sagare, A.P.1    Deane, R.2    Zetterberg, H.3    Wallin, A.4    Blennow, K.5    Zlokovic, B.V.6
  • 23
    • 3442894794 scopus 로고    scopus 로고
    • Blood-brain barrier permeability precedes senile plaque formation in an Alzheimer disease model
    • DOI 10.1038/sj.mn.7800212
    • Ujiie, M., Dickstein, D. L., Carlow, D. A., and Jefferies, W. A. (2003) Blood-brain barrier permeability precedes senile plaque formation in an Alzheimer disease model. Microcirculation 10, 463-470 (Pubitemid 39004272)
    • (2003) Microcirculation , vol.10 , Issue.6 , pp. 463-470
    • Ujiie, M.1    Dickstein, D.L.2    Carlow, D.A.3    Jefferies, W.A.4
  • 26
    • 80053971718 scopus 로고    scopus 로고
    • Current and emerging drug treatment options for Alzheimer's disease. A systematic review
    • Herrmann, N., Chau, S. A., Kircanski, I., and Lanctôt, K. L. (2011) Current and emerging drug treatment options for Alzheimer's disease. A systematic review. Drugs 71, 2031-2065
    • (2011) Drugs , vol.71 , pp. 2031-2065
    • Herrmann, N.1    Chau, S.A.2    Kircanski, I.3    Lanctôt, K.L.4
  • 28
    • 80052576069 scopus 로고    scopus 로고
    • Activation of matrix metalloproteinases following anti-Aβ immunotherapy. Implications for microhemorrhage occurrence
    • Wilcock, D. M., Morgan, D., Gordon, M. N., Taylor, T. L., Ridnour, L. A., Wink, D. A., and Colton, C. A. (2011) Activation of matrix metalloproteinases following anti-Aβ immunotherapy. Implications for microhemorrhage occurrence. J. Neuroinflammation 8, 115
    • (2011) J. Neuroinflammation , vol.8 , pp. 115
    • Wilcock, D.M.1    Morgan, D.2    Gordon, M.N.3    Taylor, T.L.4    Ridnour, L.A.5    Wink, D.A.6    Colton, C.A.7
  • 29
    • 80155190179 scopus 로고    scopus 로고
    • Anti-amyloid-β single-chain antibody brain delivery via AAV reduces amyloid load but may increase cerebral hemorrhages in an Alzheimer's disease mouse model
    • Kou, J., Kim, H., Pattanayak, A., Song, M., Lim, J. E., Taguchi, H., Paul, S., Cirrito, J. R., Ponnazhagan, S., and Fukuchi, K. (2011) Anti-amyloid-β single-chain antibody brain delivery via AAV reduces amyloid load but may increase cerebral hemorrhages in an Alzheimer's disease mouse model. J. Alzheimers Dis. 27, 23-38
    • (2011) J. Alzheimers Dis. , vol.27 , pp. 23-38
    • Kou, J.1    Kim, H.2    Pattanayak, A.3    Song, M.4    Lim, J.E.5    Taguchi, H.6    Paul, S.7    Cirrito, J.R.8    Ponnazhagan, S.9    Fukuchi, K.10
  • 30
    • 84866456583 scopus 로고    scopus 로고
    • Preventing Alzheimer's disease
    • Selkoe, D. J. (2012) Preventing Alzheimer's disease. Science 337, 1488-1492
    • (2012) Science , vol.337 , pp. 1488-1492
    • Selkoe, D.J.1
  • 31
    • 73149090992 scopus 로고    scopus 로고
    • Antibody concentrations to Aβ1-42 monomer and soluble oligomers in untreated and antibody-antigen-dissociated intravenous immunoglobulin preparations
    • Klaver, A. C., Finke, J. M., Digambaranath, J., Balasubramaniam, M., and Loeffler, D. A. (2010) Antibody concentrations to Aβ1-42 monomer and soluble oligomers in untreated and antibody-antigen-dissociated intravenous immunoglobulin preparations. Int. Immunopharmacol. 10, 115-119
    • (2010) Int. Immunopharmacol. , vol.10 , pp. 115-119
    • Klaver, A.C.1    Finke, J.M.2    Digambaranath, J.3    Balasubramaniam, M.4    Loeffler, D.A.5
