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Volumn 23, Issue 6, 2002, Pages 1039-1042

Amyloid binding ligands as Alzheimer's disease therapies

Author keywords

A ; Brain amyloidosis; Drug discovery; Neurodegenerative diseases

Indexed keywords

AMYLOID; CONGO RED; THIOFLAVINE; VACCINE;

EID: 0036860355     PISSN: 01974580     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0197-4580(02)00121-5     Document Type: Article
Times cited : (72)

References (25)
  • 1
    • 0033835996 scopus 로고    scopus 로고
    • Peripherally administered antibodies against amyloid-β peptide enter the central nervous system and reduce pathology in a mouse model of Alzheimer disease
    • Bard F.et al. Peripherally administered antibodies against amyloid-β peptide enter the central nervous system and reduce pathology in a mouse model of Alzheimer disease. Nat. Med. 6:2000;916-919.
    • (2000) Nat. Med. , vol.6 , pp. 916-919
    • Bard, F.1
  • 2
    • 0035203662 scopus 로고    scopus 로고
    • Key Factors in Alzheimer's disease: Β-amyloid precursor protein processing, metablosim and intraneuronal transport
    • Bayer T.A.et al. Key Factors in Alzheimer's disease: β-amyloid precursor protein processing, metablosim and intraneuronal transport. Brain Pathol. 11:2000;1-11.
    • (2000) Brain Pathol. , vol.11 , pp. 1-11
    • Bayer, T.A.1
  • 3
    • 0033943119 scopus 로고    scopus 로고
    • Transgenic mouse models of Alzheimer's disease
    • Borneman K.D., Staufenbiel M. Transgenic mouse models of Alzheimer's disease. Ann. N.Y. Acad. Sci. 908:2000;260-266.
    • (2000) Ann. N.Y. Acad. Sci. , vol.908 , pp. 260-266
    • Borneman, K.D.1    Staufenbiel, M.2
  • 5
    • 0035112647 scopus 로고    scopus 로고
    • BACE1 is the major beta-secretase for generation of Abeta peptides by neurons
    • Cai H., Wang Y., McCarthy D., Wen H., Borchelt D.R., Price D.L.et al. BACE1 is the major beta-secretase for generation of Abeta peptides by neurons. Nat. Neurosci. 4:2001;233-234.
    • (2001) Nat. Neurosci. , vol.4 , pp. 233-234
    • Cai, H.1    Wang, Y.2    McCarthy, D.3    Wen, H.4    Borchelt, D.R.5    Price, D.L.6
  • 6
    • 0033849965 scopus 로고    scopus 로고
    • Studies on the in vitro assembly of a beta 1-40: Implications for the search for a beta fibril formation inhibitors
    • Goldsbury C.S.et al. Studies on the in vitro assembly of a beta 1-40: implications for the search for a beta fibril formation inhibitors. J. Struct. Biol. 130:2000;217-231.
    • (2000) J. Struct. Biol. , vol.130 , pp. 217-231
    • Goldsbury, C.S.1
  • 7
    • 0034718206 scopus 로고    scopus 로고
    • Approaches to discovery and characterization of inhibitors of amyloid-peptide polymerization
    • Findeis M.A.et al. Approaches to discovery and characterization of inhibitors of amyloid-peptide polymerization. Biochem. Biophys. Acta. 1502:2000;76-84.
    • (2000) Biochem. Biophys. Acta , vol.1502 , pp. 76-84
    • Findeis, M.A.1
  • 8
    • 0034700471 scopus 로고    scopus 로고
    • Aβ peptide immunization reduces behavioral impairment and plaques in a model of Alzheimer's disease
    • Janus C.et al. Aβ peptide immunization reduces behavioral impairment and plaques in a model of Alzheimer's disease. Nature. 408:2000;979-982.
