메뉴 건너뛰기




Volumn 99, Issue 3, 2006, Pages 689-707

Disease modifying therapy for AD?

Author keywords

[No Author keywords available]

Indexed keywords

ADAMANTANE DERIVATIVE; AF 267B; ALZHEIMER DISEASE VACCINE; AMYLOID BETA PROTEIN; APOLIPOPROTEIN E; AR A014418; BETA SECRETASE INHIBITOR; CAD 106; CHAPERONE; CHOLINESTERASE INHIBITOR; CLIOQUINOL; CURCUMIN; DIPEPTIDYL CARBOXYPEPTIDASE; ENDOTHELIN CONVERTING ENZYME; EPIGALLOCATECHIN GALLATE; FLURBIPROFEN; GAMMA SECRETASE INHIBITOR; HOMOTAURINE; INOSITOL DERIVATIVE; LEVO FLURBIPROFEN; MEMANTINE; MEMBRANE METALLOENDOPEPTIDASE; MUSCARINIC M1 RECEPTOR AGONIST; N METHYL DEXTRO ASPARTIC ACID RECEPTOR; NEUROPROTECTIVE AGENT; NONSTEROID ANTIINFLAMMATORY AGENT; PHENSERINE; PLASMIN; SCYLLO INOSITOL; SRN 003 556; STATINE DERIVATIVE; SULFONIC ACID DERIVATIVE; TAU PROTEIN; UNCLASSIFIED DRUG; UNINDEXED DRUG;

EID: 33750082029     PISSN: 00223042     EISSN: 14714159     Source Type: Journal    
DOI: 10.1111/j.1471-4159.2006.04211.x     Document Type: Review
Times cited : (112)

References (247)
  • 2
    • 0024780573 scopus 로고
    • Alpha 1-antichymotrypsin in brain aging and disease
    • Abraham C. R. and Potter H. (1989) Alpha 1-antichymotrypsin in brain aging and disease. Prog. Clin. Biol. Res. 317, 1037-1048.
    • (1989) Prog. Clin. Biol. Res. , vol.317 , pp. 1037-1048
    • Abraham, C.R.1    Potter, H.2
  • 3
    • 18244384051 scopus 로고    scopus 로고
    • Voluntary exercise decreases amyloid load in a transgenic model of Alzheimer's disease
    • Adlard P. A., Perreau V. M., Pop V. and Cotman C. W. (2005) Voluntary exercise decreases amyloid load in a transgenic model of Alzheimer's disease. J. Neurosci. 25, 4217-4221.
    • (2005) J. Neurosci. , vol.25 , pp. 4217-4221
    • Adlard, P.A.1    Perreau, V.M.2    Pop, V.3    Cotman, C.W.4
  • 4
    • 12444268257 scopus 로고    scopus 로고
    • Prototype Alzheimer's disease vaccine using the immunodominant B cell epitope from beta-amyloid and promiscuous T cell epitope pan HLA DR-binding peptide
    • Agadjanyan M. G., Ghochikyan A., Petrushina I., Vasilevko V., Movsesyan N., Mkrtichyan M., Saing T. and Cribbs D. H. (2005) Prototype Alzheimer's disease vaccine using the immunodominant B cell epitope from beta-amyloid and promiscuous T cell epitope pan HLA DR-binding peptide. J. Immunol. 174, 1580-1586.
    • (2005) J. Immunol. , vol.174 , pp. 1580-1586
    • Agadjanyan, M.G.1    Ghochikyan, A.2    Petrushina, I.3    Vasilevko, V.4    Movsesyan, N.5    Mkrtichyan, M.6    Saing, T.7    Cribbs, D.H.8
  • 6
    • 0034612175 scopus 로고    scopus 로고
    • Inflammation and Alzheimer's disease
    • Akiyama H., Barger S., Barnum S. et al. (2000) Inflammation and Alzheimer's disease. Neurobiol. Aging 21, 383-421.
    • (2000) Neurobiol. Aging , vol.21 , pp. 383-421
    • Akiyama, H.1    Barger, S.2    Barnum, S.3
  • 9
    • 19644368873 scopus 로고    scopus 로고
    • Inhibition of amyloid precursor protein processing by beta-secretase through site-directed antibodies
    • Arbel M., Yacoby I. and Solomon B. (2005) Inhibition of amyloid precursor protein processing by beta-secretase through site-directed antibodies. Proc. Natl Acad. Sci. U S A 102, 7718-7723.
    • (2005) Proc. Natl. Acad. Sci. U S A , vol.102 , pp. 7718-7723
    • Arbel, M.1    Yacoby, I.2    Solomon, B.3
  • 10
    • 0037452779 scopus 로고    scopus 로고
    • Epitope and isotype specificities of antibodies to beta-amyloid peptide for protection against Alzheimer's disease-like neuropathology
    • Bard F., Barbour R., Cannon C. et al. (2003) Epitope and isotype specificities of antibodies to beta-amyloid peptide for protection against Alzheimer's disease-like neuropathology. Proc. Natl Acad. Sci. U S A 100, 2023-2028.
    • (2003) Proc. Natl. Acad. Sci. U S A , vol.100 , pp. 2023-2028
    • Bard, F.1    Barbour, R.2    Cannon, C.3
  • 11
    • 0033835996 scopus 로고    scopus 로고
    • Peripherally administered antibodies against amyloid beta-peptide enter the central nervous system and reduce pathology in a mouse model of Alzheimer disease
    • Bard F., Cannon C., Barbour R. et al. (2000) Peripherally administered antibodies against amyloid beta-peptide enter the central nervous system and reduce pathology in a mouse model of Alzheimer disease. Nat. Med. 6, 916-919.
    • (2000) Nat. Med. , vol.6 , pp. 916-919
    • Bard, F.1    Cannon, C.2    Barbour, R.3
  • 12
    • 33745920161 scopus 로고    scopus 로고
    • Human amyloid-beta synthesis and clearance rates as measured in cerebrospinal fluid in vivo
    • Bateman R. J., Munsell L. Y., Morris J. C., Swarm R., Yarasheski K. E. and Holtzman D. M. (2006) Human amyloid-beta synthesis and clearance rates as measured in cerebrospinal fluid in vivo. Nat. Med. 12, 856-861.
    • (2006) Nat. Med. , vol.12 , pp. 856-861
    • Bateman, R.J.1    Munsell, L.Y.2    Morris, J.C.3    Swarm, R.4    Yarasheski, K.E.5    Holtzman, D.M.6
  • 13
    • 6344233805 scopus 로고    scopus 로고
    • Selected non-steroidal anti-inflammatory drugs and their derivatives target gamma-secretase at a novel site-evidence for an allosteric mechanism
    • Beher D., Clarke E. E., Wrigley J. D., Martin A. C., Nadin A., Churcher I. and Shearman M. S. (2004) Selected non-steroidal anti-inflammatory drugs and their derivatives target gamma-secretase at a novel site-evidence for an allosteric mechanism. J. Biol. Chem. 279, 43 419-43 426.
    • (2004) J. Biol. Chem. , vol.279 , pp. 43419-43426
    • Beher, D.1    Clarke, E.E.2    Wrigley, J.D.3    Martin, A.C.4    Nadin, A.5    Churcher, I.6    Shearman, M.S.7
  • 14
    • 0035930625 scopus 로고    scopus 로고
    • Mutations of tau protein in frontotemporal dementia promote aggregation of paired helical filaments by enhancing local beta-structure
    • von Bergen M., Barghorn S., Li L., Marx A., Biernat J., Mandelkow E. M. and Mandelkow E. (2001) Mutations of tau protein in frontotemporal dementia promote aggregation of paired helical filaments by enhancing local beta-structure. J. Biol. Chem. 276, 48 165-48 174.
    • (2001) J. Biol. Chem. , vol.276 , pp. 48165-48174
    • Von Bergen, M.1    Barghorn, S.2    Li, L.3    Marx, A.4    Biernat, J.5    Mandelkow, E.M.6    Mandelkow, E.7
  • 15
    • 33749020726 scopus 로고    scopus 로고
    • Efficacy and safety ofMPC-7869 (R.-flurbiprofen), a selective Abeta42 loering agent in mild Alzheimer's disease: Results of a 12-month phase 2 trial and 1-year follow on study
    • Black S., Wilcock G. K., Hawworth J., Hendrix S., Zavitz K., Christensen D. b. M.-H., Bass S., Laughlin M. and Swabb E. (2006) Efficacy and safety ofMPC-7869 (R.-flurbiprofen), a selective Abeta42 loering agent in mild Alzheimer's disease: results of a 12-month phase 2 trial and 1-year follow on study. Neurology 66, A347.
    • (2006) Neurology , vol.66
    • Black, S.1    Wilcock, G.K.2    Hawworth, J.3    Hendrix, S.4    Zavitz, K.5    Christensen, D.B.M.-H.6    Bass, S.7    Laughlin, M.8    Swabb, E.9
  • 16
    • 7444253126 scopus 로고    scopus 로고
    • Cerebrospinal fluid protein biomarkers for Alzheimer's disease
    • Blennow K. (2004) Cerebrospinal fluid protein biomarkers for Alzheimer's disease. Neurorx. 1, 213-225.
    • (2004) Neurorx. , vol.1 , pp. 213-225
    • Blennow, K.1
  • 17
    • 0029671454 scopus 로고    scopus 로고
    • Cholesterol modulates alpha-secretase cleavage of amyloid precursor protein
    • Bodovitz S. and Klein W. L. (1996) Cholesterol modulates alpha-secretase cleavage of amyloid precursor protein. J. Biol. Chem. 271, 4436-4440.
    • (1996) J. Biol. Chem. , vol.271 , pp. 4436-4440
    • Bodovitz, S.1    Klein, W.L.2
  • 18
    • 14444272986 scopus 로고    scopus 로고
    • Evidence that tumor necrosis factor alpha converting enzyme is involved in regulated alpha-secretase cleavage of the Alzheimer amyloid protein precursor
    • Buxbaum J. D., Liu K. N., Luo Y., Slack J. L., Stocking K. L., Peschon J. J., Johnson R. S., Castner B. J., Cerretti D. P. and Black R. A. (1998) Evidence that tumor necrosis factor alpha converting enzyme is involved in regulated alpha-secretase cleavage of the Alzheimer amyloid protein precursor. J. Biol. Chem. 273, 27 765-27 767.
    • (1998) J. Biol. Chem. , vol.273 , pp. 27765-27767
    • Buxbaum, J.D.1    Liu, K.N.2    Luo, Y.3    Slack, J.L.4    Stocking, K.L.5    Peschon, J.J.6    Johnson, R.S.7    Castner, B.J.8    Cerretti, D.P.9    Black, R.A.10
  • 21
    • 4444223956 scopus 로고    scopus 로고
    • Docosahexaenoic acid protects from dendritic pathology in an Alzheimer's disease mouse model
    • Calon F., Lim G. P., Yang F. et al. (2004) Docosahexaenoic acid protects from dendritic pathology in an Alzheimer's disease mouse model. Neuron 43, 633-645.
    • (2004) Neuron , vol.43 , pp. 633-645
    • Calon, F.1    Lim, G.P.2    Yang, F.3
  • 22
    • 33747359163 scopus 로고    scopus 로고
    • Virus and virus-like particle-based immunogens for Alzheimer's disease induce antibody responses against amyloid-beta without concomitant T cell responses
    • Chackerian B., Rangel M., Hunter Z. and Peabody D. S. (2006) Virus and virus-like particle-based immunogens for Alzheimer's disease induce antibody responses against amyloid-beta without concomitant T cell responses. Vaccine 24, 6321-6331.
    • (2006) Vaccine , vol.24 , pp. 6321-6331
    • Chackerian, B.1    Rangel, M.2    Hunter, Z.3    Peabody, D.S.4
  • 23
    • 0034964390 scopus 로고    scopus 로고
    • Treatment with a copper-zinc chelator markedly and rapidly inhibits beta-amyloid accumulation in Alzheimer's disease transgenic mice
    • Cherny R. A., Atwood C. S., Xilinas M. E. et al. (2001) Treatment with a copper-zinc chelator markedly and rapidly inhibits beta-amyloid accumulation in Alzheimer's disease transgenic mice. Neuron 30, 665-676.
    • (2001) Neuron , vol.30 , pp. 665-676
    • Cherny, R.A.1    Atwood, C.S.2    Xilinas, M.E.3
  • 25
    • 27644489474 scopus 로고    scopus 로고
    • P-glycoprotein deficiency at the blood-brain barrier increases amyloid-beta deposition in an Alzheimer disease mouse model
    • Cirrito J. R. Deane R. Fagan A. M. et al. (2005) P-glycoprotein deficiency at the blood-brain barrier increases amyloid-beta deposition in an Alzheimer disease mouse model. J. Clin. Invest 115, 3285-3290.
    • (2005) J. Clin. Invest , vol.115 , pp. 3285-3290
    • Cirrito, J.R.1    Deane, R.2    Fagan, A.M.3
  • 27
    • 28444459842 scopus 로고    scopus 로고
    • Insulin resistance syndrome and Alzheimer's disease: Age- And obesity-related effects on memory, amyloid, and inflammation
    • Craft S. (2005) Insulin resistance syndrome and Alzheimer's disease: age- and obesity-related effects on memory, amyloid, and inflammation. Neurobiol. Aging 26, 65-69.
    • (2005) Neurobiol. Aging , vol.26 , pp. 65-69
    • Craft, S.1
  • 28
    • 0036318395 scopus 로고    scopus 로고
    • Regulation of tau RNA maturation by thyroid hormone is mediated by the neural RNA-binding protein musashi-1
    • Cuadrado A., Garcia-Fernandez L. F., Imai T., Okano H. and Munoz A. (2002) Regulation of tau RNA maturation by thyroid hormone is mediated by the neural RNA-binding protein musashi-1. Mol. Cell Neurosci. 20, 198-210.
