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Volumn 13, Issue 5, 2003, Pages 809-814

Isolation of Streptomyces sp. KK65 as a produceer of β-amyloid aggregation inhibitor

Author keywords

amyloid; A aggregation inhibitor; Alzheimer's disease; Streptomyces sp.

Indexed keywords

AMYLOID BETA PROTEIN; CELL EXTRACT; CONGO RED; DIAMINOPIMELIC ACID; PROTEIN ANTIBODY; PROTEIN INHIBITOR; THIOFLAVINE;

EID: 0242551359     PISSN: 10177825     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (5)

References (20)
  • 1
    • 0035816707 scopus 로고    scopus 로고
    • Degradation of the Alzheimer's amyloid beta peptide by endothelin-converting enzyme
    • Eckman, E. A., D. K. Reed, and C. B. Eckman. 2001. Degradation of the Alzheimer's amyloid beta peptide by endothelin-converting enzyme. J. Biol. Chem. 27: 24540-24548.
    • (2001) J. Biol. Chem. , vol.27 , pp. 24540-24548
    • Eckman, E.A.1    Reed, D.K.2    Eckman, C.B.3
  • 2
    • 0031824782 scopus 로고    scopus 로고
    • Aging renders the brain vulnerable to amyloid β-protein neurotoxicity
    • Geula, C., C. Wu, L. Saroff, M. Yuan, and B. Tankner. 1998. Aging renders the brain vulnerable to amyloid β-protein neurotoxicity. Nat. Med. 4: 827-831.
    • (1998) Nat. Med. , vol.4 , pp. 827-831
    • Geula, C.1    Wu, C.2    Saroff, L.3    Yuan, M.4    Tankner, B.5
  • 3
    • 0021256895 scopus 로고
    • Alzheimer's disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid protein
    • Glenner, G. G. and C. W. Wong. 1984. Alzheimer's disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid protein. Biochim. Biophys. Res. Commun. 120: 885-890.
    • (1984) Biochim. Biophys. Res. Commun. , vol.120 , pp. 885-890
    • Glenner, G.G.1    Wong, C.W.2
  • 4
    • 0027333557 scopus 로고
    • Cellular processing of β-amyloid precursor protein and the genesis of amyloid β-peptide
    • Hasse, C. and D. J. Selkoe. 1993. Cellular processing of β-amyloid precursor protein and the genesis of amyloid β-peptide. Cell 75: 1039-1042.
    • (1993) Cell , vol.75 , pp. 1039-1042
    • Hasse, C.1    Selkoe, D.J.2
  • 7
    • 0024352110 scopus 로고
    • Quantitative evaluation of Congo red binding to amyloid-like proteins with a β-pleated sheet conformation
    • Klunk, W. E., J. W. Pettegrew, and D. J. Abraham. 1989. Quantitative evaluation of Congo red binding to amyloid-like proteins with a β-pleated sheet conformation. J. Histochem. Cytochem. 37: 1273-1281.
    • (1989) J. Histochem. Cytochem. , vol.37 , pp. 1273-1281
    • Klunk, W.E.1    Pettegrew, J.W.2    Abraham, D.J.3
  • 9
    • 0036694418 scopus 로고    scopus 로고
    • Apicularen A, a macrolide from Chondromyces sp. inhibits growth factor induced in vitro angiogenesis
    • Kwon, H. J., D. H. Kim, J. S. Shim, and J. W. Ahn. 2002. Apicularen A, a macrolide from Chondromyces sp. inhibits growth factor induced in vitro angiogenesis. J. Microbiol. Biotechnol. 12: 702-705.
    • (2002) J. Microbiol. Biotechnol. , vol.12 , pp. 702-705
    • Kwon, H.J.1    Kim, D.H.2    Shim, J.S.3    Ahn, J.W.4
  • 10
    • 0027502784 scopus 로고
    • Thioflavine T interaction with synthetic Alzheimer's disease β-amyloid peptides: Detection of amyloid aggregation in solution
    • LeVine, H. 1993. Thioflavine T interaction with synthetic Alzheimer's disease β-amyloid peptides: detection of amyloid aggregation in solution. Protein Sci. 2: 404-410.
