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Volumn 37, Issue 2, 2000, Pages 101-111

Familial Alzheimer's disease-associated mutations block translocation of full-length presenilin 1 to the nuclear envelope

Author keywords

Alzheimer's disease; Confocal microscopy; Immunocytochemistry; Nuclear envelope; Presenilin

Indexed keywords

EPITOPE; MONOCLONAL ANTIBODY; PRESENILIN 1;

EID: 0034212576     PISSN: 01680102     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0168-0102(00)00106-1     Document Type: Article
Times cited : (15)

References (39)
  • 1
    • 0029115555 scopus 로고
    • The structure of the presenilin 1 (S182) gene and identification of six novel mutations in early onset AD families
    • The structure of the presenilin 1 (S182) gene and identification of six novel mutations in early onset AD families. Nat. Genet. 11:1995;219-222.
    • (1995) Nat. Genet. , vol.11 , pp. 219-222
  • 3
    • 0030657665 scopus 로고    scopus 로고
    • Cellular expression and proteolytic processing of presenilin proteins is developmentally regulated during neuronal differentiation
    • Capell A., Saffrich R., Olivo J.C., Meyn L., Walter J., Grunberg J., Mathews P., Nixon R., Dotti C., Haass C. Cellular expression and proteolytic processing of presenilin proteins is developmentally regulated during neuronal differentiation. J. Neurochem. 69:1997;2432-2440.
    • (1997) J. Neurochem. , vol.69 , pp. 2432-2440
    • Capell, A.1    Saffrich, R.2    Olivo, J.C.3    Meyn, L.4    Walter, J.5    Grunberg, J.6    Mathews, P.7    Nixon, R.8    Dotti, C.9    Haass, C.10
  • 4
    • 0000245728 scopus 로고
    • Isolation of pure and unaltered liver nuclei morphology and biochemical composition
    • Chauveau J., Moulé Y., Rouiller C. Isolation of pure and unaltered liver nuclei morphology and biochemical composition. Exp. Cell Res. 11:1956;317-321.
    • (1956) Exp. Cell Res. , vol.11 , pp. 317-321
    • Chauveau, J.1    Moulé, Y.2    Rouiller, C.3
  • 5
    • 0030739716 scopus 로고    scopus 로고
    • Novel β-secretase cleavage of β-amyloid precursor protein in the endoplasmic reticulum/intermediate compartment of NT2N cells
    • Chyung A.S.C., Greenberg B.D., Cook D.G., Doms R.W., Lee V.M. Novel β-secretase cleavage of β-amyloid precursor protein in the endoplasmic reticulum/intermediate compartment of NT2N cells. J. Cell Biol. 138:1997;671-680.
    • (1997) J. Cell Biol. , vol.138 , pp. 671-680
    • Chyung, A.S.C.1    Greenberg, B.D.2    Cook, D.G.3    Doms, R.W.4    Lee, V.M.5
  • 8
    • 0038785079 scopus 로고    scopus 로고
    • Alzheimer's disease associated presenilin-1 holoprotein and its 18-20 kDa C-terminal fragment are death substrates for proteases of the caspase family
    • Grünberg J., Walter J., Loetscher H., Deuschle U., Jacobsen H., Haass C. Alzheimer's disease associated presenilin-1 holoprotein and its 18-20 kDa C-terminal fragment are death substrates for proteases of the caspase family. Biochemistry. 37:1998;2263-2270.
    • (1998) Biochemistry , vol.37 , pp. 2263-2270
    • Grünberg, J.1    Walter, J.2    Loetscher, H.3    Deuschle, U.4    Jacobsen, H.5    Haass, C.6
  • 9
    • 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 B.A. Developmental regulation of presenilin-1 processing in the brain suggests a role in neuronal differentiation. J. Biol. Chem. 272:1997;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
  • 12
    • 0028169925 scopus 로고
    • Visualization of Aβ42(43) and Aβ40 in senile plaques with end-specific Aβ monoclonals: Evidence that an initially deposited species is Aβ42(43)
    • Iwatsubo T., Odaka A., Suzuki N., Mizusawa H., Nukina N., Ihara Y. Visualization of Aβ42(43) and Aβ40 in senile plaques with end-specific Aβ monoclonals: evidence that an initially deposited species is Aβ42(43). Neuron. 13:1994;45-53.
    • (1994) Neuron , vol.13 , pp. 45-53
    • Iwatsubo, T.1    Odaka, A.2    Suzuki, N.3    Mizusawa, H.4    Nukina, N.5    Ihara, Y.6
  • 13
    • 0032576605 scopus 로고    scopus 로고
    • Aggresomes: A cellular response to misfolded proteins
    • Johnston J.A., Ward C.L., Kopito R.R. Aggresomes: a cellular response to misfolded proteins. J. Cell Biol. 143:1998;1883-1898.
