메뉴 건너뛰기




Volumn 3, Issue 4, 2002, Pages 281-290

γ-Secretase, notch, Aβ and alzheimer's disease: Where do the presenilins fit in?

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID BETA PROTEIN; ASPARTIC PROTEINASE; BACE1 PROTEIN, HUMAN; MEMBRANE PROTEIN; NOTCH RECEPTOR; PROTEINASE; SECRETASE; TRANSACTIVATOR PROTEIN;

EID: 0036548070     PISSN: 1471003X     EISSN: 14710048     Source Type: Journal    
DOI: 10.1038/nrn785     Document Type: Article
Times cited : (496)

References (137)
  • 1
    • 0031921466 scopus 로고    scopus 로고
    • Mutant genes in familial Alzheimer's disease and transgenic models
    • Price, D. L. & Sisodia, S. S. Mutant genes in familial Alzheimer's disease and transgenic models. Annu. Rev. Neurosci. 21, 479-505 (1998).
    • (1998) Annu. Rev. Neurosci. , vol.21 , pp. 479-505
    • Price, D.L.1    Sisodia, S.S.2
  • 2
    • 0033536163 scopus 로고    scopus 로고
    • Immunization with Aβ attenuates Alzheimer's disease-like pathology in the PDAPP mouse
    • Schenk, D. et al. Immunization with Aβ attenuates Alzheimer's disease-like pathology in the PDAPP mouse. Nature 400, 173-177 (1999).
    • (1999) Nature , vol.400 , pp. 173-177
    • Schenk, D.1
  • 3
    • 0033835996 scopus 로고    scopus 로고
    • Peripherally administered antibodies against amyloid β-peptide enter the central nervous system and reduce pathology in a mouse model of Alzheimer disease
    • Bard, F. et al. Peripherally administered antibodies against amyloid β-peptide enter the central nervous system and reduce pathology in a mouse model of Alzheimer disease. Nature Med. 6, 916-919 (2000).
    • (2000) Nature Med , vol.6 , pp. 916-919
    • Bard, F.1
  • 4
    • 0034700471 scopus 로고    scopus 로고
    • Aβ-immunization reduces behavioural impairment and dense-cored plaques in a model of Alzheimer's disease
    • Janus, C. et al. Aβ-immunization reduces behavioural impairment and dense-cored plaques in a model of Alzheimer's disease. Nature 408, 979-982 (2000).
    • (2000) Nature , vol.408 , pp. 979-982
    • Janus, C.1
  • 5
    • 84984755327 scopus 로고    scopus 로고
    • Aβ peptide vaccination prevents memory loss in an animal model of Alzheimer's disease
    • Morgan, D. et al. Aβ peptide vaccination prevents memory loss in an animal model of Alzheimer's disease. Nature 408, 982-985 (2000).
    • (2000) Nature , vol.408 , pp. 982-985
    • Morgan, D.1
  • 6
    • 0035794123 scopus 로고    scopus 로고
    • Amyloid-P interactions with chondroitin sulfate-derived monosaccharides and disaccharides. Implications for drug development
    • Fraser, P. E., Darabie, A. A. & McLaurin, J. A. Amyloid-P interactions with chondroitin sulfate-derived monosaccharides and disaccharides. Implications for drug development. J. Biol. Chem. 276, 6412-6419 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 6412-6419
    • Fraser, P.E.1    Darabie, A.A.2    McLaurin, J.A.3
  • 7
    • 0031873102 scopus 로고    scopus 로고
    • β-Sheet breaker peptides inhibit fibrillogenesis in a rat brain model of amyloidosis: Implications for Alzheimer's therapy
    • Soto, C. et al. β-Sheet breaker peptides inhibit fibrillogenesis in a rat brain model of amyloidosis: implications for Alzheimer's therapy. Nature Med. 4, 822-826 (1998).
    • (1998) Nature Med , vol.4 , pp. 822-826
    • Soto, C.1
  • 8
    • 0028913416 scopus 로고
    • Arresting amyloidosis in vivo using small- molecule anionic sulphonates or sulphates: Implications for Alzheimer's disease
    • Kisilevsky, R. et al. Arresting amyloidosis in vivo using small- molecule anionic sulphonates or sulphates: implications for Alzheimer's disease. Nature Med. 1, 143-148 (1995).
    • (1995) Nature Med , vol.1 , pp. 143-148
    • Kisilevsky, R.1
  • 9
    • 0034681260 scopus 로고    scopus 로고
    • Regulated intramembrane proteolysis: A control mechanism conserved from bacteria to humans
    • Brown, M. S., Ye, J., Rawson, R. B. & Goldstein, J. L. Regulated intramembrane proteolysis: a control mechanism conserved from bacteria to humans. Cell 100, 391-398 (2000).
    • (2000) Cell , vol.100 , pp. 391-398
    • Brown, M.S.1    Ye, J.2    Rawson, R.B.3    Goldstein, J.L.4
  • 10
    • 0023105114 scopus 로고
    • The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor
    • Kang, J. et al. The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor. Nature 325, 733-736 (1987).
    • (1987) Nature , vol.325 , pp. 733-736
    • Kang, J.1
  • 11
    • 0023132387 scopus 로고
    • Characterization and chromosomal localization of a cDNA encoding brain amyloid of Alzheimer's disease
    • Goldgaber, D. et al. Characterization and chromosomal localization of a cDNA encoding brain amyloid of Alzheimer's disease. Science 235, 877-880 (1987).
    • (1987) Science , vol.235 , pp. 877-880
    • Goldgaber, D.1
  • 13
    • 0023109592 scopus 로고
    • Amyloid β-protein gene: CDNA, mRNA distribution and genetic linkage near the Alzheimer locus
    • Tanzi, R. E. et al. Amyloid β-protein gene: cDNA, mRNA distribution and genetic linkage near the Alzheimer locus. Science 235, 880-884 (1987).
    • (1987) Science , vol.235 , pp. 880-884
    • Tanzi, R.E.1
  • 14
    • 0023872043 scopus 로고    scopus 로고
    • Novel precursor of Alzheimer's disease amyloid protein shows protease inhibitory activity
    • Kitaguchi, N., Takahashi, Y, Tokushima, Y, Shiojiri, S. & Ito, H. Novel precursor of Alzheimer's disease amyloid protein shows protease inhibitory activity. Nature 331, 530-532
    • Nature , vol.331 , pp. 530-532
    • Kitaguchi, N.1    Takahashi, Y.2    Tokushima, Y.3    Shiojiri, S.4    Ito, H.5
  • 15
    • 0024550204 scopus 로고
    • Identification, biogenesis, and localization of precursors of Alzheimer disease A4 amyloid protein
    • Weidemann, A. et al. Identification, biogenesis, and localization of precursors of Alzheimer disease A4 amyloid protein. Cell 57, 115-126 (1989).
    • (1989) Cell , vol.57 , pp. 115-126
    • Weidemann, A.1
  • 16
    • 0026735070 scopus 로고
    • Targeting of cell-surface β-amyloid precursor protein to lysosomes: Alternative processing into amyloid-bearing fragments
    • Haass, C., Koo, E. H., Mellon, A., Hung, A. Y & Selkoe, D. J. Targeting of cell-surface β-amyloid precursor protein to lysosomes: alternative processing into amyloid-bearing fragments. Nature 357, 500-503 (1992).
    • (1992) Nature , vol.357 , pp. 500-503
    • Haass, C.1    Koo, E.H.2    Mellon, A.3    Hung, A.Y.4    Selkoe, D.J.5
  • 17
    • 0027056827 scopus 로고
    • Secretion of the β -amyloid precursor protein
    • Sisodia, S. S. Secretion of the β -amyloid precursor protein. Ann. NY Acad. Sci. 674, 53-57 (1992).