    • (1993) Protein Sci. , vol.2 , pp. 404-410
    • LeVine, H.1
  • 11
    • 0021061819 scopus 로고
    • Rapid colorimetric assay for cellular growth and survival: Application to proliferation and cytotoxicity assays
    • Mosman, T. 1983. Rapid colorimetric assay for cellular growth and survival: Application to proliferation and cytotoxicity assays. J. Immunol. Methods 65: 55-63.
    • (1983) J. Immunol. Methods , vol.65 , pp. 55-63
    • Mosman, T.1
  • 13
    • 0032574993 scopus 로고
    • Notch-1 signalling requires ligand-induced proteolytic release of intracellular domain
    • Schroeter, E. H., J. A. Kisslinger, and R. Kopan. 1989. Notch-1 signalling requires ligand-induced proteolytic release of intracellular domain. Nature 393: 382-386.
    • (1989) Nature , vol.393 , pp. 382-386
    • Schroeter, E.H.1    Kisslinger, J.A.2    Kopan, R.3
  • 14
    • 0028123071 scopus 로고
    • Alzheimer's disease: A central role for amyloid
    • Selkoe, D. J. 1994. Alzheimer's disease: A central role for amyloid. J. Neuropathol. Exp. Neurol. 53: 438-447.
    • (1994) J. Neuropathol. Exp. Neurol. , vol.53 , pp. 438-447
    • Selkoe, D.J.1
  • 15
    • 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
  • 16
    • 0035960535 scopus 로고    scopus 로고
    • The functional gamma-secretase inhibitor prevents production of amyloid β 1-34 in human and murine cell lines
    • Vandermeeren, M., M. Geraerts, S. Pype, L. Dillen, C. Van Hove, and M. Mercken. 2001. The functional gamma-secretase inhibitor prevents production of amyloid β 1-34 in human and murine cell lines. Neurosci. Lett. 27: 145-148.
    • (2001) Neurosci. Lett. , vol.27 , pp. 145-148
    • Vandermeeren, M.1    Geraerts, M.2    Pype, S.3    Dillen, L.4    VanHove, C.5    Mercken, M.6
  • 17
    • 0024990330 scopus 로고
    • Neurotrophic and neurotoxic effects of amyloid β protein: Reversal by tachykinin neuropeptides
    • Yankner, B. A., L. K. Duffy, and D. A. Kirschner. 1990. Neurotrophic and neurotoxic effects of amyloid β protein: Reversal by tachykinin neuropeptides. Science 250: 279-282.
    • (1990) Science , vol.250 , pp. 279-282
    • Yankner, B.A.1    Duffy, L.K.2    Kirschner, D.A.3
  • 18
    • 0035846826 scopus 로고    scopus 로고
    • Reduced neprilysin in high plaque areas of Alzheimer brain: A possible relationship to deficient degradation of β-amyloid peptide
    • Yasojima, K., H. Akiyama, E. G. McGeer, and P. L. McGeer. 2001. Reduced neprilysin in high plaque areas of Alzheimer brain: A possible relationship to deficient degradation of β-amyloid peptide. Neurosci. Lett. 12: 97-100.
    • (2001) Neurosci. Lett. , vol.12 , pp. 97-100
    • Yasojima, K.1    Akiyama, H.2    McGeer, E.G.3    McGeer, P.L.4
  • 20
    • 0034089960 scopus 로고    scopus 로고
    • Fresh and nonfibrillar amyloid β protein (1-40) induces rapid cellular degeneration in aged human fibroblasts: Evidence for AbetaP-channel-mediated cellular toxicity
    • Zhu, Y. J., H. Lin, and R. Lal. 2000. Fresh and nonfibrillar amyloid β protein (1-40) induces rapid cellular degeneration in aged human fibroblasts: Evidence for AbetaP-channel-mediated cellular toxicity. FASEB J. 14: 1244-1254.
    • (2000) FASEB J. , vol.14 , pp. 1244-1254
    • Zhu, Y.J.1    Lin, H.2    Lal, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.