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Volumn 54, Issue 9, 1998, Pages 902-909

Monogenic determinants of familial Alzheimer's disease: Presenilin-1 mutations

Author keywords

amyloid; Alzheimer's disease; FAD; Mutations; Neurodegeneration; Presenilin 1; PS1

Indexed keywords

AMYLOID BETA PROTEIN; APOLIPOPROTEIN E; PRESENILIN 1;

EID: 0031714867     PISSN: 1420682X     EISSN: None     Source Type: Journal    
DOI: 10.1007/s000180050219     Document Type: Article
Times cited : (24)

References (86)
  • 1
    • 0027139556 scopus 로고
    • Genetic heterogenity of gene defects responsible for familial Alzheimer disease
    • Tanzi R., Gaston S., Bush A., Romano D., Pettingell W., Peppercorn J. et al. (1994) Genetic heterogenity of gene defects responsible for familial Alzheimer disease. Genetica 91: 255-263
    • (1994) Genetica , vol.91 , pp. 255-263
    • Tanzi, R.1    Gaston, S.2    Bush, A.3    Romano, D.4    Pettingell, W.5    Peppercorn, J.6
  • 2
    • 0002521732 scopus 로고
    • Molecular genetics of amyloid and apolipoprotein e in Alzheimer's disease
    • Dawbarn D. and Allen S. J. (eds), BIOS Scientific Publishers, Oxford
    • Wasco W. and Tanzi R. E. (1995) Molecular genetics of amyloid and apolipoprotein E in Alzheimer's disease. In: Neurobiology of Alzheimer's Disease, pp. 51-76, Dawbarn D. and Allen S. J. (eds), BIOS Scientific Publishers, Oxford
    • (1995) Neurobiology of Alzheimer's Disease , pp. 51-76
    • Wasco, W.1    Tanzi, R.E.2
  • 4
    • 0026648493 scopus 로고
    • Assessment of amyloid β protein precursor gene mutations in a large set of familial and sporadic Alzheimer disease cases
    • Tanzi R. E., Vaula G., Romano D. M., Mortilla M., Huang T. L., Tupler R. G. et al. (1992) Assessment of amyloid β protein precursor gene mutations in a large set of familial and sporadic Alzheimer disease cases. Am. J. Hum. Genet. 51: 273-282
    • (1992) Am. J. Hum. Genet. , vol.51 , pp. 273-282
    • Tanzi, R.E.1    Vaula, G.2    Romano, D.M.3    Mortilla, M.4    Huang, T.L.5    Tupler, R.G.6
  • 6
    • 0029899593 scopus 로고    scopus 로고
    • Incomplete penetrance of familial Alzheimer's disease in a pedigree with a novel presenilin-1 gene mutation
    • Rossor M. N., Fox N. C., Beck J., Campbell T. C. and Collinge J. (1996) Incomplete penetrance of familial Alzheimer's disease in a pedigree with a novel presenilin-1 gene mutation. Lancet 347: 1560
    • (1996) Lancet , vol.347 , pp. 1560
    • Rossor, M.N.1    Fox, N.C.2    Beck, J.3    Campbell, T.C.4    Collinge, J.5
  • 7
    • 0028985574 scopus 로고
    • Alzheimer-type neuropathology in transgenic mice overexpressing V717F β-amyloid precursor protein
    • Games D., Adams D., Alessandrini R., Barbour R., Berthelette P., Blackwell C. et al. (1995) Alzheimer-type neuropathology in transgenic mice overexpressing V717F β-amyloid precursor protein. Nature 373: 523-527
    • (1995) Nature , vol.373 , pp. 523-527
    • Games, D.1    Adams, D.2    Alessandrini, R.3    Barbour, R.4    Berthelette, P.5    Blackwell, C.6
  • 8
    • 0027526419 scopus 로고
    • Release of excess amyloid β protein from a mutant amyloid β protein precursor
    • Cai X.-D., Golde T. E. and Younkin S. G. (1993). Release of excess amyloid β protein from a mutant amyloid β protein precursor. Science 259: 514-516
    • (1993) Science , vol.259 , pp. 514-516
    • Cai, X.-D.1    Golde, T.E.2    Younkin, S.G.3
  • 9
    • 0028322017 scopus 로고
    • An increased percentage of long amyloid beta protein secreted by familial amyloid beta protein precursor (beta APP717) mutants
    • Suzuki N., Cheung T. T., Cai X. D., Odaka A., Otvos L. Jr., Eckman C. et al. (1994) An increased percentage of long amyloid beta protein secreted by familial amyloid beta protein precursor (beta APP717) mutants. Science 264: 1336-1340
    • (1994) Science , vol.264 , pp. 1336-1340
    • Suzuki, N.1    Cheung, T.T.2    Cai, X.D.3    Odaka, A.4    Otvos Jr., L.5    Eckman, C.6
  • 10
    • 0026745610 scopus 로고
    • Mutation of the β-amyloid precursor protein in familial Alzheimer's disease increases β-protein production
    • Citron M., Oltersdorf T., Haass C., McConlogue L., Hung A. Y., Seubert P. et al. (1992) Mutation of the β-amyloid precursor protein in familial Alzheimer's disease increases β-protein production. Nature 360: 672-674
    • (1992) Nature , vol.360 , pp. 672-674
