메뉴 건너뛰기




Volumn 7, Issue 5, 1997, Pages 683-688

Presenilins and Alzheimer's disease

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID BETA PROTEIN; AMYLOID PRECURSOR PROTEIN; PRESENILIN; PROTEIN; UNCLASSIFIED DRUG;

EID: 0030727230     PISSN: 09594388     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-4388(97)80089-X     Document Type: Article
Times cited : (53)

References (60)
  • 4
    • 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 EI, Sherrington R, Rogaeva EA, Levesque G, Ikeda M, Liang Y, Chi H, Lin C, Hallman K, Tsuda T 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 1995, 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    Chi, H.7    Lin, C.8    Hallman, K.9    Tsuda, T.10
  • 5
    • 0031052381 scopus 로고    scopus 로고
    • Amyloid, the presenilins and Alzheimer's disease
    • Hardy J: Amyloid, the presenilins and Alzheimer's disease. Trends Neurosci 1997, 20:154-159.
    • (1997) Trends Neurosci , vol.20 , pp. 154-159
    • Hardy, J.1
  • 6
    • 0030922421 scopus 로고    scopus 로고
    • Presenilins: Genes for life and death
    • Haass C: Presenilins: genes for life and death. Neuron 1997, 18:687-690.
    • (1997) Neuron , vol.18 , pp. 687-690
    • Haass, C.1
  • 8
    • 0342549411 scopus 로고    scopus 로고
    • Cell biology of presenilin 1
    • Thinakaran G: Cell biology of presenilin 1. Alzheimer Dis Rev 1996, 1:99-102.
    • (1996) Alzheimer Dis Rev , vol.1 , pp. 99-102
    • Thinakaran, G.1
  • 9
    • 15844425969 scopus 로고    scopus 로고
    • Endoproteolysis of presenilin 1 and accumulation of processed derivatives in vivo
    • Thinakaran G, Borchelt DR, Lee MK, Slunt HH, Spitzer L, Kim G, Ratovitsky T, Davenport F, Nordstedt C, Seeger M et al.: Endoproteolysis of presenilin 1 and accumulation of processed derivatives in vivo. Neuron 1996, 17:181-190. The first paper to describe the endoproteolysis and regulated accumulation of the proteolytic fragments of PS1. The authors reported the important findings that presenilin cleavage fragments may be the functional component of these proteins.
    • (1996) Neuron , vol.17 , pp. 181-190
    • Thinakaran, G.1    Borchelt, D.R.2    Lee, M.K.3    Slunt, H.H.4    Spitzer, L.5    Kim, G.6    Ratovitsky, T.7    Davenport, F.8    Nordstedt, C.9    Seeger, M.10
  • 10
    • 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, Noguchi K, Imahori K, Takashima A: Characterization of human presenilin 1 using N-terminal specific monoclonal antibodies: evidence that Alzheimer mutations affect proteolytic processing. FEBS Lett 1996, 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    Noguchi, K.7    Imahori, K.8    Takashima, A.9
  • 11
    • 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 MB, Citron M, Amarante P, Sherrington R, Xia W, Zhang J, Diehl T, Levesque G, Fraser P, Haass C et al.: 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 1997, 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    Diehl, T.7    Levesque, G.8    Fraser, P.9    Haass, C.10
  • 12
    • 0030890399 scopus 로고    scopus 로고
    • Endoproteolytic processing and proteasomal degradation of presenilin 2 in transfected cells
    • Kim T-W, Pettingell WH, Hallmark OG, Moir RD, Wasco W, Tanzi RE: Endoproteolytic processing and proteasomal degradation of presenilin 2 in transfected cells. J Biol Chem 1997, 272:11006-11010. The first paper to report that PS2 undergoes endoproteolytic processing and is degraded via the ubiquitin-proteasome pathway. The authors raise the possibility that proteasomal degradation may be used to regulate the levels of full-length presenilins, thereby permitting regulated endoproteolytic cleavage.
    • (1997) J Biol Chem , vol.272 , pp. 11006-11010
    • Kim, T.-W.1    Pettingell, W.H.2    Hallmark, O.G.3    Moir, R.D.4    Wasco, W.5    Tanzi, R.E.6
  • 13
    • 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 DR, Thinakaran G, Eckman CB, Lee MK, Davenport F, Ratovitsky T, Prada C-M, Kim G, Seekins S, Yager D et al.: Familial Alzheimer's disease-linked presenilin 1 variants elevate Aβ1-42/1-40 ratio in vitro and in vivo. Neuron 1996, 17:1005-1013. One of three simultaneous reports (see [29•,30•]) demonstrating increases in the Aβ42 : Aβ40 ratio in transfected cells and transgenic mice expressing FAD mutant forms of the presenilins. The results in this paper are extremely similar and confirmatory findings to those described in [29•,30•].
