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Volumn 1, Issue 3, 2000, Pages 217-224

Intramembrane proteolysis by presenilins

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID PRECURSOR PROTEIN; ASPARTIC PROTEINASE; BACE1 PROTEIN, HUMAN; MEMBRANE PROTEIN; PRESENILIN 1; PRESENILIN 2; PROTEINASE; PSEN1 PROTEIN, HUMAN; PSEN2 PROTEIN, HUMAN; SECRETASE;

EID: 0034568802     PISSN: 14710072     EISSN: None     Source Type: Journal    
DOI: 10.1038/35043065     Document Type: Review
Times cited : (149)

References (106)
  • 1
    • 0032084472 scopus 로고    scopus 로고
    • Structural and kinetic features of amyloid β-protein fibrillogenesis
    • Teplow, D. B. Structural and kinetic features of amyloid β-protein fibrillogenesis. Amyloid 5, 121-142 (1998).
    • (1998) Amyloid , vol.5 , pp. 121-142
    • Teplow, D.B.1
  • 2
    • 0344431341 scopus 로고    scopus 로고
    • Structural neurology: Are seeds at the root of neuronal degeneration?
    • Lansbury, P. T. Jr Structural neurology: are seeds at the root of neuronal degeneration? Neuron 19, 1151-1154 (1997).
    • (1997) Neuron , vol.19 , pp. 1151-1154
    • Lansbury Jr., P.T.1
  • 3
    • 0029896354 scopus 로고
    • Mechanisms of neuronal degeneration in Alzheimer's disease
    • Yankner, B. A. Mechanisms of neuronal degeneration in Alzheimer's disease. Neuron 16, 921-932 (1995).
    • (1995) Neuron , vol.16 , pp. 921-932
    • Yankner, B.A.1
  • 4
    • 0027333557 scopus 로고
    • Cellular processing of β-amyloid precursor protein and the genesis of amyloid β-peptide
    • Haass, C. & Selkoe, D. J. Cellular processing of β-amyloid precursor protein and the genesis of amyloid β-peptide. Cell 75, 1039-1042 (1993).
    • (1993) Cell , vol.75 , pp. 1039-1042
    • Haass, C.1    Selkoe, D.J.2
  • 5
    • 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
  • 6
    • 0033623415 scopus 로고    scopus 로고
    • Aβ-generating enyzmes: Recent advances in β- and γ-secretase research
    • Vassar, R. & Citron, M. Aβ-generating enyzmes: recent advances in β- and γ-secretase research. Neuron 27, 419-422 (2000).
    • (2000) Neuron , vol.27 , pp. 419-422
    • Vassar, R.1    Citron, M.2
  • 7
    • 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
  • 8
    • 0029989591 scopus 로고    scopus 로고
    • Enhanced release of amyloid β-protein from codon 670/671 'Swedish' mutant β-amyloid precursor protein occurs in both secretory and endocytic pathways
    • Perez, R. G., Squazzo, S. L & Koo, E. H. Enhanced release of amyloid β-protein from codon 670/671 'Swedish' mutant β-amyloid precursor protein occurs in both secretory and endocytic pathways. J. Biol. Chem. 271, 9100-9107 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 9100-9107
    • Perez, R.G.1    Squazzo, S.L.2    Koo, E.H.3
  • 9
    • 0033551099 scopus 로고    scopus 로고
    • Peptidomimetic probes and molecular modeling suggest that Alzheimer's γ-secretase is an intramembrane-cleaving aspartyl protease
    • Wolfe, M. S. et al. Peptidomimetic probes and molecular modeling suggest that Alzheimer's γ-secretase is an intramembrane-cleaving aspartyl protease. Biochemistry 38, 4720-4727 (1999).
    • (1999) Biochemistry , vol.38 , pp. 4720-4727
    • Wolfe, M.S.1
  • 10
    • 0032981558 scopus 로고    scopus 로고
    • Mechanism of the cleavage specif city of Alzheimer's disease γ-secretase identified by phenylalanine-scanning mutagenesis of the transmembrane domain of the amyloid precursor protein
    • Lichtenthaler, S. F. et al. Mechanism of the cleavage specif city of Alzheimer's disease γ-secretase identified by phenylalanine-scanning mutagenesis of the transmembrane domain of the amyloid precursor protein. Proc. Natl Acad. Sci. USA 96, 3053-3058 (1999).