    • Citron, M.1    Oltersdorf, T.2    Haass, C.3    McConlogue, L.4    Hung, A.Y.5    Seubert, P.6
  • 11
    • 0028899724 scopus 로고
    • Quantitative analysis of senile plaques in Alzheimer's disease: Observation of log-normal size distribution and molecular epidemiology of differences associated with ApoE genotype and trisomy 21 (Down syndrome)
    • Hymun B. T., West H. L., Rebeck G. W., Buldyrev S. V., Mantegna R. N., Ukleja M. et al. (1995) Quantitative analysis of senile plaques in Alzheimer's disease: observation of log-normal size distribution and molecular epidemiology of differences associated with ApoE genotype and trisomy 21 (Down syndrome). Proc. Natl. Acad. Sci. USA 92: 3586-3590
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 3586-3590
    • Hymun, B.T.1    West, H.L.2    Rebeck, G.W.3    Buldyrev, S.V.4    Mantegna, R.N.5    Ukleja, M.6
  • 12
    • 0031278270 scopus 로고    scopus 로고
    • Lack of apolipoprotein e dramatically reduces amyloid β-peptide deposition
    • Bales K. R., Verina T., Dodel R. C., Du Y., Altstiel L., Bender M. et al. (1997) Lack of apolipoprotein E dramatically reduces amyloid β-peptide deposition. Nature Genet. 17: 263-264
    • (1997) Nature Genet. , vol.17 , pp. 263-264
    • Bales, K.R.1    Verina, T.2    Dodel, R.C.3    Du, Y.4    Altstiel, L.5    Bender, M.6
  • 13
    • 0029004341 scopus 로고
    • Cloning of a novel gene bearing missense mutations in early onset familial Alzheimer disease
    • Sherrington R., Rogaev E. I., Liang Y., Rogaeva E. A., Levesque G., Ikeda M. et al. (1995) Cloning of a novel gene bearing missense mutations in early onset familial Alzheimer disease. Nature 375: 754-760
    • (1995) Nature , vol.375 , pp. 754-760
    • Sherrington, R.1    Rogaev, E.I.2    Liang, Y.3    Rogaeva, E.A.4    Levesque, G.5    Ikeda, M.6
  • 15
    • 0029101491 scopus 로고
    • Familial Alzheimer's disease in kindreds with missense mutation in a gene on chomosome 1 related to the Alzheimer's disease type 3 gene
    • Rogaev E. I., Sherrington R., Rogaeva E. A., Levesque G., Ikeda M., Liang Y. et al. (1995) Familial Alzheimer's disease in kindreds with missense mutation in a gene on chomosome 1 related to the Alzheimer's disease type 3 gene. Nature 376: 775-778
    • (1995) Nature , vol.376 , pp. 775-778
    • Rogaev, E.I.1    Sherrington, R.2    Rogaeva, E.A.3    Levesque, G.4    Ikeda, M.5    Liang, Y.6
  • 16
    • 0030889705 scopus 로고    scopus 로고
    • Isolation and characterization of Drosophila presenilin homolog
    • Hong C. S. and Koo E. H. (1997) Isolation and characterization of Drosophila presenilin homolog. Neuroreport 8: 665-668
    • (1997) Neuroreport , vol.8 , pp. 665-668
    • Hong, C.S.1    Koo, E.H.2
  • 18
    • 0029116848 scopus 로고
    • Facilitation of lin-12-mediated signalling by sel-12, a Caenorhabditis elegans S182 Alzheimer's disease gene
    • Levitan D. and Greenwald I. (1995) Facilitation of lin-12-mediated signalling by sel-12, a Caenorhabditis elegans S182 Alzheimer's disease gene. Nature 377: 351-354
    • (1995) Nature , vol.377 , pp. 351-354
    • Levitan, D.1    Greenwald, I.2
  • 19
    • 0030671560 scopus 로고    scopus 로고
    • HOP-1, Caenorhabditis elegans presenilin, appears to be functionally redundant with SEL-12 presenilin and to facilitate LIN-12 and GLP-1 signaling
    • Xiajun L. and Greewald I. (1997) HOP-1, Caenorhabditis elegans presenilin, appears to be functionally redundant with SEL-12 presenilin and to facilitate LIN-12 and GLP-1 signaling. Proc. Natl. Acad. Sci. USA 94: 12204-12209
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 12204-12209
    • Xiajun, L.1    Greewald, I.2
  • 20
    • 0031052381 scopus 로고    scopus 로고
    • Amyloid, the presenilins and Alzheimer's disease
    • Hardy J. (1997) Amyloid, the presenilins and Alzheimer's disease. Trends Neurosci. 20: 154-159
    • (1997) Trends Neurosci. , vol.20 , pp. 154-159
    • Hardy, J.1
  • 21
    • 0029554875 scopus 로고    scopus 로고
    • A mutation in Alzheimer's disease destroying a splice acceptor site in the presenilin-1 gene
    • Perez-Tur J., Froelich S., Prihar G., Crook R., Baker M., Duff K. et al. (1996) A mutation in Alzheimer's disease destroying a splice acceptor site in the presenilin-1 gene. Neuroreport 7: 297-301
    • (1996) Neuroreport , vol.7 , pp. 297-301
    • Perez-Tur, J.1    Froelich, S.2    Prihar, G.3    Crook, R.4    Baker, M.5    Duff, K.6
  • 22
    • 0029115555 scopus 로고