    • (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    Prada, C.-M.7    Kim, G.8    Seekins, S.9    Yager, D.10
  • 14
    • 0030868903 scopus 로고    scopus 로고
    • Alternative cleavage of Alzheimer-associated presenilins during apoptosis by a caspase-3 family protease
    • Kim T-W, Pettingell WH, Jung YK, Kovacs DM, Tanzi RE: Alternative cleavage of Alzheimer-associated presenilins during apoptosis by a caspase-3 family protease. Science 1997, 277:373-376. The first report showing that the presenilins undergo alternative endoproteolysis, which is mediated by an apoptosis-associated caspase-3 family protease and which is enhanced by the Asn141→lle FAD mutation. These findings suggest that the presenilins may be cell death substrates and that FAD mutations may lead to the enhanced activation of caspase-3 family proteases.
    • (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
  • 17
    • 0029116848 scopus 로고
    • Facilitation of lin-12-mediated signalling by sel-12, a Caenorhabditis elegans S182 Alzheimer's disease gene
    • Levitan D, Greenwald I: Facilitation of lin-12-mediated signalling by sel-12, a Caenorhabditis elegans S182 Alzheimer's disease gene. Nature 1995, 377:351-354.
    • (1995) Nature , vol.377 , pp. 351-354
    • Levitan, D.1    Greenwald, I.2
  • 19
    • 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, Haass C: The Sel-12 mutant phenotype of C. elegans is rescued independent of proteolytic processing by Wt but not mutant presenilin. Genes Function 1997, 1:149-159. One of two reports (see also [18•]) showing that human presenilins can rescue the sel-12 mutant phenotype.
    • (1997) Genes Function , vol.1 , pp. 149-159
    • Baumeister, R.1    Leimer, U.2    Zweckbronner, J.3    Jakubek, C.4    Gruenberg, J.5    Haass, C.6
  • 20
    • 17744401440 scopus 로고    scopus 로고
    • Presenilin 1 is required for Notch1 and DII1 expression in the paraxial mesoderm
    • Wong P, Zheng H, Chen H, Becher MW, Sirinathsinghji DJS, Trumbauer ME, Proce DL, Van der Ploeg LHT, Sisodia SS: Presenilin 1 is required for Notch1 and DII1 expression in the paraxial mesoderm. Nature 1997, 387:288-292. One of two reports (see [21••]) that were published simultaneously describing the phenotypes of the PS1 null mice. These data further suggest a role for PS1 in the Notch developmental pathway. PS1 expression may be required during development for proper temporal expression of Notch and Delta.
    • (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    Proce, D.L.7    Van Der Ploeg, L.H.T.8    Sisodia, S.S.9
  • 21
    • 0030779784 scopus 로고    scopus 로고
    • Skeletal and CNS defects in presenilin-1-deficient mice
    • Shen J, Bronson RT, Chen DF, Xia W, Selkoe DJ, Tonegawa S: Skeletal and CNS defects in presenilin-1-deficient mice. Cell 1997, 89:629-639. One of two reports (see [20••]) that were published simultaneously describing the phenotypes of the PS1 null mice. In this paper, additional knock-out phenotype involving neuronal loss was observed.
    • (1997) Cell , vol.89 , pp. 629-639
    • Shen, J.1    Bronson, R.T.2    Chen, D.F.3    Xia, W.4    Selkoe, D.J.5    Tonegawa, S.6
  • 22
    • 0028989016 scopus 로고
    • Notch1 is required for the coordinate segmentation of somites
    • Conlon RA, Reaume AG, Rossant J: Notch1 is required for the coordinate segmentation of somites. Development 1995, 121:1533-1545.
    • (1995) Development , vol.121 , pp. 1533-1545
    • Conlon, R.A.1    Reaume, A.G.2    Rossant, J.3
  • 23
    • 0030976083 scopus 로고    scopus 로고
    • Maintenance of somite borders in mice requires the Delta homologue DII1
    • Hrabe de Angelis M, McyIntyre J II, Gossler A: Maintenance of somite borders in mice requires the Delta homologue DII1. Nature 1997, 386:717-721.
