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Volumn 21, Issue 20, 2002, Pages 5408-5416

Presenilins mediate a dual intramembranous γ-secretase cleavage of Notch-1

Author keywords

Notch signaling; Notch 1 peptide; Presenilin; Site 4 cleavage; secretase

Indexed keywords

AMYLOID BETA PROTEIN; GAMMA SECRETASE; NOTCH RECEPTOR; PRESENILIN 1;

EID: 18644367748     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/cdf541     Document Type: Article
Times cited : (209)

References (57)
  • 1
    • 0035977071 scopus 로고    scopus 로고
    • Pharmacological knock-down of the presenilin 1 heterodimer by a novel γ-secretase inhibitor: Implications for presenilin biology
    • Beher, D., Wrigley, J.D., Nadin, A., Evin, G., Masters, C.L., Harrison, T., Castro, J.L. and Shearman, M.S. (2001) Pharmacological knock-down of the presenilin 1 heterodimer by a novel γ-secretase inhibitor: Implications for presenilin biology. J. Biol. Chem., 276, 45394-45402.
    • (2001) J. Biol. Chem , vol.276 , pp. 45394-45402
    • Beher, D.1    Wrigley, J.D.2    Nadin, A.3    Evin, G.4    Masters, C.L.5    Harrison, T.6    Castro, J.L.7    Shearman, M.S.8
  • 2
    • 0033868818 scopus 로고    scopus 로고
    • A novel proteolytic cleavage involved in Notch signaling: The role of the disintegrin-metalloprotease TACE
    • Brou, C. et al. (2000) A novel proteolytic cleavage involved in Notch signaling: The role of the disintegrin-metalloprotease TACE. Mol. Cell, 5, 207-216.
    • (2000) Mol. Cell , vol.5 , pp. 207-216
    • Brou, C.1
  • 3
    • 0035816661 scopus 로고    scopus 로고
    • A transcriptionally active complex of APP with Fe65 and histone acetyltransferase Tip60
    • Cao, X. and Sudhof, T.C (2001) A transcriptionally active complex of APP with Fe65 and histone acetyltransferase Tip60. Science, 293, 115-120.
    • (2001) Science , vol.293 , pp. 115-120
    • Cao, X.1    Sudhof, T.C.2
  • 4
    • 0033783140 scopus 로고    scopus 로고
    • Presenilin-1 differentially facilitates endoproteolysis of the β-amyloid precursor protein and Notch
    • Capell, A., Steiner, H., Romig, H., Keck, S., Baader, M., Grim, M.G., Baumeister, R. and Haass, C. (2000) Presenilin-1 differentially facilitates endoproteolysis of the β-amyloid precursor protein and Notch. Nat. Cell Biol., 2, 205-211.
    • (2000) Nat. Cell Biol , vol.2 , pp. 205-211
    • Capell, A.1    Steiner, H.2    Romig, H.3    Keck, S.4    Baader, M.5    Grim, M.G.6    Baumeister, R.7    Haass, C.8
  • 5
    • 0035204206 scopus 로고    scopus 로고
    • Nicastrin is required for presenilin-mediated transmembrane cleavage in Drosophila
    • Chung, H.M. and Struhl, G. (2001) Nicastrin is required for presenilin-mediated transmembrane cleavage in Drosophila. Nat. Cell Biol., 3, 1129-1132.
    • (2001) Nat. Cell Biol , vol.3 , pp. 1129-1132
    • Chung, H.M.1    Struhl, G.2
  • 6
    • 0034839287 scopus 로고    scopus 로고
    • The amyloid precursor protein (APP)-cytoplasmic fragment generated by γ-secretase is rapidly degraded but distributes partially in a nuclear fraction of neurones in culture
    • Cupers, P., Orlans, I., Craessaerts, K., Annaert, W. and De Strooper, B. (2001) The amyloid precursor protein (APP)-cytoplasmic fragment generated by γ-secretase is rapidly degraded but distributes partially in a nuclear fraction of neurones in culture. J. Neurochem., 78, 1168-1178.