    • The structure of the presenilin 1 (S182) gene and identification of six novel mutations in early onset AD families
    • Clark R. F. and the Alzheimer's Disease Collaboration Group (1995) The structure of the presenilin 1 (S182) gene and identification of six novel mutations in early onset AD families. Nature Genet. 11: 219-222
    • (1995) Nature Genet. , vol.11 , pp. 219-222
    • Clark, R.F.1
  • 24
    • 13344282063 scopus 로고    scopus 로고
    • Alzheimer associated presenilins 1 and 2: Neuronal expression in brain and localization to intracellular membranes in mammalian cells
    • Kovacs D. M., Fausett H. J., Page K. J., Kim T.-W., Moir R. D., Merriam D. E. et al. (1996) Alzheimer associated presenilins 1 and 2: neuronal expression in brain and localization to intracellular membranes in mammalian cells. Nature Med. 2: 224-229
    • (1996) Nature Med. , vol.2 , pp. 224-229
    • Kovacs, D.M.1    Fausett, H.J.2    Page, K.J.3    Kim, T.-W.4    Moir, R.D.5    Merriam, D.E.6
  • 25
    • 0029982341 scopus 로고    scopus 로고
    • Widespread neuronal expression of the presenilin-1 early-onset Alzheimer's disease gene in the murine brain
    • Cribbs D. H., Chen L. S., Bende S. M. and LaFerla F. M. (1996) Widespread neuronal expression of the presenilin-1 early-onset Alzheimer's disease gene in the murine brain. Am. J. Pathol. 148: 1797-1806
    • (1996) Am. J. Pathol. , vol.148 , pp. 1797-1806
    • Cribbs, D.H.1    Chen, L.S.2    Bende, S.M.3    LaFerla, F.M.4
  • 26
    • 10544229795 scopus 로고    scopus 로고
    • Expression of Presenilin 1 and 2 (PS1 and PS2) in human and murine tissues
    • Lee M. K., Slunt H. H., Martin L. J., Thinakaran G., Kim G., Gandy S. E. et al. (1996) Expression of Presenilin 1 and 2 (PS1 and PS2) in human and murine tissues. J. Neurosci. 16: 7513-7525
    • (1996) J. Neurosci. , vol.16 , pp. 7513-7525
    • Lee, M.K.1    Slunt, H.H.2    Martin, L.J.3    Thinakaran, G.4    Kim, G.5    Gandy, S.E.6
  • 27
    • 15444350008 scopus 로고    scopus 로고
    • Presenilin-1 protein expression in familial and sporadic Alzheimer's disease
    • Levey A. I., Heilman C. J., Lah J. J., Nash N. R., Rees H. D., Wakai M. et al. (1997) Presenilin-1 protein expression in familial and sporadic Alzheimer's disease. Ann. Neurol. 41: 742-753
    • (1997) Ann. Neurol. , vol.41 , pp. 742-753
    • Levey, A.I.1    Heilman, C.J.2    Lah, J.J.3    Nash, N.R.4    Rees, H.D.5    Wakai, M.6
  • 28
    • 0031006343 scopus 로고    scopus 로고
    • Neuronal localization of presenilin-1 and association with amyloid plaques and neurofibrillary tangles in Alzheimer's disease
    • Busciglio J., Hartmann H., Lorenzo A., Wong C., Baumann K., Sommer B. et al. (1997) Neuronal localization of presenilin-1 and association with amyloid plaques and neurofibrillary tangles in Alzheimer's disease. J. Neurosci. 17: 5101-5107
    • (1997) J. Neurosci. , vol.17 , pp. 5101-5107
    • Busciglio, J.1    Hartmann, H.2    Lorenzo, A.3    Wong, C.4    Baumann, K.5    Sommer, B.6
  • 29
    • 0031017795 scopus 로고    scopus 로고
    • Light and electron microscopic localization of presenilin-1 in primate brain
    • Lah J. J., Heilman C. J., Nash N. R., Rees H. D., Yi H., Counts S. E. et al. (1997) Light and electron microscopic localization of presenilin-1 in primate brain. J. Neurosci. 17: 1971-1980
    • (1997) J. Neurosci. , vol.17 , pp. 1971-1980
    • Lah, J.J.1    Heilman, C.J.2    Nash, N.R.3    Rees, H.D.4    Yi, H.5    Counts, S.E.6
  • 30
  • 31
    • 0030459831 scopus 로고    scopus 로고
    • In situ hybridisation of presenilin 1 mRNA in Alzheimer's disease and in lesioned rat brain
    • Page K., Hollister R., Tanzi R. E. and Hyman B. T. (1996) In situ hybridisation of presenilin 1 mRNA in Alzheimer's disease and in lesioned rat brain. Proc. Natl. Acad. Sci. USA 93: 14020-14024
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 14020-14024
    • Page, K.1    Hollister, R.2    Tanzi, R.E.3    Hyman, B.T.4
  • 32
    • 8044231311 scopus 로고    scopus 로고
    • The Alzheimer's disease-associated presenilins are differentially phosphorylated proteins located predominantly within the endoplasmic reticulum
    • Walter J., Capell A., Grünberg J., Pesold B., Schindzielorz A., Prior R. et al. (1996) The Alzheimer's disease-associated presenilins are differentially phosphorylated proteins located predominantly within the endoplasmic reticulum. Mol. Med. 2: 673-691