  • 32
    • 77949962484 scopus 로고    scopus 로고
    • Intravenous immunoglobulins as a treatment for Alzheimer's disease. Rationale and current evidence
    • Dodel, R., Neff, F., Noelker, C., Pul, R., Du, Y., Bacher, M., and Oertel, W. (2010) Intravenous immunoglobulins as a treatment for Alzheimer's disease. Rationale and current evidence. Drugs 70, 513-528
    • (2010) Drugs , vol.70 , pp. 513-528
    • Dodel, R.1    Neff, F.2    Noelker, C.3    Pul, R.4    Du, Y.5    Bacher, M.6    Oertel, W.7
  • 33
    • 0029780956 scopus 로고    scopus 로고
    • Protein folding and calcium binding defects arising from familial hypercholesterolemia mutations of the LDL receptor
    • DOI 10.1038/nsb0996-758
    • Blacklow, S. C., and Kim, P. S. (1996) Protein folding and calcium binding defects arising from familial hypercholesterolemia mutations of the LDL receptor. Nat. Struct. Biol. 3, 758-762 (Pubitemid 26303401)
    • (1996) Nature Structural Biology , vol.3 , Issue.9 , pp. 758-762
    • Blacklow, S.C.1    Kim, P.S.2
  • 34
    • 0032502042 scopus 로고    scopus 로고
    • Calcium is essential for the structural integrity of the cysteine-rich, ligand-binding repeat of the low-density lipoprotein receptor
    • DOI 10.1021/bi972529n
    • Atkins, A. R., Brereton, I. M., Kroon, P. A., Lee, H. T., and Smith, R. (1998) Calcium is essential for the structural integrity of the cysteine-rich, ligand-binding repeat of the low-density lipoprotein receptor. Biochemistry 37, 1662-1670 (Pubitemid 28093682)
    • (1998) Biochemistry , vol.37 , Issue.6 , pp. 1662-1670
    • Atkins, A.R.1    Brereton, I.M.2    Kroon, P.A.3    Lee, H.T.4    Smith, R.5
  • 36
    • 0030973626 scopus 로고    scopus 로고
    • Differential functions of triplicated repeats suggest two independent roles for the receptor-associated protein as a molecular chaperone
    • DOI 10.1074/jbc.272.16.10761
    • Obermoeller, L. M., Warshawsky, I., Wardell, M. R., and Bu, G. (1997) Differential functions of triplicated repeats suggest two independent roles for the receptor-associated protein as a molecular chaperone. J. Biol. Chem. 272, 10761-10768 (Pubitemid 27181089)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.16 , pp. 10761-10768
    • Obermoeller, L.M.1    Warshawsky, I.2    Wardell, M.R.3    Bu, G.4
  • 37
    • 0242424094 scopus 로고    scopus 로고
    • All Three LDL Receptor Homology Regions of the LDL Receptor-Related Protein Bind Multiple Ligands
    • DOI 10.1021/bi034752s
    • Croy, J. E., Shin, W. D., Knauer, M. F., Knauer, D. J., and Komives, E. A. (2003) All three LDL receptor homology regions of the LDL receptor-related protein bind multiple ligands. Biochemistry 42, 13049-13057 (Pubitemid 37385837)
    • (2003) Biochemistry , vol.42 , Issue.44 , pp. 13049-13057
    • Croy, J.E.1    Shin, W.D.2    Knauer, M.F.3    Knauer, D.J.4    Komives, E.A.5
  • 38
    • 0033615548 scopus 로고    scopus 로고
    • The second and fourth cluster of class A cysteine-rich repeats of the low density lipoprotein receptor-related protein share ligand-binding properties
    • Neels, J. G., van Den Berg, B. M., Lookene, A., Olivecrona, G., Pannekoek, H., and van Zonneveld, A. J. (1999) The second and fourth cluster of class A cysteine-rich repeats of the low density lipoprotein receptor-related protein share ligand-binding properties. J. Biol. Chem. 274, 31305-31311