    • (2001) J. Neurochem , vol.78 , pp. 1168-1178
    • Cupers, P.1    Orlans, I.2    Craessaerts, K.3    Annaert, W.4    De Strooper, B.5
  • 8
    • 0033535504 scopus 로고    scopus 로고
    • A presenilin-1-dependent γ-secretase-like protease mediates release of Notch intracellular domain
    • De Strooper, B. 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
  • 9
    • 0037173115 scopus 로고    scopus 로고
    • Presenilin and nicastrin regulate each other and determine amyloid β-peptide production via complex formation
    • Edbauer, D., Winkler, E., Haass, C. and Steiner, H. (2002) Presenilin and nicastrin regulate each other and determine amyloid β-peptide production via complex formation. Proc. Natl. Acad. Sci. USA, 99, 8666-8671.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 8666-8671
    • Edbauer, D.1    Winkler, E.2    Haass, C.3    Steiner, H.4
  • 10
    • 0035943345 scopus 로고    scopus 로고
    • A portrait of Alzheimer secretases-new features and familiar faces
    • Esler, W.P. and Wolfe, M.S. (2001) A portrait of Alzheimer secretases-new features and familiar faces. Science, 293, 1449-1454.
    • (2001) Science , vol.293 , pp. 1449-1454
    • Esler, W.P.1    Wolfe, M.S.2
  • 11
    • 0033780472 scopus 로고    scopus 로고
    • Transition-state analogue inhibitors of γ-secretase bind directly to presenilin-1
    • Esler, W.P. et al. (2000) Transition-state analogue inhibitors of γ-secretase bind directly to presenilin-1. Nat. Cell Biol., 2, 428-434.
    • (2000) Nat. Cell Biol , vol.2 , pp. 428-434
    • Esler, W.P.1
  • 12
    • 84984761772 scopus 로고    scopus 로고
    • Amyloid-lowering isocoumarins are not direct inhibitors of γ-secretase
    • Esler, W.P. et al. (2002a) Amyloid-lowering isocoumarins are not direct inhibitors of γ-secretase. Nat. Cell Biol., 4, 110-111.
    • (2002) Nat. Cell Biol , vol.4 , pp. 110-111
    • Esler, W.P.1
  • 14
    • 0035909901 scopus 로고    scopus 로고
    • The γ-secretase-cleaved C-terminal fragment of amyloid precursor protein mediates signaling to the nucleus
    • Gao, Y. and Pimplikar, S.W. (2001) The γ-secretase-cleaved C-terminal fragment of amyloid precursor protein mediates signaling to the nucleus. Proc. Natl. Acad. Sci. USA, 98, 14979-14984.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 14979-14984
    • Gao, Y.1    Pimplikar, S.W.2
  • 15
    • 0035929554 scopus 로고    scopus 로고
    • Distinct intramembrane cleavage of the β-amyloid precursor protein family resembling γ-secretase-like cleavage of Notch
    • Gu, Y., Misonou, H., Sato, T., Dohmae, N., Takio, K. and Ihara, Y. (2001) Distinct intramembrane cleavage of the β-amyloid precursor protein family resembling γ-secretase-like cleavage of Notch. J. Biol. Chem., 276, 35235-35238.
    • (2001) J. Biol. Chem , vol.276 , pp. 35235-35238
    • Gu, Y.1    Misonou, H.2    Sato, T.3    Dohmae, N.4    Takio, K.5    Ihara, Y.6
  • 16
    • 0027333557 scopus 로고
    • Cellular processing of β-amyloid precursor protein and the genesis of amyloid β-peptide
    • Haass, C. and Selkoe, D.J. (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
    • Haass, C.1    Selkoe, D.J.2
  • 17
    • 0027535111 scopus 로고
    • β-amyloid peptide and a 3-kDa fragment are derived by distinct cellular mechanisms
    • Haass, C., Hung, A.Y., Schlossmacher, M.G., Teplow, D.B. and Selkoe, D.J. (1993) β-amyloid peptide and a 3-kDa fragment are derived by distinct cellular mechanisms. J. Biol. Chem., 268, 3021-3024.
    • (1993) J. Biol. Chem , vol.268 , pp. 3021-3024
    • Haass, C.1    Hung, A.Y.2    Schlossmacher, M.G.3    Teplow, D.B.4    Selkoe, D.J.5
  • 18
    • 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
  • 19
    • 0035955693 scopus 로고    scopus 로고
    • The intracellular domain of the β-amyloid precursor protein is stabilized by Fe65 and translocates to the nucleus in a Notch-like manner
    • Kimberly, W.T., Zheng, J.B., Guenette, S.Y. and Selkoe, D.J. (2001) The intracellular domain of the β-amyloid precursor protein is stabilized by Fe65 and translocates to the nucleus in a Notch-like manner. J. Biol. Chem., 276, 40288-40292.
