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Volumn 54, Issue , 2003, Pages 233-261

The secretases of Alzheimer's disease

Author keywords

[No Author keywords available]

Indexed keywords

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

EID: 0041357787     PISSN: 00702153     EISSN: None     Source Type: Book Series    
DOI: 10.1016/s0070-2153(03)54011-x     Document Type: Review
Times cited : (31)

References (145)
  • 1
    • 85112956152 scopus 로고    scopus 로고
    • http://www.alzforum.org/members/resources/app mutations/app table.html
  • 2
    • 85112909358 scopus 로고    scopus 로고
    • http://www.alzforum.org/members/resources/pres mutations/index.html
  • 3
    • 0033970139 scopus 로고    scopus 로고
    • The gene encoding DRAP (BACE2), a glycosylated transmembrane protein of the aspartic protease family, maps to the down critical region
    • F Acquati M Accarino C Nucci P Fumagalli L Jovine S Ottolenghi R Taramelli The gene encoding DRAP (BACE2), a glycosylated transmembrane protein of the aspartic protease family, maps to the down critical region FEBS Lett. 468 2000 59 64
    • (2000) FEBS Lett. , vol.468 , pp. 59-64
    • Acquati, F1    Accarino, M2    Nucci, C3    Fumagalli, P4    Jovine, L5    Ottolenghi, S6    Taramelli, R7
  • 4
    • 0033617522 scopus 로고    scopus 로고
    • Notch signaling: cell fate control and signal integration in development
    • S Artavanis-Tsakonas M.D Rand R.J Lake Notch signaling: cell fate control and signal integration in development Science 284 1999 770 776
    • (1999) Science , vol.284 , pp. 770-776
    • Artavanis-Tsakonas, S1    Rand, M.D2    Lake, R.J3
  • 6
    • 0033944273 scopus 로고    scopus 로고
    • Aspartate mutations in presenilin and γ-secretase inhibitors both impair Notch1 proteolysis and nuclear translocation with relative preservation of Notch1 signaling
    • O Berezovska C Jack P McLean J.C Aster C Hicks W Xia M.S Wolfe W.T Kimberly G Weinmaster D.J Selkoe B.T Hyman Aspartate mutations in presenilin and γ-secretase inhibitors both impair Notch1 proteolysis and nuclear translocation with relative preservation of Notch1 signaling J. Neurochem. 75 2000 583 593
    • (2000) J. Neurochem. , vol.75 , pp. 583-593
    • Berezovska, O1    Jack, C2    McLean, P3    Aster, J.C4    Hicks, C5    Xia, W6    Wolfe, M.S7    Kimberly, W.T8    Weinmaster, G9    Selkoe, D.J10    Hyman, B.T11
  • 7
    • 0014313861 scopus 로고
    • The association between quantitative measure of dementia and of senile change in the cerebral grey matter of elderly subjects
    • G Blessed B.E Tomlinson M Roth The association between quantitative measure of dementia and of senile change in the cerebral grey matter of elderly subjects Brit. J. Psychiat. 114 1968 797 811
    • (1968) Brit. J. Psychiat. , vol.114 , pp. 797-811
    • Blessed, G1    Tomlinson, B.E2    Roth, M3
  • 9
    • 0030909336 scopus 로고    scopus 로고
    • Modulation of Ras and a-factor function by carboxyl-terminal proteolysis
    • V.L Boyartchuk M.N Ashby J Rine Modulation of Ras and a-factor function by carboxyl-terminal proteolysis Science 275 1997 1796 1800
    • (1997) Science , vol.275 , pp. 1796-1800
    • Boyartchuk, V.L1    Ashby, M.N2    Rine, J3
  • 11
    • 0027435535 scopus 로고
    • Protein phosphorylation inhibits production of Alzheimer amyloid beta/A4 peptide
    • J.D Buxbaum E.H Koo P Greengard Protein phosphorylation inhibits production of Alzheimer amyloid beta/A4 peptide Proc. Natl. Acad. Sci. USA 90 1993 9195 9198
    • (1993) , pp. 9195-9198
    • Buxbaum, J.D1    Koo, E.H2    Greengard, P3
  • 12
    • 14444272986 scopus 로고    scopus 로고
    • Evidence that tumor necrosis factor α converting enzyme is involved in regulated a-secretase cleavage of the Alzheimer's amyloid protein precursor
    • J.D Buxbaum K.N Liu Y Luo J.L Slack K.L Stocking J.J Peschon R.S Johnson B.J Castner D.P Cerretti R.A Black Evidence that tumor necrosis factor α converting enzyme is involved in regulated a-secretase cleavage of the Alzheimer's amyloid protein precursor J. Biol. Chem. 273 1998 27765 27767
    • (1998) J. Biol. Chem. , vol.273 , pp. 27765-27767
    • Buxbaum, J.D1    Liu, K.N2    Luo, Y3    Slack, J.L4    Stocking, K.L5    Peschon, J.J6    Johnson, R.S7    Castner, B.J8    Cerretti, D.P9    Black, R.A10
  • 14
    • 0027526419 scopus 로고
    • Release of excess amyloid beta protein from a mutant amyloid beta protein precursor
    • X.D Cai T.E Golde S.G Younkin Release of excess amyloid beta protein from a mutant amyloid beta protein precursor Science 259 1993 514 516
    • (1993) Science , vol.259 , pp. 514-516
    • Cai, X.D1    Golde, T.E2    Younkin, S.G3
  • 16
    • 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
    • A Capell J Grunberg B Pesold A Diehlmann M Citron R Nixon K Beyreuther D.J Selkoe C Haass 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 1998 3205 3211
    • (1998) J. Biol. Chem. , vol.273 , pp. 3205-3211
    • Capell, A1    Grunberg, J2    Pesold, B3    Diehlmann, A4    Citron, M5    Nixon, R6    Beyreuther, K7    Selkoe, D.J8    Haass, C9
  • 17
    • 0033783140 scopus 로고    scopus 로고