    • (1996) Mol. Med. , vol.2 , pp. 673-691
    • Walter, J.1    Capell, A.2    Grünberg, J.3    Pesold, B.4    Schindzielorz, A.5    Prior, R.6
  • 33
    • 0029812077 scopus 로고    scopus 로고
    • Expression and analysis of presenilin 1 in a human neuronal system: Localization in cell bodies and dendrites
    • Cook D. G., Sung J. C., Golde T. E., Felsenstein K. M., Wojczyk B. S., Tanzi R. E. et al. (1996) Expression and analysis of presenilin 1 in a human neuronal system: localization in cell bodies and dendrites. Proc. Natl. Acad. Sci. USA 93: 9223-9228
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 9223-9228
    • Cook, D.G.1    Sung, J.C.2    Golde, T.E.3    Felsenstein, K.M.4    Wojczyk, B.S.5    Tanzi, R.E.6
  • 34
    • 15444341611 scopus 로고    scopus 로고
    • Phosphorylalion, subcellular localization, and membrane orientation of the Alzheimer's disease-associated presenilins
    • Strooper B., Beullens M., Contreras B., Levesque L., Craessaerts K., Cordell B. et al. (1997) Phosphorylalion, subcellular localization, and membrane orientation of the Alzheimer's disease-associated presenilins. J. Biol. Chem. 272: 3590-3598
    • (1997) J. Biol. Chem. , vol.272 , pp. 3590-3598
    • Strooper, B.1    Beullens, M.2    Contreras, B.3    Levesque, L.4    Craessaerts, K.5    Cordell, B.6
  • 35
    • 0030924177 scopus 로고    scopus 로고
    • Cell surface expression of the Alzheimer disease-related presenilin proteins
    • Dewji N. N. and Singer S. J. (1997) Cell surface expression of the Alzheimer disease-related presenilin proteins. Proc. Natl. Acad. Sci. USA 94: 9926-9931
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 9926-9931
    • Dewji, N.N.1    Singer, S.J.2
  • 36
    • 0030761059 scopus 로고    scopus 로고
    • Alzheimer presenilins in the nuclear membrane, interphase kinetochores and centrosomes suggest a role in chromosome segregation
    • Li J., Xu M., Zhou H., Ma J. and Potter H. (1997) Alzheimer presenilins in the nuclear membrane, interphase kinetochores and centrosomes suggest a role in chromosome segregation. Cell 90: 917-927
    • (1997) Cell , vol.90 , pp. 917-927
    • Li, J.1    Xu, M.2    Zhou, H.3    Ma, J.4    Potter, H.5
  • 38
    • 12644264304 scopus 로고    scopus 로고
    • Proteolytic processing of the Alzheimer disease-associated presenilin-1 gene generates an in vivo substrate for protein kinase C
    • Walter J., Grünberg J., Capell A., Pesold B., Schindzielorz A., Citron M. et al. (1997) Proteolytic processing of the Alzheimer disease-associated presenilin-1 gene generates an in vivo substrate for protein kinase C. Proc. Natl. Acad. Sci. USA 94: 5349-5354
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 5349-5354
    • Walter, J.1    Grünberg, J.2    Capell, A.3    Pesold, B.4    Schindzielorz, A.5    Citron, M.6
  • 40
    • 0030922146 scopus 로고    scopus 로고
    • Evidence for a six-transmembrane domain structure of presenilin 1
    • Lehmann S., Chiesa R. and Harris D. A. (1997) Evidence for a six-transmembrane domain structure of presenilin 1. J. Biol. Chem. 272: 12047-12051
    • (1997) J. Biol. Chem. , vol.272 , pp. 12047-12051
    • Lehmann, S.1    Chiesa, R.2    Harris, D.A.3
  • 42
    • 15844425969 scopus 로고    scopus 로고
    • Endoproteolysis of presenilin 1 and accumulation of processed derivatives in vivo
    • Thinakaran G., Borchelt D., Lee M., Slunt H., Spitzer L., Kim G. et al. (1996) Endoproteolysis of presenilin 1 and accumulation of processed derivatives in vivo. Neuron 17: 181-190
    • (1996) Neuron , vol.17 , pp. 181-190
    • Thinakaran, G.1    Borchelt, D.2    Lee, M.3    Slunt, H.4    Spitzer, L.5    Kim, G.6
  • 43
    • 0030575338 scopus 로고    scopus 로고
    • Characterization of human presenilin 1 using N-terminal specific monoclonal antibodies: Evidence that Alzheimer mutations affect proteolytic processing
    • Mercken M., Takahashi H., Honda T., Sato K., Murayama M., Nakazato Y. et al. (1996) Characterization of human presenilin 1 using N-terminal specific monoclonal antibodies: evidence that Alzheimer mutations affect proteolytic processing. FEBS Lett. 389: 297-303
    • (1996) FEBS Lett. , vol.389 , pp. 297-303
    • Mercken, M.1    Takahashi, H.2    Honda, T.3    Sato, K.4    Murayama, M.5    Nakazato, Y.6
  • 45
    • 0030890399 scopus 로고    scopus 로고
    • Endoproteolytic processing and proteasomal degradation of presenilin 2 in transfected cells