    • (2001) J. Biol. Chem , vol.276 , pp. 40288-40292
    • Kimberly, W.T.1    Zheng, J.B.2    Guenette, S.Y.3    Selkoe, D.J.4
  • 20
    • 0030003538 scopus 로고    scopus 로고
    • Signal transduction by activated mNotch: Importance of proteolytic processing and its regulation by the extracellular domain
    • Kopan, R., Schroeter, E.H, Weintraub, H. and Nye, J.S. (1996) Signal transduction by activated mNotch: Importance of proteolytic processing and its regulation by the extracellular domain. Proc. Natl. Acad. Sci. USA, 93, 1683-1688.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 1683-1688
    • Kopan, R.1    Schroeter, E.H.2    Weintraub, H.3    Nye, J.S.4
  • 23
    • 0343819757 scopus 로고    scopus 로고
    • Presenilin 1 is linked with γ-secretase activity in the detergent solubilized state
    • Li, Y.M. et al. (2000) Presenilin 1 is linked with γ-secretase activity in the detergent solubilized state. Proc. Natl. Acad. Sci. USA, 97, 6138-6143.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 6138-6143
    • Li, Y.M.1
  • 24
    • 0036007118 scopus 로고    scopus 로고
    • Drosophila nicastrin is essential for the intramembranous cleavage of Notch
    • Lopez-Schier, H. and St Johnston, D. (2002) Drosophila nicastrin is essential for the intramembranous cleavage of Notch. Dev. Cell, 2, 79-89.
    • (2002) Dev. Cell , vol.2 , pp. 79-89
    • Lopez-Schier, H.1    St Johnston, D.2
  • 25
    • 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. 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
  • 27
    • 0037166319 scopus 로고    scopus 로고
    • Proteolytic processing of LRP mediates regulated release of its intracellular domain
    • May, P., Reddy, Y.K. and Herz, J. (2002) Proteolytic processing of LRP mediates regulated release of its intracellular domain. J. Biol. Chem., 277, 18736-18743.
    • (2002) J. Biol. Chem , vol.277 , pp. 18736-18743
    • May, P.1    Reddy, Y.K.2    Herz, J.3
  • 28
    • 0035979241 scopus 로고    scopus 로고
    • Conservation of the biochemical mechanisms of signal transduction among mammalian Notch family members
    • Mizutani, T., Taniguchi, Y., Aoki, T., Hashimoto, N. and Honjo, T. (2001) Conservation of the biochemical mechanisms of signal transduction among mammalian Notch family members. Proc. Natl. Acad. Sci. USA, 98, 9026-9031.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 9026-9031
    • Mizutani, T.1    Taniguchi, Y.2    Aoki, T.3    Hashimoto, N.4    Honjo, T.5
  • 29
    • 18444391830 scopus 로고    scopus 로고
    • Presenilin-I mutations of leucine 166 equally affect the generation of Notch and APP intracellular domains independent of their effect on Aβ42 production
    • Moehlmann, T. et al. (2002) Presenilin-I mutations of leucine 166 equally affect the generation of Notch and APP intracellular domains independent of their effect on Aβ42 production. Proc. Natl. Acad. Sci. USA, 99, 8025-8030.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 8025-8030
    • Moehlmann, T.1
  • 30
    • 0034671686 scopus 로고    scopus 로고
    • Notch signaling: From the outside in
    • Mumm, J.S. and Kopan, R. (2000) Notch signaling: From the outside in. Dev. Biol., 228, 151-165.
    • (2000) Dev. Biol , vol.228 , pp. 151-165
    • Mumm, J.S.1    Kopan, R.2
  • 31
    • 0033867521 scopus 로고    scopus 로고
    • A ligand-induced extracellular cleavage regulates γ-secretase-like proteolytic activation of Notchl
    • Mumm, J.S., Schroeter, E.H., Saxena, M.T., Griesemer, A., Tian, X., Pan, DJ., Ray, W.J. and Kopan, R.A. (2000) A ligand-induced extracellular cleavage regulates γ-secretase-like proteolytic activation of Notchl. Mol. Cell, 5, 197-206.