    • Presenilin-1 differentially facilitates endoproteolysis of the beta-amyloid precursor protein and Notch
    • A Capell H Steiner H Romig S Keck M Baader M.G Grim R Baumeister C Haass Presenilin-1 differentially facilitates endoproteolysis of the beta-amyloid precursor protein and Notch Nat. Cell. Biol. 2 2000 205 211
    • (2000) Nat. Cell. Biol. , vol.2 , pp. 205-211
    • Capell, A1    Steiner, H2    Romig, H3    Keck, S4    Baader, M5    Grim, M.G6    Baumeister, R7    Haass, C8
  • 19
    • 0035204206 scopus 로고    scopus 로고
    • Nicastrin is required for Presenilin-mediated transmembrane cleavage in Drosophila
    • H.M Chung G Struhl Nicastrin is required for Presenilin-mediated transmembrane cleavage in Drosophila Nat. Cell Biol. 3 2001 1129 1132
    • (2001) Nat. Cell Biol. , vol.3 , pp. 1129-1132
    • Chung, H.M1    Struhl, G2
  • 21
    • 0028924248 scopus 로고
    • Generation of amyloid beta protein from its precursor is sequence specific
    • M Citron D.B Teplow D.J Selkoe Generation of amyloid beta protein from its precursor is sequence specific Neuron 14 1995 661 670
    • (1995) Neuron , vol.14 , pp. 661-670
    • Citron, M1    Teplow, D.B2    Selkoe, D.J3
  • 22
    • 0028099612 scopus 로고
    • Excessive production of amyloid beta-protein by peripheral cells of symptomatic and presymptomatic patients carrying the Swedish familial Alzheimer disease mutation
    • M Citron C Vigo-Pelfrey D.B Teplow C Miller D Schenk J Johnston B Winblad N Venizelos L Lannfelt D.J Selkoe Excessive production of amyloid beta-protein by peripheral cells of symptomatic and presymptomatic patients carrying the Swedish familial Alzheimer disease mutation Proc. Natl. Acad. Sci. USA 91 1994 11993 11997
    • (1994) , pp. 11993-11997
    • Citron, M1    Vigo-Pelfrey, C2    Teplow, D.B3    Miller, C4    Schenk, D5    Johnston, J6    Winblad, B7    Venizelos, N8    Lannfelt, L9    Selkoe, D.J10
  • 24
    • 0028972701 scopus 로고
    • Image analysis of β -amyloid load in Alzheimer's disease and relation to dementia severity
    • B.J Cummings C.W Cotman Image analysis of β -amyloid load in Alzheimer's disease and relation to dementia severity Lancet 346 1995 1524 1528
    • (1995) Lancet , vol.346 , pp. 1524-1528
    • Cummings, B.J1    Cotman, C.W2
  • 30
    • 0032504202 scopus 로고    scopus 로고
    • Second-site cleavage in sterol regulatory element-binding protein occurs at transmembrane junction as determined by cysteine panning
    • E.A Duncan U.P Dave J Sakai J.L Goldstein M.S Brown Second-site cleavage in sterol regulatory element-binding protein occurs at transmembrane junction as determined by cysteine panning J. Biol. Chem. 273 1998 17801 17809
    • (1998) J. Biol. Chem. , vol.273 , pp. 17801-17809
    • Duncan, E.A1    Dave, U.P2    Sakai, J3    Goldstein, J.L4    Brown, M.S5
  • 34
    • 0037022644 scopus 로고    scopus 로고
    • Activity-dependent isolation of the presenilin/γ -secretase complex reveals nicastrin and a γ substrate
    • W.P Esler W.T Kimberly B.L Ostaszewski W Ye T.S Diehl D.J Selkoe M.S Wolfe Activity-dependent isolation of the presenilin/γ -secretase complex reveals nicastrin and a γ substrate Proc. Natl. Acad. Sci. USA 99 2002 2720 2725
    • (2002) , pp. 2720-2725
    • Esler, W.P1    Kimberly, W.T2    Ostaszewski, B.L3    Ye, W4    Diehl, T.S5    Selkoe, D.J6    Wolfe, M.S7
  • 35
    • 0034662929 scopus 로고    scopus 로고
    • BACE2, a beta-secretase homolog, cleaves at the beta site and within the amyloid-beta region of the amyloid-beta precursor protein
    • M Farzan C.E Schnitzler N Vasilieva D Leung H Choe BACE2, a beta-secretase homolog, cleaves at the beta site and within the amyloid-beta region of the amyloid-beta precursor protein Proc. Natl. Acad. Sci. USA 97 2000 9712 9717
    • (2000) , pp. 9712-9717
    • Farzan, M1    Schnitzler, C.E2    Vasilieva, N3    Leung, D4    Choe, H5
  • 36
    • 0028264451 scopus 로고
    • Reversal of the Swedish familial Alzheimer's disease mutant phenotype in cultured cells treated with phorbol 12,13-dibutyrate
    • K.M Felsenstein K.M Ingalls L.W Hunihan S.B Roberts Reversal of the Swedish familial Alzheimer's disease mutant phenotype in cultured cells treated with phorbol 12,13-dibutyrate Neurosci. Lett. 174 1994 173 176
    • (1994) Neurosci. Lett. , vol.174 , pp. 173-176
    • Felsenstein, K.M1    Ingalls, K.M2    Hunihan, L.W3    Roberts, S.B4
  • 37
    • 0031922062 scopus 로고    scopus 로고
    • Astrocytes containing amyloid beta-protein (Abeta)-positive granules are associated with Abeta40-positive diffuse plaques in the aged human brain
    • H Funato M Yoshimura T Yamazaki T.C Saido Y Ito J Yokofujita R Okeda Y Ihara Astrocytes containing amyloid beta-protein (Abeta)-positive granules are associated with Abeta40-positive diffuse plaques in the aged human brain Am. J. Pathol. 152 1998 983 992
    • (1998) Am. J. Pathol. , vol.152 , pp. 983-992
    • Funato, H1    Yoshimura, M2    Yamazaki, T3    Saido, T.C4    Ito, Y5    Yokofujita, J6    Okeda, R7    Ihara, Y8
  • 40
    • 0037085353 scopus 로고    scopus 로고
    • Substrate and inhibitor profile of BACE (beta-secretase) and comparison with other mammalian aspartic proteases