    • (2002) Mol. Cell Neurosci. , vol.20 , pp. 198-210
    • Cuadrado, A.1    Garcia-Fernandez, L.F.2    Imai, T.3    Okano, H.4    Munoz, A.5
  • 29
    • 0035827681 scopus 로고    scopus 로고
    • Alzheimer's disease amyloid-beta binds copper and zinc to generate an allosterically ordered membrane-penetrating structure containing superoxide dismutase-like subunits
    • Curtain C. C., Ali F., Volitakis I., Cherny R. A., Norton R. S., Beyreuther K., Barrow C. J., Masters C. L., Bush A. I. and Barnham K. J. (2001) Alzheimer's disease amyloid-beta binds copper and zinc to generate an allosterically ordered membrane-penetrating structure containing superoxide dismutase-like subunits. J. Biol. Chem. 276, 20 466-20 473.
    • (2001) J. Biol. Chem. , vol.276 , pp. 20466-20473
    • Curtain, C.C.1    Ali, F.2    Volitakis, I.3    Cherny, R.A.4    Norton, R.S.5    Beyreuther, K.6    Barrow, C.J.7    Masters, C.L.8    Bush, A.I.9    Barnham, K.J.10
  • 30
    • 0036752545 scopus 로고    scopus 로고
    • Open peer commentary regarding Abeta immunization and CNS inflammation by Pasinetti et al.
    • Das P., Golde T. E. (2002) Open peer commentary regarding Abeta immunization and CNS inflammation by Pasinetti et al. Neurobiol. Aging 23, 671.
    • (2002) Neurobiol. Aging , vol.23 , pp. 671
    • Das, P.1    Golde, T.E.2
  • 31
    • 0141457897 scopus 로고    scopus 로고
    • Amyloid-beta immunization effectively reduces amyloid deposition in FcRgamma-/- Knock-out mice
    • Das P., Howard V., Loosbrock N., Dickson D., Murphy M. P. and Golde T. E. (2003) Amyloid-beta immunization effectively reduces amyloid deposition in FcRgamma-/- knock-out mice. J. Neurosci. 23, 8532-8538.
    • (2003) J. Neurosci. , vol.23 , pp. 8532-8538
    • Das, P.1    Howard, V.2    Loosbrock, N.3    Dickson, D.4    Murphy, M.P.5    Golde, T.E.6
  • 32
    • 0034746897 scopus 로고    scopus 로고
    • Reduced effectiveness of Abeta1-42 immunization in APP transgenic mice with significant amyloid deposition
    • Das P., Murphy M. P., Younkin L. H., Younkin S. G. and Golde T. E. (2001) Reduced effectiveness of Abeta1-42 immunization in APP transgenic mice with significant amyloid deposition. Neurobiol. Aging 22, 721-727.
    • (2001) Neurobiol. Aging , vol.22 , pp. 721-727
    • Das, P.1    Murphy, M.P.2    Younkin, L.H.3    Younkin, S.G.4    Golde, T.E.5
  • 33
    • 0033535504 scopus 로고    scopus 로고
    • A presenilin-1-dependent gamma-secretase-like protease mediates release of Notch intracellular domain
    • De Strooper B., Annaert W., Cupers P. et al. (1999) A presenilin-1-dependent gamma-secretase-like protease mediates release of Notch intracellular domain. Nature 398, 518-522.
    • (1999) Nature , vol.398 , pp. 518-522
    • De Strooper, B.1    Annaert, W.2    Cupers, P.3
  • 34
    • 4043061467 scopus 로고    scopus 로고
    • LRP/amyloid beta-peptide interaction mediates differential brain efflux of Abeta isoforms
    • Deane R., Wu Z., Sagare A. et al. (2004b) LRP/amyloid beta-peptide interaction mediates differential brain efflux of Abeta isoforms. Neuron 43, 333-344.
    • (2004) Neuron , vol.43 , pp. 333-344
    • Deane, R.1    Wu, Z.2    Sagare, A.3
  • 35
    • 7644225312 scopus 로고    scopus 로고
    • RAGE (yin) versus LRP (yang) balance regulates alzheimer amyloid beta-peptide clearance through transport across the blood-brain barrier
    • Deane R., Wu Z. and Zlokovic B. V. (2004a) RAGE (yin) versus LRP (yang) balance regulates alzheimer amyloid beta-peptide clearance through transport across the blood-brain barrier. Stroke 35, 2628-2631.
    • (2004) Stroke , vol.35 , pp. 2628-2631
    • Deane, R.1    Wu, Z.2    Zlokovic, B.V.3
  • 36
    • 0035902619 scopus 로고    scopus 로고
    • Peripheral anti-A beta antibody alters CNS and plasma a beta clearance and decreases brain a beta burden in a mouse model of Alzheimer's disease
    • DeMattos R. B., Bales K. R., Cummins D. J., Dodart J. C., Paul S. M. and Holtzman D. M. (2001) Peripheral anti-A beta antibody alters CNS and plasma A beta clearance and decreases brain A beta burden in a mouse model of Alzheimer's disease. Proc. Natl Acad. Sci. U S A 98, 8850-8855.
    • (2001) Proc. Natl. Acad. Sci. U S A , vol.98 , pp. 8850-8855
    • DeMattos, R.B.1    Bales, K.R.2    Cummins, D.J.3    Dodart, J.C.4    Paul, S.M.5    Holtzman, D.M.6
  • 37
    • 0037155581 scopus 로고    scopus 로고
    • Brain to plasma amyloid-beta efflux: A measure of brain amyloid burden in a mouse model of Alzheimer's disease
    • DeMattos R. B., Bales K. R., Cummins D. J., Paul S. M. and Holtzman D. M. (2002a) Brain to plasma amyloid-beta efflux: a measure of brain amyloid burden in a mouse model of Alzheimer's disease. Science 295, 2264-2267.
    • (2002) Science , vol.295 , pp. 2264-2267
    • DeMattos, R.B.1    Bales, K.R.2    Cummins, D.J.3    Paul, S.M.4    Holtzman, D.M.5
  • 39
    • 33646246733 scopus 로고    scopus 로고
    • HSP induction mediates selective clearance of tau phosphorylated at proline-directed Ser/Thr sites but not KXGS (MARK) sites
    • Dickey C. A., Dunmore J., Lu B., Wang J. W., Lee W. C., Kamal A., Burrows F., Eckman C., Hutton M. and Petrucelli L. (2006a) HSP induction mediates selective clearance of tau phosphorylated at proline-directed Ser/Thr sites but not KXGS (MARK) sites. Faseb J. 20, 753-755.
    • (2006) Faseb J. , vol.20 , pp. 753-755
    • Dickey, C.A.1    Dunmore, J.2    Lu, B.3    Wang, J.W.4    Lee, W.C.5    Kamal, A.6    Burrows, F.7    Eckman, C.8    Hutton, M.9    Petrucelli, L.10
  • 40
    • 33745959291 scopus 로고    scopus 로고
    • Deletion of the ubiquitin ligase CHIP leads to the accumulation, but not the aggregation, of both endogenous phospho- and caspase-3-cleaved tau species
    • Dickey C. A., Yue M., Lin W. L. et al. (2006b) Deletion of the ubiquitin ligase CHIP leads to the accumulation, but not the aggregation, of both endogenous phospho- and caspase-3-cleaved tau species. J. Neurosci. 26, 6985-6996.
    • (2006) J. Neurosci. , vol.26 , pp. 6985-6996
    • Dickey, C.A.1    Yue, M.2    Lin, W.L.3
  • 41
    • 0036240395 scopus 로고    scopus 로고
    • Immunization reverses memory deficits without reducing brain Abeta burden in Alzheimer's disease model
    • Dodart J. C., Bales K. R., Gannon K. S. et al. (2002) Immunization reverses memory deficits without reducing brain Abeta burden in Alzheimer's disease model. Nat. Neurosci. 5, 452-457.
    • (2002) Nat. Neurosci. , vol.5 , pp. 452-457
    • Dodart, J.C.1    Bales, K.R.2    Gannon, K.S.3
  • 43
    • 24744449320 scopus 로고    scopus 로고
    • Phenotypic and biochemical analyses of BACE1- And BACE2-deficient mice
    • Dominguez D., Tournoy J., Hartmann D. et al. (2005) Phenotypic and biochemical analyses of BACE1- and BACE2-deficient mice. J. Biol. Chem. 280, 30 797-30 806.
    • (2005) J. Biol. Chem. , vol.280 , pp. 30797-30806
    • Dominguez, D.1    Tournoy, J.2    Hartmann, D.3
  • 44
    • 33747634776 scopus 로고    scopus 로고
    • Stabilization of the TAU exon 10 stem loop alters pre-mRNA splicing
    • Donahue C. P., Muratore C., Wu J. Y., Kosik K. S. and Wolfe M. S. (2006) Stabilization of the TAU exon 10 stem loop alters pre-mRNA splicing. J. Biol. Chem. 281, 23 302-23 306.
    • (2006) J. Biol. Chem. , vol.281 , pp. 23302-23306
    • Donahue, C.P.1    Muratore, C.2    Wu, J.Y.3    Kosik, K.S.4    Wolfe, M.S.5
  • 45
    • 4644275963 scopus 로고    scopus 로고
    • Intravenous immunoglobulins containing antibodies against beta-amyloid for the treatment of Alzheimer's disease
    • Dodel R. C. Du Y., Depboylu C. et al. (2004) Intravenous immunoglobulins containing antibodies against beta-amyloid for the treatment of Alzheimer's disease. J. Neurol. Neurosurg. Psychiatry 75, 1472-1474.
    • (2004) J. Neurol. Neurosurg. Psychiatry , vol.75 , pp. 1472-1474
    • Dodel, R.C.1    Du, Y.2    Depboylu, C.3
  • 47
    • 27844442718 scopus 로고    scopus 로고
    • Abeta-degrading enzymes: Modulators of Alzheimer's disease pathogenesis and targets for therapeutic intervention
    • Eckman E. A. and Eckman C. B. (2005) Abeta-degrading enzymes: modulators of Alzheimer's disease pathogenesis and targets for therapeutic intervention. Biochem. Soc. Trans. 33, 1101-1105.
    • (2005) Biochem. Soc. Trans. , vol.33 , pp. 1101-1105
    • Eckman, E.A.1    Eckman, C.B.2
  • 48
    • 0035816707 scopus 로고    scopus 로고
    • Degradation of the Alzheimer's amyloid beta peptide by endothelin- Converting enzyme
    • Eckman E. A., Reed D. K. and Eckman C. B. (2001) Degradation of the Alzheimer's amyloid beta peptide by endothelin- converting enzyme. J. Biol. Chem. 276, 24 540-24 548.
    • (2001) J. Biol. Chem. , vol.276 , pp. 24540-24548
    • Eckman, E.A.1    Reed, D.K.2    Eckman, C.B.3
  • 49
    • 0037462769 scopus 로고    scopus 로고
    • Alzheimer's disease beta-amyloid peptide is increased in mice deficient in endothelin-converting enzyme
    • Eckman E. A., Watson M., Marlow L., Sambamurti K. and Eckman C. B. (2003) Alzheimer's disease beta-amyloid peptide is increased in mice deficient in endothelin-converting enzyme. J. Biol. Chem. 278, 2081-2084.
    • (2003) J. Biol. Chem. , vol.278 , pp. 2081-2084
    • Eckman, E.A.1    Watson, M.2    Marlow, L.3    Sambamurti, K.4    Eckman, C.B.5
  • 50
    • 33646922314 scopus 로고    scopus 로고
    • Full reversal of Alzheimer's disease-like phenotype in a mouse model with conditional overexpression of glycogen synthase kinase-3
    • Engel T., Hernandez F., Avila J. and Lucas J. J. (2006) Full reversal of Alzheimer's disease-like phenotype in a mouse model with conditional overexpression of glycogen synthase kinase-3. J. Neurosci. 26, 5083-5090.
    • (2006) J. Neurosci. , vol.26 , pp. 5083-5090
    • Engel, T.1    Hernandez, F.2    Avila, J.3    Lucas, J.J.4
  • 51
    • 85047691727 scopus 로고    scopus 로고
    • NSAIDs and enantiomers of flurbiprofen target gamma-secretase and lower Abeta 42 in vivo
    • Eriksen J. L., Sagi S. A., Smith T. E. et al. (2003) NSAIDs and enantiomers of flurbiprofen target gamma-secretase and lower Abeta 42 in vivo. J. Clin. Invest. 112, 440-449.
    • (2003) J. Clin. Invest. , vol.112 , pp. 440-449
    • Eriksen, J.L.1    Sagi, S.A.2    Smith, T.E.3
  • 52
    • 13544273507 scopus 로고    scopus 로고
    • Elevated amyloid beta protein (Abeta42) and late onset Alzheimer's disease are associated with single nucleotide polymorphisms in the urokinase-type plasminogen activator gene
    • Ertekin-Taner N., Ronald J., Feuk L. et al. (2005) Elevated amyloid beta protein (Abeta42) and late onset Alzheimer's disease are associated with single nucleotide polymorphisms in the urokinase-type plasminogen activator gene. Hum. Mol. Genet. 14, 447-460.
    • (2005) Hum. Mol. Genet. , vol.14 , pp. 447-460
    • Ertekin-Taner, N.1    Ronald, J.2    Feuk, L.3
  • 55
    • 33644832047 scopus 로고    scopus 로고
    • Inverse relation between in vivo amyloid imaging load and cerebrospinal fluid Abeta (42) in humans
    • Fagan A. M., Mintun M. A., Mach R. H. et al. (2005) Inverse relation between in vivo amyloid imaging load and cerebrospinal fluid Abeta (42) in humans. Ann. Neurol. 59, 512-519.