    • (1992) Ann. NY Acad. Sci. , vol.674 , pp. 53-57
    • Sisodia, S.S.1
  • 18
    • 0028057224 scopus 로고
    • Selective ectodomain phosphorylation and regulated cleavage of β-amyloid precursor protein
    • Hung, A. Y & Selkoe, D. J. Selective ectodomain phosphorylation and regulated cleavage of β-amyloid precursor protein. EMBO J. 13, 534-542 (1994).
    • (1994) EMBO J , vol.13 , pp. 534-542
    • Hung, A.Y.1    Selkoe, D.J.2
  • 19
    • 0031030058 scopus 로고    scopus 로고
    • Ectodomain phosphorylation of β-amyloid precursor protein at two distinct cellular locations
    • Walter, J. et al. Ectodomain phosphorylation of β-amyloid precursor protein at two distinct cellular locations. J. Biol. Chem. 272, 1896-1903 (1997).
    • (1997) J. Biol. Chem , vol.272 , pp. 1896-1903
    • Walter, J.1
  • 20
    • 0029873515 scopus 로고    scopus 로고
    • Mice deficient for the amyloid precursor protein gene
    • Zheng, H. et al. Mice deficient for the amyloid precursor protein gene. Ann. NY Acad. Sci. 777, 421-426 (1996).
    • (1996) Ann. NY Acad. Sci , vol.777 , pp. 421-426
    • Zheng, H.1
  • 21
    • 0024395366 scopus 로고
    • Secreted form of amyloid β-protein is involved in the growth regulation of fibroblasts
    • Saitoh, T. et al. Secreted form of amyloid β-protein is involved in the growth regulation of fibroblasts. Cell 58, 615-622 (1989).
    • (1989) Cell , vol.58 , pp. 615-622
    • Saitoh, T.1
  • 22
    • 0026663993 scopus 로고
    • The amyloid protein precursor of Alzheimer disease is a mediator of the effects of NGF on neurite outgrowth
    • Milward, A. E. et al. The amyloid protein precursor of Alzheimer disease is a mediator of the effects of NGF on neurite outgrowth. Neuron 9, 129-137 (1992).
    • (1992) Neuron , vol.9 , pp. 129-137
    • Milward, A.E.1
  • 23
    • 0027447656 scopus 로고
    • Alzheimer amyloid protein precursor complexes with brain GTP-binding protein Go
    • Nishimoto, I. et al. Alzheimer amyloid protein precursor complexes with brain GTP-binding protein Go. Nature 362, 75-79 (1993).
    • (1993) Nature , vol.362 , pp. 75-79
    • Nishimoto, I.1
  • 24
    • 0035818998 scopus 로고    scopus 로고
    • Kinesin-mediated axonal transport of a membrane compartment containing P-secretase and presenilin-1 requires APP
    • Kamal, A., Almenar-Queralt, A., LeBlanc, J. F, Roberts, E. A. & Goldstein, L. S. Kinesin-mediated axonal transport of a membrane compartment containing P-secretase and presenilin-1 requires APP. Nature 414, 643-648 (2001).
    • (2001) Nature , vol.414 , pp. 643-648
    • Kamal, A.1    Almenar-Queralt, A.2    Leblanc, J.F.3    Roberts, E.A.4    Goldstein, L.S.5
  • 25
    • 0035816661 scopus 로고    scopus 로고
    • A transcriptionally active complex of APP with Fe65 and histone acetyltransferase Tip60
    • Cao, X. & Sudhof, T. C. A transcriptionally active complex of APP with Fe65 and histone acetyltransferase Tip60. Science 293, 115-120 (2001).
    • (2001) Science , vol.293 , pp. 115-120
    • Cao, X.1    Sudhof, T.C.2
  • 26
    • 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. et al. 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).
    • (2001) EMBO Rep , vol.2 , pp. 835-841
    • Sastre, M.1
  • 27
    • 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. & De Strooper, B. 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).
    • (2001) J. Neurochem , vol.78 , pp. 1168-1178
    • Cupers, P.1    Orlans, I.2    Craessaerts, K.3    Annaert, W.4    De Strooper, B.5
  • 28
    • 0842297602 scopus 로고
    • The β-amyloid protein precursor of Alzheimer disease has soluble derivatives found in human brain and cerebrospinal fluid
    • Palmert, M. R. et al. The β-amyloid protein precursor of Alzheimer disease has soluble derivatives found in human brain and cerebrospinal fluid. Proc. Natl Acad. Sci. USA 86, 6338-6342 (1989).
    • (1989) Proc. Natl Acad. Sci. USA , vol.86 , pp. 6338-6342
    • Palmert, M.R.1
  • 29
    • 0025295039 scopus 로고
    • Cleavage of amyloid β-peptide during constitutive processing of its precursor
    • Esch, F S. et al. Cleavage of amyloid β-peptide during constitutive processing of its precursor. Science 248, 1122-1124 (1990).
    • (1990) Science , vol.248 , pp. 1122-1124
    • Esch, F.S.1
  • 30
    • 0025373508 scopus 로고
    • Evidence that β-amyloid protein in Alzheimer's disease is not derived by normal processing
    • Sisodia, S. S., Koo, E. H., Beyreuther, K., Unterbeck, A. & Price, D. Evidence that β-amyloid protein in Alzheimer's disease is not derived by normal processing. Science 248, 492-495 (1990).
    • (1990) Science , vol.248 , pp. 492-495
    • Sisodia, S.S.1    Koo, E.H.2    Beyreuther, K.3    Unterbeck, A.4    Price, D.5
  • 31
    • 0026045172 scopus 로고
    • Secretion of the β/A4 amyloid precursor protein. Identification of a cleavage site in cultured mammalian cells
    • Wang, R., Meschia, J. F, Cotter, R. J. & Sisodia, S. S. Secretion of the β/A4 amyloid precursor protein. Identification of a cleavage site in cultured mammalian cells. J. Biol. Chem. 266, 16960-16964 (1991).
    • (1991) J. Biol. Chem , vol.266 , pp. 16960-16964
    • Wang, R.1    Meschia, J.F.2    Cotter, R.J.3    Sisodia, S.S.4
  • 32
    • 0027228190 scopus 로고
    • Enzymatic generation of the amino terminus of the β-amyloid peptide
    • Sahasrabudhe, S. R. et al. Enzymatic generation of the amino terminus of the β-amyloid peptide. J. Biol. Chem. 268, 16699-16705 (1993).
    • (1993) J. Biol. Chem , vol.268 , pp. 16699-16705
    • Sahasrabudhe, S.R.1
  • 33
    • 14444272986 scopus 로고    scopus 로고
    • Evidence that tumor necrosis factor-α converting enzyme is involved in regulated α-secretase cleavage of the Alzheimer amyloid protein precursor
    • Buxbaum, J. D. et al. Evidence that tumor necrosis factor-α converting enzyme is involved in regulated α-secretase cleavage of the Alzheimer amyloid protein precursor. J. Biol. Chem. 273, 27765-27767 (1998).
    • (1998) J. Biol. Chem , vol.273 , pp. 27765-27767
    • Buxbaum, J.D.1
  • 34
    • 0026476297 scopus 로고
    • Release of Alzheimer amyloid precursor derivatives stimulated by activation of muscarinic acetylcholine receptors
    • Nitsch, R. M., Slack, B. E., Wurtman, R. J. & Growden, J. H. Release of Alzheimer amyloid precursor derivatives stimulated by activation of muscarinic acetylcholine receptors. Science 258, 304-307 (1992).
    • (1992) Science , vol.258 , pp. 304-307
    • Nitsch, R.M.1    Slack, B.E.2    Wurtman, R.J.3    Growden, J.H.4
  • 35
    • 0028859466 scopus 로고
    • Regulated formation of Golgi secretory vesicles containing Alzheimer β-amyloid precursor protein
    • Xu, H., Greengard, P & Gandy, S. Regulated formation of Golgi secretory vesicles containing Alzheimer β-amyloid precursor protein. J. Biol. Chem. 270, 23243-23245 (1995).