    • F Gruninger-Leitch D Schlatter E Kung P Nelbock H Dobeli Substrate and inhibitor profile of BACE (beta-secretase) and comparison with other mammalian aspartic proteases J. Biol. Chem. 277 2002 4687 4693
    • (2002) J. Biol. Chem. , vol.277 , pp. 4687-4693
    • Gruninger-Leitch, F1    Schlatter, D2    Kung, E3    Nelbock, P4    Dobeli, H5
  • 41
    • 0028246308 scopus 로고
    • Mutations associated with a locus for familial Alzheimer's disease result in alternative processing of amyloid beta-protein precursor
    • C Haass A.Y Hung D.J Selkoe D.B Teplow Mutations associated with a locus for familial Alzheimer's disease result in alternative processing of amyloid beta-protein precursor J. Biol. Chem. 269 1994 17741 17748
    • (1994) J. Biol. Chem. , vol.269 , pp. 17741-17748
    • Haass, C1    Hung, A.Y2    Selkoe, D.J3    Teplow, D.B4
  • 43
    • 0031052381 scopus 로고    scopus 로고
    • Amyloid, the presenilins and Alzheimer's disease
    • J Hardy Amyloid, the presenilins and Alzheimer's disease Trends Neurosci. 20 1997 154 159
    • (1997) Trends Neurosci. , vol.20 , pp. 154-159
    • Hardy, J1
  • 48
    • 0034613320 scopus 로고    scopus 로고
    • Structure of the protease domain of memapsin 2 (beta-secretase) complexed with inhibitor
    • L Hong G Koelsch X Lin S Wu S Terzyan A.K Ghosh X.C Zhang J Tang Structure of the protease domain of memapsin 2 (beta-secretase) complexed with inhibitor Science 290 2000 150 153
    • (2000) Science , vol.290 , pp. 150-153
    • Hong, L1    Koelsch, G2    Lin, X3    Wu, S4    Terzyan, S5    Ghosh, A.K6    Zhang, X.C7    Tang, J8
  • 49
    • 0036007117 scopus 로고    scopus 로고
    • Nicastrin is required for gamma-secretase cleavage of the Drosophila Notch receptor
    • Y Hu Y Ye M.E Fortini Nicastrin is required for gamma-secretase cleavage of the Drosophila Notch receptor Dev. Cell 2 2002 69 78
    • (2002) Dev. Cell , vol.2 , pp. 69-78
    • Hu, Y1    Ye, Y2    Fortini, M.E3
  • 50
    • 0025952925 scopus 로고
    • HIV protease: a novel chemotherapeutic target for AIDS
    • J.R Huff HIV protease: a novel chemotherapeutic target for AIDS J. Med. Chem. 34 1991 2305 2314
    • (1991) J. Med. Chem. , vol.34 , pp. 2305-2314
    • Huff, J.R1
  • 52
    • 0034702303 scopus 로고    scopus 로고
    • Embryonic lethality in mice homozygous for a processing-deficient allele of Notch1
    • S.S Huppert A Le E.H Schroeter J.S Mumm M.T Saxena L.A Milner R Kopan Embryonic lethality in mice homozygous for a processing-deficient allele of Notch1 Nature 405 2000 966 970
    • (2000) Nature , vol.405 , pp. 966-970
    • Huppert, S.S1    Le, A2    Schroeter, E.H3    Mumm, J.S4    Saxena, M.T5    Milner, L.A6    Kopan, R7
  • 53
    • 0034721842 scopus 로고    scopus 로고
    • Maturation and endosomal targeting of beta-site amyloid precursor protein-cleaving enzyme
    • J.T Huse D.S Pijak G.J Leslie V.M Lee R.W Doms Maturation and endosomal targeting of beta-site amyloid precursor protein-cleaving enzyme The Alzheimer's disease β-secretase J. Biol. Chem. 275 2000 33729 33737
    • (2000) , pp. 33729-33737
    • Huse, J.T1    Pijak, D.S2    Leslie, G.J3    Lee, V.M4    Doms, R.W5
  • 56
    • 0028169925 scopus 로고
    • Visualization of A beta 42(43) and A beta 40 in senile plaques with end-specific A beta monoclonals: evidence that an initially deposited species is A beta 42(43)
    • T Iwatsubo A Odaka N Suzuki H Mizusawa N Nukina Y Ihara Visualization of A beta 42(43) and A beta 40 in senile plaques with end-specific A beta monoclonals: evidence that an initially deposited species is A beta 42(43) Neuron 13 1994 45 53
    • (1994) Neuron , vol.13 , pp. 45-53
    • Iwatsubo, T1    Odaka, A2    Suzuki, N3    Mizusawa, H4    Nukina, N5    Ihara, Y6
  • 58
    • 0026720426 scopus 로고
    • Crystallographic analysis of transition state mimics bound to penicillopepsin: difluorostatine- and difluorostatone-containing peptides
    • M.N James A.R Sielecki K Hayakawa M.H Gelb Crystallographic analysis of transition state mimics bound to penicillopepsin: difluorostatine- and difluorostatone-containing peptides Biochemistry 31 1992 3872 3886
    • (1992) Biochemistry , vol.31 , pp. 3872-3886
    • James, M.N1    Sielecki, A.R2    Hayakawa, K3    Gelb, M.H4
  • 59
    • 0027258525 scopus 로고
    • The carboxy terminus of the beta amyloid protein is critical for the seeding of amyloid formation: implications for the pathogenesis of Alzheimer's disease
    • J.T Jarrett E.P Berger P.T Lansbury Jr. The carboxy terminus of the beta amyloid protein is critical for the seeding of amyloid formation: implications for the pathogenesis of Alzheimer's disease Biochemistry 32 1993 4693 4697
    • (1993) Biochemistry , vol.32 , pp. 4693-4697
    • Jarrett, J.T1    Berger, E.P2    Lansbury, P.T3
  • 61
    • 0000792598 scopus 로고    scopus 로고
    • The transmembrane aspartates in presenilin 1 and 2 are obligatory for γ-secretase activity and amyloid β-protein generation
    • W.T Kimberly W Xia T Rahmati M.S Wolfe D.J Selkoe The transmembrane aspartates in presenilin 1 and 2 are obligatory for γ-secretase activity and amyloid β-protein generation J. Biol. Chem. 275 2000 3173 3178
