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Volumn 86, Issue 6, 2005, Pages 1861-1867

No influence of amyloid-β-degrading neprilysin activity on prion pathogenesis

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID BETA PROTEIN; MEMBRANE METALLOENDOPEPTIDASE; METALLOPROTEINASE; PRION PROTEIN;

EID: 20044371003     PISSN: 00221317     EISSN: None     Source Type: Journal    
DOI: 10.1099/vir.0.80811-0     Document Type: Article
Times cited : (6)

References (24)
  • 1
    • 0242300624 scopus 로고    scopus 로고
    • Games played by rogue proteins in prion disorders and Alzheimer's disease
    • Aguzzi, A. & Haass, C. (2003). Games played by rogue proteins in prion disorders and Alzheimer's disease. Science 302, 814-818.
    • (2003) Science , vol.302 , pp. 814-818
    • Aguzzi, A.1    Haass, C.2
  • 2
    • 0842281643 scopus 로고    scopus 로고
    • Mammalian prion biology: One century of evolving concepts
    • Aguzzi, A. & Polymenidou, M. (2004). Mammalian prion biology: one century of evolving concepts. Cell 116, 313-327.
    • (2004) Cell , vol.116 , pp. 313-327
    • Aguzzi, A.1    Polymenidou, M.2
  • 3
    • 0029852887 scopus 로고    scopus 로고
    • Matrix metalloproteinase-9 (MMP-9) is synthesized in neurons of the human hippocampus and is capable of degrading the amyloid-β peptide (1-40)
    • Backstrom, J. R., Lim, G. P., Cullen, M. J. & Tökés, Z. A. (1996). Matrix metalloproteinase-9 (MMP-9) is synthesized in neurons of the human hippocampus and is capable of degrading the amyloid-β peptide (1-40). J Neurosci 16, 7910-7919.
    • (1996) J. Neurosci. , vol.16 , pp. 7910-7919
    • Backstrom, J.R.1    Lim, G.P.2    Cullen, M.J.3    Tökés, Z.A.4
  • 4
    • 0030499678 scopus 로고    scopus 로고
    • A vector for expressing foreign genes in the brains and hearts of transgenic mice
    • & 8 other authors
    • Borchelt, D. R., Davis, J., Fischer, M. & 8 other authors (1996). A vector for expressing foreign genes in the brains and hearts of transgenic mice. Genet Anal 13, 159-163.
    • (1996) Genet. Anal. , vol.13 , pp. 159-163
    • Borchelt, D.R.1    Davis, J.2    Fischer, M.3
  • 7
    • 0036890486 scopus 로고    scopus 로고
    • Alzheimer's and prion diseases: Distinct pathologies, common proteolytic denominators
    • Checler, F. & Vincent B. (2002). Alzheimer's and prion diseases: distinct pathologies, common proteolytic denominators. Trends Neurosci 25, 616-620.
    • (2002) Trends Neurosci. , vol.25 , pp. 616-620
    • Checler, F.1    Vincent, B.2
  • 9
    • 0035979274 scopus 로고    scopus 로고
    • Scrapie prion protein accumulation by scrapie-infected neuroblastoma cells abrogated by exposure to a prion protein antibody
    • Enari, M., Flechsig, E. & Weissmann, C. (2001). Scrapie prion protein accumulation by scrapie-infected neuroblastoma cells abrogated by exposure to a prion protein antibody. Proc Natl Acad Sci U S A 98, 9295-9299.
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 9295-9299
    • Enari, M.1    Flechsig, E.2    Weissmann, C.3
  • 10
    • 0029863648 scopus 로고    scopus 로고
    • Prion protein (PrP) with amino-proximal deletions restoring susceptibility of PrP knockout mice to scrapie
    • Fischer, M., Rülicke, T., Raeber, A., Sailer, A, Moser, M., Oesch, B., Brandner, S., Aguzzi, A. & Weissmann, C. (1996). Prion protein (PrP) with amino-proximal deletions restoring susceptibility of PrP knockout mice to scrapie. EMBO J 15, 1255-1264.
    • (1996) EMBO J. , vol.15 , pp. 1255-1264
    • Fischer, M.1    Rülicke, T.2    Raeber, A.3    Sailer, A.4    Moser, M.5    Oesch, B.6    Brandner, S.7    Aguzzi, A.8    Weissmann, C.9
  • 11
    • 0033763178 scopus 로고    scopus 로고
    • C expression in the peripheral nervous system is a determinant of prion neuroinvasion
    • C expression in the peripheral nervous system is a determinant of prion neuroinvasion. J Gen Virol 81, 2813-2821.