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 3053-3058
    • Lichtenthaler, S.F.1
  • 11
    • 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
  • 12
    • 0027407570 scopus 로고
    • Generation of β-amyloid in the secretory pathway in neuronal and nonneuronal cells
    • Busciglio, J., Gabuzda, D. H., Matsudaira, P. & Yankner. B. A. Generation of β-amyloid in the secretory pathway in neuronal and nonneuronal cells. Proc. Natl Acad. Sci. USA 90, 2092-2096 (1993).
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 2092-2096
    • Busciglio, J.1    Gabuzda, D.H.2    Matsudaira, P.3    Yankner, B.A.4
  • 13
    • 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
  • 14
    • 0026646605 scopus 로고
    • Isolation and quantification of soluble Alzheimer's β-peptide from biological fluids
    • Seubert, P. et al. Isolation and quantification of soluble Alzheimer's β-peptide from biological fluids. Nature 359, 325-327 (1992).
    • (1992) Nature , vol.359 , pp. 325-327
    • Seubert, P.1
  • 15
    • 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
  • 16
    • 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
  • 17
    • 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
  • 18
    • 0034141195 scopus 로고    scopus 로고
    • The ADAM gene family: Surface proteins with adhesion and protease activity
    • Primakoff, P. & Myles, D. G. The ADAM gene family: surface proteins with adhesion and protease activity. Trends Genet. 16, 83-87 (2000).
    • (2000) Trends Genet. , vol.16 , pp. 83-87
    • Primakoff, P.1    Myles, D.G.2
  • 19
    • 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 (1992).
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 6075-6079
    • Sisodia, S.S.1
  • 20
    • 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
  • 21
    • 0029101491 scopus 로고
    • Familial Alzheimer's disease in kindreds with missense mutations in a 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 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
  • 22
    • 0029087026 scopus 로고
    • Candidate gene for the chromosome 1 familial Alzheimer's disease focus
    • Levy-Lahad, E. et al. Candidate gene for the chromosome 1 familial Alzheimer's disease focus. Science 269, 973-977 (1995).
    • (1995) Science , vol.269 , pp. 973-977
    • Levy-Lahad, E.1
  • 23
    • 6844240203 scopus 로고    scopus 로고
    • A novel Polish presenilin-1 mutation (P117L) is associated with familial Alzheimer's disease and leads to death as early as the age of 28 years
    • Wisniewski, T. et al. A novel Polish presenilin-1 mutation (P117L) is associated with familial Alzheimer's disease and leads to death as early as the age of 28 years. Neuroreport 9, 217-221 (1998).
    • (1998) Neuroreport , vol.9 , pp. 217-221
    • Wisniewski, T.1
  • 24
    • 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). First demonstration that presenilins undergo endoproteolysis and occur as stable amino- and carboxy-terminal fragments in vivo.
    • (1996) Neuron , vol.17 , pp. 181-190
    • Thinakaran, G.1
  • 25
    • 12644290265 scopus 로고    scopus 로고
    • Evidence for phosphorylation and oligomeric assembly of presenilin 1
    • Seeger, M. et al. Evidence for phosphorylation and oligomeric assembly of presenilin 1. Proc. Natl Acad. Sci. USA 94, 5090-5094 (1997).
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 5090-5094
    • Seeger, M.1
  • 26
    • 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
  • 27
    • 0032568821 scopus 로고    scopus 로고
    • The presenuin 1 protein is a component of a high molecular weight intracellular complex that contains β-catenin
    • Yu, G. et al. The presenuin 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
  • 28
    • 0031920383 scopus 로고    scopus 로고
    • Stable association of presenilin derivatives and absence of presenilin interactions with APR Neurobiol
    • Thinakaran, G. et al. Stable association of presenilin derivatives and absence of presenilin interactions with APR Neurobiol. Dis. 4, 438-453 (1998).
    • (1998) Dis. , vol.4 , pp. 438-453
    • Thinakaran, G.1
  • 29
    • 0033553564 scopus 로고    scopus 로고
    • Evidence that intramolecular associations between presenilin domains are obligatory for endoproteolytic processing
    • Saura, C. A. et al. Evidence that intramolecular associations between presenilin domains are obligatory for endoproteolytic processing. J. Biol. Chem. 274, 13818-13823 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 13818-13823
    • Saura, C.A.1
  • 30
    • 0030293854 scopus 로고    scopus 로고
    • Protein topology of presenilin 1
    • Doan, A. et al. Protein topology of presenilin 1. Neuron 17, 1023-1030 (1996).