    • (2000) Mol. Cell , vol.5 , pp. 197-206
    • Mumm, J.S.1    Schroeter, E.H.2    Saxena, M.T.3    Griesemer, A.4    Tian, X.5    Pan, D.J.6    Ray, W.J.7    Kopan, R.A.8
  • 32
    • 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
  • 33
    • 0035956428 scopus 로고    scopus 로고
    • Proteolytic release of CD44 intracellular domain and its role in the CD44 signaling pathway
    • Okamoto, I., Kawano, Y., Murakami, D., Sasayama, T., Araki, N., Miki, T., Wong, A.J. and Saya, H. (2001) Proteolytic release of CD44 intracellular domain and its role in the CD44 signaling pathway. J. Cell Biol., 155, 755-762.
    • (2001) J. Cell Biol , vol.155 , pp. 755-762
    • Okamoto, I.1    Kawano, Y.2    Murakami, D.3    Sasayama, T.4    Araki, N.5    Miki, T.6    Wong, A.J.7    Saya, H.8
  • 34
    • 0034731432 scopus 로고    scopus 로고
    • A loss of function mutant of the presenilin homologue SEL-12 undergoes aberrant endoproteolysis in Caenorhabditis elegans and increases Aβ 42 generation in human cells
    • Okochi, M., Eimer, S., Bottcher, A., Baumeister, R., Romig, H., Walter, J., Capell, A., Steiner, H. and Haass, C. (2000) A loss of function mutant of the presenilin homologue SEL-12 undergoes aberrant endoproteolysis in Caenorhabditis elegans and increases Aβ 42 generation in human cells. J. Biol. Chem., 275, 40925-40932.
    • (2000) J. Biol. Chem , vol.275 , pp. 40925-40932
    • Okochi, M.1    Eimer, S.2    Bottcher, A.3    Baumeister, R.4    Romig, H.5    Walter, J.6    Capell, A.7    Steiner, H.8    Haass, C.9
  • 35
    • 0035005101 scopus 로고    scopus 로고
    • New protease inhibitors prevent γ-secretase-mediated production of Aβ40/42 without affecting Notch cleavage
    • Petit, A., Bihel, F., Alves da Costa, C., Pourquie, O., Checler, F. and Kraus, J.L. (2001) New protease inhibitors prevent γ-secretase-mediated production of Aβ40/42 without affecting Notch cleavage. Nat. Cell Biol., 3, 507-511.
    • (2001) Nat. Cell Biol , vol.3 , pp. 507-511
    • Petit, A.1    Bihel, F.2    Alves da Costa, C.3    Pourquie, O.4    Checler, F.5    Kraus, J.L.6
  • 37
    • 0036290522 scopus 로고    scopus 로고
    • γ-secretase-like cleavages of Notch and βAPP are mutually exclusive in human cells
    • Petit, A., St George-Hyslop, P., Fraser, P. and Checler, F. (2002b) γ-secretase-like cleavages of Notch and βAPP are mutually exclusive in human cells. Biochem. Biophys. Res. Commun., 290, 1408-1410.
    • (2002) Biochem. Biophys. Res. Commun , vol.290 , pp. 1408-1410
    • Petit, A.1    St George-Hyslop, P.2    Fraser, P.3    Checler, F.4
  • 38
    • 0034774969 scopus 로고    scopus 로고
    • Presenilin-dependent γ-secretase processing of β-amyloid precursor protein at a site corresponding to the S3 cleavage of Notch
    • Sastre, M., Steiner, H., Fuchs, K., Capell, A., Multhaup, G., Condron, M.M., Teplow, D.B. and Haass, C. (2001) Presenilin-dependent γ-secretase processing of β-amyloid precursor protein at a site corresponding to the S3 cleavage of Notch. EMBO Rep. 2, 835-841.
    • (2001) EMBO Rep , vol.2 , pp. 835-841
    • Sastre, M.1    Steiner, H.2    Fuchs, K.3    Capell, A.4    Multhaup, G.5    Condron, M.M.6    Teplow, D.B.7    Haass, C.8
  • 39
    • 0035955604 scopus 로고    scopus 로고
    • Murine notch homologs (NI-4) undergo presenilin-dependent proteolysis
    • Saxena, M.T., Schroeter, E.H., Mumm, J.S. and Kopan, R. (2001) Murine notch homologs (NI-4) undergo presenilin-dependent proteolysis. J. Biol. Chem., 276, 40268-40273.