    • (2000) Nature , vol.408 , pp. 979-982
    • Janus, C.1
  • 9
    • 0033857342 scopus 로고    scopus 로고
    • X-34, a fluorescent derivative of Congo red: A novel stochemical stain for Alzheimer's disease pathology
    • Styren S.D., Hamilton R.L., Styren G.C., Klunk W.W. X-34, a fluorescent derivative of Congo red: a novel histochemical stain for Alzheimer's disease pathology. J. Histo. Cytochem. 48:2000;1223-1232.
    • (2000) J. Histo. Cytochem. , vol.48 , pp. 1223-1232
    • Styren, S.D.1    Hamilton, R.L.2    Styren, G.C.3    Klunk, W.W.4
  • 11
    • 0011933729 scopus 로고    scopus 로고
    • Novel beta amyloid probes
    • Fillit HM, O'Connell AW, editors. Berlin: Springer
    • Kung M-P, et al. Novel beta amyloid probes. In: Fillit HM, O'Connell AW, editors. Drug Discovery and Development for Alzheimer's Disease. Berlin: Springer; 2000, p. 50-6.
    • (2000) Drug Discovery and Development for Alzheimer's Disease , pp. 50-56
    • Kung, M.-P.1
  • 12
    • 0033616682 scopus 로고    scopus 로고
    • Evolution of amyloid: What normal protein folding may tell us about fibrillogenesis and disease
    • Lansbury P.T. Evolution of amyloid: what normal protein folding may tell us about fibrillogenesis and disease. Proc. Natl. Acad. Sci. U.S.A. 96:1999;3342-3344.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 3342-3344
    • Lansbury, P.T.1
  • 13
    • 0037022828 scopus 로고    scopus 로고
    • Glu11 Site cleavage and N-terminally truncated Aβ production upon BACE overexpression
    • Liu K., Doms R.W., Lee V.M.-Y. Glu11 Site cleavage and N-terminally truncated Aβ production upon BACE overexpression. Biochemistry. 41:2002;3128-3136.
    • (2002) Biochemistry , vol.41 , pp. 3128-3136
    • Liu, K.1    Doms, R.W.2    Lee, V.M.-Y.3
  • 14
    • 0028172886 scopus 로고
    • Veta-amyloid neurotoxicity requires fibril formation and is inhibited by congo red
    • Lorenzo A., Yankner B.A. Veta-amyloid neurotoxicity requires fibril formation and is inhibited by congo red. Proc. Natl. Acad. Sci. U.S.A. 91:1994;12243-12247.
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 12243-12247
    • Lorenzo, A.1    Yankner, B.A.2
  • 15
    • 18744435477 scopus 로고    scopus 로고
    • Presenilin-1 mutations in Alzheimer's disease
    • Russo C.et al. Presenilin-1 mutations in Alzheimer's disease. Nature. 405:2001;531-532.
    • (2001) Nature , vol.405 , pp. 531-532
    • Russo, C.1
  • 16
    • 0033536163 scopus 로고    scopus 로고
    • Immunization with amyloid-β attenuates Alzheimer disease-like pathology in the PDAPP mouse
    • Schenk D. Immunization with amyloid-β attenuates Alzheimer disease-like pathology in the PDAPP mouse. Nature. 400:1999;173-177.
    • (1999) Nature , vol.400 , pp. 173-177
    • Schenk, D.1
  • 17
    • 0002680504 scopus 로고    scopus 로고
    • Biology of β-amyloid precursor protein and the mechanism of Alzheimer's disease
    • Terry, RD, Katzman, R, Bick, KL, Sisodia, SS, editors. Philadelphia, PA: Lippincot Williams & Wilkins
    • D.J. Selkoe, Biology of β-amyloid precursor protein and the mechanism of Alzheimer's disease. In: Terry, RD, Katzman, R, Bick, KL, Sisodia, SS, editors. Alzheimer's Disease. Philadelphia, PA: Lippincot Williams & Wilkins; 1999, p. 293-310.
    • (1999) Alzheimer's Disease , pp. 293-310