    • (1996) Neuron , vol.17 , pp. 1023-1030
    • Doan, A.1
  • 31
    • 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
  • 32
    • 0032499750 scopus 로고    scopus 로고
    • Additional evidence for an eight-transmembrane-domain topology for Caenorhabditis elegans and human presenilins
    • Li, X. & Greenwald, I. Additional evidence for an eight-transmembrane-domain topology for Caenorhabditis elegans and human presenilins. Proc. Natl Acad. Sci. USA 95, 7109-7114 (1998).
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 7109-7114
    • Li, X.1    Greenwald, I.2
  • 33
    • 0030922146 scopus 로고    scopus 로고
    • Evidence for a six-transmembrane domain structure of presenilin 1
    • Lehmann, S., Chiesa, R & Harris, D. A. Evidence for a six-transmembrane domain structure of presenilin 1. J. Biol. Chem. 272, 12047-12051 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 12047-12051
    • Lehmann, S.1    Chiesa, R.2    Harris, D.A.3
  • 34
    • 0033551742 scopus 로고    scopus 로고
    • Membrane topology of Alzheimer's disease-related presenilin 1. Evidence for the existence of a molecular species with a seven membrane-spanning and one membrane-embedded structure
    • Nakai, T. et al. Membrane topology of Alzheimer's disease-related presenilin 1. Evidence for the existence of a molecular species with a seven membrane-spanning and one membrane-embedded structure. J. Biol. Chem. 274, 23647-23658 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 23647-23658
    • Nakai, T.1
  • 35
    • 16044373524 scopus 로고    scopus 로고
    • Secreted amyloid β-protein similar to that in the senile plaques of Alzheimer's disease is increased in vivo by the presenilin 1 and 2 and APP mutations linked to familial Alzheimer's disease
    • Scheuner, D. et al. Secreted amyloid β-protein similar to that in the senile plaques of Alzheimer's disease is increased in vivo by the presenilin 1 and 2 and APP mutations linked to familial Alzheimer's disease. Nature Med. 2, 864-870 (1996). Familial Alzheimer's disease-linked mutations of PS1 and PS2 enhance Aβ42 production in vivo.
    • (1996) Nature Med. , vol.2 , pp. 864-870
    • Scheuner, D.1
  • 36
    • 0033600274 scopus 로고    scopus 로고
    • Translating cell biology into therapeutic advances in Alzheimer's disease
    • Selkoe, D. J. Translating cell biology into therapeutic advances in Alzheimer's disease. Nature 399, A23-A31 (1999).
    • (1999) Nature , vol.399
    • Selkoe, D.J.1
  • 37
  • 38
    • 0028989016 scopus 로고
    • Notch1 is required for tne coordinate segmentation of somites
    • Conlon, R. A., Reaume, A. G. S Rossant, J. Notch1 is required for tne coordinate segmentation of somites. Development 121, 1533-1545 (1995).
    • (1995) Development , vol.121 , pp. 1533-1545
    • Conlon, R.A.1    Reaume, A.G.S.2    Rossant, J.3
  • 39
    • 0034671686 scopus 로고    scopus 로고
    • Notch signaling: From the outside in
    • On the press
    • Mumm, J. S. & Kopan, R. Notch signaling: From the outside in. Dev. Biol. On the press).
    • Dev. Biol.
    • Mumm, J.S.1    Kopan, R.2
  • 40
    • 17744401440 scopus 로고    scopus 로고
    • Presenilin 1 is required for Notch 1 and DII1 expression in the paraxial mesoderm
    • Wong, P. C. et al. Presenilin 1 is required for Notch 1 and DII1 expression in the paraxial mesoderm. Nature 387, 288-292 (1997).
    • (1997) Nature , vol.387 , pp. 288-292
    • Wong, P.C.1
  • 41
    • 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
  • 42
    • 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
  • 43
    • 0032728957 scopus 로고    scopus 로고
    • Mice lacking both presenilin genes exhibit early embryonic patterning defects
    • Donoviel, D. B. 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.B.1
  • 44
    • 0029116848 scopus 로고
    • Facilitation of lin-72-mediated signalling by sel-12, a Caenorhabditis elegans S182 Alzheimer's disease gene
    • Levitan, D. & Greenwald, I. Facilitation of lin-72-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
  • 45
    • 0029906585 scopus 로고    scopus 로고
    • Assessment of normal and mutant human presenilin function in Caenorhabditis elegans
    • Levitan, D. et al. Assessment of normal and mutant human presenilin function in Caenorhabditis elegans. Proc. Natl Acad. Sci. USA 93, 14940-14944 (1996).