    • (1997) Nature , vol.386 , pp. 717-721
    • Hrabe De Angelis, M.1    McyIntyre J. II2    Gossler, A.3
  • 26
    • 0030788767 scopus 로고    scopus 로고
    • Presenilin 1 interaction in the brain with a novel member of the Armadillo family
    • Zhou J, Liyanage U, Medina M, Ho C, Simmons AD, Lovett M, Kosik KS: Presenilin 1 interaction in the brain with a novel member of the Armadillo family. Neuroreport 1997, 8:1489-1494. This report shows that in the brain, PS1 interacts with δ-catenin, a putative novel mammalian homologue of the Drosophila Armadillo family, suggesting a role for PS1 in the Wingless signaling pathway.
    • (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    Kosik, K.S.7
  • 27
    • 0029670476 scopus 로고    scopus 로고
    • Interaction between Wingless and Notch signaling pathways mediated by Dishevelled
    • Axelrod JD, Matsuno K, Artavanis-Tsakonas S, Perrimon N: Interaction between Wingless and Notch signaling pathways mediated by Dishevelled. Science 1996, 271:1826-1832.
    • (1996) Science , vol.271 , pp. 1826-1832
    • Axelrod, J.D.1    Matsuno, K.2    Artavanis-Tsakonas, S.3    Perrimon, N.4
  • 28
    • 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, Bird TD, Hardy J, Hutton M, Kukull W et al.: Aβ42(43) is increased in vivo by the PS1/2 and APP mutations linked to familial Alzheimer's disease. Nat Med 1996, 2:864-870. The first report to demonstrate increased Aβ42 in plasma and fibroblasts derived from FAD patients carrying PS1, PS2, or APP mutations. This seminar paper was the first to demonstrate a common phenotype for FAD mutations in APP and presenilins, causing a relative increase in the highly amyloidogenic peptide Aβ42.
    • (1996) Nat Med , vol.2 , pp. 864-870
    • Scheuner, D.1    Eckman, C.2    Jensen, M.3    Song, X.4    Citron, M.5    Suzuki, N.6    Bird, T.D.7    Hardy, J.8    Hutton, M.9    Kukull, W.10
  • 29
    • 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, Johnson-Wood K, Lee M, Seubert P, Davis A, Kholodenko D et al.: Mutant presenilins of Alzheimer's disease increase production of 42-residue amyloid beta-protein in both transfected cells and transgenic mice. Nat Med 1996, 3:67-72. One of three simultaneous reports (see [13•,30•]) demonstrating increases in the Aβ42 : Aβ40 ratio in transfected cells and transgenic mice expressing FAD mutant forms of the presenilins. The results in this paper are extremely similar and confirmatory findings to those described in [13•,30•].
    • (1996) Nat Med , vol.3 , pp. 67-72
    • Citron, M.1    Westaway, D.2    Xia, W.3    Carlson, G.4    Diehl, T.5    Levesque, G.6    Johnson-Wood, K.7    Lee, M.8    Seubert, P.9    Davis, A.10    Kholodenko, D.11
  • 30
    • 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, Hutton M, Buee L, Harigaya Y, Yager D et al.: Increased amyloid-β42(43) in brains of mice expressing mutant presenilin 1. Nature 1996, 383:710-713. One of three simultaneous reports (see [13•,29•]) demonstrating increases in the Aβ42 : Aβ40 ratio in transfected cells and transgenic mice expressing FAD mutant forms of the presenilins. The results in this paper are extremely similar and confirmatory findings to those described in [13•,29•]. Uniquely, in this paper, increase of endogenous mouse Aβ42/Aβ40 is observed due to the expression of FAD mutant PS1 transgene.
    • (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    Hutton, M.7    Buee, L.8    Harigaya, Y.9    Yager, D.10
  • 31
    • 12644258498 scopus 로고    scopus 로고
    • The presenilin 2 mutation (N141I) 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 TC, Kume H, Shinozaki K, Tokuhiro S, Capell A, Walter J, Grünberg J, Haass C et al.: The presenilin 2 mutation (N141I) 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 1997, 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    Capell, A.7    Walter, J.8    Grünberg, J.9    Haass, C.10
  • 32
    • 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 MB, Teplow DB, Haass C, Seubert P, Koo EH, Selkoe DJ: Enhanced production and oligomerization of the 42-residue amyloid beta protein by Chinese hamster ovary cells stably expressing mutant presenilins. J Biol Chem 1997, 272:7977-7982.