    • (1995) J. Biol. Chem , vol.270 , pp. 23243-23245
    • Xu, H.1    Greengard, P.2    Gandy, S.3
  • 36
    • 0032503959 scopus 로고    scopus 로고
    • The secretases that cleave angiotensin converting enzyme and the amyloid precursor protein are distinct from tumour necrosis factor-a convertase
    • Parvathy, S., Karran, E. H., Turner, A. J. & Hooper, N. M. The secretases that cleave angiotensin converting enzyme and the amyloid precursor protein are distinct from tumour necrosis factor-a convertase. FEBS Lett. 431, 63-65 (1998).
    • (1998) FEBS Lett , vol.431 , pp. 63-65
    • Parvathy, S.1    Karran, E.H.2    Turner, A.J.3    Hooper, N.M.4
  • 37
    • 0033616716 scopus 로고    scopus 로고
    • Constitutive and regulated α-secretase cleavage of Alzheimer's amyloid precursor protein by a disintegrin metalloprotease
    • Lammich, S. et al. Constitutive and regulated α-secretase cleavage of Alzheimer's amyloid precursor protein by a disintegrin metalloprotease. Proc. Natl Acad. Sci. USA 96, 3922-3927 (1999).
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 3922-3927
    • Lammich, S.1
  • 38
    • 0033595706 scopus 로고    scopus 로고
    • β-Secretase cleavage of Alzheimer's amyloid precursor protein by the transmembrane aspartic protease BACE
    • Vassar
    • Vassar, R. et al. β-Secretase cleavage of Alzheimer's amyloid precursor protein by the transmembrane aspartic protease BACE. Science 286, 735-741 (1999).
    • (1999) Science , vol.286 , pp. 735-741
  • 39
    • 0033382226 scopus 로고    scopus 로고
    • Identification of a novel aspartic protease (Asp2) as β-secretase
    • Hussain, I. et al. Identification of a novel aspartic protease (Asp2) as β-secretase. Mol. Cell. Neurosci. 14, 419-427 (1999).
    • (1999) Mol. Cell. Neurosci. , vol.14 , pp. 419-427
    • Hussain, I.1
  • 40
    • 0033518251 scopus 로고    scopus 로고
    • Purification and cloning of amyloid precursor protein P-secretase from human brain
    • Sinha, S. et al. Purification and cloning of amyloid precursor protein P-secretase from human brain. Nature 402, 537-540 (1999).
    • (1999) Nature , vol.402 , pp. 537-540
    • Sinha, S.1
  • 41
    • 0033518264 scopus 로고    scopus 로고
    • Membrane-anchored aspartyl protease with Alzheimer's disease β-secretase activity
    • Yan, R. et al. Membrane-anchored aspartyl protease with Alzheimer's disease β-secretase activity. Nature 402, 533-537 (1999).
    • (1999) Nature , vol.402 , pp. 533-537
    • Yan, R.1
  • 42
    • 0026760261 scopus 로고
    • Production of the Alzheimer amyloid β protein by normal proteolytic processing
    • Shoji, M. et al. Production of the Alzheimer amyloid β protein by normal proteolytic processing. Science 258, 126-129 (1992).
    • (1992) Science , vol.258 , pp. 126-129
    • Shoji, M.1
  • 43
    • 0026646604 scopus 로고
    • Amyloid β-peptide is produced by cultured cells during normal metabolism
    • Haass, C. et al. Amyloid β-peptide is produced by cultured cells during normal metabolism. Nature 359, 322-325 (1992).
    • (1992) Nature , vol.359 , pp. 322-325
    • Haass, C.1
  • 44
    • 0027195933 scopus 로고
    • Seeding one-dimensional crystallization of amyloid: A pathogenic mechanism in Alzheimer's disease and scrapie?
    • Jarrett, J. T. & Lansbury, P. T. Seeding one-dimensional crystallization of amyloid: a pathogenic mechanism in Alzheimer's disease and scrapie? Cell 73, 1055-1058 (1993).
    • (1993) Cell , vol.73 , pp. 1055-1058
    • Jarrett, J.T.1    Lansbury, P.T.2
  • 45
    • 0024990330 scopus 로고
    • Neurotrophic and neurotoxic effects of amyloid β protein: Reversal by tachykinin neuropeptides
    • Yankner, B. A., Duffy, L. K. & Kirschner, D. A. Neurotrophic and neurotoxic effects of amyloid β protein: reversal by tachykinin neuropeptides. Science 250, 279-282 (1990).
    • (1990) Science , vol.250 , pp. 279-282
    • Yankner, B.A.1    Duffy, L.K.2    Kirschner, D.A.3
  • 46
    • 0027447286 scopus 로고
    • Neurodegeneration induced by β-amyloid peptides in vitro: The role of peptide assembly state
    • Pike, C. J., Burdick, D., Walencewicz, A. J., Glabe, C. G. & Cotman, C. W. Neurodegeneration induced by β-amyloid peptides in vitro: the role of peptide assembly state. J. Neurosci. 13, 1676-1678 (1993).
    • (1993) J. Neurosci , vol.13 , pp. 1676-1678
    • Pike, C.J.1    Burdick, D.2    Walencewicz, A.J.3    Glabe, C.G.4    Cotman, C.W.5
  • 47
    • 0028172886 scopus 로고
    • β-Amyloid neurotoxicity requires fibril formation and is inhibited by Congo red
    • Lorenzo, A. & Yanker, B. A. β-Amyloid neurotoxicity requires fibril formation and is inhibited by Congo red. Proc. Natl Acad. Sci. USA 91, 12243-12247 (1994).
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 12243-12247
    • Lorenzo, A.1    Yanker, B.A.2
  • 48
    • 0028276801 scopus 로고
    • Evidence that production and release of amyloid β-protein precursor involves the endocytic pathway
    • Koo, E. H. & Squazzo, S. L. Evidence that production and release of amyloid β-protein precursor involves the endocytic pathway. J. Biol. Chem. 269, 17386-17389 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 17386-17389
    • Koo, E.H.1    Squazzo, S.L.2
  • 49
    • 0029950149 scopus 로고    scopus 로고
    • Trafficking of cell-surface amyloid β-protein precursor. I. Secretion, endocytosis and recycling as detected by labeled monoclonal antibody
    • Koo, E. H., Squazzo, S. L., Selkoe, D. J. & Koo, C. H. Trafficking of cell-surface amyloid β-protein precursor. I. Secretion, endocytosis and recycling as detected by labeled monoclonal antibody. J. Cell Sci. 109, 991-998 (1996).
    • (1996) J. Cell Sci , vol.109 , pp. 991-998
    • Koo, E.H.1    Squazzo, S.L.2    Selkoe, D.J.3    Koo, C.H.4
  • 50
    • 0030769092 scopus 로고    scopus 로고
    • Alzheimer A β1-42 peptide is generated in the endoplasmic reticulum/intermediate compartment of NT2N cells
    • 1-42 peptide is generated in the endoplasmic reticulum/intermediate compartment of NT2N cells. Nature Med. 3, 1021-1023 (1997).
    • (1997) Nature Med , vol.3 , pp. 1021-1023
    • Cook, D.G.1
  • 51
    • 0030769091 scopus 로고    scopus 로고
    • Distinct sites of intracellular production for Alzheimer's disease A β40/42 amyloid peptides
    • 40/42 amyloid peptides. Nature Med. 3, 1016-1020 (1997).
    • (1997) Nature Med , vol.3 , pp. 1016-1020
    • Hartmann, T.1
  • 52
    • 0029803744 scopus 로고    scopus 로고
    • Evidence that the 42- and 40-amino-acid forms of amyloid β protein are generated from the β-amyloid precursor protein by different protease activities
    • Citron, M. et al. Evidence that the 42- and 40-amino-acid forms of amyloid β protein are generated from the β-amyloid precursor protein by different protease activities. Proc. Natl Acad. Sci. USA 93, 13170-13175 (1996).