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 14940-14944
    • Levitan, D.1
  • 46
    • 0031108103 scopus 로고    scopus 로고
    • Human presenilin-1, but not familial Alzheimer's disease (FAD) mutants, facilitate Caenorhabditis elegans Notch signalling independently of proteolytic processing
    • Baumeister, R. et al. Human presenilin-1, but not familial Alzheimer's disease (FAD) mutants, facilitate Caenorhabditis elegans Notch signalling independently of proteolytic processing. Genes Funct. 1, 149-159 (1997).
    • (1997) Genes Funct. , vol.1 , pp. 149-159
    • Baumeister, R.1
  • 47
    • 0033214070 scopus 로고    scopus 로고
    • A loss of function mutation of preseniln-2 interferes with amyloid β-peptide production and Notch signaling
    • Steiner, H. et al. A loss of function mutation of preseniln-2 interferes with amyloid β-peptide production and Notch signaling. J. Biol. Chem. 274, 28669-28673 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 28669-28673
    • Steiner, H.1
  • 48
    • 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
  • 49
    • 0034691513 scopus 로고    scopus 로고
    • Presenilin is required for proper morphology and function of neurons in C. elegans
    • Wittenburg, N. et al. Presenilin is required for proper morphology and function of neurons in C. elegans. Nature 406, 306-309 (2000).
    • (2000) Nature , vol.406 , pp. 306-309
    • Wittenburg, N.1
  • 50
    • 0033535555 scopus 로고    scopus 로고
    • Neurogenic phenotypes and altered Notch processing in Drosophila Presenilin mutants
    • Ye, Y., Lukinova, N. & Fortini, M. E. Neurogenic phenotypes and altered Notch processing in Drosophila Presenilin mutants. Nature 398, 525-529 (1999).
    • (1999) Nature , vol.398 , pp. 525-529
    • Ye, Y.1    Lukinova, N.2    Fortini, M.E.3
  • 51
    • 0033535508 scopus 로고    scopus 로고
    • Presenilin is required for activity and nuclear access of Notch in Drosophila
    • Struhl, G. & Greenwald, I. Presenilin is required for activity and nuclear access of Notch in Drosophila. Nature 398, 522-525 (1999).
    • (1999) Nature , vol.398 , pp. 522-525
    • Struhl, G.1    Greenwald, I.2
  • 52
    • 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). Pioneering work showing that PS1-knockout cells are deficient In γ-secretase cleavage of βAPP.
    • (1998) Nature , vol.391 , pp. 387-390
    • De Strooper, B.1
  • 53
    • 0032574993 scopus 로고    scopus 로고
    • Notch-1 signalling requires ligand-induced proteofytic release of intracellular domain
    • Schroeter, E. H., Kisslinger, J. A. & Kopan, R. Notch-1 signalling requires ligand-induced proteofytic 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
  • 54
    • 0032524325 scopus 로고    scopus 로고
    • Nuclear access and action of Notch in vivo
    • Struhl, G. & Adachi, A. Nuclear access and action of Notch in vivo. Cell 93, 649-660 (1998).
    • (1998) Cell , vol.93 , pp. 649-660
    • Struhl, G.1    Adachi, A.2
  • 55
    • 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
  • 56
    • 0033535504 scopus 로고    scopus 로고
    • A presenilin-1 -dependent γ-secretase-like protease mediates release of Notch intracellar domain
    • De Strooper, B. et al. A presenilin-1 -dependent γ-secretase-like protease mediates release of Notch intracellar domain. Nature 398, 518-522 (1999). PS1 deficiency as well as γ-secretase inhibitors block the γ-secretase-like cleavage of Notch.
    • (1999) Nature , vol.398 , pp. 518-522
    • De Strooper, B.1
  • 57
    • 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. et al. 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).
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 6959-6963
    • Song, W.1
  • 58
    • 0033779635 scopus 로고    scopus 로고
    • Presenilins are required for γ-secretase cleavage of βAPP and transmembrane cleavage of Notch-1
    • Zhang, Z. et al. Presenilins are required for γ-secretase cleavage of βAPP 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
  • 59
    • 0033775709 scopus 로고    scopus 로고
    • Total inactivation of β-secretase activity in presenilin-deficient embryonic stem cells
    • Herreman, A. et al. Total inactivation of β-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
  • 60
    • 0032493302 scopus 로고    scopus 로고
    • The Notch1 receptor is cleaved constitutivety by a furin-like convertase
    • Logeat, F. et al. The Notch1 receptor is cleaved constitutivety by a furin-like convertase. Proc. Natl Acad. Sci. USA 95, 8108-8112 (1998).