    • (1998) J. Cell Biol. , vol.143 , pp. 1883-1898
    • Johnston, J.A.1    Ward, C.L.2    Kopito, R.R.3
  • 14
    • 0030868903 scopus 로고    scopus 로고
    • Alternative cleavage of Alzheimer-associated presenilins during apoptosis by a caspase-3 family protease
    • Kim T.W., Pettingell W.H., Jung Y.K., Kovacs D.M., Tanzi R.E. Alternative cleavage of Alzheimer-associated presenilins during apoptosis by a caspase-3 family protease. Science. 277:1997;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
  • 17
    • 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., Potter H. Alzheimer presenilins in the nuclear membrane, interphase kinetochores, and centrosomes suggest a role in chromosome segregation. Cell. 90:1997;917-927.
    • (1997) Cell , vol.90 , pp. 917-927
    • Li, J.1    Xu, M.2    Zhou, H.3    Ma, J.4    Potter, H.5
  • 20
    • 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. 389:1996;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
  • 22
    • 0013653350 scopus 로고
    • Isolation and characterization of cytoplasmic components of cancer cells
    • Busch H. New York: Academic Press
    • Murray R.K., Suss R., Pitot H.C. Isolation and characterization of cytoplasmic components of cancer cells. Busch H. Methods in Cancer Research. 2:1967;239-286 Academic Press, New York.
    • (1967) Methods in Cancer Research , vol.2 , pp. 239-286
    • Murray, R.K.1    Suss, R.2    Pitot, H.C.3
  • 25
    • 0028855851 scopus 로고
    • Dominant and differential deposition of distinct β-amyloid peptide species, Aβ N3(pE), in senile plaques
    • Saido T.C., Iwatsubo T., Mann D.M., Shimada H., Ihara Y., Kawashima S. Dominant and differential deposition of distinct β-amyloid peptide species, Aβ N3(pE), in senile plaques. Neuron. 14:1995;457-466.
    • (1995) Neuron , vol.14 , pp. 457-466
    • Saido, T.C.1    Iwatsubo, T.2    Mann, D.M.3    Shimada, H.4    Ihara, Y.5    Kawashima, S.6
  • 26
    • 0030582387 scopus 로고    scopus 로고
    • Amino- and carboxyl-terminal heterogeneity of β-amyloid peptides deposited in human brain
    • Saido T.C., Yamao-Harigaya W., Iwatsubo T., Kawashima S. Amino- and carboxyl-terminal heterogeneity of β-amyloid peptides deposited in human brain. Neurosci. Lett. 215:1996;173-176.
    • (1996) Neurosci. Lett. , vol.215 , pp. 173-176
    • Saido, T.C.1    Yamao-Harigaya, W.2    Iwatsubo, T.3    Kawashima, S.4
  • 29
    • 0028322017 scopus 로고
    • An increased percentage of long amyloid β protein secreted by familial amyloid β protein precursor (βAPP717) mutants
    • Suzuki N., Cheung T.T., Cai X.D., Odaka A., Otvos L. Jr, Eckman C., Golde T.E., Younkin S.G. An increased percentage of long amyloid β protein secreted by familial amyloid β protein precursor (βAPP717) mutants. Science. 264:1994;1336-1340.
    • (1994) Science , vol.264 , pp. 1336-1340
    • Suzuki, N.1    Cheung, T.T.2    Cai, X.D.3    Odaka, A.4    Otvos L., Jr.5    Eckman, C.6    Golde, T.E.7    Younkin, S.G.8
  • 31
    • 0032545273 scopus 로고    scopus 로고
    • Abrogation of the presenilin 1/β-catenin interaction and preservation of the heterodimeric presenilin 1 complex following caspase activation
    • Tesco G., Kim T.W., Diehlmann A., Beyreuther K., Tanzi R.E. Abrogation of the presenilin 1/β-catenin interaction and preservation of the heterodimeric presenilin 1 complex following caspase activation. J. Biol. Chem. 273:1998;33909-33914.
    • (1998) J. Biol. Chem. , vol.273 , pp. 33909-33914
    • Tesco, G.1    Kim, T.W.2    Diehlmann, A.3    Beyreuther, K.4    Tanzi, R.E.5
  • 36
    • 16944365745 scopus 로고    scopus 로고
    • Enhanced production and oligomerization of the 42-residue amyloid β-protein by Chinese hamster ovary cells stably expressing mutant presenilins
    • Xia W., Zhang J., Kholodenko D., Citron M., Podlisny M.B., Teplow D.B., Haass C., Seubert P., Koo E.H., Selkoe D.J. Enhanced production and oligomerization of the 42-residue amyloid β-protein by Chinese hamster ovary cells stably expressing mutant presenilins. J. Biol. Chem. 272:1997;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
  • 39


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.