    • Kim T.-W., Pettingell W. H., Hallmark O. G., Moir R. D., Wasco W. and Tanzi R. E. (1997) Endoproteolytic processing and proteasomal degradation of presenilin 2 in transfected cells. J. Biol. Chem. 272: 11006-11010(a)
    • (1997) J. Biol. Chem. , vol.272
    • Kim, T.-W.1    Pettingell, W.H.2    Hallmark, O.G.3    Moir, R.D.4    Wasco, W.5    Tanzi, R.E.6
  • 46
    • 0030667426 scopus 로고    scopus 로고
    • Evidence that levels of presenilins (PS1 and PS2) are coordinately regulated by competition for limiting cellular factors
    • Thinakaran G., Harris C. L., Ratovitsky T., Davenport F., Slunt H., Price D. L. et al. (1997) Evidence that levels of presenilins (PS1 and PS2) are coordinately regulated by competition for limiting cellular factors. J. Biol. Chem. 272: 28415-28422
    • (1997) J. Biol. Chem. , vol.272 , pp. 28415-28422
    • Thinakaran, G.1    Harris, C.L.2    Ratovitsky, T.3    Davenport, F.4    Slunt, H.5    Price, D.L.6
  • 48
    • 0030889220 scopus 로고    scopus 로고
    • Presenilin proteins undergo heterogenous endoproteolysis between Thr291 and Ala299 and occur as Stable N- and C-terminal fragments in normal and Alzheimer brain tissue
    • Podlisny M. B., Citron M., Amarante P., Sherrington R., Xia W., Zhang J. et al. (1997) Presenilin proteins undergo heterogenous endoproteolysis between Thr291 and Ala299 and occur as Stable N- and C-terminal fragments in normal and Alzheimer brain tissue. Neurobiol. Dis. 3: 325-337
    • (1997) Neurobiol. Dis. , vol.3 , pp. 325-337
    • Podlisny, M.B.1    Citron, M.2    Amarante, P.3    Sherrington, R.4    Xia, W.5    Zhang, J.6
  • 49
    • 0030868903 scopus 로고    scopus 로고
    • Alternative cleavage of Alzheimer-associated presenilins during apoptosis by caspase-3 family protease
    • Kim T.-W., Pettingell W. H., Jung Y.-K., Kovacs D. M. and Tanzi R. E. (1997) Alternative cleavage of Alzheimer-associated presenilins during apoptosis by caspase-3 family protease. Science 277: 373-376
    • (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
  • 51
    • 0031004532 scopus 로고    scopus 로고
    • Developmental regulation of presenilin-1 processing in the brain suggests a role in neuronal differentiation
    • Hartmann H., Busciglio J., Baumann K.-H., Staufenbiel M. and Yankner B. A. (1997) Developmental regulation of presenilin-1 processing in the brain suggests a role in neuronal differentiation. J. Biol. Chem. 272: 14505-14508
    • (1997) J. Biol. Chem. , vol.272 , pp. 14505-14508
    • Hartmann, H.1    Busciglio, J.2    Baumann, K.-H.3    Staufenbiel, M.4    Yankner, B.A.5
  • 52
    • 0030657665 scopus 로고    scopus 로고
    • Cellular expression and proteolytic processing of presenilin proteins is developmentally regulated during neuronal differentiation
    • Capell A., Saffrick R., Olivo J.-C., Meyn L., Walter J., Grünberg J. et al., (1997) Cellular expression and proteolytic processing of presenilin proteins is developmentally regulated during neuronal differentiation. J. Neurochem. 69: 2432-2440
    • (1997) J. Neurochem. , vol.69 , pp. 2432-2440
    • Capell, A.1    Saffrick, R.2    Olivo, J.-C.3    Meyn, L.4    Walter, J.5    Grünberg, J.6
  • 53
    • 0030680151 scopus 로고    scopus 로고
    • Generation of anti-apoptotic presenilin-2 polypeptides by alternative transcription, proteolysis and caspase-3 cleavage
    • Vito P., Ghayurt T. and D'Adamio L. (1997) Generation of anti-apoptotic presenilin-2 polypeptides by alternative transcription, proteolysis and caspase-3 cleavage. J. Biol. Chem. 272: 28315-28320
    • (1997) J. Biol. Chem. , vol.272 , pp. 28315-28320
    • Vito, P.1    Ghayurt, T.2    D'Adamio, L.3
  • 54
    • 0030891662 scopus 로고    scopus 로고
    • Alzheimer's PS-1 mutation perturbs calcium homeostasis and sensitizes PC12 cells to death induced by amyloid β-peptide
    • Guo Q., Furukawa K., Sopher B. L., Pham D. G., Xie J., Robinson N. et al. (1996) Alzheimer's PS-1 mutation perturbs calcium homeostasis and sensitizes PC12 cells to death induced by amyloid β-peptide. Neuroreport 8: 379-383
    • (1996) Neuroreport , vol.8 , pp. 379-383
    • Guo, Q.1    Furukawa, K.2    Sopher, B.L.3    Pham, D.G.4    Xie, J.5    Robinson, N.6
  • 55
    • 10544224542 scopus 로고    scopus 로고
    • PS2 participates in cellular apoptosis: Constitutive activity conferred by Alzheimer mutation