    • (2000) J. Biol. Chem. , vol.275 , pp. 3173-3178
    • Kimberly, W.T1    Xia, W2    Rahmati, T3    Wolfe, M.S4    Selkoe, D.J5
  • 62
    • 0035923502 scopus 로고    scopus 로고
    • Alzheimer's beta-secretase, beta-site amyloid precursor protein-cleaving enzyme, is responsible for cleavage secretion of a Golgi-resident sialyltransferase
    • S Kitazume Y Tachida R Oka K Shirotani T.C Saido Y Hashimoto Alzheimer's beta-secretase, beta-site amyloid precursor protein-cleaving enzyme, is responsible for cleavage secretion of a Golgi-resident sialyltransferase Proc. Natl. Acad. Sci. USA 98 2001 13554 13559
    • (2001) , pp. 13554-13559
    • Kitazume, S1    Tachida, Y2    Oka, R3    Shirotani, K4    Saido, T.C5    Hashimoto, Y6
  • 63
    • 0033616716 scopus 로고    scopus 로고
    • Constitutive and regulated alpha-secretase cleavage of Alzheimer's amyloid precursor protein by a disintegrin metalloprotease
    • S Lammich E Kojro R Postina S Gilbert R Pfeiffer M Jasionowski C Haass F Fahrenholz Constitutive and regulated alpha-secretase cleavage of Alzheimer's amyloid precursor protein by a disintegrin metalloprotease Proc. Natl. Acad. Sci. USA 96 1999 3922 3927
    • (1999) , pp. 3922-3927
    • Lammich, S1    Kojro, E2    Postina, R3    Gilbert, S4    Pfeiffer, R5    Jasionowski, M6    Haass, C7    Fahrenholz, F8
  • 64
    • 0033978638 scopus 로고    scopus 로고
    • The type 4 prepilin peptidases comprise a novel family of aspartic acid proteases
    • C.F Lapointe R.K Taylor The type 4 prepilin peptidases comprise a novel family of aspartic acid proteases J. Biol. Chem. 275 2000 1502 1510
    • (2000) J. Biol. Chem. , vol.275 , pp. 1502-1510
    • Lapointe, C.F1    Taylor, R.K2
  • 65
    • 0029147583 scopus 로고
    • Amyloid precursor protein processing is stimulated by metabotropic glutamate receptors
    • R.K Lee R.J Wurtman A.J Cox R.M Nitsch Amyloid precursor protein processing is stimulated by metabotropic glutamate receptors Proc. Natl. Acad. Sci. USA 92 1995 8083 8087
    • (1995) , pp. 8083-8087
    • Lee, R.K1    Wurtman, R.J2    Cox, A.J3    Nitsch, R.M4
  • 66
    • 0033550061 scopus 로고    scopus 로고
    • Zebrafish (Danio rerio) presenilin promotes aberrant amyloid beta-peptide production and requires a critical aspartate residue for its function in amyloidogenesis
    • U Leimer K Lun H Romig J Walter J Grunberg M Brand C Haass Zebrafish (Danio rerio) presenilin promotes aberrant amyloid beta-peptide production and requires a critical aspartate residue for its function in amyloidogenesis Biochemistry 38 1999 13602 13609
    • (1999) Biochemistry , vol.38 , pp. 13602-13609
    • Leimer, U1    Lun, K2    Romig, H3    Walter, J4    Grunberg, J5    Brand, M6    Haass, C7
  • 67
    • 0033055648 scopus 로고    scopus 로고
    • The AMY antigen co-occurs with abeta and follows its deposition in the amyloid plaques of Alzheimer's disease and Down syndrome
    • C.A Lemere T.J Grenfell D.J Selkoe The AMY antigen co-occurs with abeta and follows its deposition in the amyloid plaques of Alzheimer's disease and Down syndrome Am. J. Pathol. 155 1999 29 37
    • (1999) Am. J. Pathol. , vol.155 , pp. 29-37
    • Lemere, C.A1    Grenfell, T.J2    Selkoe, D.J3
  • 68
  • 71
    • 0026688633 scopus 로고
    • Mutation of a putative sperm membrane protein in Caenorhabditis elegans prevents sperm differentiation but not its associated meiotic divisions
    • S.W L'Hernault P.M Arduengo Mutation of a putative sperm membrane protein in Caenorhabditis elegans prevents sperm differentiation but not its associated meiotic divisions J. Cell. Biol. 119 1992 55 68
    • (1992) J. Cell. Biol. , vol.119 , pp. 55-68
    • L'Hernault, S.W1    Arduengo, P.M2
  • 74
    • 0037022360 scopus 로고    scopus 로고
    • The intramembrane cleavage site of the amyloid precursor protein depends on the length of its transmembrane domain
    • S.F Lichtenthaler D Beher H.S Grimm R Wang M.S Shearman C.L Masters K Beyreuther The intramembrane cleavage site of the amyloid precursor protein depends on the length of its transmembrane domain Proc. Natl. Acad. Sci. USA 99 2002 1365 1370
    • (2002) , pp. 1365-1370
    • Lichtenthaler, S.F1    Beher, D2    Grimm, H.S3    Wang, R4    Shearman, M.S5    Masters, C.L6    Beyreuther, K7
  • 75
    • 0032981558 scopus 로고    scopus 로고
    • Mechanism of the cleavage specificity of Alzheimer's disease gamma-secretase identified by phenylalanine-scanning mutagenesis of the transmembrane domain of the amyloid precursor protein
    • S.F Lichtenthaler R Wang H Grimm S.N Uljon C.L Masters K Beyreuther Mechanism of the cleavage specificity of Alzheimer's disease gamma-secretase identified by phenylalanine-scanning mutagenesis of the transmembrane domain of the amyloid precursor protein Proc. Natl. Acad. Sci. USA 96 1999 3053 3058
    • (1999) , pp. 3053-3058
    • Lichtenthaler, S.F1    Wang, R2    Grimm, H3    Uljon, S.N4    Masters, C.L5    Beyreuther, K6
  • 76
    • 0032693398 scopus 로고    scopus 로고
    • Cognitive changes and modified processing of amyloid precursor protein in the cortical and hippocampal system after cholinergic synapse loss and muscarinic receptor activation