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 13170-13175
    • Citron, M.1
  • 53
    • 0035846826 scopus 로고    scopus 로고
    • Reduced neprilysin in high plaque areas of Alzheimer brain: A possible relationship to deficient degradation of β-amyloid peptide
    • Yasojima, K., Akiyama, H., McGeer, E. G. & McGeer, P. L. Reduced neprilysin in high plaque areas of Alzheimer brain: a possible relationship to deficient degradation of β-amyloid peptide. Neurosci. Lett. 297, 97-100 (2001).
    • (2001) Neurosci. Lett , vol.297 , pp. 97-100
    • Yasojima, K.1    Akiyama, H.2    McGeer, E.G.3    McGeer, P.L.4
  • 54
    • 0000398342 scopus 로고    scopus 로고
    • Insulin-degrading enzyme regulates extracellular levels of amyloid β-protein by degradation
    • Qiu, W. Q. et al. Insulin-degrading enzyme regulates extracellular levels of amyloid β-protein by degradation. J. Biol. Chem. 273, 32730-32738 (1998).
    • (1998) J. Biol. Chem , vol.273 , pp. 32730-32738
    • Qiu, W.Q.1
  • 55
    • 0034667518 scopus 로고    scopus 로고
    • Purified recombinant insulin-degrading enzyme degrades amyloid β-protein but does not promote its oligomerization
    • Chesneau, V., Vekrellis, K., Rosner, M. R. & Selkoe, D. J. Purified recombinant insulin-degrading enzyme degrades amyloid β-protein but does not promote its oligomerization. Biochem. J. 351, 509-516 (2000).
    • (2000) Biochem. J , vol.351 , pp. 509-516
    • Chesneau, V.1    Vekrellis, K.2    Rosner, M.R.3    Selkoe, D.J.4
  • 56
    • 0026088977 scopus 로고
    • Segregation of a missense mutation in the amyloid precursor protein gene with familial Alzheimer disease
    • Goate, A. M. et al. Segregation of a missense mutation in the amyloid precursor protein gene with familial Alzheimer disease. Nature 349, 704-706 (1991).
    • (1991) Nature , vol.349 , pp. 704-706
    • Goate, A.M.1
  • 57
    • 0029004341 scopus 로고
    • Cloning of a gene bearing missense mutations in early onset familial Alzheimer's disease
    • Sherrington, R. et al. Cloning of a gene bearing missense mutations in early onset familial Alzheimer's disease. Nature 375, 754-760 (1995).
    • (1995) Nature , vol.375 , pp. 754-760
    • Sherrington, R.1
  • 58
    • 0029150716 scopus 로고
    • A familial Alzheimer's disease locus on chromosome 1
    • Levy-Lahad, E. et al. A familial Alzheimer's disease locus on chromosome 1. Science 269, 970-973 (1995).
    • (1995) Science , vol.269 , pp. 970-973
    • Levy-Lahad, E.1
  • 59
    • 0029101491 scopus 로고
    • Familial Alzheimer's disease in kindreds with missense mutations in a novel gene on chromosome 1 related to the Alzheimer's disease type 3 gene
    • Rogaev, E. I. et al. Familial Alzheimer's disease in kindreds with missense mutations in a novel gene on chromosome 1 related to the Alzheimer's disease type 3 gene. Nature 376, 775-778 (1995).
    • (1995) Nature , vol.376 , pp. 775-778
    • Rogaev, E.I.1
  • 60
    • 0026745610 scopus 로고
    • Mutation of the β-amyloid precursor protein in familial Alzheimer's disease increases β-protein production
    • Citron, M. et al. Mutation of the β-amyloid precursor protein in familial Alzheimer's disease increases β-protein production. Nature 360, 672-674 (1992).
    • (1992) Nature , vol.360 , pp. 672-674
    • Citron, M.1
  • 61
    • 0028246308 scopus 로고
    • Mutations associated with a locus for familial Alzheimer's disease result in alternative processing of amyloid β-protein precursor
    • Haass, C., Hung, A. Y., Selkoe, D. J. & Teplow, D. B. Mutations associated with a locus for familial Alzheimer's disease result in alternative processing of amyloid β-protein precursor. J. Biol. Chem. 269, 17741-17748 (1994).
    • (1994) J. Biol. Chem , vol.269 , pp. 17741-17748
    • Haass, C.1    Hung, A.Y.2    Selkoe, D.J.3    Teplow, D.B.4
  • 62
    • 16044373524 scopus 로고    scopus 로고
    • Secreted amyloid- β protein similar to that in the senile plaques of Alzheimer disease is increased in vivo by presenilin 1 and 2 and APP mutations linked to FAD
    • Scheuner, D. et al. Secreted amyloid- β protein similar to that in the senile plaques of Alzheimer disease is increased in vivo by presenilin 1 and 2 and APP mutations linked to FAD. Nature Med. 2, 864-870 (1996).
    • (1996) Nature Med , vol.2 , pp. 864-870
    • Scheuner, D.1
  • 63
    • 0030293676 scopus 로고    scopus 로고
    • Familial Alzheimer's disease linked presenilin 1 variants elevate Aβ1-42/1-40 ratio in vitro and in vivo
    • Borchelt, D. R. et al. Familial Alzheimer's disease linked presenilin 1 variants elevate Aβ1-42/1-40 ratio in vitro and in vivo. Neuron 17, 1005-1013 (1996).
    • (1996) Neuron , vol.17 , pp. 1005-1013
    • Borchelt, D.R.1
  • 64
    • 16044366039 scopus 로고    scopus 로고
    • Increased amyloid- β42(43) in brains of mice expressing mutant presenilin 1
    • Duff, K. et al. Increased amyloid- β42(43) in brains of mice expressing mutant presenilin 1. Nature 383, 710-713.(1996).
    • (1996) Nature , vol.383 , pp. 710-713
    • Duff, K.1
  • 65
    • 16944362157 scopus 로고    scopus 로고
    • Mutant presenilins of Alzheimer's disease increase production of 42-residue amyloid β-protein in both transfected cells and transgenic mice
    • Citron, M. et al. Mutant presenilins of Alzheimer's disease increase production of 42-residue amyloid β-protein in both transfected cells and transgenic mice. Nature Med. 3, 67-72 (1997).
    • (1997) Nature Med , vol.3 , pp. 67-72
    • Citron, M.1
  • 66
    • 0026688633 scopus 로고
    • Mutation of a putative sperm membrane protein in Caenorhabditis elegans prevents sperm differentiation but not its associated meiotic divisions
    • L'Hernault, S. W. L. & Arduengo, P. M. Mutation of a putative sperm membrane protein in Caenorhabditis elegans prevents sperm differentiation but not its associated meiotic divisions. J. Cell Biol. 119, 55-69 (1992).
    • (1992) J. Cell Biol , vol.119 , pp. 55-69
    • L'hernault, S.W.L.1    Arduengo, P.M.2
  • 67
    • 0029116848 scopus 로고
    • Facilitation of lin-12--mediated signalling by sel-12, a Caenorhabditis elegans S182 Alzheimer's disease gene
    • Levitan, D. & Greenwald, I. Facilitation of lin-12--mediated signalling by sel-12, a Caenorhabditis elegans S182 Alzheimer's disease gene. Nature 377, 351-354 (1995).
    • (1995) Nature , vol.377 , pp. 351-354
    • Levitan, D.1    Greenwald, I.2
  • 68
    • 0030671560 scopus 로고    scopus 로고
    • HOP-1, a Caenorhabditis elegans presenilin, appears to be functionally redundant with SEL-12 presenilin and to facilitate LIN-12 and GLP-1 signalling
    • Li, X. & Greenwald, I. HOP-1, a Caenorhabditis elegans presenilin, appears to be functionally redundant with SEL-12 presenilin and to facilitate LIN-12 and GLP-1 signalling. Proc. Natl Acad. Sci. USA 94, 12204-12209 (1998).