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 8108-8112
    • Logeat, F.1
  • 61
    • 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
  • 62
    • 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
  • 63
    • 0000138540 scopus 로고    scopus 로고
    • Effects of PS1 deficiency on membrane protein trafficking in neurons
    • Naruse, S. et al. Effects of PS1 deficiency on membrane protein trafficking in neurons. Neuron 21, 1213-1221 (1998).
    • (1998) Neuron , vol.21 , pp. 1213-1221
    • Naruse, S.1
  • 64
    • 0034254585 scopus 로고    scopus 로고
    • L-685,458, an aspartyt protease transition state mimic, is a potent inhibitor of amyloid β-protein precursor γ-secretase activity
    • Shearman, M. S. et al. L-685,458, an aspartyt protease transition state mimic, is a potent inhibitor of amyloid β-protein precursor γ-secretase activity. Biochemistry 39, 8698-8704 (2000).
    • (2000) Biochemistry , vol.39 , pp. 8698-8704
    • Shearman, M.S.1
  • 65
    • 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). Mutational analysis of two conserved aspartates within TM6 and TM7 indicates that presenilins may be unusual aspartyl proteases identical with γ-secretase.
    • (1999) Nature , vol.398 , pp. 513-517
    • Wolfe, M.S.1
  • 66
    • 0034255029 scopus 로고    scopus 로고
    • Presenilin complexes with the C-terminal fragments of amyloid precursor protein at the sites of amyloid β-protein generation
    • Xia, W. et al. Presenilin complexes with the C-terminal fragments of amyloid precursor protein at the sites of amyloid β-protein generation. Proc. Natl Acad. Sci. USA 97, 9299-9304 (2000).
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 9299-9304
    • Xia, W.1
  • 67
    • 0000792598 scopus 로고    scopus 로고
    • The transmembrane aspartates in presenilin 1 and 2 are obligatory for γ-secretase activity and amyloid β-protein generation
    • Kimberly, W. T., Xia, W., Rahmati, T. Wolfe, M. S. & Selkoe, D. J. The transmembrane aspartates in presenilin 1 and 2 are obligatory for γ-secretase activity and amyloid β-protein generation. J. Biol. Chem. 275, 3173-3178 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 3173-3178
    • Kimberly, W.T.1    Xia, W.2    Rahmati, T.3    Wolfe, M.S.4    Selkoe, D.J.5
  • 68
    • 0033550061 scopus 로고    scopus 로고
    • Zebrafish (Danio rerio) presenilin promotes aberrant amyloid β-peptide production and requires a critical aspartate residue for its function in amyloidogenesis
    • Leimer, U. et al. Zebrafish (Danio rerio) presenilin promotes aberrant amyloid β-peptide production and requires a critical aspartate residue for its function in amyloidogenesis. Biochemistry 38, 13602-13609 (1999).
    • (1999) Biochemistry , vol.38 , pp. 13602-13609
    • Leimer, U.1
  • 69
    • 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
  • 70
    • 0032507667 scopus 로고    scopus 로고
    • Caspase-mediated cleavage is not required for the activity of presenilins in amyloidogenesis and Notch signaling
    • Brockhaus, M. et al. Caspase-mediated cleavage is not required for the activity of presenilins in amyloidogenesis and Notch signaling. Neuroreport 9, 1481-1486 (1998).