    • (1997) J Biol Chem , vol.272 , pp. 7977-7982
    • Xia, W.1    Zhang, J.2    Kholodenko, D.3    Citron, M.4    Podlisny, M.B.5    Teplow, D.B.6    Haass, C.7    Seubert, P.8    Koo, E.H.9    Selkoe, D.J.10
  • 36
    • 0030614569 scopus 로고    scopus 로고
    • Amyloid (Aβ) deposition in chromosome 1-linked Alzheimer's disease: The Volga German families
    • Mann DMA, Iwatsubo T, Nochlin D, Sumi SM, Levy-Lahad E, Bird TD: Amyloid (Aβ) deposition in chromosome 1-linked Alzheimer's disease: the Volga German families. Ann Neurol 1997, 41:52-57.
    • (1997) Ann Neurol , vol.41 , pp. 52-57
    • Mann, D.M.A.1    Iwatsubo, T.2    Nochlin, D.3    Sumi, S.M.4    Levy-Lahad, E.5    Bird, T.D.6
  • 37
    • 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 CL, Beyreuther K: Formation of stable complexes between two Alzheimer's disease gene products: presenilin-2 and β-amyloid precursor protein. Nat Med 1997, 3:328-332.
    • (1997) Nat 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    Beyreuther, K.7
  • 38
    • 0030753089 scopus 로고    scopus 로고
    • In vivo interaction between amyloid precursor protein and presenilins in mammalian cells: Implication for the pathogenesis of Alzheimer's disease
    • Xia W, Zhang J, Koo EH, Selkoe DJ: In vivo interaction between amyloid precursor protein and presenilins in mammalian cells: implication for the pathogenesis of Alzheimer's disease. Proc Natl Acad Sci USA 1997, 94:8208-8213.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 8208-8213
    • Xia, W.1    Zhang, J.2    Koo, E.H.3    Selkoe, D.J.4
  • 40
    • 0030922146 scopus 로고    scopus 로고
    • Evidence for a six-transmembrane domain structure of presenilin 1
    • Lehmann S, Chiesa R, Harris DA: Evidence for a six-transmembrane domain structure of presenilin 1. J Biol Chem 1997, 272:12047-12051.
    • (1997) J Biol Chem , vol.272 , pp. 12047-12051
    • Lehmann, S.1    Chiesa, R.2    Harris, D.A.3
  • 41
    • 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, Haass C: Intracellular generation and accumulation of amyloid β-peptide terminating at amino acid 42. J Biol Chem 1997, 272:16085-16088. This report demonstrates that Aβ42 is generated primarily in the endoplasmic reticulum. The generation of intracellular Aβ could be an initial step in AD neuropathogenesis.
    • (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    Haass, C.7
  • 42
    • 0030769092 scopus 로고    scopus 로고
    • Alzheimer's Aβ(1-42) is generated in the endoplasmic reticulum/intermediate compartment of NT2N cells
    • Cook DG, Forman MS, Sung JC, Leight S, Kolson DL, Iwatsubo T, Lee VM-Y, Doms RW: Alzheimer's Aβ(1-42) is generated in the endoplasmic reticulum/intermediate compartment of NT2N cells. Nat Med 1997, 3:1021-1023. This paper definitely shows that Aβ42, primary component of senile plaques in AD, can be generated in the endoplasmic reticulum, suggesting that this may be the initial site of AD pathogenesis. See also annotation [43••].
    • (1997) Nat 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    Lee, V.M.-Y.7    Doms, R.W.8
  • 43
    • 0030769091 scopus 로고    scopus 로고
    • Distinct sites of intracellular production of Alzheimer's disease Aβ40/42 amyloid peptides
    • Hartmann T, Bieger SC, Brühl B, Tienari PJ, Ida N, Allsop D, Roberts GW, Masters CL, Dotti CG, Unsicker K, Beyreuther K: Distinct sites of intracellular production of Alzheimer's disease Aβ40/42 amyloid peptides. Nat Med 1997, 3:1016-1020. This is the first report to show that while Aβ42 is mainly localized in the endoplasmic reticulum, Aβ40 is present in the Golgi and cell surface. Along with other reports [41••,42••], these data point to the endoplasmic reticulum as an initial cellular compartment of AD neuropathogenesis.
    • (1997) Nat Med , vol.3 , pp. 1016-1020
    • Hartmann, T.1    Bieger, S.C.2    Brühl, B.3    Tienari, P.J.4    Ida, N.5    Allsop, D.6    Roberts, G.W.7    Masters, C.L.8    Dotti, C.G.9    Unsicker, K.10    Beyreuther, K.11
  • 44
    • 0029784838 scopus 로고    scopus 로고
    • Amyloid β-protein and the genetics of Alzheimer's disease
    • Selkoe DJ: Amyloid β-protein and the genetics of Alzheimer's disease. J Biol Chem 1996, 271:18295-18298.