    • (1998) Proc. Natl Acad. Sci. USA , vol.94 , pp. 12204-12209
    • Li, X.1    Greenwald, I.2
  • 69
    • 0030293854 scopus 로고    scopus 로고
    • Protein topology of presenilin
    • Doan, A. et al. Protein topology of presenilin. Neuron 17, 1023-1030 (1996).
    • (1996) Neuron , vol.17 , pp. 1023-1030
    • Doan, A.1
  • 70
    • 0030293894 scopus 로고    scopus 로고
    • Membrane topology of the C. Elegans SEL-12 presenilin
    • Li, X. & Greenwald, I. Membrane topology of the C. elegans SEL-12 presenilin. Neuron 17, 1015-1021 (1996).
    • (1996) Neuron , vol.17 , pp. 1015-1021
    • Li, X.1    Greenwald, I.2
  • 71
    • 15444341611 scopus 로고    scopus 로고
    • Phosphorylation, subcellular localization, and membrane orientation of the Alzheimer's disease-associated presenilins
    • De Strooper, B. et al. Phosphorylation, subcellular localization, and membrane orientation of the Alzheimer's disease-associated presenilins. J. Biol. Chem. 272, 3590-3598 (1997).
    • (1997) J. Biol. Chem , vol.272 , pp. 3590-3598
    • De Strooper, B.1
  • 72
    • 15844425969 scopus 로고    scopus 로고
    • Endoproteolysis of presenilin 1 and accumulation of processed derivatives in vivo
    • Thinakaran, G. et al. Endoproteolysis of presenilin 1 and accumulation of processed derivatives in vivo. Neuron 17, 181-190 (1996).
    • (1996) Neuron , vol.17 , pp. 181-190
    • Thinakaran, G.1
  • 73
    • 0030811016 scopus 로고    scopus 로고
    • Hyperaccumulation of FAD-linked presenilin-1 variants in vivo
    • Lee, M. K. et al. Hyperaccumulation of FAD-linked presenilin-1 variants in vivo. Nature Med. 3, 756-760 (1997).
    • (1997) Nature Med , vol.3 , pp. 756-760
    • Lee, M.K.1
  • 74
    • 0030667426 scopus 로고    scopus 로고
    • Evidence that levels of presenilins (PS1 and PS2) are coordinately regulated by competition for limiting cellular factors
    • Thinakaran, G. et al. Evidence that levels of presenilins (PS1 and PS2) are coordinately regulated by competition for limiting cellular factors. J. Biol. Chem. 272, 28415-28422.(1997).
    • (1997) J. Biol. Chem , vol.272 , pp. 28415-28422
    • Thinakaran, G.1
  • 75
    • 0032568821 scopus 로고    scopus 로고
    • The presenilin 1 protein is a component of a high molecular weight intracellular complex that contains β-catenin
    • Yu, G. et al. The presenilin 1 protein is a component of a high molecular weight intracellular complex that contains β-catenin. J. Biol. Chem. 273, 16470-16475 (1998).
    • (1998) J. Biol. Chem , vol.273 , pp. 16470-16475
    • Yu, G.1
  • 76
    • 0031920383 scopus 로고    scopus 로고
    • Stable association of the presenilin derivatives and absence of presenilin interactions with APP
    • Thinakaran, G. et al. Stable association of the presenilin derivatives and absence of presenilin interactions with APP. Neurobiol. Dis. 4, 438-453 (1998).
    • (1998) Neurobiol. Dis , vol.4 , pp. 438-453
    • Thinakaran, G.1
  • 77
    • 0032488995 scopus 로고    scopus 로고
    • The proteolytic fragments of the Alzheimer's disease associated presenilin-1 form heterodimers and occur as a 100-150 kDa molecular mass complex
    • Capell, A. et al. The proteolytic fragments of the Alzheimer's disease associated presenilin-1 form heterodimers and occur as a 100-150 kDa molecular mass complex. J. Biol. Chem. 273, 3205-3211 (1998).
    • (1998) J. Biol. Chem , vol.273 , pp. 3205-3211
    • Capell, A.1
  • 78
    • 0343819757 scopus 로고    scopus 로고
    • Presenilin 1 is linked with γ-secretase activity in the detergent solubilized state
    • Li, Y -M. et al. Presenilin 1 is linked with γ-secretase activity in the detergent solubilized state. Proc. Natl Acad. Sci. USA 97, 6138-6143 (2000).
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 6138-6143
    • Li, Y.-M.1
  • 79
    • 8044231311 scopus 로고    scopus 로고
    • The Alzheimer's disease associated presenilins are differentially phosphorylated proteins located predominantly within the endoplasmic reticulum
    • Walter, J. et al. The Alzheimer's disease associated presenilins are differentially phosphorylated proteins located predominantly within the endoplasmic reticulum. Mol. Med. 2, 673-691 (1996).
    • (1996) Mol. Med , vol.2 , pp. 673-691
    • Walter, J.1
  • 80
    • 0032720496 scopus 로고    scopus 로고
    • Presenilin 1 controls γ-secretase processing of amyloid precursor protein in pre-Golgi compartments of hippocampal neurons
    • Annaert, W. G. et al. Presenilin 1 controls γ-secretase processing of amyloid precursor protein in pre-Golgi compartments of hippocampal neurons. J. Cell Biol. 147, 277-294 (1999).
    • (1999) J. Cell Biol , vol.147 , pp. 277-294
    • Annaert, W.G.1
  • 81
    • 0035921427 scopus 로고    scopus 로고
    • The discrepancy between presenilin subcellular localization and y-secretase processing of amyloid precursor protein
    • Cupers, P. et al. The discrepancy between presenilin subcellular localization and y-secretase processing of amyloid precursor protein. J. Cell Biol. 154, 731-740 (2001).
    • (2001) J. Cell Biol , vol.154 , pp. 731-740
    • Cupers, P.1
  • 82
    • 0033579505 scopus 로고    scopus 로고
    • Cell surface presenilin 1 participates in the γ-secretase-like proteolysis of Notch
    • Ray, W. J. et al. Cell surface presenilin 1 participates in the γ-secretase-like proteolysis of Notch. J. Biol. Chem. 274, 36801-36807 (1999).
    • (1999) J. Biol. Chem , vol.274 , pp. 36801-36807
    • Ray, W.J.1
  • 83
    • 0035956921 scopus 로고    scopus 로고
    • Presenilin-1 binds cytoplasmic epithelial cadherin, inhibits cadherin/p120 association, and regulates stability and function of the cadherin/catenin adhesion complex
    • Baki, L. et al. Presenilin-1 binds cytoplasmic epithelial cadherin, inhibits cadherin/p120 association, and regulates stability and function of the cadherin/catenin adhesion complex. Proc. Natl Acad. Sci. USA 98, 2381-2386 (2001).
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 2381-2386
    • Baki, L.1
  • 84
    • 0033401526 scopus 로고    scopus 로고
    • Presenilin-1 forms complexes with the cadherin/catenin cell-cell adhesion system and is recruited to intercellular and synaptic contacts
    • Georgakopoulos, A. et al. Presenilin-1 forms complexes with the cadherin/catenin cell-cell adhesion system and is recruited to intercellular and synaptic contacts. Mol. Cell 4, 893-902 (1999).
    • (1999) Mol. Cell , vol.4 , pp. 893-902
    • Georgakopoulos, A.1
  • 85
    • 0035204206 scopus 로고    scopus 로고
    • Nicastrin is required for Presenilin- mediated transmembrane cleavage in Drosophila
    • Chung, H.-M. & Struhl, G. Nicastrin is required for Presenilin- mediated transmembrane cleavage in Drosophila. Nature Cell Biol. 3, 1129-1132 (2001).
    • (2001) Nature Cell Biol , vol.3 , pp. 1129-1132
    • Chung, H.-M.1    Struhl, G.2
  • 86
    • 0030788767 scopus 로고    scopus 로고
    • Presenilin 1 interacts with a novel member of the armadillo family
    • Zhou, J. et al. Presenilin 1 interacts with a novel member of the armadillo family. Neuroreport 8, 2085-2090 (1997).
