메뉴 건너뛰기




Volumn 64, Issue 17, 2007, Pages 2211-2218

The molecular link between β- and γ-secretase activity on the amyloid β precursor protein

Author keywords

secretase; Alzheimer's disease; Amyloid ; BACE1; Oxidative stress; PS1

Indexed keywords

AMYLOID PRECURSOR PROTEIN; BETA SECRETASE; GAMMA SECRETASE; PRESENILIN 1;

EID: 34548306686     PISSN: 1420682X     EISSN: 15691632     Source Type: Journal    
DOI: 10.1007/s00018-007-7219-3     Document Type: Review
Times cited : (54)

References (77)
  • 1
    • 0037176727 scopus 로고    scopus 로고
    • A novel epsilon-cleavage within the transmembrane domain of the Alzheimer amyloid precursor protein demonstrates homology with Notch processing
    • Weidemann, A., Eggert, S., Reinhard, F. B., Vogel, M., Paliga, K., Baier, G., Masters, C. L., Beyreuther, K. and Evin, G. (2002) A novel epsilon-cleavage within the transmembrane domain of the Alzheimer amyloid precursor protein demonstrates homology with Notch processing. Biochemistry 41, 2825-2835.
    • (2002) Biochemistry , vol.41 , pp. 2825-2835
    • Weidemann, A.1    Eggert, S.2    Reinhard, F.B.3    Vogel, M.4    Paliga, K.5    Baier, G.6    Masters, C.L.7    Beyreuther, K.8    Evin, G.9
  • 3
    • 3943092621 scopus 로고    scopus 로고
    • Pathways towards and away from Alzheimer's disease
    • Mattson, M. P. (2004) Pathways towards and away from Alzheimer's disease. Nature 430, 631-639.
    • (2004) Nature , vol.430 , pp. 631-639
    • Mattson, M.P.1
  • 4
    • 10944259134 scopus 로고    scopus 로고
    • Identification of a new presenilin-dependent zeta-cleavage site within the transmembrane domain of amyloid precursor protein
    • Zhao, G., Mao, G., Tan, J., Dong, J., Cui, M. Z., Kim, S. H. and Xu, X. (2004) Identification of a new presenilin-dependent zeta-cleavage site within the transmembrane domain of amyloid precursor protein. J. Biol. Chem. 279, 50647-50650.
    • (2004) J. Biol. Chem , vol.279 , pp. 50647-50650
    • Zhao, G.1    Mao, G.2    Tan, J.3    Dong, J.4    Cui, M.Z.5    Kim, S.H.6    Xu, X.7
  • 5
    • 27844441278 scopus 로고    scopus 로고
    • γ-Cleavage is dependent on ζ-cleavage during the proteolytic processing of amyloid precursor protein within its transmembrane domain
    • Zhao, G., Cui, M. Z., Mao, G., Dong, Y., Tan, J., Sun, L. and Xu, X. (2005) γ-Cleavage is dependent on ζ-cleavage during the proteolytic processing of amyloid precursor protein within its transmembrane domain. J. Biol. Chem. 280, 37689-37697.
    • (2005) J. Biol. Chem , vol.280 , pp. 37689-37697
    • Zhao, G.1    Cui, M.Z.2    Mao, G.3    Dong, Y.4    Tan, J.5    Sun, L.6    Xu, X.7
  • 6
    • 0029896354 scopus 로고    scopus 로고
    • Mechanisms of neuronal degeneration in Alzheimer's disease
    • Yankner, B. A. (1996). Mechanisms of neuronal degeneration in Alzheimer's disease. Neuron 16, 921-932.
