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Volumn 44, Issue 11, 2005, Pages 4450-4457

Characterization of the reconstituted γ-secretase complex from Sf9 cells co-expressing presenilin 1, nacastrin, aph-1a, and pen-2

Author keywords

[No Author keywords available]

Indexed keywords

CATALYSIS; CELLS; COMPLEXATION; DISEASES; MEMBRANES; MUTAGENESIS; SUBSTRATES;

EID: 15544378384     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0481500     Document Type: Article
Times cited : (24)

References (36)
  • 1
    • 0035066332 scopus 로고    scopus 로고
    • Alzheimer's disease: Genes, proteins, and therapy
    • Selkoe, D. (2001) Alzheimer's disease: Genes, proteins, and therapy, Physiol. Rev. 81, 741-766.
    • (2001) Physiol. Rev. , vol.81 , pp. 741-766
    • Selkoe, D.1
  • 2
    • 0032574993 scopus 로고    scopus 로고
    • Notch-1 signalling requires ligand-induced proteolytic release of intracellular domain
    • Schroeter, E. H., Kisslinger, J. A., and Kopan, R. (1998) Notch-1 signalling requires ligand-induced proteolytic release of intracellular domain, Nature 393, 382-386.
    • (1998) Nature , vol.393 , pp. 382-386
    • Schroeter, E.H.1    Kisslinger, J.A.2    Kopan, R.3
  • 3
    • 0035824391 scopus 로고    scopus 로고
    • γ-secretase cleavage and nuclear localization of ErbB-4 receptor tyrosine kinase
    • Ni, C.-Y., Murphy, M. P., Golde, T. E., and Carpenter, G. (2001) γ-Secretase cleavage and nuclear localization of ErbB-4 receptor tyrosine kinase, Science 294, 2179-2181.
    • (2001) Science , vol.294 , pp. 2179-2181
    • Ni, C.-Y.1    Murphy, M.P.2    Golde, T.E.3    Carpenter, G.4
  • 4
    • 0347785491 scopus 로고    scopus 로고
    • Presenilin-dependent intramembrane proteolysis of CD44 leads to the liberation of its intracellular domain and the secretion of an Aβ-like peptide
    • Lammich, S., Okochi, M., Takeda, M., Kaether, C., Capeli, A., Zimmer, A. K., Edbauer, D., Walter, J., Steiner, H., and Haass, C. (2002) Presenilin-dependent intramembrane proteolysis of CD44 leads to the liberation of its intracellular domain and the secretion of an Aβ-like peptide, J. Biol. Chem. 277, 44754-44759.
    • (2002) J. Biol. Chem. , vol.277 , pp. 44754-44759
    • Lammich, S.1    Okochi, M.2    Takeda, M.3    Kaether, C.4    Capeli, A.5    Zimmer, A.K.6    Edbauer, D.7    Walter, J.8    Steiner, H.9    Haass, C.10
  • 5
    • 0037424348 scopus 로고    scopus 로고
    • The Notch ligands, Delta1 and Jagged2, are substrates for presenilin-dependent "γ-secretase" cleavage
    • Ikeuchi, T., and Sisodia, S. S. (2003) The Notch ligands, Delta1 and Jagged2, are substrates for presenilin-dependent "γ-secretase" cleavage, J. Biol. Chem. 278, 7751-7754.
    • (2003) J. Biol. Chem. , vol.278 , pp. 7751-7754
    • Ikeuchi, T.1    Sisodia, S.S.2
  • 7
    • 0037431082 scopus 로고    scopus 로고
    • Aph-1, pen-2 and nicastrin with presenilin generate an active γ-secretase complex
    • De Strooper, B. (2003) Aph-1, pen-2 and nicastrin with presenilin generate an active γ-secretase complex, Neuron 38, 9-12.
    • (2003) Neuron , vol.38 , pp. 9-12
    • De Strooper, B.1
  • 12
    • 0033535553 scopus 로고    scopus 로고
