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Volumn 1, Issue , 2004, Pages 132-133

Yapsin 2

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EID: 84944031120     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1016/B978-0-12-079611-3.50042-2     Document Type: Chapter
Times cited : (1)

References (8)
  • 1
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    • J. Ash, M. Dominguez, J.J. Bergeron, D.Y. Thomas and Y. Bourbonnais (1995) The yeast proprotein convertase encoded by YAP3 is a glycophosphatidylinositol-anchored protein that localizes to the plasma membrane. J. Biol. Chem. 270 20847-20854.
    • (1995) J. Biol. Chem. , vol.270 , pp. 20847-20854
    • Ash, J.1    Dominguez, M.2    Bergeron, J.J.3    Thomas, D.Y.4    Bourbonnais, Y.5
  • 2
    • 0029016869 scopus 로고
    • Secretion of yeast aspartic protease 3 is regulated by its carboxyterminal tail: characterization of secreted YAP3p
    • N.X. Cawley, M. Wong, L.P. Pu, W. Tam and Y.P. Loh (1995) Secretion of yeast aspartic protease 3 is regulated by its carboxyterminal tail: characterization of secreted YAP3p. Biochemistry 34 7430-7437.
    • (1995) Biochemistry , vol.34 , pp. 7430-7437
    • Cawley, N.X.1    Wong, M.2    Pu, L.P.3    Tam, W.4    Loh, Y.P.5
  • 3
    • 0032521638 scopus 로고    scopus 로고
    • Expression, processing and secretion of a proteolytically-sensitive insect diuretic hormone by Saccharomyces cerevisiae requires the use of a yeast strain lacking genes encoding the Yap3 and Mkc7 endoproteases found in the secretory pathway
    • K.S. Copley, S.M. Alm, D.A. Schooley and W.E. Courchesne (1998) Expression, processing and secretion of a proteolytically-sensitive insect diuretic hormone by Saccharomyces cerevisiae requires the use of a yeast strain lacking genes encoding the Yap3 and Mkc7 endoproteases found in the secretory pathway. Biochem. J. 330 1333-1340.
    • (1998) Biochem. J. , vol.330 , pp. 1333-1340
    • Copley, K.S.1    Alm, S.M.2    Schooley, D.A.3    Courchesne, W.E.4
  • 4
    • 0025394708 scopus 로고
    • A novel aspartyl protease allowing KEX2-independent MFα propheromone processing in yeast
    • M. Egel-Mitani, H.P. Flygenring and M.T. Hansen (1990) A novel aspartyl protease allowing KEX2-independent MFα propheromone processing in yeast. Yeast 6 127-137.
    • (1990) Yeast , vol.6 , pp. 127-137
    • Egel-Mitani, M.1    Flygenring, H.P.2    Hansen, M.T.3
  • 5
    • 0028848292 scopus 로고
    • Shared functions in vivo of a glycosyl-phosphatidylinositol-linked aspartyl protease, Mkc7, and the proprotein-processing protease Kex2 in yeast
    • H. Komano and R.S. Fuller (1995) Shared functions in vivo of a glycosyl-phosphatidylinositol-linked aspartyl protease, Mkc7, and the proprotein-processing protease Kex2 in yeast. Proc. Natl. Acad. Sci. USA 92 10752-10756.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 10752-10756
    • Komano, H.1    Fuller, R.S.2
  • 6
    • 0033610816 scopus 로고    scopus 로고
    • Involvement of cell surface glycosylphosphatidylinositol-linked aspartyl proteases in α-secretase type cleavage and ectodomain solubilization of human Alzheimer β-amyloid precursor protein in yeast
    • H. Komano, M. Seeger, S.E. Gandy, G.T. Wang, G.A. Krafft and R.S. Fuller (1998) Involvement of cell surface glycosylphosphatidylinositol-linked aspartyl proteases in α-secretase type cleavage and ectodomain solubilization of human Alzheimer β-amyloid precursor protein in yeast. J. Biol. Chem. 273 31648-31651.
    • (1998) J. Biol. Chem. , vol.273 , pp. 31648-31651
    • Komano, H.1    Seeger, M.2    Gandy, S.E.3    Wang, G.T.4    Krafft, G.A.5    Fuller, R.S.6
  • 7
    • 0033588223 scopus 로고    scopus 로고
    • Purification and characterization of the yeast GPI-anchored, monobasic-specific aspartyl protease yapsin 2 (Mkc7p)
    • H. Komano, N. Rockwell, G. Wang, G. Krafft and R.S. Fuller (1999) Purification and characterization of the yeast GPI-anchored, monobasic-specific aspartyl protease yapsin 2 (Mkc7p). J. Biol. Chem. 274 24431-24437.
    • (1999) J. Biol. Chem. , vol.274 , pp. 24431-24437
    • Komano, H.1    Rockwell, N.2    Wang, G.3    Krafft, G.4    Fuller, R.S.5
  • 8
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    • Characterization of beta-amyloid peptide precursor processing by the yeast Yap3 and Mkc7 proteases
    • W. Zhang, D. Espinoza, V. Hines, M. Innis, P. Mehta and D.L. Miller (1997) Characterization of beta-amyloid peptide precursor processing by the yeast Yap3 and Mkc7 proteases. Biochim. Biophys. Acta 1359 110-122.
    • (1997) Biochim. Biophys. Acta , vol.1359 , pp. 110-122
    • Zhang, W.1    Espinoza, D.2    Hines, V.3    Innis, M.4    Mehta, P.5    Miller, D.L.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.