    • L Lin B Georgievska A Mattsson O Isacson Cognitive changes and modified processing of amyloid precursor protein in the cortical and hippocampal system after cholinergic synapse loss and muscarinic receptor activation Proc. Natl. Acad. Sci. USA 96 1999 12108 12113
    • (1999) , pp. 12108-12113
    • Lin, L1    Georgievska, B2    Mattsson, A3    Isacson, O4
  • 78
    • 0034652309 scopus 로고    scopus 로고
    • Human aspartic protease memapsin 2 cleaves the beta-secretase site of beta-amyloid precursor protein
    • X Lin G Koelsch S Wu D Downs A Dashti J Tang Human aspartic protease memapsin 2 cleaves the beta-secretase site of beta-amyloid precursor protein Proc. Natl. Acad. Sci. USA 97 2000 1456 1460
    • (2000) , pp. 1456-1460
    • Lin, X1    Koelsch, G2    Wu, S3    Downs, D4    Dashti, A5    Tang, J6
  • 79
    • 0032493302 scopus 로고    scopus 로고
    • The Notch1 receptor is cleaved constitutively by a furin-like convertase
    • F Logeat C Bessia C Brou O Lebail S Jarriault N.G Seidah A Israel The Notch1 receptor is cleaved constitutively by a furin-like convertase Proc. Natl. Acad. Sci. USA 95 1998 8108 8112
    • (1998) , pp. 8108-8112
    • Logeat, F1    Bessia, C2    Brou, C3    Lebail, O4    Jarriault, S5    Seidah, N.G6    Israel, A7
  • 80
    • 0036007118 scopus 로고    scopus 로고
    • Drosophila nicastrin is essential for the intramembranous cleavage of notch
    • H Lopez-Schier D St Johnston Drosophila nicastrin is essential for the intramembranous cleavage of notch Dev. Cell 2 2002 79 89
    • (2002) Dev. Cell , vol.2 , pp. 79-89
    • Lopez-Schier, H1    St Johnston, D2
  • 82
    • 0017091634 scopus 로고
    • Mode of inhibition of acid proteases by pepstatin
    • J Marciniszyn Jr. J.A Hartsuck J Tang Mode of inhibition of acid proteases by pepstatin J. Biol. Chem. 251 1976 7088 7094
    • (1976) J. Biol. Chem. , vol.251 , pp. 7088-7094
    • Marciniszyn, J1    Hartsuck, J.A2    Tang, J3
  • 83
    • 4244025305 scopus 로고    scopus 로고
    • Functional analysis of beta-secretase using mutagenesis and structural homology modeling
    • L.C McConlogue D.A Agard O Nobuyuki G Tatsuno Functional analysis of beta-secretase using mutagenesis and structural homology modeling Neurobiol. Aging 21 2000 S278
    • (2000) Neurobiol. Aging , vol.21 , pp. S278
    • McConlogue, L.C1    Agard, D.A2    Nobuyuki, O3    Tatsuno, G4
  • 85
    • 0032514633 scopus 로고    scopus 로고
    • Memory-enhancing effects of secreted forms of the beta-amyloid precursor protein in normal and amnestic mice
    • H Meziane J.C Dodart C Mathis S Little J Clemens S.M Paul A Ungerer Memory-enhancing effects of secreted forms of the beta-amyloid precursor protein in normal and amnestic mice Proc. Natl. Acad. Sci. USA 95 1998 12683 12688
    • (1998) , pp. 12683-12688
    • Meziane, H1    Dodart, J.C2    Mathis, C3    Little, S4    Clemens, J5    Paul, S.M6    Ungerer, A7
  • 86
    • 0034618705 scopus 로고    scopus 로고
    • Difluoro ketone peptidomimetics suggest a large S1 pocket for Alzheimer's γ-secretase: Implications for inhibitor design
    • C.L Moore D.D Leatherwood T.S Diehl D.J Selkoe M.S Wolfe Difluoro ketone peptidomimetics suggest a large S1 pocket for Alzheimer's γ-secretase: Implications for inhibitor design J. Med. Chem. 43 2000 3434 3442
    • (2000) J. Med. Chem. , vol.43 , pp. 3434-3442
    • Moore, C.L1    Leatherwood, D.D2    Diehl, T.S3    Selkoe, D.J4    Wolfe, M.S5
  • 87
    • 0033867521 scopus 로고    scopus 로고
    • A ligand-induced extracellular cleavage regulates-gamma-secretase-like proteolytic activation of Notch1
    • J.S Mumm E.H Schroeter M.T Saxena A Griesemer X Tian D.J Pan W.J Ray R Kopan A ligand-induced extracellular cleavage regulates-gamma-secretase-like proteolytic activation of Notch1 Mol. Cell 5 2000 197 206
    • (2000) Mol. Cell , vol.5 , pp. 197-206
    • Mumm, J.S1    Schroeter, E.H2    Saxena, M.T3    Griesemer, A4    Tian, X5    Pan, D.J6    Ray, W.J7    Kopan, R8
  • 88
    • 0025950987 scopus 로고
    • A mutation in the amyloid precursor protein associated with hereditary Alzheimer's disease
    • J Murrell M Farlow B Ghetti M.D Benson A mutation in the amyloid precursor protein associated with hereditary Alzheimer's disease Science 254 1991 97 99
    • (1991) Science , vol.254 , pp. 97-99
    • Murrell, J1    Farlow, M2    Ghetti, B3    Benson, M.D4
  • 89
    • 0035824391 scopus 로고    scopus 로고
    • gamma-Secretase cleavage and nuclear localization of ErbB-4 receptor tyrosine kinase
    • C.Y Ni M.P Murphy T.E Golde G Carpenter gamma-Secretase cleavage and nuclear localization of ErbB-4 receptor tyrosine kinase Science 294 2001 2179 2181
    • (2001) Science , vol.294 , pp. 2179-2181
    • Ni, C.Y1    Murphy, M.P2    Golde, T.E3    Carpenter, G4
  • 90
    • 0026476297 scopus 로고
    • Release of Alzheimer amyloid precursor derivatives stimulated by activation of muscarinic acetylcholine receptors
    • R.M Nitsch B.E Slack R.J Wurtman J.H Growdon Release of Alzheimer amyloid precursor derivatives stimulated by activation of muscarinic acetylcholine receptors Science 258 1992 304 307
    • (1992) Science , vol.258 , pp. 304-307