    • (1998) Neuroreport , vol.9 , pp. 1481-1486
    • Brockhaus, M.1
  • 71
    • 0033610863 scopus 로고    scopus 로고
    • Expression of Alzheimer's disease-associated presenilin-1 is controlled by proteolytic degradation and complex formation
    • Steiner, H. et al. Expression of Alzheimer's disease-associated presenilin-1 is controlled by proteolytic degradation and complex formation. J. Biol. Chem. 273, 32322-32331 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 32322-32331
    • Steiner, H.1
  • 72
    • 0032516821 scopus 로고    scopus 로고
    • Molecular dissection of domains in mutant presenilin 2 that mediate overproduction of amyloidogenic forms of amyloid β-peptides. Inability of truncated forms of PS2 with familial Alzheimer's disease mutation to increase secretion of Aβ42
    • Tomita, T. et al. Molecular dissection of domains in mutant presenilin 2 that mediate overproduction of amyloidogenic forms of amyloid β-peptides. Inability of truncated forms of PS2 with familial Alzheimer's disease mutation to increase secretion of Aβ42. J. Biol. Chem. 273, 21153-21160 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 21153-21160
    • Tomita, T.1
  • 73
    • 0031710159 scopus 로고    scopus 로고
    • Additive effects of PS1 and APP mutations on secretion of the 42-residue amyloid β-protein
    • Citron, M. et al. Additive effects of PS1 and APP mutations on secretion of the 42-residue amyloid β-protein. Neurobiol. Disord. 5, 107-116 (1998).
    • (1998) Neurobiol. Disord. , vol.5 , pp. 107-116
    • Citron, M.1
  • 74
    • 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
  • 75
    • 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, 428-433 (2000). References 74 and 75 show that transition-state analogue inhibitors bind to preseniuns, indicating that presenilins may contain the active site of γ-secretase.
    • (2000) Nature Cell Biol. , vol.2 , pp. 428-433
    • Esler, W.P.1
  • 76
    • 0033517844 scopus 로고    scopus 로고
    • Amyloidogenic function of the Alzheimer's disease-associated presenilin 1 in the absence of endoproteolysis
    • Steiner, H. et al. Amyloidogenic function of the Alzheimer's disease-associated presenilin 1 in the absence of endoproteolysis. Biochemistry 38, 14600-14605 (1999).
    • (1999) Biochemistry , vol.38 , pp. 14600-14605
    • Steiner, H.1
  • 77
    • 0033521141 scopus 로고    scopus 로고
    • The influence of endoproteolytic processing of familial Alzheimer's disease presenilin 2 on Aγ42 amyloid peptide formation
    • Jacobsen, H. et al. The influence of endoproteolytic processing of familial Alzheimer's disease presenilin 2 on Aγ42 amyloid peptide formation. J. Biol. Chem. 274, 35233-35239 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 35233-35239
    • Jacobsen, H.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). Identification of nicastrin, a component of the presenilin complex that modulates γ-secretase activity.
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 6138-6143
    • Li, Y.-M.1
  • 79
    • 0034618715 scopus 로고    scopus 로고
    • Nicastrin modulates presenilin-mediated notch/glp-1 signal transduction and βAPP processing
    • Yu, G. et al. Nicastrin modulates presenilin-mediated notch/glp-1 signal transduction and βAPP processing. Nature 407, 48-54 (2000).
    • (2000) Nature , vol.407 , pp. 48-54
    • Yu, G.1
  • 80
    • 0028861041 scopus 로고
    • Molecular genetic analysis of familial early-onset Alzheimer's disease linked to chromosome 14q24.3
    • Cruts, M. et al. Molecular genetic analysis of familial early-onset Alzheimer's disease linked to chromosome 14q24.3. Hum. Mol. Genet. 4, 2363-2371 (1995).
    • (1995) Hum. Mol. Genet. , vol.4 , pp. 2363-2371
    • Cruts, M.1
  • 81
    • 0030297259 scopus 로고    scopus 로고
    • Sequence analysis of presenilin-1 gene mutation in Japanese Alzheimer's disease patients
    • Tanahashi, H. et al. Sequence analysis of presenilin-1 gene mutation in Japanese Alzheimer's disease patients. Neurosci. Lett. 218, 139-141 (1996).
    • (1996) Neurosci. Lett. , vol.218 , pp. 139-141
    • Tanahashi, H.1
  • 82
    • 0032587237 scopus 로고    scopus 로고
    • Evidence that Aβ42 plasma levels in presenilin-1 mutation carriers do not allow for prediction of their clinical phenotype
    • De Jonghe, C. et al. Evidence that Aβ42 plasma levels in presenilin-1 mutation carriers do not allow for prediction of their clinical phenotype. Neurobiol. Disord. 6, 280-287 (1999).
    • (1999) Neurobiol. Disord. , vol.6 , pp. 280-287
    • De Jonghe, C.1
  • 83
    • 0033778262 scopus 로고    scopus 로고
    • Glycine 384 is required for presenilin-1 function and is conserved in polytopic bacterial aspartyl proteases
    • Steiner, H. et al. Glycine 384 is required for presenilin-1 function and is conserved in polytopic bacterial aspartyl proteases. Nature Cell Biol. 2, 848-851 (2000). Presenilins share sequence homology around an active site aspartate with polytopic bacterial aspartyl proteases.