    • Wolozin B., Iwasaki K., Vito P., Ganjei K., Lacana E., Sunderland T. et al. (1996) PS2 participates in cellular apoptosis: constitutive activity conferred by Alzheimer mutation. Science 274: 1710-1713
    • (1996) Science , vol.274 , pp. 1710-1713
    • Wolozin, B.1    Iwasaki, K.2    Vito, P.3    Ganjei, K.4    Lacana, E.5    Sunderland, T.6
  • 56
    • 0030580281 scopus 로고    scopus 로고
    • Alzheimer-associated presenilin-2 confers increased sensitivity to apoptosis in PC12 cells
    • Denp G., Pike C. J. and Cotman C. W. (1996) Alzheimer-associated presenilin-2 confers increased sensitivity to apoptosis in PC12 cells. FEBS Lett. 397: 50-54
    • (1996) FEBS Lett. , vol.397 , pp. 50-54
    • Denp, G.1    Pike, C.J.2    Cotman, C.W.3
  • 57
    • 0030771534 scopus 로고    scopus 로고
    • Increased apoptosis arising from increased expression of the Alzheimer's disease-associated presenilin-2 mutation (N1411)
    • Janicki S. and Monteiro M. J. (1997) Increased apoptosis arising from increased expression of the Alzheimer's disease-associated presenilin-2 mutation (N1411). J. Cell Biol. 139: 485-495
    • (1997) J. Cell Biol. , vol.139 , pp. 485-495
    • Janicki, S.1    Monteiro, M.J.2
  • 58
    • 0029671219 scopus 로고    scopus 로고
    • 2+-binding protein ALG-2 and Alzheimer's Disease Gene ALG-3
    • 2+-binding protein ALG-2 and Alzheimer's Disease Gene ALG-3. Science 271: 521-525
    • (1996) Science , vol.271 , pp. 521-525
    • Vito, P.1    Lancana, E.2    D'Adamio, L.3
  • 59
    • 0028019105 scopus 로고
    • Possible role of neuronal apoptosis in Alzheimer's disease
    • Johnson E. M. (1994) Possible role of neuronal apoptosis in Alzheimer's disease. Neurobiol. Aging 15: 5187-5189
    • (1994) Neurobiol. Aging , vol.15 , pp. 5187-5189
    • Johnson, E.M.1
  • 60
    • 0029245289 scopus 로고
    • A potential role for apoptosis in neurodegeneration and Alzheimer's disease
    • Cotman C. W. and Anderson A. J. (1995) A potential role for apoptosis in neurodegeneration and Alzheimer's disease. Mol. Neurobiol. 10: 19-45
    • (1995) Mol. Neurobiol. , vol.10 , pp. 19-45
    • Cotman, C.W.1    Anderson, A.J.2
  • 61
    • 0001796872 scopus 로고    scopus 로고
    • Apoptosis and Alzheimer's disease
    • Wasco W. and Tanzi R. E. (eds), Humana Press, Totowa, NJ
    • LeBlanc A. (1996) Apoptosis and Alzheimer's disease. In: Molecular Mechanisms of Dementia, pp. 57-71, Wasco W. and Tanzi R. E. (eds), Humana Press, Totowa, NJ
    • (1996) Molecular Mechanisms of Dementia , pp. 57-71
    • Leblanc, A.1
  • 62
    • 0011856830 scopus 로고
    • Mechanisms of molecular sorting in polarized cells: Relevance to Alzheimer's disease
    • Kosik K. S., Christen V. and Selkoe D. J. (eds), Springer, Berlin
    • Mellman I., Matter K., Yamamoto E., Pollack N., Roome J., Felsenstein K. et al. (1995) Mechanisms of molecular sorting in polarized cells: relevance to Alzheimer's disease. In: Alzheimer's Disease: Lessons from Cell Biology, pp. 14-26, Kosik K. S., Christen V. and Selkoe D. J. (eds), Springer, Berlin
    • (1995) Alzheimer's Disease: Lessons from Cell Biology , pp. 14-26
    • Mellman, I.1    Matter, K.2    Yamamoto, E.3    Pollack, N.4    Roome, J.5    Felsenstein, K.6
  • 63
    • 4244135802 scopus 로고
    • Physiological roduction and polarized secretion of the amyloid β-peptide in epithelial cells: A route to the mechanism of Alzheimer's disease
    • Kosik K. S., Christen V. and Selkoe D. J. (eds), Springer, Berlin
    • Selkoe D. J. (1995) Physiological roduction and polarized secretion of the amyloid β-peptide in epithelial cells: a route to the mechanism of Alzheimer's disease. In: Alzheimer's Disease: Lessons from Cell Biology, pp. 70-77, Kosik K. S., Christen V. and Selkoe D. J. (eds), Springer, Berlin
    • (1995) Alzheimer's Disease: Lessons from Cell Biology , pp. 70-77
    • Selkoe, D.J.1
  • 64
    • 16044373524 scopus 로고    scopus 로고
    • Aβ42(43) is increased in vivo by the PS1/2 and APP mutations linked to familial Alzheimer's disease
    • Scheuner D., Eckman C., Jensen M., Song X., Citron M., Suzuki N. et al. (1996) Aβ42(43) is increased in vivo by the PS1/2 and APP mutations linked to familial Alzheimer's disease. Nature Med. 2: 864-870
    • (1996) Nature Med. , vol.2 , pp. 864-870
    • Scheuner, D.1    Eckman, C.2    Jensen, M.3    Song, X.4    Citron, M.5    Suzuki, N.6
  • 65
    • 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., Thinakaran G., Eckman C. B., Lee M. K., Davenport F., Ratovitsky T. et al. (1996) Familial Alzheimer's disease-linked presenilin 1 variants elevate Aβ1-42/1-40 ratio in vitro and in vivo. Neuron 17: 1005-1013