    • (1996) Neuron , vol.16 , pp. 921-932
    • Yankner, B.A.1
  • 7
    • 33745236883 scopus 로고    scopus 로고
    • Tau aggregation and progressive neuronal degeneration in the absence of changes in spine density and morphology after targeted expression of Alzheimer's disease-relevant tau constructs in organotypic hippocampal slices
    • Shahani, N., Subramaniam, S., Wolf, T., Tackenberg, C. and Brandt, R. (2006) Tau aggregation and progressive neuronal degeneration in the absence of changes in spine density and morphology after targeted expression of Alzheimer's disease-relevant tau constructs in organotypic hippocampal slices. J. Neurosci. 26, 6130-6134.
    • (2006) J. Neurosci , vol.26 , pp. 6130-6134
    • Shahani, N.1    Subramaniam, S.2    Wolf, T.3    Tackenberg, C.4    Brandt, R.5
  • 8
    • 34249862316 scopus 로고    scopus 로고
    • The role of tau phosphorylation and cleavage in neuronal cell death
    • Chun, W. and Johnson, G. V. ( 2007) The role of tau phosphorylation and cleavage in neuronal cell death. Front. Biosci. 12, 733-756.
    • (2007) Front. Biosci , vol.12 , pp. 733-756
    • Chun, W.1    Johnson, G.V.2
  • 9
    • 84880186196 scopus 로고    scopus 로고
    • Segregation of a missense mutation in the amyloid beta-protein precursor gene familial Alzheimer's disease
    • Goate, A. (2006) Segregation of a missense mutation in the amyloid beta-protein precursor gene familial Alzheimer's disease. J. Alzheimer Dis. 9, 341-347.
    • (2006) J. Alzheimer Dis , vol.9 , pp. 341-347
    • Goate, A.1
  • 10
    • 4143091289 scopus 로고    scopus 로고
    • Apolipoprotein E: Diversity of cellular origins, structural and biophysical properties, and effects in Alzheimer's disease
    • Huang, Y., Weisgraber, K. H., Mucke, L. and Mahley, R. W. (2004) Apolipoprotein E: diversity of cellular origins, structural and biophysical properties, and effects in Alzheimer's disease. J. Mol. Neurosci. 23, 189-204.
    • (2004) J. Mol. Neurosci , vol.23 , pp. 189-204
    • Huang, Y.1    Weisgraber, K.H.2    Mucke, L.3    Mahley, R.W.4
  • 11
    • 33947201115 scopus 로고    scopus 로고
    • Loss-of-function presenilin mutations in Alzheimer's disease. Talking point on the role of presenilin mutations in Alzheimer disease
    • 8, 141-146
    • De Strooper, B. (2007) Loss-of-function presenilin mutations in Alzheimer's disease. Talking point on the role of presenilin mutations in Alzheimer disease. EMBO Rep. 8, 141-146.
    • (2007) EMBO Rep
    • De Strooper, B.1
  • 12
    • 33947644871 scopus 로고    scopus 로고
    • Protein oxidation and lipid peroxidation in brain of subjects with Alzheimer's disease: Insights into mechanism of neurodegeneration from redox proteomics
    • Sultana, R., Perluigi, M. and Butterfield, D. A. (2006) Protein oxidation and lipid peroxidation in brain of subjects with Alzheimer's disease: insights into mechanism of neurodegeneration from redox proteomics. Antiox. Redox Signal. 8, 2021-2037.
    • (2006) Antiox. Redox Signal , vol.8 , pp. 2021-2037
    • Sultana, R.1    Perluigi, M.2    Butterfield, D.A.3
  • 13
    • 0036592758 scopus 로고    scopus 로고
    • The role of the metabolic lesion in Alzheimer's disease
    • Blass, J. P., Gibson, G. E. and Hoyer, S. (2002) The role of the metabolic lesion in Alzheimer's disease. J. Alzheimer Dis. 4, 225-232.
    • (2002) J. Alzheimer Dis , vol.4 , pp. 225-232
    • Blass, J.P.1    Gibson, G.E.2    Hoyer, S.3
  • 14
    • 22144492630 scopus 로고    scopus 로고
    • Kawahara, M. (2004) Disruption of calcium homeostasis in the pathogenesis of Alzheimer's disease and other conformational diseases. Curr. Alzheimer Res. 1, 87-95.
