메뉴 건너뛰기




Volumn 99, Issue 5, 2006, Pages 1403-1412

Ubiquitin-proteasome pathway mediates degradation of APH-1

Author keywords

secretase; Alzheimer's disease; Anterior pharynx defective 1; Proteasome; Ubiquitin

Indexed keywords

AMYLOID BETA PROTEIN; ANTERIOR PHARYNX DEFECTIVE 1 PROTEIN; BENZYLOXYCARBONYLLEUCYLLEUCYLLEUCINAL; GAMMA SECRETASE; LACTACYSTIN; PROTEASOME; PROTEASOME INHIBITOR; UBIQUITIN;

EID: 33750927699     PISSN: 00223042     EISSN: 14714159     Source Type: Journal    
DOI: 10.1111/j.1471-4159.2006.04184.x     Document Type: Article
Times cited : (25)

References (59)
  • 1
    • 1642336602 scopus 로고    scopus 로고
    • Pen-2 is sequestered in the endoplasmic reticulum and subjected to ubiquitylation and proteasome-mediated degradation in the absence of presenilin
    • Bergman A., Hansson E. M., Pursglove S. E., Farmery M. R., Lannfelt L., Lendahl U., Lundkvist J. and Naslund J. (2004) Pen-2 is sequestered in the endoplasmic reticulum and subjected to ubiquitylation and proteasome-mediated degradation in the absence of presenilin. J. Biol. Chem. 279, 16 744-16 753.
    • (2004) J. Biol. Chem. , vol.279 , pp. 16744-16753
    • Bergman, A.1    Hansson, E.M.2    Pursglove, S.E.3    Farmery, M.R.4    Lannfelt, L.5    Lendahl, U.6    Lundkvist, J.7    Naslund, J.8
  • 5
    • 0033535504 scopus 로고    scopus 로고
    • A presenilin-1-dependent γ-secretase-like protease mediates release of Notch intracellular domain
    • De Strooper B., Annaert W., Cupers P. et al. (1999) A presenilin-1-dependent γ-secretase-like protease mediates release of Notch intracellular domain. Nature 398, 518-522.
    • (1999) Nature , vol.398 , pp. 518-522
    • De Strooper, B.1    Annaert, W.2    Cupers, P.3
  • 7
    • 33644781725 scopus 로고    scopus 로고
    • Catabolism of endogenous and overexpressed APH1a and PEN2: Evidence for artifactual involvement of the proteasome in the degradation of overexpressed proteins
    • Dunys J., Kawarai T., Wilk S., St George-Hyslop P., Alves da Costa C. and Checler F. (2006) Catabolism of endogenous and overexpressed APH1a and PEN2: evidence for artifactual involvement of the proteasome in the degradation of overexpressed proteins. Biochem. J. 394, 501-509.
    • (2006) Biochem. J. , vol.394 , pp. 501-509
    • Dunys, J.1    Kawarai, T.2    Wilk, S.3    St George-Hyslop, P.4    Alves Da Costa, C.5    Checler, F.6
  • 9
    • 0029033981 scopus 로고
    • Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin
    • Fenteany G., Standaert R. F., Lane W. S., Choi S., Corey E. J. and Schreiber S. L. (1995) Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin. Science 268, 726-731.
    • (1995) Science , vol.268 , pp. 726-731
    • Fenteany, G.1    Standaert, R.F.2    Lane, W.S.3    Choi, S.4    Corey, E.J.5    Schreiber, S.L.6
  • 10
    • 0942298101 scopus 로고    scopus 로고
    • Membrane topology and nicastrin-enhanced endoproteolysis of APH-1, a component of the γ-secretase complex
    • Fortna R. R., Crystal A. S., Morais V. A., Pijak D. S., Lee V. M. and Doms R. W. (2004) Membrane topology and nicastrin-enhanced endoproteolysis of APH-1, a component of the γ-secretase complex. J. Biol. Chem. 279, 3685-3693.