    • (2005) Ann. Neurol. , vol.59 , pp. 512-519
    • Fagan, A.M.1    Mintun, M.A.2    Mach, R.H.3
  • 56
    • 0034528425 scopus 로고    scopus 로고
    • Alpha-secretase activity of the disintegrin metalloprotease ADAM 10. Influences of domain structure
    • Fahrenholz F., Gilbert S., Kojro E., Lammich S. and Postina R. (2000) Alpha-secretase activity of the disintegrin metalloprotease ADAM 10. Influences of domain structure. Ann. N Y Acad. Sci. 920, 215-222.
    • (2000) Ann. N Y Acad. Sci. , vol.920 , pp. 215-222
    • Fahrenholz, F.1    Gilbert, S.2    Kojro, E.3    Lammich, S.4    Postina, R.5
  • 57
    • 25844517893 scopus 로고    scopus 로고
    • Lithium chloride increases the production of amyloid-beta peptide independently from its inhibition of glycogen synthase kinase 3
    • Feyt C., Kienlen-Campard P., Leroy K., N'Kuli F., Courtoy P. J., Brion J. P. and Octave J. N. (2005) Lithium chloride increases the production of amyloid-beta peptide independently from its inhibition of glycogen synthase kinase 3. J. Biol. Chem. 280, 33 220-33 227.
    • (2005) J. Biol. Chem. , vol.280 , pp. 33220-33227
    • Feyt, C.1    Kienlen-Campard, P.2    Leroy, K.3    N'Kuli, F.4    Courtoy, P.J.5    Brion, J.P.6    Octave, J.N.7
  • 58
    • 18144415471 scopus 로고    scopus 로고
    • Effects of A{beta} immunization (AN1792) on MRI measures of cerebral Volume in Alzheimer disease
    • Fox N. C., Black R. S., Gilman S., Rossor M. N., Griffith S. G., Jenkins L. and Koller M. (2005) Effects of A{beta} immunization (AN1792) on MRI measures of cerebral Volume in Alzheimer disease. Neurology. 64, 1563-1572.
    • (2005) Neurology , vol.64 , pp. 1563-1572
    • Fox, N.C.1    Black, R.S.2    Gilman, S.3    Rossor, M.N.4    Griffith, S.G.5    Jenkins, L.6    Koller, M.7
  • 59
    • 0035928402 scopus 로고    scopus 로고
    • Imaging of onset and progression of Alzheimer's disease with voxel- compression mapping of serial magnetic resonance images
    • Fox N. C., Crum W. R., Scahill R. I., Stevens J. M., Janssen J. C. and Rossor M. N. (2001) Imaging of onset and progression of Alzheimer's disease with voxel- compression mapping of serial magnetic resonance images. Lancet 358, 201-205.
    • (2001) Lancet , vol.358 , pp. 201-205
    • Fox, N.C.1    Crum, W.R.2    Scahill, R.I.3    Stevens, J.M.4    Janssen, J.C.5    Rossor, M.N.6
  • 60
    • 29644431788 scopus 로고    scopus 로고
    • gamma-Secretase substrate selectivity can be modulated directly via interaction with a nucleotide-binding site
    • Fraering P. C. Ye W., LaVoie M. J., Ostaszewski B. L., Selkoe D. J. and Wolfe M. S. (2005) gamma-Secretase substrate selectivity can be modulated directly via interaction with a nucleotide-binding site. J. Biol. Chem. 280, 41 987-41 996.
    • (2005) J. Biol. Chem. , vol.280 , pp. 41987-41996
    • Fraering, P.C.1    Ye, W.2    LaVoie, M.J.3    Ostaszewski, B.L.4    Selkoe, D.J.5    Wolfe, M.S.6
  • 61
    • 0035686083 scopus 로고    scopus 로고
    • Phenolic anti-inflammatory antioxidant reversal of Abeta-induced cognitive deficits and neuropathology
    • Frautschy S. A., Hu W., Kim P., Miller S. A., Chu T., Harris-White M. E. and Cole G. M. (2001) Phenolic anti-inflammatory antioxidant reversal of Abeta-induced cognitive deficits and neuropathology. Neurobiol. Aging 22, 993-1005.
    • (2001) Neurobiol. Aging , vol.22 , pp. 993-1005
    • Frautschy, S.A.1    Hu, W.2    Kim, P.3    Miller, S.A.4    Chu, T.5    Harris-White, M.E.6    Cole, G.M.7
  • 63
    • 24644435506 scopus 로고    scopus 로고
    • Nasal vaccination with a proteosome-based adjuvant and glatiramer acetate clears beta-amyloid in a mouse model of Alzheimer disease
    • Frenkel D., Maron R., Burt D. S. and Weiner H. L. (2005) Nasal vaccination with a proteosome-based adjuvant and glatiramer acetate clears beta-amyloid in a mouse model of Alzheimer disease. J. Clin. Invest. 115, 2423-2433.
    • (2005) J. Clin. Invest. , vol.115 , pp. 2423-2433
    • Frenkel, D.1    Maron, R.2    Burt, D.S.3    Weiner, H.L.4
  • 65
    • 0347594304 scopus 로고    scopus 로고
    • Modeling tau polymerization in vitro: A review and synthesis
    • Gamblin T. C., Berry R. W. and Binder L. I. (2003) Modeling tau polymerization in vitro: a review and synthesis. Biochemistry 42, 15 009-15 017.
    • (2003) Biochemistry , vol.42 , pp. 15009-15017
    • Gamblin, T.C.1    Berry, R.W.2    Binder, L.I.3
  • 66
    • 0034705192 scopus 로고    scopus 로고
    • In vitro polymerization of tau protein monitored by laser light scattering: Method and application to the study of FTDP-17 mutants
    • Gamblin T. C., King M. E., Dawson H., Vitek M. P., Kuret J., Berry R. W. and Binder L. I. (2000) In vitro polymerization of tau protein monitored by laser light scattering: method and application to the study of FTDP-17 mutants. Biochemistry 39, 6136-6144.
    • (2000) Biochemistry , vol.39 , pp. 6136-6144
    • Gamblin, T.C.1    King, M.E.2    Dawson, H.3    Vitek, M.P.4    Kuret, J.5    Berry, R.W.6    Binder, L.I.7
  • 67
    • 0028030517 scopus 로고
    • Regulated cleavage of the Alzheimer amyloid precursor protein: Molecular and cellular basis
    • [Review]
    • Gandy S. and Greengard P. (1994) Regulated cleavage of the Alzheimer amyloid precursor protein: molecular and cellular basis. [Review]. Biochimie 76, 300-303.
    • (1994) Biochimie , vol.76 , pp. 300-303
    • Gandy, S.1    Greengard, P.2
  • 68
    • 0344688272 scopus 로고    scopus 로고
    • Tau phosphorylation, tangles, and neurodegeneration: The chicken or the egg?
    • Geschwind D. H. (2003) Tau phosphorylation, tangles, and neurodegeneration: the chicken or the egg? Neuron 40, 457-460.
    • (2003) Neuron , vol.40 , pp. 457-460
    • Geschwind, D.H.1
  • 69
    • 20944448555 scopus 로고    scopus 로고
    • Clinical effects of A{beta} immunization (AN1792) in patients with AD in an interrupted trial
    • Gilman S., Koller M., Black R. S. et al. (2005) Clinical effects of A{beta} immunization (AN1792) in patients with AD in an interrupted trial. Neurology 64, 1553-1562.
    • (2005) Neurology , vol.64 , pp. 1553-1562
    • Gilman, S.1    Koller, M.2    Black, R.S.3
  • 70
    • 33645107783 scopus 로고    scopus 로고
    • The alternative splicing of tau exon 10 and its regulatory proteins CLK2 and TRA2-BETA1 changes in sporadic Alzheimer's disease
    • Glatz D. C., Rujescu D., Tang Y. et al. (2006) The alternative splicing of tau exon 10 and its regulatory proteins CLK2 and TRA2-BETA1 changes in sporadic Alzheimer's disease. J. Neurochem. 96, 635-644.
    • (2006) J. Neurochem. , vol.96 , pp. 635-644
    • Glatz, D.C.1    Rujescu, D.2    Tang, Y.3
  • 71
    • 0023818885 scopus 로고
    • Alzheimer's disease: Its proteins and genes
    • Glenner G. G. (1988) Alzheimer's disease: its proteins and genes. Cell 52, 307-308.
    • (1988) Cell , vol.52 , pp. 307-308
    • Glenner, G.G.1
  • 72
    • 11144258263 scopus 로고    scopus 로고
    • Mutations causing neurodegenerative tauopathies
    • Goedert M. and Jakes R. (2005) Mutations causing neurodegenerative tauopathies. Biochim. Biophys. Acta 1739, 240-250.
    • (2005) Biochim. Biophys. Acta , vol.1739 , pp. 240-250
    • Goedert, M.1    Jakes, R.2
  • 73
    • 0026595846 scopus 로고
    • Tau proteins of Alzheimer paired helical filaments: Abnormal phosphorylation of all six brain isoforms
    • Goedert M., Sisodia S. S. and Price D. L. (1992) Tau proteins of Alzheimer paired helical filaments: Abnormal phosphorylation of all six brain isoforms. Neuron 8, 159-168.
    • (1992) Neuron , vol.8 , pp. 159-168
    • Goedert, M.1    Sisodia, S.S.2    Price, D.L.3
  • 74
    • 0037248301 scopus 로고    scopus 로고
    • Alzheimer disease therapy: Can the amyloid cascade be halted?
    • Golde T. E. (2003) Alzheimer disease therapy: Can the amyloid cascade be halted? J. Clin. Invest. 111, 11-18.
    • (2003) J. Clin. Invest. , vol.111 , pp. 11-18
    • Golde, T.E.1
  • 75
    • 13544272023 scopus 로고    scopus 로고
    • The Abeta hypothesis: Leading us to rationally-designed therapeutic strategies for the treatment or prevention of Alzheimer disease
    • Golde T. E. (2005) The Abeta hypothesis: leading us to rationally-designed therapeutic strategies for the treatment or prevention of Alzheimer disease. Brain Pathol. 15, 84-87.
    • (2005) Brain Pathol. , vol.15 , pp. 84-87
    • Golde, T.E.1
  • 76
    • 0037418440 scopus 로고    scopus 로고
    • Physiologic and pathologic events mediated by intramembranous and juxtamembranous proteolysis
    • Golde T. E. and Eckman C. B. (2003) Physiologic and pathologic events mediated by intramembranous and juxtamembranous proteolysis. Sci. STKE 2003, RE4.
    • (2003) Sci. STKE , vol.2003
    • Golde, T.E.1    Eckman, C.B.2
  • 77
    • 0034718027 scopus 로고    scopus 로고
    • Biochemical detection of Abeta isoforms: Implications for pathogenesis, diagnosis, and treatment of Alzheimer's disease
    • Golde T. E., Eckman C. B. and Younkin S. G. (2000) Biochemical detection of Abeta isoforms: implications for pathogenesis, diagnosis, and treatment of Alzheimer's disease. Biochim. Biophys. Acta 1502, 172-187.
    • (2000) Biochim. Biophys. Acta , vol.1502 , pp. 172-187
    • Golde, T.E.1    Eckman, C.B.2    Younkin, S.G.3
  • 78
    • 0035808361 scopus 로고    scopus 로고
    • Tau filament formation in transgenic mice expressing P301L tau
    • Gotz J., Chen F., Barmettler R. and Nitsch R. M. (2001) Tau filament formation in transgenic mice expressing P301L tau. J. Biol. Chem. 276, 529-534.
    • (2001) J. Biol. Chem. , vol.276 , pp. 529-534
    • Gotz, J.1    Chen, F.2    Barmettler, R.3    Nitsch, R.M.4
  • 79
    • 22144494112 scopus 로고    scopus 로고
    • An overview of phenserine tartrate, a novel acetylcholinesterase inhibitor for the treatment of Alzheimer's disease
    • Greig N. H., Sambamurti K. YuQ. S., Brossi A., Bruinsma G. B. and Lahiri D. K. (2005) An overview of phenserine tartrate, a novel acetylcholinesterase inhibitor for the treatment of Alzheimer's disease. Curr. Alzheimer Res. 2, 281-290.
    • (2005) Curr. Alzheimer Res. , vol.2 , pp. 281-290
    • Greig, N.H.1    Sambamurti, K.2    Yu, Q.S.3    Brossi, A.4    Bruinsma, G.B.5    Lahiri, D.K.6
  • 81
    • 0026683725 scopus 로고
    • The Alzheimer-like phosphorylation of tau protein reduces microtubule binding and involves Ser-Pro and Thr-Pro motifs
    • Gustke N., Steiner B., Mandelkow E. M., Biernat J., Meyer H. E., Goedert M. and Mandelkow E. (1992) The Alzheimer-like phosphorylation of tau protein reduces microtubule binding and involves Ser-Pro and Thr-Pro motifs. FEBS Lett. 307, 199-205.
    • (1992) FEBS Lett. , vol.307 , pp. 199-205
    • Gustke, N.1    Steiner, B.2    Mandelkow, E.M.3    Biernat, J.4    Meyer, H.E.5    Goedert, M.6    Mandelkow, E.7
  • 83
    • 0026597063 scopus 로고
    • Alzheimer's disease: The amyloid cascade hypothesis
    • Hardy J. A. and Higgins G. A. (1992) Alzheimer's disease: the amyloid cascade hypothesis. Science 256, 184-185.
    • (1992) Science , vol.256 , pp. 184-185
    • Hardy, J.A.1    Higgins, G.A.2
  • 84
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics
    • 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. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 85
    • 27844534846 scopus 로고    scopus 로고
    • Amyloid beta-protein is degraded by cellular angiotensin-converting enzyme (ACE) and elevated by an ACE inhibitor
    • Hemming M. L. and Selkoe D. J. (2005) Amyloid beta-protein is degraded by cellular angiotensin-converting enzyme (ACE) and elevated by an ACE inhibitor. J. Biol. Chem. 280, 37 644-37 650.