    • Kawahara, M. (2004) Disruption of calcium homeostasis in the pathogenesis of Alzheimer's disease and other conformational diseases. Curr. Alzheimer Res. 1, 87-95.
  • 16
    • 0034529080 scopus 로고    scopus 로고
    • A furin-like convertase mediates propeptide cleavage of BACE the Alzheimer's beta secretase
    • Bennett, B. D., Denis, P., Haniu, M., Teplow, D. B., Kahn, S., Louis, J. C. Citron, M. and Vassar, R. (2000) A furin-like convertase mediates propeptide cleavage of BACE the Alzheimer's beta secretase. J. Biol. Chem. 275, 37712-37717.
    • (2000) J. Biol. Chem , vol.275 , pp. 37712-37717
    • Bennett, B.D.1    Denis, P.2    Haniu, M.3    Teplow, D.B.4    Kahn, S.5    Louis, J.C.6    Citron, M.7    Vassar, R.8
  • 20
    • 0035815635 scopus 로고    scopus 로고
    • Post-translational processing of beta-secretase (beta-amyloid-converting enzyme) and its ectodomain shedding. The pro- and transmembrane/cytosolic domains affect its cellular activity and amyloid-beta production
    • Benjannet, S., Elagoz, A., Wuickham, L., Mamarbachi, M., Munzer, J. S., Basak, A., Lazure, C., Cromlish, J. A., Sisodia, S., Checler, C. et al. (2001) Post-translational processing of beta-secretase (beta-amyloid-converting enzyme) and its ectodomain shedding. The pro- and transmembrane/cytosolic domains affect its cellular activity and amyloid-beta production. J. Biol. Chem. 276, 10879-10887.
    • (2001) J. Biol. Chem , vol.276 , pp. 10879-10887
    • Benjannet, S.1    Elagoz, A.2    Wuickham, L.3    Mamarbachi, M.4    Munzer, J.S.5    Basak, A.6    Lazure, C.7    Cromlish, J.A.8    Sisodia, S.9    Checler, C.10
  • 21
    • 0034721842 scopus 로고    scopus 로고
    • Maturation and endosomal targeting of beta-site amyloid precursor protein-cleaving enzyme. The Alzheimer's disease beta-secretase
    • Huse, J. T., Pijak, D. S., Leslie, G. J., Lee, V. M. and Doms, R. W. (2000) Maturation and endosomal targeting of beta-site amyloid precursor protein-cleaving enzyme. The Alzheimer's disease beta-secretase. J. Biol. Chem. 275, 33729-33737.
    • (2000) J. Biol. Chem , vol.275 , pp. 33729-33737
    • Huse, J.T.1    Pijak, D.S.2    Leslie, G.J.3    Lee, V.M.4    Doms, R.W.5
  • 22
    • 0036200884 scopus 로고    scopus 로고
    • The carboxyl-terminus of BACE contains a sorting signal that regulates BACE trafficking but not the formation of total A(beta)
    • Pastorino, L., Ikin, A. F., Nairn, A. C., Pursnani, A. and Buxbaum, J. D. (2002) The carboxyl-terminus of BACE contains a sorting signal that regulates BACE trafficking but not the formation of total A(beta). Mol. Cell. Neurosci. 19, 175-185.
    • (2002) Mol. Cell. Neurosci , vol.19 , pp. 175-185
    • Pastorino, L.1    Ikin, A.F.2    Nairn, A.C.3    Pursnani, A.4    Buxbaum, J.D.5
  • 23
    • 15744380393 scopus 로고    scopus 로고
    • GGA proteins mediate the recycling of memapsin 2 (BACE)
    • He, X., Li, F., Chang, W. P. and Tang, J. (2005) GGA proteins mediate the recycling of memapsin 2 (BACE). J. Biol. Chem. 280, 11696-11703.