    • (2001) J. Biol. Chem , vol.276 , pp. 40268-40273
    • Saxena, M.T.1    Schroeter, E.H.2    Mumm, J.S.3    Kopan, R.4
  • 40
    • 0032574993 scopus 로고    scopus 로고
    • Notch-I signalling requires ligand-induced proteolytic release of intracellular domain
    • Schroeter, E.H., Kisslinger, J.A. and Kopan, R. (1998) Notch-I 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
  • 41
    • 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
  • 42
    • 0034254585 scopus 로고    scopus 로고
    • L-685, 458, an aspartyl protease transition state mimic, is a potent inhibitor of amyloid β-protein precursor γ-secretase activity
    • Shearman, M.S. et al. (2000) L-685, 458, an aspartyl protease transition state mimic, is a potent inhibitor of amyloid β-protein precursor γ-secretase activity. Biochemistry, 39, 8698-8704.
    • (2000) Biochemistry , vol.39 , pp. 8698-8704
    • Shearman, M.S.1
  • 43
    • 0036548070 scopus 로고    scopus 로고
    • γ-secretase, Notch, Aβ and Alzheimer's disease: Where do the presenilins fit in?
    • Sisodia, S.S. and St George-Hyslop, P.H. (2002) γ-secretase, Notch, Aβ and Alzheimer's disease: Where do the presenilins fit in? Nat. Rev. Neurosci., 3, 281-290.
    • (2002) Nat. Rev. Neurosci , vol.3 , pp. 281-290
    • Sisodia, S.S.1    St George-Hyslop, P.H.2
  • 44
    • 0033536072 scopus 로고    scopus 로고
    • Proteolytic release and nuclear translocation of Notch-I are induced by presenilin-1 and impaired by pathogenic presenilin-I mutations
    • Song, W., Nadeau, P., Yuan, M., Yang, X., Shen, J. and Yankner, B.A. (1999) Proteolytic release and nuclear translocation of Notch-I are induced by presenilin-1 and impaired by pathogenic presenilin-I 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
  • 45
    • 0034568802 scopus 로고    scopus 로고
    • Intramembrane proteolysis by presenilins
    • Steiner, H. and Haass, C. (2000) Intramembrane proteolysis by presenilins. Nat. Rev. Mol. Cell. Biol., 1, 217-224.
    • (2000) Nat. Rev. Mol. Cell. Biol , vol.1 , pp. 217-224
    • Steiner, H.1    Haass, C.2
  • 46
    • 0035173296 scopus 로고    scopus 로고
    • Nuclear signaling: A common function of presenilin substrates?
    • Steiner, H. and Haass, C. (2001) Nuclear signaling: A common function of presenilin substrates? J. Mol. Neurosci., 17, 193-198.
    • (2001) J. Mol. Neurosci , vol.17 , pp. 193-198
    • Steiner, H.1    Haass, C.2
  • 47
    • 0033214070 scopus 로고    scopus 로고
    • A loss of function mutation of presenilin-2 interferes with amyloid β-peptide production and Notch signaling
    • Steiner, H. et al. (1999a) A loss of function mutation of presenilin-2 interferes with amyloid β-peptide production and Notch signaling. J. Biol. Chem., 274, 28669-28673.
    • (1999) J. Biol. Chem , vol.274 , pp. 28669-28673
    • Steiner, H.1
  • 48
    • 0033517844 scopus 로고    scopus 로고
    • Amyloidogenic function of Alzheimer's disease associated presenilin-1 in the absence of endoproteolysis
    • Steiner, H., Romig, H., Pesold, B., Baader, M., Citron, M., Loetscher, H., Jacobsen, H. and Haass, C. (1999b) Amyloidogenic function of Alzheimer's disease associated presenilin-1 in the absence of endoproteolysis. Biochemistry, 38, 14600-14605.
    • (1999) Biochemistry , vol.38 , pp. 14600-14605
    • Steiner, H.1    Romig, H.2    Pesold, B.3    Baader, M.4    Citron, M.5    Loetscher, H.6    Jacobsen, H.7    Haass, C.8
  • 49
    • 0033778262 scopus 로고    scopus 로고
    • Glycine 384 is required for presenilin-1 function and is conserved in bacterial polytopic aspartyl proteases
    • Steiner, H. et al. (2000) Glycine 384 is required for presenilin-1 function and is conserved in bacterial polytopic aspartyl proteases. Nat. Cell Biol., 2, 848-851.