    • (2005) J. Biol. Chem. , vol.280 , pp. 37644-37650
    • Hemming, M.L.1    Selkoe, D.J.2
  • 87
    • 30044441879 scopus 로고    scopus 로고
    • The absence of ABCA1 decreases soluble ApoE levels but does not diminish amyloid deposition in two murine models of Alzheimer disease
    • Hirsch-Reinshagen V., Maia L. F., Burgess B. L. et al. (2005) The absence of ABCA1 decreases soluble ApoE levels but does not diminish amyloid deposition in two murine models of Alzheimer disease. J. Biol. Chem. 280, 43 243-43 256.
    • (2005) J. Biol. Chem. , vol.280 , pp. 43243-43256
    • Hirsch-Reinshagen, V.1    Maia, L.F.2    Burgess, B.L.3
  • 88
    • 0038100154 scopus 로고    scopus 로고
    • Antibodies against beta-amyloid slow cognitive decline in Alzheimer's disease
    • Hock C., Konietzko U., Streffer J. R. et al. (2003) Antibodies against beta-amyloid slow cognitive decline in Alzheimer's disease. Neuron 38, 547-554.
    • (2003) Neuron , vol.38 , pp. 547-554
    • Hock, C.1    Konietzko, U.2    Streffer, J.R.3
  • 89
    • 4143138471 scopus 로고    scopus 로고
    • In vivo effects of ApoE and clusterin on amyloid-beta metabolism and neuropathology
    • Holtzman D. M. (2004) In vivo effects of ApoE and clusterin on amyloid-beta metabolism and neuropathology. J. Mol. Neurosci. 23, 247-254.
    • (2004) J. Mol. Neurosci. , vol.23 , pp. 247-254
    • Holtzman, D.M.1
  • 91
    • 0034680781 scopus 로고    scopus 로고
    • Alternate aggregation pathways of the Alzheimer beta-amyloid peptide. An in vitro model of preamyloid
    • Huang T. H., Yang D. S., Fraser P. E. and Chakrabartty A. (2000a) Alternate aggregation pathways of the Alzheimer beta-amyloid peptide. An in vitro model of preamyloid. J. Biol. Chem. 275, 36 436-36 440.
    • (2000) J. Biol. Chem. , vol.275 , pp. 36436-36440
    • Huang, T.H.1    Yang, D.S.2    Fraser, P.E.3    Chakrabartty, A.4
  • 93
    • 0033382226 scopus 로고    scopus 로고
    • Identification of a Novel Aspartic Protease (Asp 2) as beta-Secretase
    • Hussain I., Powell D., Howlett D. R. et al. (1999) Identification of a Novel Aspartic Protease (Asp 2) as beta-Secretase. Mol. Cell Neurosci. 14, 419-427.
    • (1999) Mol. Cell Neurosci. , vol.14 , pp. 419-427
    • Hussain, I.1    Powell, D.2    Howlett, D.R.3
  • 94
    • 0034530634 scopus 로고    scopus 로고
    • Molecular genetics of chromosome 17 tauopathies
    • Hutton M. (2000) Molecular genetics of chromosome 17 tauopathies. Ann. N Y Acad. Sci. 920, 63-73.
    • (2000) Ann. N Y Acad. Sci. , vol.920 , pp. 63-73
    • Hutton, M.1
  • 95
    • 0032543684 scopus 로고    scopus 로고
    • Association of missense and 5′-splice-site mutations in tau with the inherited dementia FTDP-17
    • Hutton M., Lendon C. L., Rizzu P. et al. (1998) Association of missense and 5′-splice-site mutations in tau with the inherited dementia FTDP-17. Nature 393, 702-705.
    • (1998) Nature , vol.393 , pp. 702-705
    • Hutton, M.1    Lendon, C.L.2    Rizzu, P.3
  • 96
    • 0033969771 scopus 로고    scopus 로고
    • Muscle weakness, hyperactivity, and impairment in fear conditioning in tau-deficient mice
    • Ikegami S., Harada A. and Hirokawa N. (2000) Muscle weakness, hyperactivity, and impairment in fear conditioning in tau-deficient mice. Neurosci. Lett. 279, 129-132.
    • (2000) Neurosci. Lett. , vol.279 , pp. 129-132
    • Ikegami, S.1    Harada, A.2    Hirokawa, N.3
  • 97
    • 4344673143 scopus 로고    scopus 로고
    • Biomarkers of Alzheimer disease in plasma
    • Irizarry M. C. (2004) Biomarkers of Alzheimer disease in plasma. Neurorx 1, 226-234.
    • (2004) Neurorx , vol.1 , pp. 226-234
    • Irizarry, M.C.1
  • 99
    • 0033621739 scopus 로고    scopus 로고
    • Identification of the major Abeta1-42-degrading catabolic pathway in brain parenchyma: Suppression leads to biochemical and pathological deposition
    • Iwata N., Tsubuki S., Takaki Y. et al. (2000) Identification of the major Abeta1-42-degrading catabolic pathway in brain parenchyma: suppression leads to biochemical and pathological deposition. Nat. Med. 6, 143-150.
    • (2000) Nat. Med. , vol.6 , pp. 143-150
    • Iwata, N.1    Tsubuki, S.2    Takaki, Y.3
  • 100
    • 29644440011 scopus 로고    scopus 로고
    • Persistent amyloidosis following suppression of Abeta production in a transgenic model of Alzheimer disease
    • Jankowsky J. L., Slunt H. H., Gonzales V. et al. (2005) Persistent amyloidosis following suppression of Abeta production in a transgenic model of Alzheimer disease. PLoS Medical 2, e355.
    • (2005) PLoS Medical , vol.2
    • Jankowsky, J.L.1    Slunt, H.H.2    Gonzales, V.3
  • 101
    • 0027195933 scopus 로고
    • Seeding 'one dimensional crystallization' of amyloid: A pathogenic mechanism in Alzheimer's disease and Scrapie?
    • Jarrett J. T. and Lansbury P. T. Jr (1993) Seeding 'one dimensional crystallization' of amyloid: a pathogenic mechanism in Alzheimer's disease and Scrapie? Cell 73, 1055-1058.
    • (1993) Cell , vol.73 , pp. 1055-1058
    • Jarrett, J.T.1    Lansbury Jr., P.T.2
  • 102
    • 14744300176 scopus 로고    scopus 로고
    • Caspase-3-mediated cleavage of PHF-1 tau during apoptosis irrespective of excitotoxicity and oxidative stress: An implication to Alzheimer's disease
    • Kang H. J., Yoon W. J., Moon G. J., Kim D. Y., Sohn S., Kwon H. J. and Gwag B. J. (2005) Caspase-3-mediated cleavage of PHF-1 tau during apoptosis irrespective of excitotoxicity and oxidative stress: an implication to Alzheimer's disease. Neurobiol. Dis 18, 450-458.
    • (2005) Neurobiol. Dis. , vol.18 , pp. 450-458
    • Kang, H.J.1    Yoon, W.J.2    Moon, G.J.3    Kim, D.Y.4    Sohn, S.5    Kwon, H.J.6    Gwag, B.J.7
  • 103
    • 33644851265 scopus 로고    scopus 로고
    • Inducible expression of Tau repeat domain in cell models of tauopathy: Aggregation is toxic to cells but can be reversed by inhibitor drugs
    • Khlistunova I., Biernat J., Wang Y., Pickhardt M., von Bergen M., Gazova Z., Mandelkow E. and Mandelkow E. M. (2006) Inducible expression of Tau repeat domain in cell models of tauopathy: aggregation is toxic to cells but can be reversed by inhibitor drugs. J. Biol. Chem. 281, 1205-1214.
    • (2006) J. Biol. Chem. , vol.281 , pp. 1205-1214
    • Khlistunova, I.1    Biernat, J.2    Wang, Y.3    Pickhardt, M.4    Von Bergen, M.5    Gazova, Z.6    Mandelkow, E.7    Mandelkow, E.M.8
  • 107
    • 15944413832 scopus 로고    scopus 로고
    • The non-amyloidogenic pathway: Structure and function of alpha-secretases
    • Kojro E. and Fahrenholz F. (2005) The non-amyloidogenic pathway: structure and function of alpha-secretases. Subcell Biochem. 38, 105-127.
    • (2005) Subcell Biochem. , vol.38 , pp. 105-127
    • Kojro, E.1    Fahrenholz, F.2
  • 108
    • 0035826909 scopus 로고    scopus 로고
    • Low cholesterol stimulates the nonamyloidogenic pathway by its effect on the alpha-secretase ADAM 10
    • Kojro E., Gimpl G., Lammich S., Marz W. and Fahrenholz F. (2001) Low cholesterol stimulates the nonamyloidogenic pathway by its effect on the alpha-secretase ADAM 10. Proc. Natl Acad. Sci. U S A 98, 5815-5820.
    • (2001) Proc. Natl. Acad. Sci. U S A , vol.98 , pp. 5815-5820
    • Kojro, E.1    Gimpl, G.2    Lammich, S.3    Marz, W.4    Fahrenholz, F.5
  • 109
    • 30044438463 scopus 로고    scopus 로고
    • Lack of ABCA1 considerably decreases brain ApoE level and increases amyloid deposition in APP23 mice
    • Koldamova R., Staufenbiel M. and Lefterov I. (2005) Lack of ABCA1 considerably decreases brain ApoE level and increases amyloid deposition in APP23 mice. J. Biol. Chem. 280, 43 224-43 235.
    • (2005) J. Biol. Chem. , vol.280 , pp. 43224-43235
    • Koldamova, R.1    Staufenbiel, M.2    Lefterov, I.3
  • 110
    • 0030912611 scopus 로고    scopus 로고
    • Phorbol esters affect multiple steps in beta-amyloid precursor protein trafficking and amyloid beta-protein production
    • Koo E. H. (1997) Phorbol esters affect multiple steps in beta-amyloid precursor protein trafficking and amyloid beta-protein production. Mol. Med. 3, 204-211.
    • (1997) Mol. Med. , vol.3 , pp. 204-211
    • Koo, E.H.1
  • 111
    • 0033621165 scopus 로고    scopus 로고
    • Amyloid diseases: Abnormal protein aggregation in neurodegeneration
    • Koo E. H., Lansbury P. T. Jr and Kelly J. W. (1999) Amyloid diseases: abnormal protein aggregation in neurodegeneration. Proc. Natl Acad. Sci. U S A 96, 9989-9990.
    • (1999) Proc. Natl. Acad. Sci. U S A , vol.96 , pp. 9989-9990
    • Koo, E.H.1    Lansbury Jr., P.T.2    Kelly, J.W.3
  • 116
    • 27944450035 scopus 로고    scopus 로고
    • Inhibitors of TACE and Caspase-1 as anti-inflammatory drugs
    • Le G. T. and Abbenante G. (2005) Inhibitors of TACE and Caspase-1 as anti-inflammatory drugs. Curr. Med. Chem. 12, 2963-2977.
    • (2005) Curr. Med. Chem. , vol.12 , pp. 2963-2977
    • Le, G.T.1    Abbenante, G.2
  • 117
    • 33745449875 scopus 로고    scopus 로고
    • An inhibitor of tau hyperphosphorylation prevents severe motor impairments in tau transgenic mice
    • Le Corre S., Klafki H. W., Plesnila N. et al. (2006) An inhibitor of tau hyperphosphorylation prevents severe motor impairments in tau transgenic mice. Proc. Natl Acad. Sci. U S A 103, 9673-9678.
    • (2006) Proc. Natl. Acad. Sci. U S A , vol.103 , pp. 9673-9678
    • Le Corre, S.1    Klafki, H.W.2    Plesnila, N.3
  • 118
    • 0034573026 scopus 로고    scopus 로고
    • Brain plasmin enhances APP alpha-cleavage and Abeta degradation and is reduced in Alzheimer's disease brains
    • Ledesma M. D., Da Silva J. S., Crassaerts K., Delacourte A., De Strooper B. and Dotti C. G. (2000) Brain plasmin enhances APP alpha-cleavage and Abeta degradation and is reduced in Alzheimer's disease brains. EMBO Rep. 1, 530-535.
    • (2000) EMBO Rep. , vol.1 , pp. 530-535
    • Ledesma, M.D.1    Da Silva, J.S.2    Crassaerts, K.3    Delacourte, A.4    De Strooper, B.5    Dotti, C.G.6
  • 120
    • 0026941497 scopus 로고
    • The disordered neuronal cytoskeleton in Alzheimer's disease
    • Lee V. M.-Y. and Trojanowski J. Q. (1992) The disordered neuronal cytoskeleton in Alzheimer's disease. Current Opinion Neurobiol. 2, 653-656.
    • (1992) Current Opinion Neurobiol. , vol.2 , pp. 653-656
    • Lee, V.M.-Y.1    Trojanowski, J.Q.2
  • 121
    • 0034873177 scopus 로고    scopus 로고
    • Parkinson's disease: Clinical signs and symptoms, neural mechanisms, positron emission tomography, and therapeutic interventions
    • Leenders K. L. and Oertel W. H. (2001) Parkinson's disease: clinical signs and symptoms, neural mechanisms, positron emission tomography, and therapeutic interventions. Neural. Plast. 8, 99-110.
    • (2001) Neural. Plast. , vol.8 , pp. 99-110
    • Leenders, K.L.1    Oertel, W.H.2
  • 122
    • 0346101885 scopus 로고    scopus 로고
    • Enhanced proteolysis of beta-amyloid in APP transgenic mice prevents plaque formation, secondary pathology, and premature death
    • Leissring M. A., Farris W., Chang A. Y., Walsh D. M., Wu X., Sun X., Frosch M. P. and Selkoe D. J. (2003) Enhanced proteolysis of beta-amyloid in APP transgenic mice prevents plaque formation, secondary pathology, and premature death. Neuron 40, 1087-1093.