    • Nitsch, R.M1    Slack, B.E2    Wurtman, R.J3    Growdon, J.H4
  • 91
    • 0032502033 scopus 로고    scopus 로고
    • Alzheimer's amyloid precursor protein alpha-secretase is inhibited by hydroxamic acid-based zinc metalloprotease inhibitors: similarities to the angiotensin converting enzyme secretase
    • S Parvathy I Hussain E.H Karran A.J Turner N.M Hooper Alzheimer's amyloid precursor protein alpha-secretase is inhibited by hydroxamic acid-based zinc metalloprotease inhibitors: similarities to the angiotensin converting enzyme secretase Biochemistry 37 1998 1680 1685
    • (1998) Biochemistry , vol.37 , pp. 1680-1685
    • Parvathy, S1    Hussain, I2    Karran, E.H3    Turner, A.J4    Hooper, N.M5
  • 92
    • 0032503959 scopus 로고    scopus 로고
    • The secretases that cleave angiotensin converting enzyme and the amyloid precursor protein are distinct from tumour necrosis factor-alpha convertase
    • S Parvathy E.H Karran A.J Turner N.M Hooper The secretases that cleave angiotensin converting enzyme and the amyloid precursor protein are distinct from tumour necrosis factor-alpha convertase FEBS Lett. 431 1998 63 65
    • (1998) FEBS Lett. , vol.431 , pp. 63-65
    • Parvathy, S1    Karran, E.H2    Turner, A.J3    Hooper, N.M4
  • 93
    • 0018078940 scopus 로고
    • Correlation of cholinergic abnormalities with senile plaques and mental test scores in senile dementia
    • E.K Perry B.E Tomlinson G Blessed K Bergmann P.H Gibson R.H Perry Correlation of cholinergic abnormalities with senile plaques and mental test scores in senile dementia Brit. Med. J. 2 1978 1457 1459
    • (1978) Brit. Med. J. , vol.2 , pp. 1457-1459
    • Perry, E.K1    Tomlinson, B.E2    Blessed, G3    Bergmann, K4    Gibson, P.H5    Perry, R.H6
  • 97
    • 0031301274 scopus 로고    scopus 로고
    • Complementation cloning of S2P, a gene encoding a putative metalloprotease required for intramembrane cleavage of SREBPs
    • R.B Rawson N.G Zelenski D Nijhawan J Ye J Sakai M.T Hasan T.Y Chang M.S Brown J.L Goldstein Complementation cloning of S2P, a gene encoding a putative metalloprotease required for intramembrane cleavage of SREBPs Mol. Cell 1 1997 47 57
    • (1997) Mol. Cell , vol.1 , pp. 47-57
    • Rawson, R.B1    Zelenski, N.G2    Nijhawan, D3    Ye, J4    Sakai, J5    Hasan, M.T6    Chang, T.Y7    Brown, M.S8    Goldstein, J.L9
  • 100
    • 0033593022 scopus 로고    scopus 로고
    • A family of membrane-embedded metalloproteases involved in regulated proteolysis of membrane-associated transcription factors
    • D.Z Rudner P Fawcett R Losick A family of membrane-embedded metalloproteases involved in regulated proteolysis of membrane-associated transcription factors Proc. Natl. Acad. Sci. USA 96 1999 14765 14770
    • (1999) , pp. 14765-14770
    • Rudner, D.Z1    Fawcett, P2    Losick, R3
  • 104
    • 0032574993 scopus 로고    scopus 로고
    • Notch-1 signalling requires ligand-induced proteolytic release of intracellular domain
    • E.H Schroeter J.A Kisslinger R Kopan Notch-1 signalling requires ligand-induced proteolytic release of intracellular domain Nature 393 1998 382 386
    • (1998) Nature , vol.393 , pp. 382-386
    • Schroeter, E.H1    Kisslinger, J.A2    Kopan, R3
  • 106
    • 0028170818 scopus 로고
    • Cell biology of the amyloid beta-protein precursor and the mechanism of Alzheimer's disease
    • D.J Selkoe Cell biology of the amyloid beta-protein precursor and the mechanism of Alzheimer's disease Annu. Rev. Cell. Biol. 10 1994 373 403
    • (1994) Annu. Rev. Cell. Biol. , vol.10 , pp. 373-403
    • Selkoe, D.J1
  • 107
    • 0033600274 scopus 로고    scopus 로고
    • Translating cell biology into therapeutic advances in Alzheimer's disease
    • D.J Selkoe Translating cell biology into therapeutic advances in Alzheimer's disease Nature 399 1999 A23 A31
    • (1999) Nature , vol.399 , pp. A23-A31
    • Selkoe, D.J1
  • 109
    • 0034254585 scopus 로고    scopus 로고
    • L-685,458, an aspartyl protease transition state mimic, is a potent inhibitor of amyloid beta-protein precursor gamma-secretase activity
    • M.S Shearman D Beher E.E Clarke H.D Lewis T Harrison P Hunt A Nadin A.L Smith G Stevenson J.L Castro L-685,458, an aspartyl protease transition state mimic, is a potent inhibitor of amyloid beta-protein precursor gamma-secretase activity Biochemistry 39 2000 8698 8704
    • (2000) Biochemistry , vol.39 , pp. 8698-8704
    • Shearman, M.S1    Beher, D2    Clarke, E.E3    Lewis, H.D4    Harrison, T5    Hunt, P6    Nadin, A7    Smith, A.L8    Stevenson, G9    Castro, J.L10
  • 113
    • 0029863567 scopus 로고    scopus 로고
    • Inhibition and catalytic mechanism of HIV-1 aspartic protease
    • A.M Silva R.E Cachau H.L Sham J.W Erickson Inhibition and catalytic mechanism of HIV-1 aspartic protease J. Mol. Biol. 255 1996 321 346
    • (1996) J. Mol. Biol. , vol.255 , pp. 321-346
    • Silva, A.M1    Cachau, R.E2    Sham, H.L3    Erickson, J.W4
  • 115
    • 0026721943 scopus 로고
    • Beta-amyloid precursor protein cleavage by a membrane-bound protease
    • S.S Sisodia Beta-amyloid precursor protein cleavage by a membrane-bound protease Proc. Natl. Acad. Sci. USA 89 1992 6075 6079