    • (1996) Neuron , vol.17 , pp. 1005-1013
    • Borchelt, D.R.1    Thinakaran, G.2    Eckman, C.B.3    Lee, M.K.4    Davenport, F.5    Ratovitsky, T.6
  • 66
    • 16944362157 scopus 로고    scopus 로고
    • Mutant presenilins of Alzheimer's disease increase production of 42-residue amyloid beta-protein in both transfected cells and transgenic mice
    • Citron M., Westaway D., Xia W., Carlson G., Diehl T., Levesque G. et al. (1996) Mutant presenilins of Alzheimer's disease increase production of 42-residue amyloid beta-protein in both transfected cells and transgenic mice. Nature Med. 3: 67-72
    • (1996) Nature Med. , vol.3 , pp. 67-72
    • Citron, M.1    Westaway, D.2    Xia, W.3    Carlson, G.4    Diehl, T.5    Levesque, G.6
  • 67
    • 16044366039 scopus 로고    scopus 로고
    • Increased amyloid-β42(43) in brains of mice expressing mutant presenilin 1
    • Duff K., Eckman C., Zehr C., Yu X., Prada C-M., Perez-Tur J. et al. (1996) Increased amyloid-β42(43) in brains of mice expressing mutant presenilin 1. Nature 383: 710-713
    • (1996) Nature , vol.383 , pp. 710-713
    • Duff, K.1    Eckman, C.2    Zehr, C.3    Yu, X.4    Prada, C.-M.5    Perez-Tur, J.6
  • 68
    • 12644258498 scopus 로고    scopus 로고
    • The presenilin 2 mutation (N1411) linked to familial Alzheimer Disease (Volga German families) increases the secretion of amyloid β protein ending at the 42nd (or 43rd) residue
    • Tomita T., Maruyama K., Saido T. C., Kume H., Shinozaki K., Tokuhiro S. et al. (1997) The presenilin 2 mutation (N1411) linked to familial Alzheimer Disease (Volga German families) increases the secretion of amyloid β protein ending at the 42nd (or 43rd) residue. Proc. Natl. Acad. Sci. USA 94: 2025-2030
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 2025-2030
    • Tomita, T.1    Maruyama, K.2    Saido, T.C.3    Kume, H.4    Shinozaki, K.5    Tokuhiro, S.6
  • 69
    • 16944365745 scopus 로고    scopus 로고
    • Enhanced production and oligomerization of the 42-residue amyloid beta protein by Chinese hamster ovary cells stably expressing mutant presenilins
    • Xia W., Zhang J., Kholodenko D., Citron M., Podlisny M. B., Teplow D. B. et al. (1997) Enhanced production and oligomerization of the 42-residue amyloid beta protein by Chinese hamster ovary cells stably expressing mutant presenilins. J. Biol. Chem. 272: 7977-7982(a)
    • (1997) J. Biol. Chem. , vol.272
    • Xia, W.1    Zhang, J.2    Kholodenko, D.3    Citron, M.4    Podlisny, M.B.5    Teplow, D.B.6
  • 70
    • 16044365171 scopus 로고    scopus 로고
    • The E280A presenilin 1 Alzheimer mutation produces increased Aβ42 deposition and severe cerebellar pathology
    • Lemere C. A., Lopera F., Kosik K. S., Lendon C. L., Ossa J., Saido T. C. et al. (1996) The E280A presenilin 1 Alzheimer mutation produces increased Aβ42 deposition and severe cerebellar pathology. Nature Med. 2: 1146-1150
    • (1996) Nature Med. , vol.2 , pp. 1146-1150
    • Lemere, C.A.1    Lopera, F.2    Kosik, K.S.3    Lendon, C.L.4    Ossa, J.5    Saido, T.C.6
  • 72
    • 9444276544 scopus 로고    scopus 로고
    • Amyloid β protein (Aβ) deposition in chromosome 14-linked Alzheimer's disease: Predominance of Aβ42(43)
    • Mann D. M. A., Iwatsubo T., Cairns N. J., Lantos P. L., Nochlin D., Sumi S. M. et al. (1996) Amyloid β protein (Aβ) deposition in chromosome 14-linked Alzheimer's disease: predominance of Aβ42(43). Ann. Neurol. 40: 149-156
    • (1996) Ann. Neurol. , vol.40 , pp. 149-156
    • Mann, D.M.A.1    Iwatsubo, T.2    Cairns, N.J.3    Lantos, P.L.4    Nochlin, D.5    Sumi, S.M.6
  • 73
    • 0030769091 scopus 로고    scopus 로고
    • Distinct sites of intracellular production for Alzheimer's disease Aβ40/42 amyloid peptides
    • Hartmann T., Bieger S. C., Bruhl B., Tienari P. J., Ida N., Allsop D. et al. (1997) Distinct sites of intracellular production for Alzheimer's disease Aβ40/42 amyloid peptides. Nature Med. 3: 1016-1020
    • (1997) Nature Med. , vol.3 , pp. 1016-1020
    • Hartmann, T.1    Bieger, S.C.2    Bruhl, B.3    Tienari, P.J.4    Ida, N.5    Allsop, D.6
  • 74
    • 0030769092 scopus 로고    scopus 로고
    • Alzheimer's Aβ(1-42) is generated in the endoplasmic reticulum intermediate compartment of NT2N cells