    • (2003) Neuron , vol.40 , pp. 1087-1093
    • Leissring, M.A.1    Farris, W.2    Chang, A.Y.3    Walsh, D.M.4    Wu, X.5    Sun, X.6    Frosch, M.P.7    Selkoe, D.J.8
  • 123
    • 0038661168 scopus 로고    scopus 로고
    • Neuroprotection and neurorescue against Abeta toxicity and PKC-dependent release of nonamyloidogenic soluble precursor protein by green tea polyphenol (-)-epigallocatechin-3-gallate
    • Levites Y., Amit T., Mandel S. and Youdim M. B. (2003) Neuroprotection and neurorescue against Abeta toxicity and PKC-dependent release of nonamyloidogenic soluble precursor protein by green tea polyphenol (-)-epigallocatechin-3-gallate. Faseb J. 17, 952-954.
    • (2003) Faseb J. , vol.17 , pp. 952-954
    • Levites, Y.1    Amit, T.2    Mandel, S.3    Youdim, M.B.4
  • 124
    • 33845639102 scopus 로고    scopus 로고
    • Insights into the Mechanisms of Action of Anti-Aβ Antibodies in Alzheimer's Disease Mouse Models
    • in press
    • Levites Y., Smithson L. A., Price R. W. et al. (2006) Insights into the Mechanisms of Action of Anti-Aβ Antibodies in Alzheimer's Disease Mouse Models. FASEB J. in press
    • (2006) FASEB J.
    • Levites, Y.1    Smithson, L.A.2    Price, R.W.3
  • 125
    • 17944382037 scopus 로고    scopus 로고
    • Enhanced neurofibrillary degeneration in transgenic mice expressing mutant tau and APP
    • Lewis J., Dickson D. W., Lin W. L. et al. (2001) Enhanced neurofibrillary degeneration in transgenic mice expressing mutant tau and APP. Science 293, 1487-1491.
    • (2001) Science , vol.293 , pp. 1487-1491
    • Lewis, J.1    Dickson, D.W.2    Lin, W.L.3
  • 126
    • 0034426011 scopus 로고    scopus 로고
    • Neurofibrillary tangles, amyotrophy and progressive motor disturbance in mice expressing mutant (P301L) tau protein
    • Lewis J., McGowan E., Rockwood J. et al. (2000) Neurofibrillary tangles, amyotrophy and progressive motor disturbance in mice expressing mutant (P301L) tau protein. Nat. Genet. 25, 402-405.
    • (2000) Nat. Genet. , vol.25 , pp. 402-405
    • Lewis, J.1    McGowan, E.2    Rockwood, J.3
  • 127
    • 0034621824 scopus 로고    scopus 로고
    • Photoactivated gamma-secretase inhibitors directed to the active site covalently label presenilin 1
    • Li Y. M., Xu M., Lai M. T. et al. (2000) Photoactivated gamma-secretase inhibitors directed to the active site covalently label presenilin 1. Nature 405, 689-694.
    • (2000) Nature , vol.405 , pp. 689-694
    • Li, Y.M.1    Xu, M.2    Lai, M.T.3
  • 128
    • 0035503597 scopus 로고    scopus 로고
    • The curry spice curcumin reduces oxidative damage and amyloid pathology in an Alzheimer transgenic mouse
    • Lim G. P., Chu T., Yang F., Beech W., Frautschy S. A. and Cole G. M. (2001) The curry spice curcumin reduces oxidative damage and amyloid pathology in an Alzheimer transgenic mouse. J. Neurosci. 21, 8370-8377.
    • (2001) J. Neurosci. , vol.21 , pp. 8370-8377
    • Lim, G.P.1    Chu, T.2    Yang, F.3    Beech, W.4    Frautschy, S.A.5    Cole, G.M.6
  • 129
    • 20844460621 scopus 로고    scopus 로고
    • The molecular basis of memantine action in Alzheimer's disease and other neurologic disorders: Low-affinity, uncompetitive antagonism
    • Lipton S. A. (2005) The molecular basis of memantine action in Alzheimer's disease and other neurologic disorders: low-affinity, uncompetitive antagonism. Curr. Alzheimer Res. 2, 155-165.
    • (2005) Curr. Alzheimer Res. , vol.2 , pp. 155-165
    • Lipton, S.A.1
  • 131
    • 0033600242 scopus 로고    scopus 로고
    • The prolyl isomerase PIN1 restores the function of Alzheimer-associated phosphorylated tau protein
    • Lu P. J., Wulf G., Zhou X. Z., Davies P. and Lu K. P. (1999) The prolyl isomerase PIN1 restores the function of Alzheimer-associated phosphorylated tau protein. Nature 399, 784-788.
    • (1999) Nature , vol.399 , pp. 784-788
    • Lu, P.J.1    Wulf, G.2    Zhou, X.Z.3    Davies, P.4    Lu, K.P.5
  • 132
    • 0035116273 scopus 로고    scopus 로고
    • Mice deficient in BACE1, the Alzheimer's beta-secretase, have normal phenotype and abolished beta-amyloid generation
    • Luo Y., Bolon B., Kahn S. et al. (2001) Mice deficient in BACE1, the Alzheimer's beta-secretase, have normal phenotype and abolished beta-amyloid generation. Nat. Neurosci. 4, 231-232.
    • (2001) Nat. Neurosci. , vol.4 , pp. 231-232
    • Luo, Y.1    Bolon, B.2    Kahn, S.3
  • 133
    • 33646938005 scopus 로고    scopus 로고
    • Short amyloid-beta (Abeta) immunogens reduce cerebral Abeta load and learning deficits in an Alzheimer's disease mouse model in the absence of an Abeta-specific cellular immune response
    • Maier M., Seabrook T. J., Lazo N. D., Jiang L., Das P., Janus C. and Lemere C. A. (2006) Short amyloid-beta (Abeta) immunogens reduce cerebral Abeta load and learning deficits in an Alzheimer's disease mouse model in the absence of an Abeta-specific cellular immune response. J. Neurosci. 26, 4717-4728.
    • (2006) J. Neurosci. , vol.26 , pp. 4717-4728
    • Maier, M.1    Seabrook, T.J.2    Lazo, N.D.3    Jiang, L.4    Das, P.5    Janus, C.6    Lemere, C.A.7
  • 134
    • 25144520056 scopus 로고    scopus 로고
    • Modulation of the humoral and cellular immune response in Abeta immunotherapy by the adjuvants monophosphoryl lipid a (MPL), cholera toxin B subunit (CTB) and E. coli enterotoxin LT (R192G)
    • Maier M., Seabrook T. J. and Lemere C. A. (2005) Modulation of the humoral and cellular immune response in Abeta immunotherapy by the adjuvants monophosphoryl lipid A (MPL), cholera toxin B subunit (CTB) and E. coli enterotoxin LT (R192G). Vaccine 23, 5149-5159.
    • (2005) Vaccine , vol.23 , pp. 5149-5159
    • Maier, M.1    Seabrook, T.J.2    Lemere, C.A.3
  • 139
    • 0028921915 scopus 로고
    • Characterization of apolipoprotein J-Alzheimer's a beta interaction
    • Matsubara E., Frangione B. and Ghiso J. (1995) Characterization of apolipoprotein J-Alzheimer's A beta interaction. J. Biol. Chem. 270, 7563-7567.
    • (1995) J. Biol. Chem. , vol.270 , pp. 7563-7567
    • Matsubara, E.1    Frangione, B.2    Ghiso, J.3
  • 140
    • 0037223101 scopus 로고    scopus 로고
    • Novel therapeutic approach for the treatment of Alzheimer's disease by peripheral administration of agents with an affinity to beta-amyloid
    • Matsuoka Y., Saito M., LaFrancois J. et al. (2003) Novel therapeutic approach for the treatment of Alzheimer's disease by peripheral administration of agents with an affinity to beta-amyloid. J. Neurosci. 23, 29-33.
    • (2003) J. Neurosci. , vol.23 , pp. 29-33
    • Matsuoka, Y.1    Saito, M.2    LaFrancois, J.3
  • 141
    • 0029811901 scopus 로고    scopus 로고
    • Arthritis and anti-inflammatory agents as possible protective factors for Alzheimer's disease: A review of 17 epidemiologic studies
    • [see comments]
    • McGeer P. L., Schulzer M. and McGeer E. G. (1996) Arthritis and anti-inflammatory agents as possible protective factors for Alzheimer's disease: a review of 17 epidemiologic studies [see comments]. Neurology 47, 425-432.
    • (1996) Neurology , vol.47 , pp. 425-432
    • McGeer, P.L.1    Schulzer, M.2    McGeer, E.G.3
  • 142
    • 0033572813 scopus 로고    scopus 로고
    • Interactions of Alzheimer amyloid-beta peptides with glycosaminoglycans effects on fibril nucleation and growth
    • McLaurin J., Franklin T., Zhang X., Deng J. and Fraser P. E. (1999) Interactions of Alzheimer amyloid-beta peptides with glycosaminoglycans effects on fibril nucleation and growth. Eur. J. Biochem. 266, 1101-1110.
    • (1999) Eur. J. Biochem. , vol.266 , pp. 1101-1110
    • McLaurin, J.1    Franklin, T.2    Zhang, X.3    Deng, J.4    Fraser, P.E.5
  • 143
    • 0034674785 scopus 로고    scopus 로고
    • Inositol stereoisomers stabilize an oligomeric aggregate of Alzheimer amyloid beta peptide and inhibit abeta-induced toxicity
    • McLaurin J., Golomb R., Jurewicz A., Antel J. P. and Fraser P. E. (2000) Inositol stereoisomers stabilize an oligomeric aggregate of Alzheimer amyloid beta peptide and inhibit abeta-induced toxicity. J. Biol. Chem. 275, 18 495-18 502.
    • (2000) J. Biol. Chem. , vol.275 , pp. 18495-18502
    • McLaurin, J.1    Golomb, R.2    Jurewicz, A.3    Antel, J.P.4    Fraser, P.E.5
  • 144
    • 33745922350 scopus 로고    scopus 로고
    • Cyclohexanehexol inhibitors of Abeta aggregation prevent and reverse Alzheimer phenotype in a mouse model
    • McLaurin J., Kierstead M. E., Brown M. E. et al. (2006) Cyclohexanehexol inhibitors of Abeta aggregation prevent and reverse Alzheimer phenotype in a mouse model. Nat. Med. 12, 801-808.
    • (2006) Nat. Med. , vol.12 , pp. 801-808
    • McLaurin, J.1    Kierstead, M.E.2    Brown, M.E.3
  • 145
    • 1642359902 scopus 로고    scopus 로고
    • Anti-amyloid activity of neprilysin in plaque-bearing mouse models of Alzheimer's disease
    • Mohajeri M. H., Kuehnle K., Li H., Poirier R., Tracy J. and Nitsch R. M. (2004) Anti-amyloid activity of neprilysin in plaque-bearing mouse models of Alzheimer's disease. FEBS Lett. 562, 16-21.
    • (2004) FEBS Lett. , vol.562 , pp. 16-21
    • Mohajeri, M.H.1    Kuehnle, K.2    Li, H.3    Poirier, R.4    Tracy, J.5    Nitsch, R.M.6
  • 146
    • 33645517069 scopus 로고    scopus 로고
    • Abeta-induced meningoencephalitis is IFN-gamma-dependent and is associated with T cell-dependent clearance of Abeta in a mouse model of Alzheimer's disease
    • Monsonego A., Imitola J., Petrovic S., Zota V., Nemirovsky A., Baron R., Fisher Y., Owens T. and Weiner H. L. (2006) Abeta-induced meningoencephalitis is IFN-gamma-dependent and is associated with T cell-dependent clearance of Abeta in a mouse model of Alzheimer's disease. Proc. Natl Acad. Sci. U S A 103, 5048-5053.
    • (2006) Proc. Natl. Acad. Sci. U S A , vol.103 , pp. 5048-5053
    • Monsonego, A.1    Imitola, J.2    Petrovic, S.3    Zota, V.4    Nemirovsky, A.5    Baron, R.6    Fisher, Y.7    Owens, T.8    Weiner, H.L.9
  • 147
    • 0033011181 scopus 로고    scopus 로고
    • Accelerated filament formation from tau protein with specific FTDP-17 missense mutations
    • Nacharaju P., Lewis J., Easson C., Yen S., Hackett J., Hutton M. and Yen S. H. (1999) Accelerated filament formation from tau protein with specific FTDP-17 missense mutations. FEBS Lett. 447, 195-199.
    • (1999) FEBS Lett. , vol.447 , pp. 195-199
    • Nacharaju, P.1    Lewis, J.2    Easson, C.3    Yen, S.4    Hackett, J.5    Hutton, M.6    Yen, S.H.7
  • 148
    • 28844481487 scopus 로고    scopus 로고
    • Chronic lithium treatment decreases tau lesions by promoting ubiquitination in a mouse model of tauopathies
    • Nakashima H., Ishihara T., Suguimoto P. et al. (2005) Chronic lithium treatment decreases tau lesions by promoting ubiquitination in a mouse model of tauopathies. Acta Neuropathol (Berl) 110, 547-556.
    • (2005) Acta Neuropathol (Berl) , vol.110 , pp. 547-556
    • Nakashima, H.1    Ishihara, T.2    Suguimoto, P.3
  • 149
    • 0025864064 scopus 로고
    • High affinity interactions between the Alzheimer's beta-amyloid precursor proteins and the basement membrane form of heparan sulfate proteoglycan
    • Narindrasorasak S., Lowery D., Gonzalez-DeWhitt P., Poorman R. A., Greenberg B. and Kisilevsky R. (1991) High affinity interactions between the Alzheimer's beta-amyloid precursor proteins and the basement membrane form of heparan sulfate proteoglycan. J. Biol. Chem. 266, 12 878-12 883.
    • (1991) J. Biol. Chem. , vol.266 , pp. 12878-12883
    • Narindrasorasak, S.1    Lowery, D.2    Gonzalez-DeWhitt, P.3    Poorman, R.A.4    Greenberg, B.5    Kisilevsky, R.6
  • 152
    • 0037393454 scopus 로고    scopus 로고
    • Neuropathology of human Alzheimer disease after immunization with amyloid-beta peptide: A case report
    • Nicoll J. A., Wilkinson D., Holmes C., Steart P., Markham H. and Weller R. O. (2003) Neuropathology of human Alzheimer disease after immunization with amyloid-beta peptide: a case report. Nat. Med. 9, 448-452.