    • (2000) Nature Cell Biol. , vol.2 , pp. 848-851
    • Steiner, H.1
  • 84
    • 0033583047 scopus 로고    scopus 로고
    • The biological and pathological function of the presenilin-1 Δexon 9 mutation is independent of its defect to undergo proteolytic processing
    • Steiner, H. et al. The biological and pathological function of the presenilin-1 Δexon 9 mutation is independent of its defect to undergo proteolytic processing. J. Biol. Chem. 274, 7615-7618 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 7615-7618
    • Steiner, H.1
  • 85
    • 0033978638 scopus 로고    scopus 로고
    • The type 4 prepilin peptidases comprise a novel family of aspartic acid proteases
    • LaPointe, C. F. & Taylor, R. K. The type 4 prepilin peptidases comprise a novel family of aspartic acid proteases. J. Biol. Chem. 275, 1502-1510 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 1502-1510
    • LaPointe, C.F.1    Taylor, R.K.2
  • 86
    • 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
  • 87
    • 0033518251 scopus 로고    scopus 로고
    • Purification and cloning of amyloid precursor protein β-secretase from human brain
    • Sinha, S. et al. Purification and cloning of amyloid precursor protein β-secretase from human brain. Nature 402, 537-540 (1999).
    • (1999) Nature , vol.402 , pp. 537-540
    • Sinha, S.1
  • 88
    • 0031915681 scopus 로고    scopus 로고
    • A substrate-based difluoroketone selectively inhibits Alzheimer's γ-secretase activity
    • Wolfe, M. S. et al. A substrate-based difluoroketone selectively inhibits Alzheimer's γ-secretase activity. J. Med. Chem. 41, 6-9 (1998).
    • (1998) J. Med. Chem. , vol.41 , pp. 6-9
    • Wolfe, M.S.1
  • 89
    • 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
  • 90
    • 0034161516 scopus 로고    scopus 로고
    • Neurons regulate extracellular levels of amyloid β-protein via proteolysis by insulin-degrading enzyme
    • Vekrellis, K. et al. Neurons regulate extracellular levels of amyloid β-protein via proteolysis by insulin-degrading enzyme. J. Neurosci. 20, 1657-1665 (2000).
    • (2000) J. Neurosci. , vol.20 , pp. 1657-1665
    • Vekrellis, K.1
  • 91
    • 0033621739 scopus 로고    scopus 로고
    • Identification of the major Aβ1-42-degrading catabolic pathway in brain parenchyma: Suppression leads to biochemical and pathological deposition
    • Iwata, N. et al. Identification of the major Aβ1-42-degrading catabolic pathway in brain parenchyma: suppression leads to biochemical and pathological deposition. Nature Med. 6, 143-150 (2000).
    • (2000) Nature Med. , vol.6 , pp. 143-150
    • Iwata, N.1
  • 92
    • 0033536163 scopus 로고    scopus 로고
    • Immunization with amyloid-β attenuates Alzheimer-disease-like pathology in the PDAPP mouse
    • Schenk, D. et al. Immunization with amyloid-β attenuates Alzheimer-disease-like pathology in the PDAPP mouse. Nature 400, 173-177 (1999).
    • (1999) Nature , vol.400 , pp. 173-177
    • Schenk, D.1
  • 93
    • 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
  • 94
    • 0033639117 scopus 로고    scopus 로고
    • Requirements for presenilin-dependent cleavage of Notch and other transmembrane proteins
    • Struhl, G. & Adachi, A. Requirements for presenilin-dependent cleavage of Notch and other transmembrane proteins. Mol. Cell 6, 625-636 (2000). Presenilins may have a general role in endoproteolysis of transmembrane domains of type I transmembrane proteins, which undergo ectodomain shedding.
    • (2000) Mol. Cell , vol.6 , pp. 625-636
    • Struhl, G.1    Adachi, A.2
  • 95
    • 0028322017 scopus 로고
    • An increased percentage of long amyloid β-protein secreted by familial amyloid β-protein precursor (β-APP717) mutants
    • Suzuki, N. et al. An increased percentage of long amyloid β-protein secreted by familial amyloid β-protein precursor (β-APP717) mutants. Science 264, 1336-1340 (1994).