    • (1992) , pp. 6075-6079
    • Sisodia, S.S1
  • 116
    • 0032983536 scopus 로고    scopus 로고
    • Association of microglia with amyloid plaques in brains of APP23 transgenic mice
    • M Stalder A Phinney A Probst B Sommer M Staufenbiel M Jucker Association of microglia with amyloid plaques in brains of APP23 transgenic mice Am. J. Pathol. 154 1999 1673 1684
    • (1999) Am. J. Pathol. , vol.154 , pp. 1673-1684
    • Stalder, M1    Phinney, A2    Probst, A3    Sommer, B4    Staufenbiel, M5    Jucker, M6
  • 117
    • 0033610863 scopus 로고    scopus 로고
    • Expression of Alzheimer's disease-associated presenilin-1 is controlled by proteolytic degradation and complex formation
    • H Steiner A Capell B Pesold M Citron P.M Kloetzel D.J Selkoe H Romig K Mendla C Haass Expression of Alzheimer's disease-associated presenilin-1 is controlled by proteolytic degradation and complex formation J. Biol. Chem. 273 1998 32322 32331
    • (1998) J. Biol. Chem. , vol.273 , pp. 32322-32331
    • Steiner, H1    Capell, A2    Pesold, B3    Citron, M4    Kloetzel, P.M5    Selkoe, D.J6    Romig, H7    Mendla, K8    Haass, C9
  • 119
    • 0033583047 scopus 로고    scopus 로고
    • The biological and pathological function of the presenilin-1 exon 9 mutation is independent of its defect to undergo proteolytic processing
    • H Steiner H Romig M.G Grim U Philipp B Pesold M Citron R Baumeister C Haass The biological and pathological function of the presenilin-1 exon 9 mutation is independent of its defect to undergo proteolytic processing J. Biol. Chem. 274 1999 7615 7618
    • (1999) J. Biol. Chem. , vol.274 , pp. 7615-7618
    • Steiner, H1    Romig, H2    Grim, M.G3    Philipp, U4    Pesold, B5    Citron, M6    Baumeister, R7    Haass, C8
  • 120
  • 121
    • 0028322017 scopus 로고
    • An increased percentage of long amyloid beta protein secreted by familial amyloid beta protein precursor (beta APP717) mutants
    • N Suzuki T.T Cheung X.D Cai A Odaka L Otvos Jr. C Eckman T.E Golde S.G Younkin An increased percentage of long amyloid beta protein secreted by familial amyloid beta protein precursor (beta APP717) mutants Science 264 1994 1336 1340
    • (1994) Science , vol.264 , pp. 1336-1340
    • Suzuki, N1    Cheung, T.T2    Cai, X.D3    Odaka, A4    Otvos, L5    Eckman, C6    Golde, T.E7    Younkin, S.G8
  • 122
    • 0035861547 scopus 로고    scopus 로고
    • The multispanning membrane protein Ste24p catalyzes CAAX proteolysis and NH2-terminal processing of the yeast a-factor precursor
    • A Tam W.K Schmidt S Michaelis The multispanning membrane protein Ste24p catalyzes CAAX proteolysis and NH2-terminal processing of the yeast a-factor precursor J. Biol. Chem. 276 2001 46798 46806
    • (2001) J. Biol. Chem. , vol.276 , pp. 46798-46806
    • Tam, A1    Schmidt, W.K2    Michaelis, S3
  • 124
    • 0022504190 scopus 로고
    • Design and synthesis of potent and specific renin inhibitors containing difluorostatine, difluorostatone, and related analogues
    • S Thaisrivongs D.T Pals W.M Kati S.R Turner L.M Thomasco W Watt Design and synthesis of potent and specific renin inhibitors containing difluorostatine, difluorostatone, and related analogues J. Med. Chem. 29 1986 2080 2087
    • (1986) J. Med. Chem. , vol.29 , pp. 2080-2087
    • Thaisrivongs, S1    Pals, D.T2    Kati, W.M3    Turner, S.R4    Thomasco, L.M5    Watt, W6
  • 126
  • 127
    • 12644258498 scopus 로고    scopus 로고
    • The presenilin 2 mutation (N141I) linked to familial Alzheimer disease (Volga German families) increases the secretion of amyloid beta protein ending at the 42nd (or 43rd) residue
    • T Tomita K Maruyama T.C Saido H Kume K Shinozaki S Tokuhiro A Capell J Walter J Grunberg C Haass T Iwatsubo K Obata The presenilin 2 mutation (N141I) linked to familial Alzheimer disease (Volga German families) increases the secretion of amyloid beta protein ending at the 42nd (or 43rd) residue Proc. Natl. Acad. Sci. USA 94 1997 2025 2030
    • (1997) , pp. 2025-2030
    • Tomita, T1    Maruyama, K2    Saido, T.C3    Kume, H4    Shinozaki, K5    Tokuhiro, S6    Capell, A7    Walter, J8    Grunberg, J9    Haass, C10    Iwatsubo, T11    Obata, K12
  • 128
    • 0035913908 scopus 로고    scopus 로고
    • Drosophila rhomboid-1 defines a family of putative intramembrane serine proteases
    • S Urban J.R Lee M Freeman Drosophila rhomboid-1 defines a family of putative intramembrane serine proteases Cell 107 2001 173 182
    • (2001) Cell , vol.107 , pp. 173-182
    • Urban, S1    Lee, J.R2    Freeman, M3
  • 131
    • 0033564290 scopus 로고    scopus 로고
    • Effects of the amyloid precursor protein Glu693 .Gln ‘Dutch’ mutation on the production and stability of amyloid beta-protein
    • D.J Watson D.J Selkoe D.B Teplow Effects of the amyloid precursor protein Glu693 .Gln ‘Dutch’ mutation on the production and stability of amyloid beta-protein Biochem. J. 340 1999 703 709
    • (1999) Biochem. J. , vol.340 , pp. 703-709
    • Watson, D.J1    Selkoe, D.J2    Teplow, D.B3
  • 132
    • 0031470904 scopus 로고    scopus 로고
    • SUP-17, a Caenorhabditis elegans ADAM protein related to Drosophila KUZBANIAN, and its role in LIN-12/NOTCH signalling