    • (2003) Nat. Med. , vol.9 , pp. 448-452
    • Nicoll, J.A.1    Wilkinson, D.2    Holmes, C.3    Steart, P.4    Markham, H.5    Weller, R.O.6
  • 153
    • 0035282790 scopus 로고    scopus 로고
    • Alpha-1-antichymotrypsin promotes beta-sheet amyloid plaque deposition in a transgenic mouse model of Alzheimer's disease
    • Nilsson L. N., Bales K. R., DiCarlo G., Gordon M. N., Morgan D., Paul S. M. and Potter H. (2001) Alpha-1-antichymotrypsin promotes beta-sheet amyloid plaque deposition in a transgenic mouse model of Alzheimer's disease. J. Neurosci. 21, 1444-1451.
    • (2001) J. Neurosci. , vol.21 , pp. 1444-1451
    • Nilsson, L.N.1    Bales, K.R.2    DiCarlo, G.3    Gordon, M.N.4    Morgan, D.5    Paul, S.M.6    Potter, H.7
  • 154
    • 0030497927 scopus 로고    scopus 로고
    • From acetylcholine to amyloid: Neurotransmitters and the pathology of Alzheimer's disease
    • Nitsch R. M. (1996) From acetylcholine to amyloid: neurotransmitters and the pathology of Alzheimer's disease. Neurodegeneration 5, 477-482.
    • (1996) Neurodegeneration , vol.5 , pp. 477-482
    • Nitsch, R.M.1
  • 155
    • 0038689162 scopus 로고    scopus 로고
    • Cdk5 is a key factor in tau aggregation and tangle formation in vivo
    • Noble W., Olm V., Takata K. et al. (2003) Cdk5 is a key factor in tau aggregation and tangle formation in vivo. Neuron 38, 555-565.
    • (2003) Neuron , vol.38 , pp. 555-565
    • Noble, W.1    Olm, V.2    Takata, K.3
  • 156
    • 21044449225 scopus 로고    scopus 로고
    • Inhibition of glycogen synthase kinase-3 by lithium correlates with reduced tauopathy and degeneration in vivo
    • Noble W., Planel E., Zehr C. et al. (2005) Inhibition of glycogen synthase kinase-3 by lithium correlates with reduced tauopathy and degeneration in vivo. Proc. Natl Acad. Sci. U S A 102, 6990-6995.
    • (2005) Proc. Natl. Acad. Sci. U S A , vol.102 , pp. 6990-6995
    • Noble, W.1    Planel, E.2    Zehr, C.3
  • 157
    • 33745209915 scopus 로고    scopus 로고
    • ADAM10 activation is required for green tea (-)-epigallocatechin-3- gallate-induced alpha-secretase cleavage of amyloid precursor protein
    • Obregon D. F., Rezai-Zadeh K., Bai Y. et al. (2006) ADAM10 activation is required for green tea (-)-epigallocatechin-3-gallate-induced alpha-secretase cleavage of amyloid precursor protein. J. Biol. Chem. 281, 16 419-16 427.
    • (2006) J. Biol. Chem. , vol.281 , pp. 16419-16427
    • Obregon, D.F.1    Rezai-Zadeh, K.2    Bai, Y.3
  • 158
    • 0028828044 scopus 로고
    • Clusterin (apoJ) alters the aggregation of amyloid beta-peptide (A beta
    • Oda T., Wals P., Osterburg H. H. et al. (1995) Clusterin (apoJ) alters the aggregation of amyloid beta-peptide (A beta 1-42) and forms slowly sedimenting A beta complexes that cause oxidative stress. Exp. Neurol. 136, 22-31.
    • (1995) Exp. Neurol. , vol.136 , pp. 22-31
    • Oda, T.1    Wals, P.2    Osterburg, H.H.3
  • 159
    • 10744230547 scopus 로고    scopus 로고
    • Subacute meningoencephalitis in a subset of patients with AD after Abeta42 immunization
    • Orgogozo J. M., Gilman S., Dartigues J. F. et al. (2003) Subacute meningoencephalitis in a subset of patients with AD after Abeta42 immunization. Neurology 61, 46-54.
    • (2003) Neurology , vol.61 , pp. 46-54
    • Orgogozo, J.M.1    Gilman, S.2    Dartigues, J.F.3
  • 160
    • 33645300736 scopus 로고    scopus 로고
    • The prolyl isomerase PIN1 regulates amyloid precursor protein processing and amyloid-beta production
    • Pastorino L., Sun A., Lu P. J. et al. (2006) The prolyl isomerase PIN1 regulates amyloid precursor protein processing and amyloid-beta production. Nature 440, 528-534.
    • (2006) Nature , vol.440 , pp. 528-534
    • Pastorino, L.1    Sun, A.2    Lu, P.J.3
  • 162
    • 0036615884 scopus 로고    scopus 로고
    • Reduction of amyloid load and cerebral damage in a transgenic mouse model of Alzheimer's disease by treatment with a beta-sheet breaker peptide
    • Permanne B., Adessi C., Saborio G. P. et al. (2002) Reduction of amyloid load and cerebral damage in a transgenic mouse model of Alzheimer's disease by treatment with a beta-sheet breaker peptide. Faseb J. 16, 860-862.
    • (2002) Faseb J. , vol.16 , pp. 860-862
    • Permanne, B.1    Adessi, C.2    Saborio, G.P.3
  • 163
    • 11144356089 scopus 로고    scopus 로고
    • CHIP and Hsp70 regulate tau ubiquitination, degradation and aggregation
    • Petrucelli L., Dickson D., Kehoe K. et al. (2004) CHIP and Hsp70 regulate tau ubiquitination, degradation and aggregation. Hum. Mol. Genet. 13, 703-714.
    • (2004) Hum. Mol. Genet. , vol.13 , pp. 703-714
    • Petrucelli, L.1    Dickson, D.2    Kehoe, K.3
  • 165
    • 0038187674 scopus 로고    scopus 로고
    • GSK-3alpha regulates production of Alzheimer's disease amyloid-beta peptides
    • Phiel C. J., Wilson C. A., Lee V. M. and Klein P. S. (2003) GSK-3alpha regulates production of Alzheimer's disease amyloid-beta peptides. Nature 423, 435-439.
    • (2003) Nature , vol.423 , pp. 435-439
    • Phiel, C.J.1    Wilson, C.A.2    Lee, V.M.3    Klein, P.S.4
  • 166
    • 33748752882 scopus 로고    scopus 로고
    • The roles of cyclin-dependent kinase 5 and glycogen synthase kinase 3 in tau hyperphosphorylation
    • Plattner F., Angelo M. and Giese K. P. (2006) The roles of cyclin-dependent kinase 5 and glycogen synthase kinase 3 in tau hyperphosphorylation. J. Biol. Chem. 281, 25 457-25 465.
    • (2006) J. Biol. Chem. , vol.281 , pp. 25457-25465
    • Plattner, F.1    Angelo, M.2    Giese, K.P.3
  • 167
    • 85047690140 scopus 로고    scopus 로고
    • A disintegrin-metalloproteinase prevents amyloid plaque formation and hippocampal defects in an Alzheimer disease mouse model
    • Postina R., Schroeder A., Dewachter I. et al. (2004) A disintegrin-metalloproteinase prevents amyloid plaque formation and hippocampal defects in an Alzheimer disease mouse model. J. Clin. Invest. 113, 1456-1464.
    • (2004) J. Clin. Invest. , vol.113 , pp. 1456-1464
    • Postina, R.1    Schroeder, A.2    Dewachter, I.3
  • 168
    • 0035696320 scopus 로고    scopus 로고
    • The inflammation-induced pathological chaperones ACT and apo-E are necessary catalysts of Alzheimer amyloid formation
    • Potter H., Wefes I. M. and Nilsson L. N. (2001) The inflammation-induced pathological chaperones ACT and apo-E are necessary catalysts of Alzheimer amyloid formation. Neurobiol. Aging 22, 923-930.
    • (2001) Neurobiol. Aging , vol.22 , pp. 923-930
    • Potter, H.1    Wefes, I.M.2    Nilsson, L.N.3
  • 169
    • 0031921466 scopus 로고    scopus 로고
    • Mutant genes in familial Alzheimer's disease and transgenic models
    • Price D. L. and Sisodia S. S. (1998) Mutant genes in familial Alzheimer's disease and transgenic models. Annu. Rev. Neuroscience 21, 479-505.
    • (1998) Annu. Rev. Neuroscience , vol.21 , pp. 479-505
    • Price, D.L.1    Sisodia, S.S.2
  • 171
    • 0000398342 scopus 로고    scopus 로고
    • Insulin-degrading enzyme regulates extracellular levels of amyloid beta- Protein by degradation
    • Qiu W. Q., Walsh D. M. Ye Z. et al. (1998) Insulin-degrading enzyme regulates extracellular levels of amyloid beta- protein by degradation. J. Biol. Chem. 273, 32 730-32 738.
    • (1998) J. Biol. Chem. , vol.273 , pp. 32730-32738
    • Qiu, W.Q.1    Walsh, D.M.2    Ye, Z.3
  • 172
    • 19944431509 scopus 로고    scopus 로고
    • Exacerbation of cerebral amyloid angiopathy-associated microhemorrhage in amyloid precursor protein transgenic mice by immunotherapy is dependent on antibody recognition of deposited forms of amyloid beta
    • Racke M. M., Boone L. I., Hepburn D. L. et al. (2005) Exacerbation of cerebral amyloid angiopathy-associated microhemorrhage in amyloid precursor protein transgenic mice by immunotherapy is dependent on antibody recognition of deposited forms of amyloid beta. J. Neurosci. 25, 629-636.
    • (2005) J. Neurosci. , vol.25 , pp. 629-636
    • Racke, M.M.1    Boone, L.I.2    Hepburn, D.L.3
  • 173
    • 4143055668 scopus 로고    scopus 로고
    • Apolipoprotein E4 as a target for developing new therapeutics for Alzheimer's disease
    • Refolo L. M. and Fillit H. M. (2004) Apolipoprotein E4 as a target for developing new therapeutics for Alzheimer's disease. J. Mol. Neurosci. 23, 151-155.
    • (2004) J. Mol. Neurosci. , vol.23 , pp. 151-155
    • Refolo, L.M.1    Fillit, H.M.2
  • 174
    • 0035160066 scopus 로고    scopus 로고
    • A cholesterol-lowering drug reduces beta-amyloid pathology in a transgenic mouse model of Alzheimer's disease
    • Refolo L. M., Pappolla M. A., LaFrancois J. et al. (2001) A cholesterol-lowering drug reduces beta-amyloid pathology in a transgenic mouse model of Alzheimer's disease. Neurobiol. Dis. 8, 890-899.
    • (2001) Neurobiol. Dis. , vol.8 , pp. 890-899
    • Refolo, L.M.1    Pappolla, M.A.2    LaFrancois, J.3
  • 175
    • 25444500410 scopus 로고    scopus 로고
    • Green tea epigallocatechin-3-gallate (EGCG) modulates amyloid precursor protein cleavage and reduces cerebral amyloidosis in Alzheimer transgenic mice
    • Rezai-Zadeh K., Shytle D., Sun N. et al. (2005) Green tea epigallocatechin-3-gallate (EGCG) modulates amyloid precursor protein cleavage and reduces cerebral amyloidosis in Alzheimer transgenic mice. J. Neurosci. 25, 8807-8814.
    • (2005) J. Neurosci. , vol.25 , pp. 8807-8814
    • Rezai-Zadeh, K.1    Shytle, D.2    Sun, N.3
  • 178
    • 0345059236 scopus 로고    scopus 로고
    • The neuroprotective effects of Cerebrolysin in a transgenic model of Alzheimer's disease are associated with improved behavioral performance
    • Rockenstein E., Adame A., Mante M., Moessler H., Windisch M. and Masliah E. (2003) The neuroprotective effects of Cerebrolysin in a transgenic model of Alzheimer's disease are associated with improved behavioral performance. J. Neural. Transm. 110, 1313-1327.
    • (2003) J. Neural. Transm. , vol.110 , pp. 1313-1327
    • Rockenstein, E.1    Adame, A.2    Mante, M.3    Moessler, H.4    Windisch, M.5    Masliah, E.6
  • 179
    • 27744459938 scopus 로고    scopus 로고
    • Translational research on the way to effective therapy for Alzheimer disease
    • Rosenberg R. N. (2005) Translational research on the way to effective therapy for Alzheimer disease. Arch. General Psychiatry 62, 1186-1192.
    • (2005) Arch. General Psychiatry , vol.62 , pp. 1186-1192
    • Rosenberg, R.N.1
  • 180
    • 0033802581 scopus 로고    scopus 로고
    • Constitutive overactivation of protein kinase C in guinea pig brain increases alpha-secretory APP processing without decreasing beta-amyloid generation
    • Rossner S., Beck M., Stahl T., Mendla K., Schliebs R. and Bigl V. (2000) Constitutive overactivation of protein kinase C in guinea pig brain increases alpha-secretory APP processing without decreasing beta-amyloid generation. Eur. J. Neurosci. 12, 3191-3200.
    • (2000) Eur. J. Neurosci. , vol.12 , pp. 3191-3200
    • Rossner, S.1    Beck, M.2    Stahl, T.3    Mendla, K.4    Schliebs, R.5    Bigl, V.6
  • 181
    • 4344659648 scopus 로고    scopus 로고
    • A synthetic peptide blocking the apolipoprotein E/beta-amyloid binding mitigates beta-amyloid toxicity and fibril formation in vitro and reduces beta-amyloid plaques in transgenic mice
    • Sadowski M., Pankiewicz J., Scholtzova H. et al. (2004) A synthetic peptide blocking the apolipoprotein E/beta-amyloid binding mitigates beta-amyloid toxicity and fibril formation in vitro and reduces beta-amyloid plaques in transgenic mice. Am. J. Pathol. 165, 937-948.