    • (1994) Science , vol.264 , pp. 1336-1340
    • Suzuki, N.1
  • 96
    • 0028169925 scopus 로고
    • Visualization of Aβ-42(43) and Aβ-40 in senile plaques with end-specific Aβ-monoclonals: Evidence that an initially deposited species is Aβ-42(43)
    • Iwatsubo, T. et al. Visualization of Aβ-42(43) and Aβ-40 in senile plaques with end-specific Aβ-monoclonals: evidence that an initially deposited species is Aβ-42(43). Neuron 13, 45-53 (1994).
    • (1994) Neuron , vol.13 , pp. 45-53
    • Iwatsubo, T.1
  • 97
    • 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
  • 98
    • 0033845327 scopus 로고    scopus 로고
    • Endogenous presenilin-1 targets to endocytic rather than biosynthetic compartments
    • Lah, J. J. & Levey, A. I. Endogenous presenilin-1 targets to endocytic rather than biosynthetic compartments. Mol. Cell. Neurosci. 16, 111-126 (2000).
    • (2000) Mol. Cell. Neurosci. , vol.16 , pp. 111-126
    • Lah, J.J.1    Levey, A.I.2
  • 99
    • 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
  • 100
    • 0034716887 scopus 로고    scopus 로고
    • Tripartite management of unfolded proteins in the endoplasmic reticulum
    • Mori, K. Tripartite management of unfolded proteins in the endoplasmic reticulum. Cell 101, 451-454 (2000).
    • (2000) Cell , vol.101 , pp. 451-454
    • Mori, K.1
  • 101
    • 0033671650 scopus 로고    scopus 로고
    • Upregulation of BiP and CHOP by the unfolded protein response is independent of presenilin expression
    • Sato, N. et al. Upregulation of BiP and CHOP by the unfolded protein response is independent of presenilin expression. Nature Cell Biol. 2, 863-870 (2000).
    • (2000) Nature Cell Biol. , vol.2 , pp. 863-870
    • Sato, N.1
  • 102
    • 0033598996 scopus 로고    scopus 로고
    • A role for presenilin-1 in nuclear accumulation of Ire1 fragments and induction of the mammalian unfolded protein response
    • Niwa, M., Sidrauski, C., Kaufman, R. J. & Walter, P. A role for presenilin-1 in nuclear accumulation of Ire1 fragments and induction of the mammalian unfolded protein response. Cell 99, 691-702 (1999).
    • (1999) Cell , vol.99 , pp. 691-702
    • Niwa, M.1    Sidrauski, C.2    Kaufman, R.J.3    Walter, P.4
  • 103
    • 0033258544 scopus 로고    scopus 로고
    • Presenilin-1 mutations downregulate the signalling pathway of the unfolded-protein response
    • Katayama, T. et al. Presenilin-1 mutations downregulate the signalling pathway of the unfolded-protein response. Nature Cell Biol. 1, 479-485 (1999).
    • (1999) Nature Cell Biol. , vol.1 , pp. 479-485
    • Katayama, T.1
  • 104
    • 10544224542 scopus 로고    scopus 로고
    • Participation of presenilin 2 in apoptosis: Enhanced basal activity conferred by an Alzheimer mutation
    • Wolozin, B. et al. Participation of presenilin 2 in apoptosis: enhanced basal activity conferred by an Alzheimer mutation. Science 274, 1710-1713 (1996).
    • (1996) Science , vol.274 , pp. 1710-1713
    • Wolozin, B.1
  • 105
    • 0030868903 scopus 로고    scopus 로고
    • Alternative cleavage of Alzheimer-associated presenilins during apoptosis by a caspase-3 family protease
    • Kim, T. W., Pettingell, W. H., Jung, Y. K., Kovacs, D. M. & Tanzi, R. E. Alternative cleavage of Alzheimer-associated presenilins during apoptosis by a caspase-3 family protease. Science 277, 373-376 (1997).
    • (1997) Science , vol.277 , pp. 373-376
    • Kim, T.W.1    Pettingell, W.H.2    Jung, Y.K.3    Kovacs, D.M.4    Tanzi, R.E.5
  • 106
    • 0033712477 scopus 로고    scopus 로고
    • Presenilin-mediated modulation of capacitative calcium entry
    • Yoo, A. S. et al. Presenilin-mediated modulation of capacitative calcium entry. Neuron 27, 561-572 (2000).
    • (2000) Neuron , vol.27 , pp. 561-572
    • Yoo, A.S.1


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