    • Two transmembrane aspartates in presenilin-1 required for presenilin endoproteolysis and γ-secretase activity
    • Wolfe, M. S., Xia, W., Ostaszewski, B. L., Diehl, T. S., Kimberly, W. T., and Selkoe, D. J. (1999) Two transmembrane aspartates in presenilin-1 required for presenilin endoproteolysis and γ-secretase activity, Nature 398, 513-517.
    • (1999) Nature , vol.398 , pp. 513-517
    • Wolfe, M.S.1    Xia, W.2    Ostaszewski, B.L.3    Diehl, T.S.4    Kimberly, W.T.5    Selkoe, D.J.6
  • 18
    • 2442450572 scopus 로고    scopus 로고
    • Myeloproliferative disease in mice with reduced presenilin gene dosage: Effect of γ-secretase blockage
    • Qyang, Y., Chambers, S. M., Wang, P., Xia, X., Chen, X., Goodell, M. A., and Zheng, H. (2004) Myeloproliferative disease in mice with reduced presenilin gene dosage: Effect of γ-secretase blockage, Biochemistry 43, 5352-5359.
    • (2004) Biochemistry , vol.43 , pp. 5352-5359
    • Qyang, Y.1    Chambers, S.M.2    Wang, P.3    Xia, X.4    Chen, X.5    Goodell, M.A.6    Zheng, H.7
  • 20
    • 0037154158 scopus 로고    scopus 로고
    • APH-1 is a multipass membrane protein essential for the Notch signaling pathway in Caenorhabditis elegans embryos
    • Goutte, C., Tsunozaki, M., Hale, V. A., and Priess, J. R. (2002) APH-1 is a multipass membrane protein essential for the Notch signaling pathway in Caenorhabditis elegans embryos, Proc. Natl. Acad. Sci. U.S.A. 99, 775-779.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 775-779
    • Goutte, C.1    Tsunozaki, M.2    Hale, V.A.3    Priess, J.R.4
  • 21
    • 0033009194 scopus 로고    scopus 로고
    • Increased vulnerability of hippocampal neurons from presenilin-1 mutant knock-in mice to amyloid β-peptide toxicity: Central roles of superoxide production and caspase activation
    • Guo, Q., Sebastian, L., Sopher, B. L., Miller, M. W., Ware, C. B., Martin, G. M., and Mattson, M. P. (1999) Increased vulnerability of hippocampal neurons from presenilin-1 mutant knock-in mice to amyloid β-peptide toxicity: Central roles of superoxide production and caspase activation, J. Neurochem. 72, 1019-1029.
    • (1999) J. Neurochem. , vol.72 , pp. 1019-1029
    • Guo, Q.1    Sebastian, L.2    Sopher, B.L.3    Miller, M.W.4    Ware, C.B.5    Martin, G.M.6    Mattson, M.P.7
  • 22
    • 0035834145 scopus 로고    scopus 로고
    • PS1 N- and C-terminal fragments form a complex that functions in APP processing and Notch signaling
    • Levitan, D., Lee, J., Song, L., Manning, R., Wong, G., Parker, E., and Zhang, L. (2001) PS1 N- and C-terminal fragments form a complex that functions in APP processing and Notch signaling, Proc. Natl. Acad. Sci. U.S.A. 98, 12186-12190.
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 12186-12190
    • Levitan, D.1    Lee, J.2    Song, L.3    Manning, R.4    Wong, G.5    Parker, E.6    Zhang, L.7
  • 23
    • 0035942322 scopus 로고    scopus 로고
    • Biochemical characterization of the γ-secretase activity that produces β-amyloid peptides
    • Zhang, L., Song, L., Terracina, G., Liu, Y., Pramanik, B., and Parker, E. (2001) Biochemical characterization of the γ-secretase activity that produces β-amyloid peptides, Biochemistry 40, 5049-5055.
    • (2001) Biochemistry , vol.40 , pp. 5049-5055