    • (2000) Nat. Cell Biol , vol.2 , pp. 848-851
    • Steiner, H.1
  • 50
    • 0032524325 scopus 로고    scopus 로고
    • Nuclear access and action of Notch in vivo
    • Struhl, G. and Adachi, A. (1998) Nuclear access and action of Notch in vivo. Cell, 93, 649-660.
    • (1998) Cell , vol.93 , pp. 649-660
    • Struhl, G.1    Adachi, A.2
  • 51
    • 0037133688 scopus 로고    scopus 로고
    • Notch receptor cleavage depends on but is not directly executed by presenilins
    • Taniguchi, Y. et al. (2002) Notch receptor cleavage depends on but is not directly executed by presenilins. Proc. Natl. Acad. Sci. USA, 99, 4014-4019.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 4014-4019
    • Taniguchi, Y.1
  • 52
    • 0029752755 scopus 로고    scopus 로고
    • The profile of soluble amyloid β protein in cultured cell media. Detection and quantification of amyloid β protein and variants by immunoprecipitation-mass spectrometry
    • Wang, R., Sweeney, D., Gandy, S.E. and Sisodia, S.S. (1996) The profile of soluble amyloid β protein in cultured cell media. Detection and quantification of amyloid β protein and variants by immunoprecipitation-mass spectrometry. J. Biol. Chem., 271, 31894-31902.
    • (1996) J. Biol. Chem , vol.271 , pp. 31894-31902
    • Wang, R.1    Sweeney, D.2    Gandy, S.E.3    Sisodia, S.S.4
  • 53
    • 0037176727 scopus 로고    scopus 로고
    • Novel ε-cleavage within the transmembrane domain of the Alzheimer amyloid precursor protein demonstrates homology with Notch processing
    • Weidemann, A., Eggert, S., Reinhard, F.B., Vogel, M., Paliga, K., Baier, G., Masters, C.L., Beyreuther, K. and Evin, G.A. (2002) Novel ε-cleavage within the transmembrane domain of the Alzheimer amyloid precursor protein demonstrates homology with Notch processing. Biochemistry, 41, 2825-2835.
    • (2002) Biochemistry , vol.41 , pp. 2825-2835
    • Weidemann, A.1    Eggert, S.2    Reinhard, F.B.3    Vogel, M.4    Paliga, K.5    Baier, G.6    Masters, C.L.7    Beyreuther, K.8    Evin, G.A.9
  • 54
    • 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
  • 55
    • 0035941278 scopus 로고    scopus 로고
    • Characterization of a presenilin-mediated amyloid precursor protein carboxyl-terminal fragment γ. Evidence for distinct mechanisms involved in γ-secretase processing of the APP and Notchl transmembrane domains
    • Yu, C., Kim, S.H., Ikeuchi, T., Xu, H., Gasparini, L., Wang, R. and Sisodia, S.S. (2001) Characterization of a presenilin-mediated amyloid precursor protein carboxyl-terminal fragment γ. Evidence for distinct mechanisms involved in γ-secretase processing of the APP and Notchl transmembrane domains. J. Biol. Chem., 276, 43756-43760.
    • (2001) J. Biol. Chem , vol.276 , pp. 43756-43760
    • Yu, C.1    Kim, S.H.2    Ikeuchi, T.3    Xu, H.4    Gasparini, L.5    Wang, R.6    Sisodia, S.S.7
  • 56
    • 0034618715 scopus 로고    scopus 로고
    • Nicastrin modulates presenilin-mediated notch/glp-I signal transduction and βAPP processing
    • Yu, G. et al. (2000) Nicastrin modulates presenilin-mediated notch/glp-I signal transduction and βAPP processing. Nature, 407, 48-54.
    • (2000) Nature , vol.407 , pp. 48-54
    • Yu, G.1
  • 57
    • 0037177826 scopus 로고    scopus 로고
    • Proteolysis of chimeric β-amyloid precursor proteins containing the Notch transmembrane domain yields amyloid β-like peptides
    • Zhang, J., Ye, W., Wang, R., Wolfe, M.S., Greenberg, B.D. and Selkoe, D.J. (2002) Proteolysis of chimeric β-amyloid precursor proteins containing the Notch transmembrane domain yields amyloid β-like peptides. J. Biol. Chem., 277, 15069-15075.
    • (2002) J. Biol. Chem , vol.277 , pp. 15069-15075
    • Zhang, J.1    Ye, W.2    Wang, R.3    Wolfe, M.S.4    Greenberg, B.D.5    Selkoe, D.J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.