    • Cook D. G., Forman M. S., Sung J. C., Leight S., Kolson D. L., Iwatsubo T. et al. (1997) Alzheimer's Aβ(1-42) is generated in the endoplasmic reticulum intermediate compartment of NT2N cells. Nature Med. 3: 1021-1023
    • (1997) Nature Med. , vol.3 , pp. 1021-1023
    • Cook, D.G.1    Forman, M.S.2    Sung, J.C.3    Leight, S.4    Kolson, D.L.5    Iwatsubo, T.6
  • 75
    • 0030952217 scopus 로고    scopus 로고
    • Intracellular generation and accumulation of amyloid β-peptide terminating at amino acid 42
    • Wild-Bode C., Yamazaki T., Capell A., Leimer U., Steiner H., Ihara Y. et al. (1997) Intracellular generation and accumulation of amyloid β-peptide terminating at amino acid 42. J. Biol. Chem. 272: 16085-16088
    • (1997) J. Biol. Chem. , vol.272 , pp. 16085-16088
    • Wild-Bode, C.1    Yamazaki, T.2    Capell, A.3    Leimer, U.4    Steiner, H.5    Ihara, Y.6
  • 76
    • 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., Diehl T. S., Gordon G., Biere A. L., Seubert P. and Selkoe D. J. (1996) 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) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 13170-13175
    • Citron, M.1    Diehl, T.S.2    Gordon, G.3    Biere, A.L.4    Seubert, P.5    Selkoe, D.J.6
  • 77
    • 0031054505 scopus 로고    scopus 로고
    • Formation of stable complexes between two Alzheimer's disease gene products: Presenilin-2 and β-amyloid precursor protein
    • Weidemann A., Paliga K., Dürrwang U., Czech C., Evin G., Masters C. L. et al. (1997) Formation of stable complexes between two Alzheimer's disease gene products: presenilin-2 and β-amyloid precursor protein. Nature Med. 3: 328-332
    • (1997) Nature Med. , vol.3 , pp. 328-332
    • Weidemann, A.1    Paliga, K.2    Dürrwang, U.3    Czech, C.4    Evin, G.5    Masters, C.L.6
  • 78
    • 0030753089 scopus 로고    scopus 로고
    • Interaction between amyloid precursor protein and presenilins in mammalian cells: Implication for the pathogenesis of Alzheimer's disease
    • Xia W., Zhang J., Koo E. H. and Selkoe D. J. (1997) Interaction between amyloid precursor protein and presenilins in mammalian cells: implication for the pathogenesis of Alzheimer's disease. Proc. Natl. Acad. Sci. USA 94: 8208-8213(b)
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94
    • Xia, W.1    Zhang, J.2    Koo, E.H.3    Selkoe, D.J.4
  • 80
    • 0031108103 scopus 로고    scopus 로고
    • The Sel-12 mutant phenotype of C. elegans is rescued independent of proteolytic processing by Wt but not mutant presenilin
    • Baumeister R., Leimer U., Zweckbronner J., Jakubek C., Gruenberg J. and Haass C. (1997) The Sel-12 mutant phenotype of C. elegans is rescued independent of proteolytic processing by Wt but not mutant presenilin. Genes Funct. 1: 149-159
    • (1997) Genes Funct. , vol.1 , pp. 149-159
    • Baumeister, R.1    Leimer, U.2    Zweckbronner, J.3    Jakubek, C.4    Gruenberg, J.5    Haass, C.6
  • 84
    • 17744401440 scopus 로고    scopus 로고
    • Presenilin 1 is required for Notch 1 and Dll1 expression in the paraxial mesoderm
    • Wong P., Zheng H., Chen H., Becher M. W., Sirinathsinghji D. J. S., Trumbauer M. E. et al. (1997) Presenilin 1 is required for Notch 1 and Dll1 expression in the paraxial mesoderm. Nature 387: 288-292
    • (1997) Nature , vol.387 , pp. 288-292
    • Wong, P.1    Zheng, H.2    Chen, H.3    Becher, M.W.4    Sirinathsinghji, D.J.S.5    Trumbauer, M.E.6
  • 85
    • 0030904751 scopus 로고    scopus 로고
    • Presenilin 1 interacts in brain with a novel member of the Armadillo family
    • Zhou J., Liyanage U., Medina M., Ho C., Simmons A. D., Lovett M. et al. (1997) Presenilin 1 interacts in brain with a novel member of the Armadillo family. Neuroreport 8: 1489-1494
    • (1997) Neuroreport , vol.8 , pp. 1489-1494
    • Zhou, J.1    Liyanage, U.2    Medina, M.3    Ho, C.4    Simmons, A.D.5    Lovett, M.6
  • 86
    • 0031301274 scopus 로고    scopus 로고
    • Complementation cloning of S2P. a gene encoding a putative metalloprotease required for intramembrane cleavage of SREBPs
    • Rawson R. B., Zelenski N. G., Nijhawan D., Ye J., Sakai J., Hasan M. T. et al. (1997) Complementation cloning of S2P. a gene encoding a putative metalloprotease required for intramembrane cleavage of SREBPs. Mol. Cell 1: 47-57
    • (1997) Mol. Cell , vol.1 , pp. 47-57
    • Rawson, R.B.1    Zelenski, N.G.2    Nijhawan, D.3    Ye, J.4    Sakai, J.5    Hasan, M.T.6


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