    • (2004) Am. J. Pathol. , vol.165 , pp. 937-948
    • Sadowski, M.1    Pankiewicz, J.2    Scholtzova, H.3
  • 183
    • 22344438508 scopus 로고    scopus 로고
    • Tau suppression in a neurodegenerative mouse model improves memory function
    • Santacruz K., Lewis J., Spires T. et al. (2005) Tau suppression in a neurodegenerative mouse model improves memory function. Science 309, 476-481.
    • (2005) Science , vol.309 , pp. 476-481
    • Santacruz, K.1    Lewis, J.2    Spires, T.3
  • 184
    • 0242609178 scopus 로고    scopus 로고
    • Nonsteroidal anti-inflammatory drugs and peroxisome proliferator- activated receptor-gamma agonists modulate immunostimulated processing of amyloid precursor protein through regulation of beta-secretase
    • Sastre M., Dewachter I., Landreth G. E., Willson T. M., Klockgether T., van Leuven F. and Heneka M. T. (2003) Nonsteroidal anti-inflammatory drugs and peroxisome proliferator-activated receptor-gamma agonists modulate immunostimulated processing of amyloid precursor protein through regulation of beta-secretase. J. Neurosci. 23, 9796-9804.
    • (2003) J. Neurosci. , vol.23 , pp. 9796-9804
    • Sastre, M.1    Dewachter, I.2    Landreth, G.E.3    Willson, T.M.4    Klockgether, T.5    Van Leuven, F.6    Heneka, M.T.7
  • 185
    • 0035955604 scopus 로고    scopus 로고
    • Murine notch homologs (n1-4) undergo presenilin-dependent proteolysis
    • Saxena M. T., Schroeter E. H., Mumm J. S. and Kopan R. (2001) Murine notch homologs (n1-4) undergo presenilin-dependent proteolysis. J. Biol. Chem. 276, 40 268-40 273.
    • (2001) J. Biol. Chem. , vol.276 , pp. 40268-40273
    • Saxena, M.T.1    Schroeter, E.H.2    Mumm, J.S.3    Kopan, R.4
  • 186
    • 0036780877 scopus 로고    scopus 로고
    • Opinion: Amyloid-beta immunotherapy for Alzheimer's disease: The end of the beginning
    • Schenk D. (2002) Opinion: Amyloid-beta immunotherapy for Alzheimer's disease: the end of the beginning. Nat Rev. Neurosci. 3, 824-828.
    • (2002) Nat Rev. Neurosci. , vol.3 , pp. 824-828
    • Schenk, D.1
  • 187
    • 0033536163 scopus 로고    scopus 로고
    • Immunization with amyloid-beta attenuates Alzheimer-disease-like pathology in the PDAPP mouse
    • Schenk D., Barbour R., Dunn W. et al. (1999) Immunization with amyloid-beta attenuates Alzheimer-disease-like pathology in the PDAPP mouse. Nature 400, 173-177.
    • (1999) Nature , vol.400 , pp. 173-177
    • Schenk, D.1    Barbour, R.2    Dunn, W.3
  • 189
    • 0034602419 scopus 로고    scopus 로고
    • Presenilin-1 and - 2 are molecular targets for gamma-secretase inhibitors
    • [In Process Citation]
    • Seiffert D., Bradley J. D., Rominger C. M. et al. (2000) Presenilin-1 and - 2 are molecular targets for gamma-secretase inhibitors [In Process Citation]. J. Biol. Chem 275, 34 086-34 091.
    • (2000) J. Biol. Chem , vol.275 , pp. 34086-34091
    • Seiffert, D.1    Bradley, J.D.2    Rominger, C.M.3
  • 190
    • 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
  • 191
    • 0041355557 scopus 로고    scopus 로고
    • Notch and Presenilin: Regulated intramembrane proteolysis links development and degeneration
    • Selkoe D. and Kopan R. (2003) Notch and Presenilin: regulated intramembrane proteolysis links development and degeneration. Annu. Rev. Neurosci. 26, 565-597.
    • (2003) Annu. Rev. Neurosci. , vol.26 , pp. 565-597
    • Selkoe, D.1    Kopan, R.2
  • 192
    • 1042266624 scopus 로고    scopus 로고
    • CHIP-Hsc70 complex ubiquitinates phosphorylated tau and enhances cell survival
    • Shimura H., Schwartz D., Gygi S. P. and Kosik K. S. (2004) CHIP-Hsc70 complex ubiquitinates phosphorylated tau and enhances cell survival. J. Biol. Chem. 279, 4869-4876.
    • (2004) J. Biol. Chem. , vol.279 , pp. 4869-4876
    • Shimura, H.1    Schwartz, D.2    Gygi, S.P.3    Kosik, K.S.4
  • 193
    • 0035877747 scopus 로고    scopus 로고
    • Neprilysin degrades both amyloid beta peptides 1-40 and 1-42 most rapidly and efficiently among thiorphan- and phosphoramidon-sensitive endopeptidases
    • Shirotani K., Tsubuki S., Iwata N. et al. (2001) Neprilysin degrades both amyloid beta peptides 1-40 and 1-42 most rapidly and efficiently among thiorphan- and phosphoramidon-sensitive endopeptidases. J. Biol. Chem. 276, 21 895-21 901.
    • (2001) J. Biol. Chem. , vol.276 , pp. 21895-21901
    • Shirotani, K.1    Tsubuki, S.2    Iwata, N.3
  • 194
    • 21544458621 scopus 로고    scopus 로고
    • Safety, tolerability, and changes in amyloid beta concentrations after administration of a gamma-secretase inhibitor in volunteers
    • Siemers E., Skinner M., Dean R. A., Gonzales C., Satterwhite J., Farlow M., Ness D. and May P. C. (2005) Safety, tolerability, and changes in amyloid beta concentrations after administration of a gamma-secretase inhibitor in volunteers. Clin. Neuropharmacol. 28, 126-132.
    • (2005) Clin. Neuropharmacol. , vol.28 , pp. 126-132
    • Siemers, E.1    Skinner, M.2    Dean, R.A.3    Gonzales, C.4    Satterwhite, J.5    Farlow, M.6    Ness, D.7    May, P.C.8
  • 197
    • 0033518251 scopus 로고    scopus 로고
    • Purification and cloning of amyloid precursor protein beta-secretase from human brain
    • [In Process Citation]
    • Sinha S., Anderson J. P., Barbour R. et al. (1999) Purification and cloning of amyloid precursor protein beta-secretase from human brain [In Process Citation]. Nature 402, 537-540.
    • (1999) Nature , vol.402 , pp. 537-540
    • Sinha, S.1    Anderson, J.P.2    Barbour, R.3
  • 198
    • 0025373508 scopus 로고
    • Evidence that β-amyloid protein in Alzheimer's disease is not derived by normal processing
    • Sisodia S. S., Koo E. H., Beyreuther K., Unterbeck A. and Price D. L. (1990) Evidence that β-amyloid protein in Alzheimer's disease is not derived by normal processing. Science 248, 492-495.
    • (1990) Science , vol.248 , pp. 492-495
    • Sisodia, S.S.1    Koo, E.H.2    Beyreuther, K.3    Unterbeck, A.4    Price, D.L.5
  • 199
    • 0034723418 scopus 로고    scopus 로고
    • Protein kinase C-dependent alpha-secretase competes with beta-secretase for cleavage of amyloid-beta precursor protein in the trans-golgi network
    • Skovronsky D. M., Moore D. B., Milla M. E., Doms R. W. and Lee V. M. (2000) Protein kinase C-dependent alpha-secretase competes with beta-secretase for cleavage of amyloid-beta precursor protein in the trans-golgi network. J. Biol. Chem. 275, 2568-2575.
    • (2000) J. Biol. Chem. , vol.275 , pp. 2568-2575
    • Skovronsky, D.M.1    Moore, D.B.2    Milla, M.E.3    Doms, R.W.4    Lee, V.M.5
  • 201
    • 0028950856 scopus 로고
    • Apolipoprotein e type 4 allele and cerebral glucose metabolism in relatives at risk for familial Alzheimer disease
    • Small G. W., Mazziotta J. C., Collins M. T. et al. (1995) Apolipoprotein E type 4 allele and cerebral glucose metabolism in relatives at risk for familial Alzheimer disease. Jama 273, 942-947.
    • (1995) Jama , vol.273 , pp. 942-947
    • Small, G.W.1    Mazziotta, J.C.2    Collins, M.T.3
  • 202
    • 0035433962 scopus 로고    scopus 로고
    • Alzheimer's disease and Abeta toxicity: From top to bottom
    • Small D. H., Mok S. S. and Bornstein J. C. (2001) Alzheimer's disease and Abeta toxicity: from top to bottom. Nat. Rev. Neurosci. 2, 595-598.
    • (2001) Nat. Rev. Neurosci. , vol.2 , pp. 595-598
    • Small, D.H.1    Mok, S.S.2    Bornstein, J.C.3
  • 203
    • 0028082136 scopus 로고
    • An important role of heparan sulfate proteoglycan (Perlecan) in a model system for the deposition and persistence of fibrillar a beta-amyloid in rat brain
    • Snow A. D., Sekiguchi R., Nochlin D., Fraser P., Kimata K., Mizutani A., Arai M., Schreier W. A. and Morgan D. G. (1994) An important role of heparan sulfate proteoglycan (Perlecan) in a model system for the deposition and persistence of fibrillar A beta-amyloid in rat brain. Neuron 12, 219-234.
    • (1994) Neuron , vol.12 , pp. 219-234
    • Snow, A.D.1    Sekiguchi, R.2    Nochlin, D.3    Fraser, P.4    Kimata, K.5    Mizutani, A.6    Arai, M.7    Schreier, W.A.8    Morgan, D.G.9
  • 204
    • 15944401392 scopus 로고    scopus 로고
    • Amyloid inhibitors and beta-sheet breakers
    • Soto C. and Estrada L. (2005) Amyloid inhibitors and beta-sheet breakers. Subcell Biochem. 38, 351-364.
    • (2005) Subcell Biochem. , vol.38 , pp. 351-364
    • Soto, C.1    Estrada, L.2
  • 205
    • 22144453835 scopus 로고    scopus 로고
    • Atorvastatin therapy lowers circulating cholesterol but not free radical activity in advance of identifiable clinical benefit in the treatment of mild-to-moderate AD
    • Sparks D. L., Sabbagh M. N., Connor D. J. et al. (2005) Atorvastatin therapy lowers circulating cholesterol but not free radical activity in advance of identifiable clinical benefit in the treatment of mild-to-moderate AD. Curr. Alzheimer Res. 2, 343-353.
    • (2005) Curr. Alzheimer Res. , vol.2 , pp. 343-353
    • Sparks, D.L.1    Sabbagh, M.N.2    Connor, D.J.3
  • 207
    • 0030897133 scopus 로고    scopus 로고
    • Risk of Alzheimer's disease and duration of NSAID use
    • [see comments]
    • Stewart W. F., Kawas C., Corrada M. and Metter E. J. (1997) Risk of Alzheimer's disease and duration of NSAID use [see comments]. Neurology 48, 626-632.
    • (1997) Neurology , vol.48 , pp. 626-632
    • Stewart, W.F.1    Kawas, C.2    Corrada, M.3    Metter, E.J.4
  • 209
    • 0034530036 scopus 로고    scopus 로고
    • Biochemical identification of the neutral endopeptidase family member responsible for the catabolism of amyloid beta peptide in the brain
    • Takaki Y., Iwata N., Tsubuki S. et al. (2000) Biochemical identification of the neutral endopeptidase family member responsible for the catabolism of amyloid beta peptide in the brain. J. Biochem. (Tokyo) 128, 897-902.
    • (2000) J. Biochem. (Tokyo) , vol.128 , pp. 897-902
    • Takaki, Y.1    Iwata, N.2    Tsubuki, S.3
  • 210
    • 0034605045 scopus 로고    scopus 로고
    • Defects in axonal elongation and neuronal migration in mice with disrupted tau and map1b genes
    • Takei Y., Teng J., Harada A. and Hirokawa N. (2000) Defects in axonal elongation and neuronal migration in mice with disrupted tau and map1b genes. J. Cell Biol. 150, 989-1000.
    • (2000) J. Cell Biol. , vol.150 , pp. 989-1000
    • Takei, Y.1    Teng, J.2    Harada, A.3    Hirokawa, N.4
  • 211
    • 0345872128 scopus 로고    scopus 로고
    • Memantine treatment in patients with moderate to severe Alzheimer disease already receiving donepezil: A randomized controlled trial
    • Tariot P. N., Farlow M. R., Grossberg G. T., Graham S. M., McDonald S. and Gergel I. (2004) Memantine treatment in patients with moderate to severe Alzheimer disease already receiving donepezil: a randomized controlled trial. Jama 291, 317-324.
    • (2004) Jama , vol.291 , pp. 317-324
    • Tariot, P.N.1    Farlow, M.R.2    Grossberg, G.T.3    Graham, S.M.4    McDonald, S.5    Gergel, I.6
  • 212
    • 33744946694 scopus 로고    scopus 로고
    • The role of biomarkers in clinical trials for Alzheimer disease
    • Thal L. J., Kantarci K., Reiman E. M. et al. (2006) The role of biomarkers in clinical trials for Alzheimer disease. Alzheimer Dis. Assoc. Disord. 20, 6-15.
    • (2006) Alzheimer Dis. Assoc. Disord. , vol.20 , pp. 6-15
    • Thal, L.J.1    Kantarci, K.2    Reiman, E.M.3
  • 213
    • 33644800389 scopus 로고    scopus 로고
    • Pgp deficiency increases amyloid concetrations in the brain
    • Thomas L. (2005) Pgp deficiency increases amyloid concetrations in the brain. Lancet Neurol. 4, 798-799.