    • (1997) Neuroreport , vol.8 , pp. 2085-2090
    • Zhou, J.1
  • 87
    • 0032972547 scopus 로고    scopus 로고
    • Presenilins interact with armadillo proteins including neural specific plakophilin related protein and β-catenin
    • Levesque, G. et al. Presenilins interact with armadillo proteins including neural specific plakophilin related protein and β-catenin. J. Neurochem. 72, 999-1008 (1999).
    • (1999) J. Neurochem , vol.72 , pp. 999-1008
    • Levesque, G.1
  • 88
    • 0034618715 scopus 로고    scopus 로고
    • Nicastrin modulates presenilin-mediated notch/glp-1 and βAPP processing
    • Yu, G. et al. Nicastrin modulates presenilin-mediated notch/glp-1 and βAPP processing. Nature 407, 48-54 (2000).
    • (2000) Nature , vol.407 , pp. 48-54
    • Yu, G.1
  • 89
    • 0034595640 scopus 로고    scopus 로고
    • The nonconserved hydrophilic loop domain of presenilin (PS) is not required for PS endoproteolysis or enhanced Aβ42 production mediated by familial early onset Alzheimer's disease-linked PS variants
    • Saura, C. A. et al. The nonconserved hydrophilic loop domain of presenilin (PS) is not required for PS endoproteolysis or enhanced Aβ42 production mediated by familial early onset Alzheimer's disease-linked PS variants. J. Biol. Chem. 275, 17136-17142 (2000).
    • (2000) J. Biol. Chem , vol.275 , pp. 17136-17142
    • Saura, C.A.1
  • 90
    • 0034193854 scopus 로고    scopus 로고
    • δ-Catenin is a nervous system-specific adherens junction protein which undergoes dynamic relocalization during development
    • Ho, C. et al. δ-Catenin is a nervous system-specific adherens junction protein which undergoes dynamic relocalization during development. J. Comp. Neurol. 420, 261-276 (2000).
    • (2000) J. Comp. Neurol , vol.420 , pp. 261-276
    • Ho, C.1
  • 91
    • 0033535058 scopus 로고    scopus 로고
    • δ-Catenin, an adhesive junction-associated protein which promotes cell scattering
    • Lu, Q. et al. δ-Catenin, an adhesive junction-associated protein which promotes cell scattering. J. Cell Biol. 144, 519-532 (1999).
    • (1999) J. Cell Biol , vol.144 , pp. 519-532
    • Lu, Q.1
  • 92
    • 0034080403 scopus 로고    scopus 로고
    • Aph-2 encodes a novel extracellular protein required for GLP-1- mediated signaling
    • Goutte, C., Hepler, W., Mickey, K. M. & Priess, J. R. aph-2 encodes a novel extracellular protein required for GLP-1- mediated signaling. Development 127, 2481-2492 (2000).
    • (2000) Development , vol.127 , pp. 2481-2492
    • Goutte, C.1    Hepler, W.2    Mickey, K.M.3    Priess, J.R.4
  • 93
    • 0035894534 scopus 로고    scopus 로고
    • APH-2/Nicastrin functions in LIN-12/Notch signalling in the C. Elegans somatic gonad
    • Levitan, D., Yu, G., St George-Hyslop, P. & Goutte, C. APH-2/Nicastrin functions in LIN-12/Notch signalling in the C. elegans somatic gonad. Dev. Biol. 240, 654-661 (2001).
    • (2001) Dev. Biol , vol.240 , pp. 654-661
    • Levitan, D.1    Yu, G.2    St George-Hyslop, P.3    Goutte, C.4
  • 94
    • 0036007118 scopus 로고    scopus 로고
    • Drosophila Nicastrin is essential for the intramembranous cleavage of Notch
    • Lopez-Schier, H. & St Johnston, D. S. Drosophila Nicastrin is essential for the intramembranous cleavage of Notch. Dev. Cell 2, 79-89 (2002).
    • (2002) Dev. Cell , vol.2 , pp. 79-89
    • Lopez-Schier, H.1    St Johnston, D.S.2
  • 95
    • 0036007117 scopus 로고    scopus 로고
    • Nicastrin is required for γ-secretase cleavage of the Drosophila Notch receptor
    • Hu, Y., Ye, Y. & Fortini, M. E. Nicastrin is required for γ-secretase cleavage of the Drosophila Notch receptor. Dev. Cell 2, 69-78 (2002).
    • (2002) Dev. Cell , vol.2 , pp. 69-78
    • Hu, Y.1    Ye, Y.2    Fortini, M.E.3
  • 96
    • 0034896955 scopus 로고    scopus 로고
    • Nicastrin binds to membrane-tethered Notch
    • Chen, F. et al. Nicastrin binds to membrane-tethered Notch. Nature Cell Biol. 3, 751-754 (2001).
    • (2001) Nature Cell Biol , vol.3 , pp. 751-754
    • Chen, F.1
  • 97
    • 0032556859 scopus 로고    scopus 로고
    • Deficiency of presenilin 1 inhibits the normal cleavage of amyloid precursor protein
    • De Strooper, B. et al. Deficiency of presenilin 1 inhibits the normal cleavage of amyloid precursor protein. Nature 391, 387-390 (1998).
    • (1998) Nature , vol.391 , pp. 387-390
    • De Strooper, B.1
  • 98
    • 0000138540 scopus 로고    scopus 로고
    • Effect of PS1 deficiency on membrane protein trafficking in neurons
    • Naruse, S. et al. Effect of PS1 deficiency on membrane protein trafficking in neurons. Neuron 21, 1213-1221 (1998).
    • (1998) Neuron , vol.21 , pp. 1213-1221
    • Naruse, S.1
  • 99
    • 0034711207 scopus 로고    scopus 로고
    • Proteolytic derivative of amyloid precursor protein accumulate in restricted and unpredicted intracellular compartments in the absence of functional presenilin 1 expression
    • Chen, F. et al. Proteolytic derivative of amyloid precursor protein accumulate in restricted and unpredicted intracellular compartments in the absence of functional presenilin 1 expression. J. Biol. Chem. 275, 36794-36802 (2000).
    • (2000) J. Biol. Chem , vol.275 , pp. 36794-36802
    • Chen, F.1
  • 100
    • 0033775709 scopus 로고    scopus 로고
    • Total inactivation of γ-secretase activity in presenilin-deficient embryonic stem cells
    • Herreman, A. et al. Total inactivation of γ-secretase activity in presenilin-deficient embryonic stem cells. Nature Cell Biol. 2, 461-462 (2000).
    • (2000) Nature Cell Biol , vol.2 , pp. 461-462
    • Herreman, A.1
  • 101
    • 0033779635 scopus 로고    scopus 로고
    • Presenilins are required for γ-secretase cleavage of β-APP and transmembrane cleavage of Notch-1
    • Zhang, Z. et al. Presenilins are required for γ-secretase cleavage of β-APP and transmembrane cleavage of Notch-1. Nature Cell Biol. 2, 463-465 (2000).
    • (2000) Nature Cell Biol , vol.2 , pp. 463-465
    • Zhang, Z.1
  • 102
    • 0033868818 scopus 로고    scopus 로고
    • A novel proteolytic cleavage involved in Notch signaling: The role of the disintegrin-metalloprotease TACE
    • Brou, C. et al. A novel proteolytic cleavage involved in Notch signaling: the role of the disintegrin-metalloprotease TACE. Mol. Cell 5, 207-216 (2000).
    • (2000) Mol. Cell , vol.5 , pp. 207-216
    • Brou, C.1
  • 103
    • 0033867521 scopus 로고    scopus 로고
    • A ligand-induced extracellular cleavage regulates γ-secretase-like proteolytic activation of Notch1
    • Mumm, J. S. et al. A ligand-induced extracellular cleavage regulates γ-secretase-like proteolytic activation of Notch1. Mol. Cell 5, 197-206 (2000).