    • (1996) J Biol Chem , vol.271 , pp. 18295-18298
    • Selkoe, D.J.1
  • 45
    • 13344282063 scopus 로고    scopus 로고
    • Alzheimer associated presenilins 1 and 2: Neuronal expression in brain and localization to intracellular membranes in mammalian cells
    • Kovacs DM, Fausett HJ, Page KJ, Kim T-W, Moir RD, Merriam DE, Hollister RD, Hallmark OG, Mancini R, Felsenstein KM et al.: Alzheimer associated presenilins 1 and 2: neuronal expression in brain and localization to intracellular membranes in mammalian cells. Nat Med 1996, 2:224-229. The first report to demonstrate the predominant neuronal expression of the presenilins in brain and their subcellular localization in the endoplasmic reticulum and Golgi of mammalian cells.
    • (1996) Nat 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    Hollister, R.D.7    Hallmark, O.G.8    Mancini, R.9    Felsenstein, K.M.10
  • 49
    • 0028577208 scopus 로고
    • Immunohistochemical evidence for apoptosis in Alzheimer's disease
    • Su J, Anderson A, Cummings B, Cotman C: Immunohistochemical evidence for apoptosis in Alzheimer's disease. Neuroreport 1994, 5:2529-2533.
    • (1994) Neuroreport , vol.5 , pp. 2529-2533
    • Su, J.1    Anderson, A.2    Cummings, B.3    Cotman, C.4
  • 50
    • 0028019105 scopus 로고
    • Possible role of neuronal apoptosis in Alzheimer's disease
    • Johnson EM: Possible role of neuronal apoptosis in Alzheimer's disease. Neurobiol Aging 1994, 15:5187-5189.
    • (1994) Neurobiol Aging , vol.15 , pp. 5187-5189
    • Johnson, E.M.1
  • 51
    • 0029245289 scopus 로고
    • A potential role for apoptosis in neurodegeneration and Alzheimer's disease
    • Cotman CW, Anderson AJ: A potential role for apoptosis in neurodegeneration and Alzheimer's disease. Mol Neurobiol 1995, 10:19-45.
    • (1995) Mol Neurobiol , vol.10 , pp. 19-45
    • Cotman, C.W.1    Anderson, A.J.2
  • 52
    • 0001796872 scopus 로고    scopus 로고
    • Apoptosis and Alzheimer's disease
    • Edited by Wasco W, Tanzi RE. Totowa, New Jersey: Humana Press
    • LeBlanc A: Apoptosis and Alzheimer's disease. In Molecular Mechanism of Dementia. Edited by Wasco W, Tanzi RE. Totowa, New Jersey: Humana Press; 1996:57-71.
    • (1996) Molecular Mechanism of Dementia , pp. 57-71
    • LeBlanc, A.1
  • 53
    • 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 1996, 271:521-524.
    • (1996) Science , vol.271 , pp. 521-524
    • Vito, P.1    Lancana, E.2    D'Adamio, L.3
  • 55
    • 0030580281 scopus 로고    scopus 로고
    • Alzheimer-associated presenilin-2 confers increased sensitivity to apoptosis in PC12 cells
    • Deng G, Pike CJ, Cotman CW: Alzheimer-associated presenilin-2 confers increased sensitivity to apoptosis in PC12 cells. FEBS Lett 1996, 397:50-54.
    • (1996) FEBS Lett , vol.397 , pp. 50-54
    • Deng, G.1    Pike, C.J.2    Cotman, C.W.3
  • 56
    • 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 BL, Pham DG, Xie J, Robinson N, Martin GM, Mattson MP: Alzheimer's PS-1 mutation perturbs calcium homeostasis and sensitizes PC12 cells to death induced by amyloid β-peptide. Neuroreport 1996, 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    Martin, G.M.7    Mattson, M.P.8
  • 59
    • 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, Yankner BA: Developmental regulation of presenilin-1 processing in the brain suggests a role in neuronal differentiation. J Biol Chem 1997, 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
  • 60
    • 0030657665 scopus 로고    scopus 로고
    • Cellular expression and proteolytic processing of presenilin proteins is developmentally regulated during neuronal differentiation
    • in press
    • Capell A, Saffrich R, Olivo J-C, Meyn L, Walter J, Grünberg J, Dotti C, Haass C: Cellular expression and proteolytic processing of presenilin proteins is developmentally regulated during neuronal differentiation. J Neurochem 1997, in press.
    • (1997) J Neurochem
    • Capell, A.1    Saffrich, R.2    Olivo, J.-C.3    Meyn, L.4    Walter, J.5    Grünberg, J.6    Dotti, C.7    Haass, C.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.