    • (2005) J. Biol. Chem , vol.280 , pp. 11696-11703
    • He, X.1    Li, F.2    Chang, W.P.3    Tang, J.4
  • 24
    • 0642371716 scopus 로고    scopus 로고
    • Beta-secretase processing of the Alzheimer's amyloid protein precursor (APP)
    • Marlow, L., Cain, M., Pappolla, M. A. and Sambamurti, K. (2003) Beta-secretase processing of the Alzheimer's amyloid protein precursor (APP). J. Mol. Neurosci. 20, 233-239.
    • (2003) J. Mol. Neurosci , vol.20 , pp. 233-239
    • Marlow, L.1    Cain, M.2    Pappolla, M.A.3    Sambamurti, K.4
  • 26
    • 0035159756 scopus 로고    scopus 로고
    • The beta-secretase, BACE: A prime target for Alzheimer's disease
    • Vassar, R. (2001) The beta-secretase, BACE: a prime target for Alzheimer's disease. J. Mol. Neurosci. 17, 157-170.
    • (2001) J. Mol. Neurosci , vol.17 , pp. 157-170
    • Vassar, R.1
  • 27
    • 17344388652 scopus 로고    scopus 로고
    • BACE knockout mice are healthy despite lacking the primary beta-secretase activity in brain: Implications for Alzheimer's disease therapeutics
    • Roberds, S. L., Anderson, J., Basi, G., Bienkowski, M. J., Branstetter, D. G., Chen, K. S., Freedman, S. B., Frigon, N. L., Games, D., Hu, K. et al. (2001) BACE knockout mice are healthy despite lacking the primary beta-secretase activity in brain: implications for Alzheimer's disease therapeutics. Hum. Mol. Genet. 10, 1317-1324.
    • (2001) Hum. Mol. Genet , vol.10 , pp. 1317-1324
    • Roberds, S.L.1    Anderson, J.2    Basi, G.3    Bienkowski, M.J.4    Branstetter, D.G.5    Chen, K.S.6    Freedman, S.B.7    Frigon, N.L.8    Games, D.9    Hu, K.10
  • 30
    • 20944440679 scopus 로고    scopus 로고
    • The structure and functions of the presenilins
    • Dewji, N. N. (2005) The structure and functions of the presenilins. Cell. Mol. Life Sci. 62, 1109-1119.
    • (2005) Cell. Mol. Life Sci , vol.62 , pp. 1109-1119
    • Dewji, N.N.1
  • 31
    • 33947609757 scopus 로고    scopus 로고
    • The role of presenilin and its interacting proteins in the biogenesis of Alzheimer's beta amyloid
    • Verdile, G., Gandy, S. E. and Martins, R. N. (2007) The role of presenilin and its interacting proteins in the biogenesis of Alzheimer's beta amyloid. Neurochem. Res. 32, 609-623.
    • (2007) Neurochem. Res , vol.32 , pp. 609-623
    • Verdile, G.1    Gandy, S.E.2    Martins, R.N.3
  • 33
    • 13044278313 scopus 로고    scopus 로고
    • Presenilin 2 deficiency causes a mild pulmonary phenotype and no changes in amyloid precursor protein processing but enhances the embryonic lethal phenotype of presenilin 1 deficiency
    • Herreman, A., Hartmann, D., Annaert, W., Saftig, P., Craessaerts, K., Serneels, L., Umans, L., Schrijvers, V., Checler, F., Vanderstichele, H. et al. (1999) Presenilin 2 deficiency causes a mild pulmonary phenotype and no changes in amyloid precursor protein processing but enhances the embryonic lethal phenotype of presenilin 1 deficiency. Proc. Natl. Acad. Sci. USA 96, 11872-11877.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 11872-11877
    • Herreman, A.1    Hartmann, D.2    Annaert, W.3    Saftig, P.4    Craessaerts, K.5    Serneels, L.6    Umans, L.7    Schrijvers, V.8    Checler, F.9    Vanderstichele, H.10
  • 35
    • 0037173115 scopus 로고    scopus 로고
    • Presenilin and nicastrin regulate each other and determine amyloid beta-peptide production via complex formation
    • Edbauer, D., Winkler, E., Haass, C. and Steiner, H. (2002) Presenilin and nicastrin regulate each other and determine amyloid beta-peptide production via complex formation. Proc. Natl. Acad. Sci. USA 99, 8666-8671.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 8666-8671
    • Edbauer, D.1    Winkler, E.2    Haass, C.3    Steiner, H.4
  • 36
    • 18444417998 scopus 로고    scopus 로고
    • Aph-1 and pen-2 are required for Notch pathway signaling, gamma-secretase cleavage of betaAPP, and presenilin protein accumulation
    • Francis, R., McGrath, G., Zhang, J., Ruddy, D. A., Sym, M., Apfeld, J., Nicoll, M., Maxwell, M., Hai, B., Ellis, M. C. et al. (2002) Aph-1 and pen-2 are required for Notch pathway signaling, gamma-secretase cleavage of betaAPP, and presenilin protein accumulation. Dev. Cell 3, 85-97.