    • (2004) J. Biol. Chem. , vol.279 , pp. 3685-3693
    • Fortna, R.R.1    Crystal, A.S.2    Morais, V.A.3    Pijak, D.S.4    Lee, V.M.5    Doms, R.W.6
  • 11
    • 18444417998 scopus 로고    scopus 로고
    • aph-1 and pen-2 are required for Notch pathway signaling, γ-secretase cleavage of βAPP, and presenilin protein accumulation
    • Francis R., McGrath G., Zhang J. et al. (2002) aph-1 and pen-2 are required for Notch pathway signaling, γ-secretase cleavage of βAPP, and presenilin protein accumulation. Dev. Cell 3, 85-97.
    • (2002) Dev. Cell , vol.3 , pp. 85-97
    • Francis, R.1    McGrath, G.2    Zhang, J.3
  • 13
    • 0021256895 scopus 로고
    • Alzheimer's disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid protein
    • Glenner G. G. and Wong C. W. (1984) Alzheimer's disease: initial report of the purification and characterization of a novel cerebrovascular amyloid protein. Biochem. Biophys. Res. Commun. 120, 885-890.
    • (1984) Biochem. Biophys. Res. Commun. , vol.120 , pp. 885-890
    • Glenner, G.G.1    Wong, C.W.2
  • 14
    • 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. USA 99, 775-779.
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 775-779
    • Goutte, C.1    Tsunozaki, M.2    Hale, V.A.3    Priess, J.R.4
  • 15
    • 0037470037 scopus 로고    scopus 로고
    • APH-1 interacts with mature and immature forms of presenilins and nicastrin and may play a role in maturation of presenilin-nicastrin complexes
    • Gu Y., Chen F., Sanjo N. et al. (2003) APH-1 interacts with mature and immature forms of presenilins and nicastrin and may play a role in maturation of presenilin-nicastrin complexes. J. Biol. Chem. 278, 7374-7380.
    • (2003) J. Biol. Chem. , vol.278 , pp. 7374-7380
    • Gu, Y.1    Chen, F.2    Sanjo, N.3
  • 18
    • 0038360879 scopus 로고    scopus 로고
    • Different cofactor activities in γ-secretase assembly: Evidence for a nicastrin-Aph-1 subcomplex
    • Hu Y. and Fortini M. E. (2003) Different cofactor activities in γ-secretase assembly: evidence for a nicastrin-Aph-1 subcomplex. J. Cell Biol. 161, 685-690.
    • (2003) J. Cell Biol. , vol.161 , pp. 685-690
    • Hu, Y.1    Fortini, M.E.2
  • 19
    • 0036007117 scopus 로고    scopus 로고
    • Nicastrin is required for γ-secretase cleavage of the Drosophila Notch receptor
    • Hu Y., Ye Y. and Fortini M. E. (2002) Nicastrin is required for γ-secretase cleavage of the Drosophila Notch receptor. Dev. Cell 2, 69-78.
    • (2002) Dev. Cell , vol.2 , pp. 69-78
    • Hu, Y.1    Ye, Y.2    Fortini, M.E.3
  • 20
    • 0037424348 scopus 로고    scopus 로고
    • The Notch ligands, Δ1 and Jagged2, are substrates for presenilin-dependent 'γ-secretase' cleavage
    • Ikeuchi T. and Sisodia S. S. (2003) The Notch ligands, Δ1 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
  • 21
    • 0037381710 scopus 로고    scopus 로고
    • Proteasome inhibition by paired helical filament-tau in brains of patients with Alzheimer's disease
    • Keck S., Nitsch R., Grune T. and Ullrich O. (2003) Proteasome inhibition by paired helical filament-tau in brains of patients with Alzheimer's disease. J. Neurochem. 85, 115-122.
    • (2003) J. Neurochem. , vol.85 , pp. 115-122
    • Keck, S.1    Nitsch, R.2    Grune, T.3    Ullrich, O.4
  • 22
    • 0037146553 scopus 로고    scopus 로고
    • Nectin-1α, an immunoglobulin-like receptor involved in the formation of synapses, is a substrate for presenilin/γ-secretase-like cleavage
    • Kim D. Y., Ingano L. A. and Kovacs D. M. (2002) Nectin-1α, an immunoglobulin-like receptor involved in the formation of synapses, is a substrate for presenilin/γ-secretase-like cleavage. J. Biol. Chem. 277, 49 976-49 981.