    • Zhang, L.1    Song, L.2    Terracina, G.3    Liu, Y.4    Pramanik, B.5    Parker, E.6
  • 25
  • 26
    • 0033605588 scopus 로고    scopus 로고
    • Calpain inhibitor I increases β-amyloid peptide production by inhibiting the degradation of the substrate of γ-secretase
    • Zhang, L., Song, L., and Parker, E. (1999) Calpain inhibitor I increases β-amyloid peptide production by inhibiting the degradation of the substrate of γ-secretase, J. Biol. Chem. 274, 8966-8972.
    • (1999) J. Biol. Chem. , vol.274 , pp. 8966-8972
    • Zhang, L.1    Song, L.2    Parker, E.3
  • 28
    • 0033616590 scopus 로고    scopus 로고
    • Unusual phenotypic alteration of β-amyloid precursor protein (βAPP) maturation by a new Val-715 → Met βAPP-770 mutation responsible for probable early-onset Alzheimer's disease
    • Ancolio, K., Dumanchin, C., Barelli, H., Warter, J. M., Brice, A., Campion, D., Frebourg, T., and Checler, F. (1999) Unusual phenotypic alteration of β-amyloid precursor protein (βAPP) maturation by a new Val-715 → Met βAPP-770 mutation responsible for probable early-onset Alzheimer's disease, Proc. Natl. Acad. Sci. U.S.A. 96, 4119-4124.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 4119-4124
    • Ancolio, K.1    Dumanchin, C.2    Barelli, H.3    Warter, J.M.4    Brice, A.5    Campion, D.6    Frebourg, T.7    Checler, F.8
  • 29
    • 0037184062 scopus 로고    scopus 로고
    • Presenilin 1 mutations activate γ 42-secretase but reciprocally inhibit ε-secretase cleavage of amyloid precursor protein (APP) and S3-cleavage of notch
    • Chen, F., Gu, Y., Hasegawa, H., Ruan, X., Arawaka, S., Fraser, P., Westaway, D., Mount, H. T., and St. George-Hyslop, P. (2002) Presenilin 1 mutations activate γ 42-secretase but reciprocally inhibit ε-secretase cleavage of amyloid precursor protein (APP) and S3-cleavage of notch, J. Biol. Chem. 277, 36521-36526.
    • (2002) J. Biol. Chem. , vol.277 , pp. 36521-36526
    • Chen, F.1    Gu, Y.2    Hasegawa, H.3    Ruan, X.4    Arawaka, S.5    Fraser, P.6    Westaway, D.7    Mount, H.T.8    St. George-Hyslop, P.9
  • 30
    • 0037117314 scopus 로고    scopus 로고
    • FAD-linked mutations in presenilin 1 alter the length of Aβ peptides derived from βAPP transmembrane domain mutants
    • Murphy, M. P., Uljon, S. N., Golde, T. E., and Wang, R. (2002) FAD-linked mutations in presenilin 1 alter the length of Aβ peptides derived from βAPP transmembrane domain mutants, Biochim. Biophys. Acta 1586, 199-209.
    • (2002) Biochim. Biophys. Acta , vol.1586 , pp. 199-209
    • Murphy, M.P.1    Uljon, S.N.2    Golde, T.E.3    Wang, R.4
  • 36
    • 4444264297 scopus 로고    scopus 로고
    • Selective reconstitution and recovery of functional γ-secretase complex on budded baculovirus particles
    • Hayashi, I., Urano, Y., Fukuda, R., Isoo, N., Kodama, T., Hamakubo, T., Tomita, T., and Iwatsubo, T. (2004) Selective reconstitution and recovery of functional γ-secretase complex on budded baculovirus particles, J. Biol. Chem. 279, 38040-38046.
    • (2004) J. Biol. Chem. , vol.279 , pp. 38040-38046
    • Hayashi, I.1    Urano, Y.2    Fukuda, R.3    Isoo, N.4    Kodama, T.5    Hamakubo, T.6    Tomita, T.7    Iwatsubo, T.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.