    • C Wen M.M Metzstein I Greenwald SUP-17, a Caenorhabditis elegans ADAM protein related to Drosophila KUZBANIAN, and its role in LIN-12/NOTCH signalling Development 124 1997 4759 4767
    • (1997) Development , vol.124 , pp. 4759-4767
    • Wen, C1    Metzstein, M.M2    Greenwald, I3
  • 133
    • 0028926941 scopus 로고
    • Muscarinic regulation of Alzheimer's disease amyloid precursor protein secretion and amyloid beta-protein production in human neuronal NT2N cells
    • B.A Wolf A.M Wertkin Y.C Jolly R.P Yasuda B.B Wolfe R.J Konrad D Manning S Ravi J.R Williamson V.M Lee Muscarinic regulation of Alzheimer's disease amyloid precursor protein secretion and amyloid beta-protein production in human neuronal NT2N cells J. Biol. Chem. 270 1995 4916 4922
    • (1995) J. Biol. Chem. , vol.270 , pp. 4916-4922
    • Wolf, B.A1    Wertkin, A.M2    Jolly, Y.C3    Yasuda, R.P4    Wolfe, B.B5    Konrad, R.J6    Manning, D7    Ravi, S8    Williamson, J.R9    Lee, V.M10
  • 134
    • 0035927426 scopus 로고    scopus 로고
    • Secretase targets for Alzheimer's disease: identification and therapeutic potential
    • M.S Wolfe Secretase targets for Alzheimer's disease: identification and therapeutic potential J. Med. Chem. 44 2001 2039 2060
    • (2001) J. Med. Chem. , vol.44 , pp. 2039-2060
    • Wolfe, M.S1
  • 135
    • 0033621152 scopus 로고    scopus 로고
    • Are presenilins intramembrane-cleaving proteases? Implications for the molecular mechanism of Alzheimer's disease
    • M.S Wolfe J De Los Angeles D.D Miller W Xia D.J Selkoe Are presenilins intramembrane-cleaving proteases? Implications for the molecular mechanism of Alzheimer's disease Biochemistry 38 1999 11223 11230
    • (1999) Biochemistry , vol.38 , pp. 11223-11230
    • Wolfe, M.S1    De Los Angeles, J2    Miller, D.D3    Xia, W4    Selkoe, D.J5
  • 136
    • 0033551099 scopus 로고    scopus 로고
    • Peptidomimetic probes and molecular modeling suggest Alzheimer's γ-secretases are intramembrane-cleaving aspartyl proteases
    • M.S Wolfe W Xia C.L Moore D.D Leatherwood B Ostaszewski I.O Donkor D.J Selkoe Peptidomimetic probes and molecular modeling suggest Alzheimer's γ-secretases are intramembrane-cleaving aspartyl proteases Biochemistry 38 1999 4720 4727
    • (1999) Biochemistry , vol.38 , pp. 4720-4727
    • Wolfe, M.S1    Xia, W2    Moore, C.L3    Leatherwood, D.D4    Ostaszewski, B5    Donkor, I.O6    Selkoe, D.J7
  • 137
    • 0033535553 scopus 로고    scopus 로고
    • Two transmembrane aspartates in presenilin-1 required for presenilin endoproteolysis and γ-secretase activity
    • M.S Wolfe W Xia B.L Ostaszewski T.S Diehl W.T Kimberly D.J Selkoe Two transmembrane aspartates in presenilin-1 required for presenilin endoproteolysis and γ-secretase activity Nature 398 1999 513 517
    • (1999) Nature , vol.398 , pp. 513-517
    • Wolfe, M.S1    Xia, W2    Ostaszewski, B.L3    Diehl, T.S4    Kimberly, W.T5    Selkoe, D.J6
  • 140
    • 0034625081 scopus 로고    scopus 로고
    • Asparagine-proline sequence within membrane-spanning segment of SREBP triggers intramembrane cleavage by site-2 protease
    • J Ye U.P Dave N.V Grishin J.L Goldstein M.S Brown Asparagine-proline sequence within membrane-spanning segment of SREBP triggers intramembrane cleavage by site-2 protease Proc. Natl. Acad. Sci. USA 97 2000 5123 5128
    • (2000) , pp. 5123-5128
    • Ye, J1    Dave, U.P2    Grishin, N.V3    Goldstein, J.L4    Brown, M.S5
  • 143
    • 0032524865 scopus 로고    scopus 로고
    • Subcellular distribution and turnover of presenilins in transfected cells
    • J Zhang D.E Kang W Xia M Okochi H Mori D.J Selkoe E.H Koo Subcellular distribution and turnover of presenilins in transfected cells J. Biol. Chem. 273 1998 12436 12442
    • (1998) J. Biol. Chem. , vol.273 , pp. 12436-12442
    • Zhang, J1    Kang, D.E2    Xia, W3    Okochi, M4    Mori, H5    Selkoe, D.J6    Koo, E.H7
  • 144
    • 0033779635 scopus 로고    scopus 로고
    • Presenilins are required for gamma-secretase cleavage of beta-APP and transmembrane cleavage of Notch-1
    • Z Zhang P Nadeau W Song D Donoviel M Yuan A Bernstein B.A Yankner Presenilins are required for gamma-secretase cleavage of beta-APP and transmembrane cleavage of Notch-1 Nat. Cell Biol. 2 2000 463 465
    • (2000) Nat. Cell Biol. , vol.2 , pp. 463-465
    • Zhang, Z1    Nadeau, P2    Song, W3    Donoviel, D4    Yuan, M5    Bernstein, A6    Yankner, B.A7
  • 145
    • 10544248594 scopus 로고    scopus 로고
    • Beta-secretase processing of the beta-amyloid precursor protein in transgenic mice is efficient in neurons but inefficient in astrocytes
    • J Zhao L Paganini L Mucke M Gordon L Refolo M Carman S Sinha T Oltersdorf I Lieberburg L McConlogue Beta-secretase processing of the beta-amyloid precursor protein in transgenic mice is efficient in neurons but inefficient in astrocytes J. Biol. Chem. 271 1996 31407 31411
    • (1996) J. Biol. Chem. , vol.271 , pp. 31407-31411
    • Zhao, J1    Paganini, L2    Mucke, L3    Gordon, M4    Refolo, L5    Carman, M6    Sinha, S7    Oltersdorf, T8    Lieberburg, I9    McConlogue, L10


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