    • (2002) J. Biol. Chem. , vol.277 , pp. 49976-49981
    • Kim, D.Y.1    Ingano, L.A.2    Kovacs, D.M.3
  • 23
    • 0141483380 scopus 로고    scopus 로고
    • Regulated hyperaccumulation of presenilin-1 and the 'γ-secretase' complex. Evidence for differential intramembranous processing of transmembrane subatrates
    • Kim S. H., Ikeuchi T., Yu C. and Sisodia S. S. (2003) Regulated hyperaccumulation of presenilin-1 and the 'γ-secretase' complex. Evidence for differential intramembranous processing of transmembrane subatrates. J. Biol. Chem. 278, 33 992-34 002.
    • (2003) J. Biol. Chem. , vol.278 , pp. 33992-34002
    • Kim, S.H.1    Ikeuchi, T.2    Yu, C.3    Sisodia, S.S.4
  • 24
    • 0030890399 scopus 로고    scopus 로고
    • Endoproteolytic cleavage and proteasomal degradation of presenilin 2 in transfected cells
    • Kim T. W., Pettingell W. H., Hallmark O. G., Moir R. D., Wasco W. and Tanzi R. E. (1997) Endoproteolytic cleavage and proteasomal degradation of presenilin 2 in transfected cells. J. Biol. Chem. 272, 11 006-11 010.
    • (1997) J. Biol. Chem. , vol.272 , pp. 11006-11010
    • Kim, T.W.1    Pettingell, W.H.2    Hallmark, O.G.3    Moir, R.D.4    Wasco, W.5    Tanzi, R.E.6
  • 26
    • 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., Capell 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    Capell, A.5    Zimmer, A.K.6    Edbauer, D.7    Walter, J.8    Steiner, H.9    Haass, C.10
  • 27
    • 0141817915 scopus 로고    scopus 로고
    • The Notch ligands, Jagged and Δ, are sequentially processed by α-secretase and presenilin/γ-secretase and release signaling fragments
    • LaVoie M. J. and Selkoe D. J. (2003) The Notch ligands, Jagged and Δ, are sequentially processed by α-secretase and presenilin/γ-secretase and release signaling fragments. J. Biol. Chem. 278, 34 427-34 437.
    • (2003) J. Biol. Chem. , vol.278 , pp. 34427-34437
    • LaVoie, M.J.1    Selkoe, D.J.2
  • 28
    • 0141733241 scopus 로고    scopus 로고
    • Assembly of the γ-secretase complex involves early formation of an intermediate subcomplex of Aph-1 and nicastrin
    • LaVoie M. J., Fraering P. C., Ostaszewski B. L., Ye W., Kimberly W. T., Wolfe M. S. and Selkoe D. J. (2003) Assembly of the γ-secretase complex involves early formation of an intermediate subcomplex of Aph-1 and nicastrin. J. Biol. Chem. 278, 37 213-37 222.
    • (2003) J. Biol. Chem. , vol.278 , pp. 37213-37222
    • Lavoie, M.J.1    Fraering, P.C.2    Ostaszewski, B.L.3    Ye, W.4    Kimberly, W.T.5    Wolfe, M.S.6    Selkoe, D.J.7
  • 29
    • 0037160063 scopus 로고    scopus 로고
    • Mammalian APH-1 interacts with presenilin and nicastrin and is required for intramembrane proteolysis of amyloid-β precursor protein and Notch
    • Lee S. F., Shah S., Li H., Yu C., Han W. and Yu G. (2002) Mammalian APH-1 interacts with presenilin and nicastrin and is required for intramembrane proteolysis of amyloid-β precursor protein and Notch. J. Biol. Chem. 277, 45 013-45 019.
    • (2002) J. Biol. Chem. , vol.277 , pp. 45013-45019
    • Lee, S.F.1    Shah, S.2    Li, H.3    Yu, C.4    Han, W.5    Yu, G.6
  • 30
    • 10744223903 scopus 로고    scopus 로고
    • A conserved GXXXG motif in APH-1 is critical for assembly and activity of the γ-secretase complex
    • Lee S. F., Shah S., Yu C. et al. (2004) A conserved GXXXG motif in APH-1 is critical for assembly and activity of the γ-secretase complex. J. Biol. Chem. 279, 4144-4152.