    • (1999) J. Biol. Chem. , vol.274 , pp. 31305-31311
    • Neels, J.G.1    Van Den Berg, B.M.2    Lookene, A.3    Olivecrona, G.4    Pannekoek, H.5    Van Zonneveld, A.J.6
  • 40
    • 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. V. (2009) Clearance of amyloid-β peptide across the blood-brain barrier. Implication for therapies in Alzheimer's disease. CNS Neurol. Disord. Drug Targets 8, 16-30
    • (2009) CNS Neurol. Disord. Drug Targets , vol.8 , pp. 16-30
    • Deane, R.1    Bell, R.D.2    Sagare, A.3    Zlokovic, B.V.4
  • 41
    • 0242668337 scopus 로고    scopus 로고
    • Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
    • DOI 10.1126/science.1079469
    • Kayed, R., Head, E., Thompson, J. L., McIntire, T. M., Milton, S. C., Cotman, C. W., and Glabe, C. G. (2003) Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis. Science 300, 486-489 (Pubitemid 36444329)
    • (2003) Science , vol.300 , Issue.5618 , pp. 486-489
    • Kayed, R.1    Head, E.2    Thompson, J.L.3    McIntire, T.M.4    Milton, S.C.5    Cotman, C.W.6    Glabel, C.G.7
  • 43
    • 0031961832 scopus 로고    scopus 로고
    • Cerebrovascular accumulation and increased blood-brain barrier permeability to circulating Alzheimer's amyloid β peptide in aged squirrel monkey with cerebral amyloid angiopathy
    • Mackic, J. B., Weiss, M. H., Miao, W., Kirkman, E., Ghiso, J., Calero, M., Bading, J., Frangione, B., and Zlokovic, B. V. (1998) Cerebrovascular accumulation and increased blood-brain barrier permeability to circulating Alzheimer's amyloid β peptide in aged squirrel monkey with cerebral amyloid angiopathy. J. Neurochem. 70, 210-215 (Pubitemid 28020845)
    • (1998) Journal of Neurochemistry , vol.70 , Issue.1 , pp. 210-215
    • Mackic, J.B.1    Weiss, M.H.2    Miao, W.3    Kirkman, E.4    Ghiso, J.5    Calero, M.6    Bading, J.7    Frangione, B.8    Zlokovic, B.V.9
  • 44
    • 30844472909 scopus 로고    scopus 로고
    • IgG-assisted age-dependent clearance of Alzheimer's amyloid β peptide by the blood-brain barrier neonatal Fc receptor
    • DOI 10.1523/JNEUROSCI.3697-05.2005
    • Deane, R., Sagare, A., Hamm, K., Parisi, M., LaRue, B., Guo, H., Wu, Z., Holtzman, D. M., and Zlokovic, B. V. (2005) IgG-assisted age-dependent clearance of Alzheimer's amyloid β peptide by the blood-brain barrier neonatal Fc receptor. J. Neurosci. 25, 11495-11503 (Pubitemid 43102486)
    • (2005) Journal of Neuroscience , vol.25 , Issue.50 , pp. 11495-11503
    • Deane, R.1    Sagare, A.2    Hamm, K.3    Parisi, M.4    LaRue, B.5    Guo, H.6    Wu, Z.7    Holtzman, D.M.8    Zlokovic, B.V.9
  • 46
    • 62649114953 scopus 로고    scopus 로고
    • Burrowing. A sensitive behavioural assay, tested in five species of laboratory rodents
    • Deacon, R. M. (2009) Burrowing. A sensitive behavioural assay, tested in five species of laboratory rodents. Behav. Brain Res. 200, 128-133
    • (2009) Behav. Brain Res. , vol.200 , pp. 128-133
    • Deacon, R.M.1
  • 49
    • 0030945761 scopus 로고    scopus 로고
    • Molecular analysis of ligand binding to the second cluster of complement-type repeats of the low density lipoprotein receptor-related protein: Evidence for an allosteric component in receptor-associated protein- mediated inhibition of ligand binding
    • DOI 10.1074/jbc.272.21.13608