    • (2005) Lancet Neurol. , vol.4 , pp. 798-799
    • Thomas, L.1
  • 214
    • 18544410708 scopus 로고    scopus 로고
    • The plasmin system is induced by and degrades amyloid-beta aggregates
    • Tucker H. M., Kihiko M., Caldwell J. N. et al. (2000b) The plasmin system is induced by and degrades amyloid-beta aggregates. J. Neurosci. 20, 3937-3946.
    • (2000) J. Neurosci. , vol.20 , pp. 3937-3946
    • Tucker, H.M.1    Kihiko, M.2    Caldwell, J.N.3
  • 215
    • 0033788789 scopus 로고    scopus 로고
    • Tissue plasminogen activator requires plasminogen to modulate amyloid- Beta neurotoxicity and deposition
    • Tucker H. M., Kihiko-Ehmann M., Wright S., Rydel R. E. and Estus S. (2000a) Tissue plasminogen activator requires plasminogen to modulate amyloid- beta neurotoxicity and deposition. J. Neurochem. 75, 2172-2177.
    • (2000) J. Neurochem. , vol.75 , pp. 2172-2177
    • Tucker, H.M.1    Kihiko-Ehmann, M.2    Wright, S.3    Rydel, R.E.4    Estus, S.5
  • 217
    • 21044458854 scopus 로고    scopus 로고
    • A phase 1 clinical trial of nerve growth factor gene therapy for Alzheimer disease
    • Tuszynski M. H., Thal L., Pay M. et al. (2005) A phase 1 clinical trial of nerve growth factor gene therapy for Alzheimer disease. Nat. Med. 11, 551-555.
    • (2005) Nat. Med. , vol.11 , pp. 551-555
    • Tuszynski, M.H.1    Thal, L.2    Pay, M.3
  • 219
    • 26244462301 scopus 로고    scopus 로고
    • Proteolytic mechanisms in amyloid-beta metabolism: Therapeutic implications for Alzheimer's disease
    • Vardy E. R., Catto A. J. and Hooper N. M. (2005) Proteolytic mechanisms in amyloid-beta metabolism: therapeutic implications for Alzheimer's disease. Trends Mol. Med. 11, 464-472.
    • (2005) Trends Mol. Med. , vol.11 , pp. 464-472
    • Vardy, E.R.1    Catto, A.J.2    Hooper, N.M.3
  • 220
    • 0033595706 scopus 로고    scopus 로고
    • Beta-Secretase celavage of Alzheimer's Amyloid Precursor Protein by the transmembrane aspartic protease BACE
    • Vassar R., Bennett B., Babu-Khan S., Rogers G. and Citron M. (1999) Beta-Secretase celavage of Alzheimer's Amyloid Precursor Protein by the transmembrane aspartic protease BACE. Science 286, 735-740.
    • (1999) Science , vol.286 , pp. 735-740
    • Vassar, R.1    Bennett, B.2    Babu-Khan, S.3    Rogers, G.4    Citron, M.5
  • 223
    • 30044442937 scopus 로고    scopus 로고
    • Deletion of Abca1 increases Abeta deposition in the PDAPP transgenic mouse model of Alzheimer disease
    • Wahrle S. E., Jiang H., Parsadanian M., Hartman R. E., Bales K. R., Paul S. M. and Holtzman D. M. (2005) Deletion of Abca1 increases Abeta deposition in the PDAPP transgenic mouse model of Alzheimer disease. J. Biol. Chem. 280, 43 236-43 242.
    • (2005) J. Biol. Chem. , vol.280 , pp. 43236-43242
    • Wahrle, S.E.1    Jiang, H.2    Parsadanian, M.3    Hartman, R.E.4    Bales, K.R.5    Paul, S.M.6    Holtzman, D.M.7
  • 224
    • 5344277556 scopus 로고    scopus 로고
    • Deciphering the molecular basis of memory failure in Alzheimer's disease
    • Walsh D. M. and Selkoe D. J. (2004) Deciphering the molecular basis of memory failure in Alzheimer's disease. Neuron 44, 181-193.
    • (2004) Neuron , vol.44 , pp. 181-193
    • Walsh, D.M.1    Selkoe, D.J.2
  • 226
    • 0035829592 scopus 로고    scopus 로고
    • A subset of NSAIDs lower amyloidogenic Abeta42 independently of cyclooxygenase activity
    • Weggen S., Eriksen J. L., Das P. et al. (2001) A subset of NSAIDs lower amyloidogenic Abeta42 independently of cyclooxygenase activity. Nature 414, 212-216.
    • (2001) Nature , vol.414 , pp. 212-216
    • Weggen, S.1    Eriksen, J.L.2    Das, P.3
  • 227
    • 0041876229 scopus 로고    scopus 로고
    • Evidence that nonsteroidal anti-inflammatory drugs decrease amyloid beta 42 production by direct modulation of gamma-secretase activity
    • Weggen S., Eriksen J. L., Sagi S. A., Pietrzik C. U., Ozols V., Fauq A., Golde T. E. and Koo E. H. (2003) Evidence that nonsteroidal anti-inflammatory drugs decrease amyloid beta 42 production by direct modulation of gamma-secretase activity. J. Biol. Chem. 278, 31 831-31 837.
    • (2003) J. Biol. Chem. , vol.278 , pp. 31831-31837
    • Weggen, S.1    Eriksen, J.L.2    Sagi, S.A.3    Pietrzik, C.U.4    Ozols, V.5    Fauq, A.6    Golde, T.E.7    Koo, E.H.8
  • 228
    • 0024550204 scopus 로고
    • Identification, biogenesis, and localization of precursors of Alzheimer's disease A4 amyloid protein
    • Weidemann A., Konig G., Bunke D., Fischer P., Salbaum J. M., Masters C. L. and Beyreuther K. (1989) Identification, biogenesis, and localization of precursors of Alzheimer's disease A4 amyloid protein. Cell 57, 115-126.
    • (1989) Cell , vol.57 , pp. 115-126
    • Weidemann, A.1    Konig, G.2    Bunke, D.3    Fischer, P.4    Salbaum, J.M.5    Masters, C.L.6    Beyreuther, K.7
  • 229
    • 33646384419 scopus 로고    scopus 로고
    • Immunology and immunotherapy of Alzheimer's disease
    • Weiner H. L. and Frenkel D. (2006) Immunology and immunotherapy of Alzheimer's disease. Nat. Rev. Immunol. 6, 404-416.
    • (2006) Nat. Rev. Immunol. , vol.6 , pp. 404-416
    • Weiner, H.L.1    Frenkel, D.2
  • 230
    • 0037531198 scopus 로고    scopus 로고
    • Intracranially administered anti-Abeta antibodies reduce beta-amyloid deposition by mechanisms both independent of and associated with microglial activation
    • Wilcock D. M., DiCarlo G., Henderson D., Jackson J., Clarke K., Ugen K. E., Gordon M. N. and Morgan D. (2003) Intracranially administered anti-Abeta antibodies reduce beta-amyloid deposition by mechanisms both independent of and associated with microglial activation. J. Neurosci. 23, 3745-3751.
    • (2003) J. Neurosci. , vol.23 , pp. 3745-3751
    • Wilcock, D.M.1    DiCarlo, G.2    Henderson, D.3    Jackson, J.4    Clarke, K.5    Ugen, K.E.6    Gordon, M.N.7    Morgan, D.8
  • 231
    • 0035544150 scopus 로고    scopus 로고
    • Number of Abeta inoculations in APP+PS1 transgenic mice influences antibody titers, microglial activation, and congophilic plaque levels
    • Wilcock D. M., Gordon M. N., Ugen K. E. et al. (2001) Number of Abeta inoculations in APP+PS1 transgenic mice influences antibody titers, microglial activation, and congophilic plaque levels. DNA Cell Biol. 20, 731-736.
    • (2001) DNA Cell Biol. , vol.20 , pp. 731-736
    • Wilcock, D.M.1    Gordon, M.N.2    Ugen, K.E.3
  • 232
    • 14244255355 scopus 로고    scopus 로고
    • Passive immunotherapy against Abeta in aged APP-transgenic mice reverses cognitive deficits and depletes parenchymal amyloid deposits in spite of increased vascular amyloid and microhemorrhage
    • Wilcock D. M., Rojiani A., Rosenthal A., Subbarao S., Freeman M. J., Gordon M. N. and Morgan D. (2004) Passive immunotherapy against Abeta in aged APP-transgenic mice reverses cognitive deficits and depletes parenchymal amyloid deposits in spite of increased vascular amyloid and microhemorrhage. J. Neuroinflammation 1, 24.
    • (2004) J. Neuroinflammation , vol.1 , pp. 24
    • Wilcock, D.M.1    Rojiani, A.2    Rosenthal, A.3    Subbarao, S.4    Freeman, M.J.5    Gordon, M.N.6    Morgan, D.7
  • 234
    • 13544268706 scopus 로고    scopus 로고
    • Immunological and anti-chaperone therapeutic approaches for Alzheimer disease
    • Wisniewski T. and Frangione B. (2005) Immunological and anti-chaperone therapeutic approaches for Alzheimer disease. Brain Pathol. 15, 72-77.
    • (2005) Brain Pathol. , vol.15 , pp. 72-77
    • Wisniewski, T.1    Frangione, B.2
  • 235
    • 0035826795 scopus 로고    scopus 로고
    • A fluid connection: Cholesterol and Abeta
    • Wolozin B. (2001) A fluid connection: cholesterol and Abeta. Proc. Natl Acad. Sci. U S A 98, 5371-5373.
    • (2001) Proc. Natl. Acad. Sci. U S A , vol.98 , pp. 5371-5373
    • Wolozin, B.1
  • 236
    • 0033518264 scopus 로고    scopus 로고
    • Membrane-anchored aspartyl protease with Alzheimer's disease beta- secretase activity
    • Yan R., Bienkowski M. J., Shuck M. E. et al. (1999) Membrane-anchored aspartyl protease with Alzheimer's disease beta- secretase activity. Nature 402, 533-537.
    • (1999) Nature , vol.402 , pp. 533-537
    • Yan, R.1    Bienkowski, M.J.2    Shuck, M.E.3
  • 237
    • 0035823610 scopus 로고    scopus 로고
    • BACE2 functions as an alternative alpha-secretase in cells
    • Yan R., Munzner J. B., Shuck M. E. and Bienkowski M. J. (2001) BACE2 functions as an alternative alpha-secretase in cells. J. Biol. Chem. 276, 34 019-34 027.
    • (2001) J. Biol. Chem. , vol.276 , pp. 34019-34027
    • Yan, R.1    Munzner, J.B.2    Shuck, M.E.3    Bienkowski, M.J.4
  • 238
    • 0041921071 scopus 로고    scopus 로고
    • Anti-inflammatory drug therapy alters beta-amyloid processing and deposition in an animal model of Alzheimer's disease
    • Yan Q., Zhang J., Liu H., Babu-Khan S., Vassar R., Biere A. L., Citron M. and Landreth G. (2003) Anti-inflammatory drug therapy alters beta-amyloid processing and deposition in an animal model of Alzheimer's disease. J. Neurosci. 23, 7504-7509.
    • (2003) J. Neurosci. , vol.23 , pp. 7504-7509
    • Yan, Q.1    Zhang, J.2    Liu, H.3    Babu-Khan, S.4    Vassar, R.5    Biere, A.L.6    Citron, M.7    Landreth, G.8
  • 239
    • 20044370990 scopus 로고    scopus 로고
    • Curcumin inhibits formation of amyloid beta oligomers and fibrils, binds plaques, and reduces amyloid in vivo
    • Yang F., Lim G. P., Begum A. N. et al. (2005) Curcumin inhibits formation of amyloid beta oligomers and fibrils, binds plaques, and reduces amyloid in vivo. J. Biol. Chem. 280, 5892-5901.
    • (2005) J. Biol. Chem. , vol.280 , pp. 5892-5901
    • Yang, F.1    Lim, G.P.2    Begum, A.N.3
  • 241
    • 0032105394 scopus 로고    scopus 로고
    • The role of a beta 42 in Alzheimer's disease
    • Younkin S. G. (1998) The role of A beta 42 in Alzheimer's disease. J. Physiol., Paris 92, 289-292.
    • (1998) J. Physiol., Paris , vol.92 , pp. 289-292
    • Younkin, S.G.1
  • 242
  • 243
    • 19944429064 scopus 로고    scopus 로고
    • Microtubule-binding drugs offset tau sequestration by stabilizing microtubules and reversing fast axonal transport deficits in a tauopathy model
    • Zhang B., Maiti A., Shively S. et al. (2005) Microtubule-binding drugs offset tau sequestration by stabilizing microtubules and reversing fast axonal transport deficits in a tauopathy model. Proc. Natl Acad. Sci. U S A 102, 227-231.
    • (2005) Proc. Natl. Acad. Sci. U S A , vol.102 , pp. 227-231
    • Zhang, B.1    Maiti, A.2    Shively, S.3
  • 244
    • 0033638180 scopus 로고    scopus 로고
    • PIN1-dependent prolyl isomerization regulates dephosphorylation of Cdc25C and tau proteins
    • Zhou X. Z., Kops O., Werner A. et al. (2000) PIN1-dependent prolyl isomerization regulates dephosphorylation of Cdc25C and tau proteins. Mol. Cell 6, 873-883.
    • (2000) Mol. Cell , vol.6 , pp. 873-883
    • Zhou, X.Z.1    Kops, O.2    Werner, A.3
  • 245
    • 2542475986 scopus 로고    scopus 로고
    • Clearing amyloid through the blood-brain barrier
    • Zlokovic B. V. (2004) Clearing amyloid through the blood-brain barrier. J. Neurochem. 89, 807-811.
    • (2004) J. Neurochem. , vol.89 , pp. 807-811
    • Zlokovic, B.V.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.