    • (2004) J. Biol. Chem. , vol.279 , pp. 4144-4152
    • Lee, S.F.1    Shah, S.2    Yu, C.3
  • 31
    • 6844258835 scopus 로고    scopus 로고
    • Frameshift mutants of b amyloid precursor protein and ubiquitin-B in Alzheimer's and Down's syndrome patients
    • van Leeuwen F. W., de Kleijn D. P., van den Hurk H. H. et al. (1998) Frameshift mutants of b amyloid precursor protein and ubiquitin-B in Alzheimer's and Down's syndrome patients. Science 279, 242-247.
    • (1998) Science , vol.279 , pp. 242-247
    • Van Leeuwen, F.W.1    De Kleijn, D.P.2    Van Den Hurk, H.H.3
  • 32
    • 0035894534 scopus 로고    scopus 로고
    • APH-2/nicastrin functions in LIN-12/Notch signaling in the Caenorhabditis elegans somatic gonad
    • Levitan D., Yu G., St George Hyslop P. and Goutte C. (2001a) APH-2/nicastrin functions in LIN-12/Notch signaling in the Caenorhabditis elegans somatic gonad. Dev Biol. 240, 654-661.
    • (2001) Dev Biol. , vol.240 , pp. 654-661
    • Levitan, D.1    Yu, G.2    St George Hyslop, P.3    Goutte, C.4
  • 33
    • 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. (2001b) PS1 N- and C-terminal fragments form a complex that functions in APP processing and Notch signaling. Proc. Natl Acad. Sci. USA 98, 12 186-12 190.
    • (2001) Proc. Natl Acad. Sci. USA , 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
  • 35
    • 18344380083 scopus 로고    scopus 로고
    • A presenilin-1/γ-secretase cleavage releases the E-cadherin intracellular domain and regulates disassembly of adherens junctions
    • Marambaud P., Shioi J., Serban G. et al. (2002) A presenilin-1/γ- secretase cleavage releases the E-cadherin intracellular domain and regulates disassembly of adherens junctions. EMBO J. 21, 1948-1956.
    • (2002) EMBO J. , vol.21 , pp. 1948-1956
    • Marambaud, P.1    Shioi, J.2    Serban, G.3
  • 36
    • 0141429160 scopus 로고    scopus 로고
    • A CBP binding transcriptional repressor produced by the PS1/epsilon-cleavage of N-cadherin is inhibited by PS1 FAD mutations
    • Marambaud P., Wen P. H., Dutt A., Shioi J., Takashima A., Siman R. and Robakis N. K. (2003) A CBP binding transcriptional repressor produced by the PS1/epsilon-cleavage of N-cadherin is inhibited by PS1 FAD mutations. Cell 114, 635-645.
    • (2003) Cell , vol.114 , pp. 635-645
    • Marambaud, P.1    Wen, P.H.2    Dutt, A.3    Shioi, J.4    Takashima, A.5    Siman, R.6    Robakis, N.K.7
  • 39
    • 0037166319 scopus 로고    scopus 로고
    • Proteolytic processing of low-density lipoprotein receptor-related protein mediates regulated release of its intracellular domain
    • May P., Reddy Y. K. and Herz J. (2002) Proteolytic processing of low-density lipoprotein receptor-related protein mediates regulated release of its intracellular domain. J. Biol. Chem. 277, 18 736-18 743.
    • (2002) J. Biol. Chem. , vol.277 , pp. 18736-18743
    • May, P.1    Reddy, Y.K.2    Herz, J.3
  • 40
    • 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
  • 41
    • 16844364135 scopus 로고    scopus 로고
    • Aph-1 contributes to the stabilization and trafficking of the γ-secretase complex through mechanisms involving intermolecular and intramolecular interactions
    • Niimura M., Isoo N., Takasugi N., Tsuruoka M., Ui-Tei K., Saigo K., Morohashi Y., Tomita T. and Iwatsubo T. (2005) Aph-1 contributes to the stabilization and trafficking of the γ-secretase complex through mechanisms involving intermolecular and intramolecular interactions. J. Biol. Chem. 280, 12 967-12 975.