    • (2000) Mol. Cell , vol.5 , pp. 197-206
    • Mumm, J.S.1
  • 104
    • 0026721943 scopus 로고
    • β-Amyloid precursor protein cleavage by a membrane-bound protease
    • Sisodia, S. S. β-Amyloid precursor protein cleavage by a membrane-bound protease. Proc. Natl Acad. Sci. USA 89, 6075-6079 (1993).
    • (1993) Proc. Natl Acad. Sci. USA , vol.89 , pp. 6075-6079
    • Sisodia, S.S.1
  • 105
    • 0032574993 scopus 로고    scopus 로고
    • Notch-1 signalling requires ligand-induced proteolytic release of intracellular domain
    • Schroeter, E. H., Kisslinger, J. A. & Kopan, R. Notch-1 signalling requires ligand-induced proteolytic release of intracellular domain. Nature 393, 382-386 (1998).
    • (1998) Nature , vol.393 , pp. 382-386
    • Schroeter, E.H.1    Kisslinger, J.A.2    Kopan, R.3
  • 106
    • 0033920919 scopus 로고    scopus 로고
    • Notch signal transduction: A real rip and more
    • Weinmaster, G. Notch signal transduction: a real rip and more. Curr. Opin. Genet. Dev. 10, 363-369 (2000).
    • (2000) Curr. Opin. Genet. Dev , vol.10 , pp. 363-369
    • Weinmaster, G.1
  • 107
    • 0033152441 scopus 로고    scopus 로고
    • Presenilins, processing of P-amyloid precursor protein, and Notch signaling
    • Chan, Y M. & Jan, Y N. Presenilins, processing of P-amyloid precursor protein, and Notch signaling. Neuron 23, 201-204 (1999).
    • (1999) Neuron , vol.23 , pp. 201-204
    • Chan, Y.M.1    Jan, Y.N.2
  • 108
    • 17744401440 scopus 로고    scopus 로고
    • Presenilin 1 is required for Notch and Dll1 expression in the paraxial mesoderm
    • Wong, P C. et al. Presenilin 1 is required for Notch and Dll1 expression in the paraxial mesoderm. Nature 387, 288-292 (1997).
    • (1997) Nature , vol.387 , pp. 288-292
    • Wong, P.C.1
  • 109
    • 0030779784 scopus 로고    scopus 로고
    • Skeletal and CNS defects in presenilin-1 deficient mice
    • Shen, J. et al. Skeletal and CNS defects in presenilin-1 deficient mice. Cell 89, 629-639 (1997).
    • (1997) Cell , vol.89 , pp. 629-639
    • Shen, J.1
  • 110
    • 0032728957 scopus 로고    scopus 로고
    • Mice lacking both presenilin genes exhibit early embryonic patterning defects
    • Donoviel, D. et al. Mice lacking both presenilin genes exhibit early embryonic patterning defects. Genes Dev. 13, 2801-2810 (1999).
    • (1999) Genes Dev , vol.13 , pp. 2801-2810
    • Donoviel, D.1
  • 111
    • 13044278313 scopus 로고    scopus 로고
    • Presenilin 2 deficiency causes a mild pulmonary phenotype and no changes in amyloid precursor protein processing but enhances the embryonic lethal phenotype of presenilin 1 deficiency
    • Herreman, A. et al. Presenilin 2 deficiency causes a mild pulmonary phenotype and no changes in amyloid precursor protein processing but enhances the embryonic lethal phenotype of presenilin 1 deficiency. Proc. Natl Acad. Sci. USA 96, 11872-11877 (1999).
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 11872-11877
    • Herreman, A.1
  • 112
    • 0033535504 scopus 로고    scopus 로고
    • A presenilin dependent γ-secretase- like protease mediates release of Notch intracellular domain
    • De Strooper, B. et al. A presenilin dependent γ-secretase- like protease mediates release of Notch intracellular domain. Nature 398, 518-522 (1999).
    • (1999) Nature , vol.398 , pp. 518-522
    • De Strooper, B.1
  • 113
    • 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. & Carpenter, G. γ-Secretase cleavage and nuclear localization of ErbB-4 receptor tyrosine kinase. Science 294, 2179-2181 (2001).
    • (2001) Science , vol.294 , pp. 2179-2181
    • Ni, C.Y.1    Murphy, M.P.2    Golde, T.E.3    Carpenter, G.4
  • 114
    • 0035824426 scopus 로고    scopus 로고
    • Wild- type and mutated nicastrins do not display aminopeptidase M- and B-like activities
    • Fergani, A., Yu, G., St George-Hyslop, P. & Checler, F. Wild- type and mutated nicastrins do not display aminopeptidase M- and B-like activities. Biochem. Biophys. Res. Commun. 289, 678-680 (2001).
    • (2001) Biochem. Biophys. Res. Commun , vol.289 , pp. 678-680
    • Fergani, A.1    Yu, G.2    St George-Hyslop, P.3    Checler, F.4
  • 115
    • 0033535553 scopus 로고    scopus 로고
    • Two transmembrane aspartates in presenilin 1 required for presenilin endoproteolysis and γ-secretase activity
    • Wolfe, M. S. et al. Two transmembrane aspartates in presenilin 1 required for presenilin endoproteolysis and γ-secretase activity. Nature 398, 513-517 (1999).
    • (1999) Nature , vol.398 , pp. 513-517
    • Wolfe, M.S.1
  • 116
    • 0034621824 scopus 로고    scopus 로고
    • Photoactivated γ-secretase inhibitors directed to the active site covalently label presenilin 1
    • Li, Y. M. et al. Photoactivated γ-secretase inhibitors directed to the active site covalently label presenilin 1. Nature 405, 689-694 (2000).
    • (2000) Nature , vol.405 , pp. 689-694
    • Li, Y.M.1
  • 117
    • 0033780472 scopus 로고    scopus 로고
    • Transition-state analogue inhibitors of γ-secretase bind directly to presenilin-1
    • Esler, W. P et al. Transition-state analogue inhibitors of γ-secretase bind directly to presenilin-1. Nature Cell Biol. 2, 428-434 (2000).
    • (2000) Nature Cell Biol , vol.2 , pp. 428-434
    • Esler, W.P.1
  • 118
    • 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. Glycine 384 is required for presenilin-1 function and is conserved in bacterial polytopic aspartyl proteases. Nature Cell Biol. 2, 848-851 (2000).
    • (2000) Nature Cell Biol , vol.2 , pp. 848-851
    • Steiner, H.1
  • 119
    • 0034702303 scopus 로고    scopus 로고
    • Embryonic lethality in mice homozygous for a processing-deficient allele of Notch1
    • Huppert, S. S. et al. Embryonic lethality in mice homozygous for a processing-deficient allele of Notch1. Nature 405, 966-970 (2000).
    • (2000) Nature , vol.405 , pp. 966-970
    • Huppert, S.S.1
  • 120
    • 0030720936 scopus 로고    scopus 로고
    • Mutations in the transmembrane domain of APP altering γ-secretase specificity
    • Lichtenthaler, S. F., Ida, N., Multhaup, G., Masters, C. L. & Beyreuther, K. Mutations in the transmembrane domain of APP altering γ-secretase specificity. Biochemistry 36, 15396-15403 (1997).
    • (1997) Biochemistry , vol.36 , pp. 15396-15403
    • Lichtenthaler, S.F.1    Ida, N.2    Multhaup, G.3    Masters, C.L.4    Beyreuther, K.5
  • 121
    • 0035941278 scopus 로고    scopus 로고
    • Characterization of a presenilin-mediated amyloid precursor protein carboxyl-terminal fragment y Evidence for distinct mechanisms involved in γ-secretase processing of the APP and Notch1 transmembrane domains
    • Yu, C. et al. Characterization of a presenilin-mediated amyloid precursor protein carboxyl-terminal fragment y Evidence for distinct mechanisms involved in γ-secretase processing of the APP and Notch1 transmembrane domains. J. Biol. Chem. 276, 43756-43760 (2001).