    • Horn, I. R., van den Berg, B. M., van der Meijden, P. Z., Pannekoek, H., and van Zonneveld, A. J. (1997) Molecular analysis of ligand binding to the second cluster of complement-type repeats of the low density lipoprotein receptor-related protein. Evidence for an allosteric component in receptor-associated protein-mediated inhibition of ligand binding. J. Biol. Chem. 272, 13608-13613 (Pubitemid 27224792)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.21 , pp. 13608-13613
    • Horn, I.R.1    Van Den, B.B.M.M.2    Van Der, M.P.Z.3    Pannekoek, H.4    Van Zonneveld, A.-J.5
  • 50
    • 0037169492 scopus 로고    scopus 로고
    • The α-chains of C4b-binding protein mediate complex formation with low density lipoprotein receptor-related protein
    • DOI 10.1074/jbc.M102293200
    • Westein, E., Denis, C. V., Bouma, B. N., and Lenting, P. J. (2002) The α-chains of C4b-binding protein mediate complex formation with low density lipoprotein receptor-related protein. J. Biol. Chem. 277, 2511-2516 (Pubitemid 34953274)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.4 , pp. 2511-2516
    • Westein, E.1    Denis, C.V.2    Bouma, B.N.3    Lenting, P.J.4
  • 52
    • 0036627214 scopus 로고    scopus 로고
    • Circulating amyloid-β peptide crosses the blood-brain barrier in aged monkeys and contributes to Alzheimer's disease lesions
    • DOI 10.1016/S1537-1891(02)00198-2, PII S1537189102001982
    • Mackic, J. B., Bading, J., Ghiso, J., Walker, L., Wisniewski, T., Frangione, B., and Zlokovic, B. V. (2002) Circulating amyloid-β peptide crosses the blood-brain barrier in aged monkeys and contributes to Alzheimer's disease lesions. Vascul. Pharmacol. 38, 303-313 (Pubitemid 36398252)
    • (2002) Vascular Pharmacology , vol.38 , Issue.6 , pp. 303-313
    • Mackic, J.B.1    Bading, J.2    Ghiso, J.3    Walker, L.4    Wisniewski, T.5    Frangione, B.6    Zlokovic, B.V.7
  • 55
    • 77954512324 scopus 로고    scopus 로고
    • Comparison of intravenous immunoglobulins for naturally occurring autoantibodies against amyloid-β
    • Balakrishnan, K., Andrei-Selmer, L. C., Selmer, T., Bacher, M., and Dodel, R. (2010) Comparison of intravenous immunoglobulins for naturally occurring autoantibodies against amyloid-β. J. Alzheimers Dis. 20, 135-143
    • (2010) J. Alzheimers Dis. , vol.20 , pp. 135-143
    • Balakrishnan, K.1    Andrei-Selmer, L.C.2    Selmer, T.3    Bacher, M.4    Dodel, R.5
  • 56
    • 84866785358 scopus 로고    scopus 로고
    • Naturally occurring autoantibodies against β-amyloid
    • Bach, J. P., and Dodel, R. (2012) Naturally occurring autoantibodies against β-amyloid. Adv. Exp. Med. Biol. 750, 91-99
    • (2012) Adv. Exp. Med. Biol. , vol.750 , pp. 91-99
    • Bach, J.P.1    Dodel, R.2
  • 59
    • 0037155581 scopus 로고    scopus 로고
    • Brain to plasma amyloid-β efflux: A measure of brain amyloid burden in a mouse model of Alzheimer's disease
    • DOI 10.1126/science.1067568
    • DeMattos, R. B., Bales, K. R., Cummins, D. J., Paul, S. M., and Holtzman, D. M. (2002) Brain to plasma amyloid-β efflux. A measure of brain amyloid burden in a mouse model of Alzheimer's disease. Science 295, 2264-2267 (Pubitemid 34258840)
    • (2002) Science , vol.295 , Issue.5563 , pp. 2264-2267
    • DeMattos, R.B.1    Bales, K.R.2    Cummins, D.J.3    Paul, S.M.4    Holtzman, D.M.5