    • Selkoe, D.J.1
  • 18
    • 0034192158 scopus 로고    scopus 로고
    • β-Secretase revealed: Starting gate for race to novel Alzheimer therapies
    • Skovronsky D.M., Lee V.M.-Y. β-Secretase revealed: starting gate for race to novel Alzheimer therapies. Trends Pharmacol. Sci. 21:2000;161-163.
    • (2000) Trends Pharmacol. Sci. , vol.21 , pp. 161-163
    • Skovronsky, D.M.1    Lee, V.M.-Y.2
  • 19
    • 0034691124 scopus 로고    scopus 로고
    • In vivo detection of amyloid plaques in a mouse model of Alzheimer's disease
    • Skovronsky D.M. In vivo detection of amyloid plaques in a mouse model of Alzheimer's disease. Proc. Natl. Acad. Sci. U.S.A. 977:2000;609-7614.
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.977 , pp. 609-7614
    • Skovronsky, D.M.1
  • 20
    • 0031873102 scopus 로고    scopus 로고
    • β-Sheet breaker peptides inhibit fibrillogenesis in a rat brain model of amyloidosis: Implication for Alzheimer's therapy
    • Soto C., Sigurdsson E.M., Morelli L., Kumar A., Castano E.M., Frangione B. β-Sheet breaker peptides inhibit fibrillogenesis in a rat brain model of amyloidosis: implication for Alzheimer's therapy. Nat. Med. 4:1998;822-826.
    • (1998) Nat. Med. , vol.4 , pp. 822-826
    • Soto, C.1    Sigurdsson, E.M.2    Morelli, L.3    Kumar, A.4    Castano, E.M.5    Frangione, B.6
  • 21
    • 85043730362 scopus 로고    scopus 로고
    • Brain degeneration linked to "fatal attractions" of proteins in Alzheimer's disease and related disorders
    • in press
    • J.Q. Trojanowski, V.M.-Y. Lee. Brain degeneration linked to "fatal attractions" of proteins in Alzheimer's disease and related disorders. J. Alzheimer's Dis., in press.
    • J. Alzheimer's Dis.
    • Trojanowski, J.Q.1    Lee, V.M.-Y.2
  • 22
    • 0033595706 scopus 로고    scopus 로고
    • β-Secretase cleavage of Alzheimer's amyloid precursor protein by the transmembrane aspartic protease BACE
    • Vassar R.et al. β-Secretase cleavage of Alzheimer's amyloid precursor protein by the transmembrane aspartic protease BACE. Science. 286:1999;735-741.
    • (1999) Science , vol.286 , pp. 735-741
    • Vassar, R.1
  • 23
    • 0032800818 scopus 로고    scopus 로고
    • Intracellular APP processing and Aβ production in Alzheimer disease
    • Wilson C.A.et al. Intracellular APP processing and Aβ production in Alzheimer disease. J. Neuropath. Exper. Neurol. 58:1999;787-794.
    • (1999) J. Neuropath. Exper. Neurol. , vol.58 , pp. 787-794
    • Wilson, C.A.1
  • 24
    • 0033535553 scopus 로고    scopus 로고
    • Two transmembrane aspartates in presenilin-1 required for presenilin endoproteolysis and gamma-secretase activity
    • Wolfe M.S.et al. Two transmembrane aspartates in presenilin-1 required for presenilin endoproteolysis and gamma-secretase activity. Nature. 398:1999;513-517.
    • (1999) Nature , vol.398 , pp. 513-517
    • Wolfe, M.S.1
  • 25
    • 0035821603 scopus 로고    scopus 로고
    • Radioiodinated styrylbenzenes and thioflavins as probes for amyloid aggregates
    • Zhuang Z.P.et al. Radioiodinated styrylbenzenes and thioflavins as probes for amyloid aggregates. J. Med. Chem. 44:2001;1905-1914.
    • (2001) J. Med. Chem. , vol.44 , pp. 1905-1914
    • Zhuang, Z.P.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.