    • (2001) J. Biol. Chem , vol.276 , pp. 43756-43760
    • Yu, C.1
  • 122
    • 0035929554 scopus 로고    scopus 로고
    • Distinct intramembrane cleavage of the β-amyloid precursor protein family resembling γ-secretase- like cleavage of Notch
    • Gu, Y. et al. Distinct intramembrane cleavage of the β-amyloid precursor protein family resembling γ-secretase- like cleavage of Notch. J. Biol. Chem. 276, 35235-35238 (2001).
    • (2001) J. Biol. Chem , vol.276 , pp. 35235-35238
    • Gu, Y.1
  • 123
    • 0034705196 scopus 로고    scopus 로고
    • Separation of presenilin function in amyloid β-peptide generation and endoproteolysis of Notch
    • Kulic, L. et al. Separation of presenilin function in amyloid β-peptide generation and endoproteolysis of Notch. Proc. Natl Acad. Sci. USA 97, 5913-5918 (2000).
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 5913-5918
    • Kulic, L.1
  • 124
    • 0035005101 scopus 로고    scopus 로고
    • New protease inhibitors prevent y-secretase- mediated Aβ40/42 production without affecting Notch cleavage
    • Petit, A. et al. New protease inhibitors prevent y-secretase- mediated Aβ40/42 production without affecting Notch cleavage. Nature Cell Biol. 3, 507-511 (2001).
    • (2001) Nature Cell Biol , vol.3 , pp. 507-511
    • Petit, A.1
  • 125
    • 0035900686 scopus 로고    scopus 로고
    • Multiple effects of aspartate mutant presenilin 1 on the processing and trafficking of amyloid precursor protein
    • Kim, S. H. et al. Multiple effects of aspartate mutant presenilin 1 on the processing and trafficking of amyloid precursor protein. J. Biol. Chem. 276, 43343-43350 (2001).
    • (2001) J. Biol. Chem , vol.276 , pp. 43343-43350
    • Kim, S.H.1
  • 126
    • 0033783140 scopus 로고    scopus 로고
    • Presenilin-1 differentially facilitates endoproteolysis of the β-amyloid precursor protein and Notch
    • Capell, A. et al. Presenilin-1 differentially facilitates endoproteolysis of the β-amyloid precursor protein and Notch. Nature Cell Biol. 2, 205-211 (2000).
    • (2000) Nature Cell Biol , vol.2 , pp. 205-211
    • Capell, A.1
  • 127
    • 0034714316 scopus 로고    scopus 로고
    • Presenilin 1 regulates pharmacologically distinct γ-secretase activities. Implications for the role of presenilin in γ-secretase cleavage
    • Murphy, M. P. et al. Presenilin 1 regulates pharmacologically distinct γ-secretase activities. Implications for the role of presenilin in γ-secretase cleavage. J. Biol. Chem. 275, 26277-26284 (2000).
    • (2000) J. Biol. Chem , vol.275 , pp. 26277-26284
    • Murphy, M.P.1
  • 128
    • 0035980073 scopus 로고    scopus 로고
    • The first proline of PALP motif at the C terminus of presenilins is obligatory for stabilization, complex formation, and γ-secretase activities of presenilins
    • Tomita, T. et al. The first proline of PALP motif at the C terminus of presenilins is obligatory for stabilization, complex formation, and γ-secretase activities of presenilins. J. Biol. Chem. 276, 33273-33281 (2001).
    • (2001) J. Biol. Chem , vol.276 , pp. 33273-33281
    • Tomita, T.1
  • 129
    • 0034282749 scopus 로고    scopus 로고
    • Mutation of conserved aspartates affects maturation of both aspartate mutant and endogenous presenilin 1 and presenilin 2 complexes
    • Yu, G. et al. Mutation of conserved aspartates affects maturation of both aspartate mutant and endogenous presenilin 1 and presenilin 2 complexes. J. Biol. Chem. 275, 27348-27353 (2000).
    • (2000) J. Biol. Chem , vol.275 , pp. 27348-27353
    • Yu, G.1
  • 130
    • 0033516554 scopus 로고    scopus 로고
    • Mutagenesis identifies new signals for β-amyloid precursor protein endocytosis, turnover, and the generation of secreted fragments, including Aβ42
    • Perez, R. G. et al. Mutagenesis identifies new signals for β-amyloid precursor protein endocytosis, turnover, and the generation of secreted fragments, including Aβ42. J. Biol. Chem. 274, 18851-18856 (1999).
    • (1999) J. Biol. Chem , vol.274 , pp. 18851-18856
    • Perez, R.G.1
  • 131
    • 0032415249 scopus 로고    scopus 로고
    • The presenilin protein family member SPE-4 localizes to an ER/Golgi derived organelle and is required for proper cytoplasmic partitioning during Caenorhabditis elegans spermatogenesis
    • Arduengo, P M., Appleberry, O. K., Chuang, P & L'Hernault, S. W. The presenilin protein family member SPE-4 localizes to an ER/Golgi derived organelle and is required for proper cytoplasmic partitioning during Caenorhabditis elegans spermatogenesis. J. Cell Sci. 111, 3645-3654 (1998).
    • (1998) J. Cell Sci , vol.111 , pp. 3645-3654
    • Arduengo, P.M.1    Appleberry, O.K.2    Chuang, P.3    L'hernault, S.W.4
  • 132
    • 0035923750 scopus 로고    scopus 로고
    • Interaction with telencephalin and the amyloid precursor protein predicts a ring structure for presenilins
    • Annaert, W. G. et al. Interaction with telencephalin and the amyloid precursor protein predicts a ring structure for presenilins. Neuron 32, 579-589 (2001).
    • (2001) Neuron , vol.32 , pp. 579-589
    • Annaert, W.G.1
  • 133
    • 0033599028 scopus 로고    scopus 로고
    • Transport-dependent proteolysis of SREBP: Relocation of site-1 protease from Golgi to ER obviates the need for SREBP transport to Golgi
    • DeBose-Boyd, R. A. et al. Transport-dependent proteolysis of SREBP: relocation of site-1 protease from Golgi to ER obviates the need for SREBP transport to Golgi. Cell 99, 703-712 (1999).
    • (1999) Cell , vol.99 , pp. 703-712
    • Debose-Boyd, R.A.1
  • 134
    • 0035112647 scopus 로고    scopus 로고
    • BACE1 is the major β-secretase for generation of Aβ peptides by neurons
    • Cai, H. et al. BACE1 is the major β-secretase for generation of Aβ peptides by neurons. Nature Neurosci. 4, 233-234 (2001).
    • (2001) Nature Neurosci , vol.4 , pp. 233-234
    • Cai, H.1
  • 135
    • 0035943450 scopus 로고    scopus 로고
    • The brain's susceptibility to amyloid plaques
    • Wong, P C., Price, D. L. & Cai, H. The brain's susceptibility to amyloid plaques. Science 293, 1434 (2001).
    • (2001) Science , vol.293 , pp. 1434
    • Wong, P.C.1    Price, D.L.2    Cai, H.3
  • 136
    • 0035912829 scopus 로고    scopus 로고
    • γ-Secretase inhibitors repress thymocyte development
    • Hadland, B. K. et al. γ-Secretase inhibitors repress thymocyte development. Proc. Natl Acad. Sci. USA 98, 7487-7491 (2001).
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 7487-7491
    • Hadland, B.K.1
  • 137
    • 0034573291 scopus 로고    scopus 로고
    • Piecing together Alzheimer's
    • St George-Hyslop, P. H. Piecing together Alzheimer's. Sci. Am. 283, 76-83 (2000)
    • (2000) Sci. Am. , vol.283 , pp. 76-83
    • St George-Hyslop, P.H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.