  • 61
    • 84864011925 scopus 로고    scopus 로고
    • Longitudinal analysis of novel Alzheimer's disease proteomic cerebrospinal fluid biomarkers during intravenous immunoglobulin therapy
    • Shayan, G., Adamiak, B., Relkin, N. R., and Lee, K. H. (2012) Longitudinal analysis of novel Alzheimer's disease proteomic cerebrospinal fluid biomarkers during intravenous immunoglobulin therapy. Electrophoresis 33, 1975-1979
    • (2012) Electrophoresis , vol.33 , pp. 1975-1979
    • Shayan, G.1    Adamiak, B.2    Relkin, N.R.3    Lee, K.H.4
  • 63
    • 34548107246 scopus 로고    scopus 로고
    • Peripheral transgene expression of plasma gelsolin reduces amyloid in transgenic mouse models of Alzheimer's disease
    • DOI 10.1038/sj.mt.6300253, PII 6300253
    • Hirko, A. C., Meyer, E. M., King, M. A., and Hughes, J. A. (2007) Peripheral transgene expression of plasma gelsolin reduces amyloid in transgenic mouse models of Alzheimer's disease. Mol. Ther. 15, 1623-1629 (Pubitemid 47289005)
    • (2007) Molecular Therapy , vol.15 , Issue.9 , pp. 1623-1629
    • Hirko, A.C.1    Meyer, E.M.2    King, M.A.3    Hughes, J.A.4
  • 65
    • 33745588826 scopus 로고    scopus 로고
    • Major involvement of low-density lipoprotein receptor-related protein 1 in the clearance of plasma free amyloid β-peptide by the liver
    • DOI 10.1007/s11095-006-0208-7
    • Tamaki, C., Ohtsuki, S., Iwatsubo, T., Hashimoto, T., Yamada, K., Yabuki, C., and Terasaki, T. (2006) Major involvement of low-density lipoprotein receptor-related protein 1 in the clearance of plasma free amyloid β-peptide by the liver. Pharm. Res. 23, 1407-1416 (Pubitemid 43993806)
    • (2006) Pharmaceutical Research , vol.23 , Issue.7 , pp. 1407-1416
    • Tamaki, C.1    Ohtsuki, S.2    Iwatsubo, T.3    Hashimoto, T.4    Yamada, K.5    Yabuki, C.6    Terasaki, T.7
  • 66
    • 0023220909 scopus 로고
    • Transport of leucine-enkephalin across the blood-brain barrier in the perfused guinea pig brain
    • Zloković, B. V., Lipovac, M. N., Begley, D. J., Davson, H., and Rakić, L. (1987) Transport of leucine-enkephalin across the blood-brain barrier in the perfused guinea pig brain. J. Neurochem. 49, 310-315
    • (1987) J. Neurochem. , vol.49 , pp. 310-315
    • Zloković, B.V.1    Lipovac, M.N.2    Begley, D.J.3    Davson, H.4    Rakić, L.5
  • 67
    • 0034609551 scopus 로고    scopus 로고
    • Specific binding of α-macroglobulin to complement-type repeat CR4 of the low-density lipoprotein receptor-related protein
    • Andersen, O. M., Christensen, P. A., Christensen, L. L., Jacobsen, C., Moestrup, S. K., Etzerodt, M., and Thogersen, H. C. (2000) Specific binding of α-macroglobulin to complement-type repeat CR4 of the low-density lipoprotein receptor-related protein. Biochemistry 39, 10627-10633
    • (2000) Biochemistry , vol.39 , pp. 10627-10633
    • Andersen, O.M.1    Christensen, P.A.2    Christensen, L.L.3    Jacobsen, C.4    Moestrup, S.K.5    Etzerodt, M.6    Thogersen, H.C.7
  • 70
    • 84863337843 scopus 로고    scopus 로고
    • Alzheimer mechanisms and therapeutic strategies
    • Huang, Y., and Mucke, L. (2012) Alzheimer mechanisms and therapeutic strategies. Cell 148, 1204-1222
    • (2012) Cell , vol.148 , pp. 1204-1222
    • Huang, Y.1    Mucke, L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.