    • (2005) J. Biol. Chem. , vol.280 , pp. 12967-12975
    • Niimura, M.1    Isoo, N.2    Takasugi, N.3    Tsuruoka, M.4    Ui-Tei, K.5    Saigo, K.6    Morohashi, Y.7    Tomita, T.8    Iwatsubo, T.9
  • 42
    • 0034797234 scopus 로고    scopus 로고
    • The C-terminal fragment of the Alzheimer's disease amyloid protein precursor is degraded by a proteasome-dependent mechanism distinct from γ-secretase
    • Nunan J., Shearman M. S., Checler F., Cappai R., Evin G., Beyreuther K., Masters C. L. and Small D. H. (2001) The C-terminal fragment of the Alzheimer's disease amyloid protein precursor is degraded by a proteasome-dependent mechanism distinct from γ-secretase. Eur. J. Biochem. 268, 5329-5336.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 5329-5336
    • Nunan, J.1    Shearman, M.S.2    Checler, F.3    Cappai, R.4    Evin, G.5    Beyreuther, K.6    Masters, C.L.7    Small, D.H.8
  • 43
    • 0242330370 scopus 로고    scopus 로고
    • Proteasome-mediated degradation of the C-terminus of the Alzheimer's disease β-amyloid protein precursor: Effect of C-terminal truncation on production of β-amyloid protein
    • Nunan J., Williamson N. A., Hill A. F., Sernee M. F., Masters C. L. and Small D. H. (2003) Proteasome-mediated degradation of the C-terminus of the Alzheimer's disease β-amyloid protein precursor: effect of C-terminal truncation on production of β-amyloid protein. J. Neurosci. Res. 74, 378-385.
    • (2003) J. Neurosci. Res. , vol.74 , pp. 378-385
    • Nunan, J.1    Williamson, N.A.2    Hill, A.F.3    Sernee, M.F.4    Masters, C.L.5    Small, D.H.6
  • 44
    • 7444250507 scopus 로고    scopus 로고
    • Degradation of BACE by the ubiquitin-proteasome pathway
    • Qing H., Zhou W., Christensen M. A., Sun X., Tong Y. and Song W. (2004) Degradation of BACE by the ubiquitin-proteasome pathway. FASEB J. 18, 1571-1573.
    • (2004) FASEB J. , vol.18 , pp. 1571-1573
    • Qing, H.1    Zhou, W.2    Christensen, M.A.3    Sun, X.4    Tong, Y.5    Song, W.6
  • 45
    • 0027980319 scopus 로고
    • Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules
    • Rock K. L., Gramm C., Rothstein L., Clark K., Stein R., Dick L., Hwang D. and Goldberg A. L. (1994) Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules. Cell 78, 761-771.
    • (1994) Cell , vol.78 , pp. 761-771
    • Rock, K.L.1    Gramm, C.2    Rothstein, L.3    Clark, K.4    Stein, R.5    Dick, L.6    Hwang, D.7    Goldberg, A.L.8
  • 46
    • 0242331600 scopus 로고    scopus 로고
    • A presenilin dimer at the core of the γ-secretase enzyme: Insights from parallel analysis of Notch 1 and APP proteolysis
    • Schroeter E. H., Ilagan M. X., Brunkan A. L. et al. (2003) A presenilin dimer at the core of the γ-secretase enzyme: insights from parallel analysis of Notch 1 and APP proteolysis. Proc. Natl Acad. Sci. USA 100, 13 075-13 080.
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 13075-13080
    • Schroeter, E.H.1    Ilagan, M.X.2    Brunkan, A.L.3
  • 48
    • 4744375540 scopus 로고    scopus 로고
    • Identification of distinct γ-secretase complexes with different APH-1 variants
    • Shirotani K., Edbauer D., Prokop S., Haass C. and Steiner H. (2004) Identification of distinct γ-secretase complexes with different APH-1 variants. J. Biol. Chem. 279, 41 340-41 345.
    • (2004) J. Biol. Chem. , vol.279 , pp. 41340-41345
    • Shirotani, K.1    Edbauer, D.2    Prokop, S.3    Haass, C.4    Steiner, H.5
  • 50
    • 0034142022 scopus 로고    scopus 로고
    • A distinct ER/IC γ-secretase competes with the proteasome for cleavage of APP
    • Skovronsky D. M., Pijak D. S., Doms R. W. and Lee V. M. (2000) A distinct ER/IC γ-secretase competes with the proteasome for cleavage of APP. Biochemistry 39, 810-817.