    • (2000) J. Gen. Virol. , vol.81 , pp. 2813-2821
    • Glatzel, M.1    Aguzzi, A.2
  • 12
    • 0034891027 scopus 로고    scopus 로고
    • Sympathetic innervation of lymphoreticular organs is rate limiting for prion neuroinvasion
    • Glatzel, M., Heppner, F. L., Albers, K. M. & Aguzzi, A. (2001). Sympathetic innervation of lymphoreticular organs is rate limiting for prion neuroinvasion. Neuron 31, 25-34.
    • (2001) Neuron , vol.31 , pp. 25-34
    • Glatzel, M.1    Heppner, F.L.2    Albers, K.M.3    Aguzzi, A.4
  • 13
    • 0242361687 scopus 로고    scopus 로고
    • Extraneural pathologic prion protein in sporadic Creutzfeldt-Jakob disease
    • Glatzel, M., Abela, E., Maissen, M. & Aguzzi, A. (2003). Extraneural pathologic prion protein in sporadic Creutzfeldt-Jakob disease. N Engl J Med 349, 1812-1820.
    • (2003) N. Engl. J. Med. , vol.349 , pp. 1812-1820
    • Glatzel, M.1    Abela, E.2    Maissen, M.3    Aguzzi, A.4
  • 14
    • 0035947207 scopus 로고    scopus 로고
    • Metabolic regulation of brain Aβ by neprilysin
    • & 7 other authors
    • Iwata, N., Tsubuki, S., Takaki, Y. & 7 other authors (2001). Metabolic regulation of brain Aβ by neprilysin. Science 292, 1550-1552.
    • (2001) Science , vol.292 , pp. 1550-1552
    • Iwata, N.1    Tsubuki, S.2    Takaki, Y.3
  • 15
    • 0031765769 scopus 로고    scopus 로고
    • Endogenous proteolytic cleavage of normal and disease-associated isoforms of the human prion protein in neural and non-neural tissues
    • Jiménez-Huete, A., Lievens, P. M. J., Vidal, R., Piccardo, P., Ghetti, B., Tagliavini, F., Frangione, B. & Prelli, F. (1998). Endogenous proteolytic cleavage of normal and disease-associated isoforms of the human prion protein in neural and non-neural tissues. Am J Pathol 153, 1561-1572.
    • (1998) Am. J. Pathol. , vol.153 , pp. 1561-1572
    • Jiménez-Huete, A.1    Lievens, P.M.J.2    Vidal, R.3    Piccardo, P.4    Ghetti, B.5    Tagliavini, F.6    Frangione, B.7    Prelli, F.8
  • 19
    • 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. & 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
  • 21
    • 0035877747 scopus 로고    scopus 로고
    • Neprilysin degrades both amyloid β peptides 1-40 and 1-42 most rapidly and efficiently among thiorphan- and phosphoramidon-sensitive endopeptidases
    • & 9 other authors
    • Shirotani, K., Tsubuki, S., Iwata, N. & 9 other authors (2001). Neprilysin degrades both amyloid β peptides 1-40 and 1-42 most rapidly and efficiently among thiorphan- and phosphoramidon-sensitive endopeptidases. J Biol Chem 276, 21895-21901.
    • (2001) J. Biol. Chem. , vol.276 , pp. 21895-21901
    • Shirotani, K.1    Tsubuki, S.2    Iwata, N.3
  • 23
    • 0038201945 scopus 로고    scopus 로고
    • Exploring the structure and function of zinc metallopeptidases: Old enzymes and new discoveries
    • Turner, A. J. (2003). Exploring the structure and function of zinc metallopeptidases: old enzymes and new discoveries. Biochem Soc Trans 31, 723-727.
    • (2003) Biochem. Soc. Trans. , vol.31 , pp. 723-727
    • Turner, A.J.1
  • 24
    • 0035851151 scopus 로고    scopus 로고
    • The disintegrins ADAM10 and TACE contribute to the constitutive and phorbol ester-regulated normal cleavage of the cellular prion protein
    • Vincent, B., Paitel, E., Saftig, P., Frobert, Y., Hartmann, D., De Strooper, B., Grassi, J., Lopez-Perez, E. & Checler, F. (2001). The disintegrins ADAM10 and TACE contribute to the constitutive and phorbol ester-regulated normal cleavage of the cellular prion protein. J Biol Chem 276, 37743-37746.
    • (2001) J. Biol. Chem. , vol.276 , pp. 37743-37746
    • Vincent, B.1    Paitel, E.2    Saftig, P.3    Frobert, Y.4    Hartmann, D.5    De Strooper, B.6    Grassi, J.7    Lopez-Perez, E.8    Checler, F.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.