    • (2000) Biochemistry , vol.39 , pp. 810-817
    • Skovronsky, D.M.1    Pijak, D.S.2    Doms, R.W.3    Lee, V.M.4
  • 51
    • 0033536072 scopus 로고    scopus 로고
    • Proteolytic release and nuclear translocation of Notch-1 are induced by presenilin-1 and impaired by pathogenic presenilin-1 mutations
    • Song W., Nadeau P., Yuan M., Yang X., Shen J. and Yankner B. A. (1999) Proteolytic release and nuclear translocation of Notch-1 are induced by presenilin-1 and impaired by pathogenic presenilin-1 mutations. Proc. Natl Acad. Sci. USA 96, 6959-6963.
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 6959-6963
    • Song, W.1    Nadeau, P.2    Yuan, M.3    Yang, X.4    Shen, J.5    Yankner, B.A.6
  • 52
    • 0037131218 scopus 로고    scopus 로고
    • PEN-2 is an integral component of the γ-secretase complex required for coordinated expression of presenilin and nicastrin
    • Steiner H., Winkler E., Edbauer D., Prokop S., Basset G., Yamasaki A., Kostka M. and Haass C. (2002) PEN-2 is an integral component of the γ-secretase complex required for coordinated expression of presenilin and nicastrin. J. Biol. Chem. 277, 39 062-39 065.
    • (2002) J. Biol. Chem. , vol.277 , pp. 39062-39065
    • Steiner, H.1    Winkler, E.2    Edbauer, D.3    Prokop, S.4    Basset, G.5    Yamasaki, A.6    Kostka, M.7    Haass, C.8
  • 54
    • 0034617297 scopus 로고    scopus 로고
    • Inhibiting amyloid precursor protein C-terminal cleavage promotes an interaction with presenilin 1
    • Verdile G., Martins R. N., Duthie M., Holmes E., St George-Hyslop P. H. and Fraser P. E. (2000) Inhibiting amyloid precursor protein C-terminal cleavage promotes an interaction with presenilin 1. J. Biol. Chem. 275, 20 794-20 798.
    • (2000) J. Biol. Chem. , vol.275 , pp. 20794-20798
    • Verdile, G.1    Martins, R.N.2    Duthie, M.3    Holmes, E.4    St George-Hyslop, P.H.5    Fraser, P.E.6
  • 55
    • 0035292759 scopus 로고    scopus 로고
    • Themes and variations on ubiquitylation
    • Weissman A. M. (2001) Themes and variations on ubiquitylation. Nat. Rev. Mol. Cell Biol. 2, 169-178.
    • (2001) Nat. Rev. Mol. Cell Biol. , vol.2 , pp. 169-178
    • Weissman, A.M.1
  • 56
    • 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
  • 57
    • 0034618715 scopus 로고    scopus 로고
    • Nicastrin modulates presenilin-mediated notch/glp-1 signal transduction and βAPP processing
    • Yu G., Nishimura M., Arawaka S. et al. (2000) Nicastrin modulates presenilin-mediated notch/glp-1 signal transduction and βAPP processing. Nature 407, 48-54.
    • (2000) Nature , vol.407 , pp. 48-54
    • Yu, G.1    Nishimura, M.2    Arawaka, S.3
  • 58
    • 20444472743 scopus 로고    scopus 로고
    • Nicastrin is critical for stability and trafficking but not association of other presenilin/γ-secretase components
    • Zhang Y. W., Luo W. J., Wang H. et al. (2005) Nicastrin is critical for stability and trafficking but not association of other presenilin/γ- secretase components. J. Biol. Chem. 280, 17 020-17 026.
    • (2005) J. Biol. Chem. , vol.280 , pp. 17020-17026
    • Zhang, Y.W.1    Luo, W.J.2    Wang, H.3
  • 59
    • 0033779635 scopus 로고    scopus 로고
    • Presenilins are required for γ-secretase cleavage of β-APP and transmembrane cleavage of Notch-1
    • Zhang Z., Nadeau P., Song W., Donoviel D., Yuan M., Bernstein A. and Yankner B. A. (2000) Presenilins are required for γ-secretase cleavage of β-APP and transmembrane cleavage of Notch-1. Nat. Cell Biol. 2, 463-465.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 463-465
    • Zhang, Z.1    Nadeau, P.2    Song, W.3    Donoviel, D.4    Yuan, M.5    Bernstein, A.6    Yankner, B.A.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.