    • (2002) Dev. Cell , vol.3 , pp. 85-97
    • Francis, R.1    McGrath, G.2    Zhang, J.3    Ruddy, D.A.4    Sym, M.5    Apfeld, J.6    Nicoll, M.7    Maxwell, M.8    Hai, B.9    Ellis, M.C.10
  • 37
    • 0034080403 scopus 로고    scopus 로고
    • Aph-2 encodes a novel extracellular protein required for GLP-1-mediated signaling
    • Goutte, C., Hepler, W., Mickey, K. M. and Priess, J. R. (2000) Aph-2 encodes a novel extracellular protein required for GLP-1-mediated signaling. Development 127, 2481-2492.
    • (2000) Development , vol.127 , pp. 2481-2492
    • Goutte, C.1    Hepler, W.2    Mickey, K.M.3    Priess, J.R.4
  • 38
    • 0038360879 scopus 로고    scopus 로고
    • Different cofactor activities in gamma-secretase assembly: Evidence for a nicastrin-Aph-1 subcomplex
    • Hu, Y. and Fortini, M. E. (2003) Different cofactor activities in gamma-secretase assembly: evidence for a nicastrin-Aph-1 subcomplex. J. Cell Biol. 161, 685-690.
    • (2003) J. Cell Biol , vol.161 , pp. 685-690
    • Hu, Y.1    Fortini, M.E.2
  • 40
    • 0036260892 scopus 로고    scopus 로고
    • Increased expression of the amyloid precursor beta-secretase in Alzheimer's Disease
    • Holsinger, R. M., McLean, C. A, Beyreuther, K., Masters, C. L. and Evin, G. (2002) Increased expression of the amyloid precursor beta-secretase in Alzheimer's Disease. Ann. Neurol. 51, 783-786.
    • (2002) Ann. Neurol , vol.51 , pp. 783-786
    • Holsinger, R.M.1    McLean, C.A.2    Beyreuther, K.3    Masters, C.L.4    Evin, G.5
  • 41
    • 0036718272 scopus 로고    scopus 로고
    • Beta-secretase protein and activity are increased in the neocortex in Alzheimer disease
    • Fukumoto, H., Cheung, B. S., Hyman, B. T. and Irizarry, M. C. (2002) Beta-secretase protein and activity are increased in the neocortex in Alzheimer disease. Arch. Neurol. 59, 1381-1389.
    • (2002) Arch. Neurol , vol.59 , pp. 1381-1389
    • Fukumoto, H.1    Cheung, B.S.2    Hyman, B.T.3    Irizarry, M.C.4
  • 43
    • 0028180518 scopus 로고
    • Amodel for beta-amyloid aggregation and neurotoxicity based on free radical generation by the peptide: Relevance to Alzheimer disease
    • Hensley, K., Carney, J. M., Mattson, M. P., Aksenova, M., Harris, M., Wu, J. F., Floyd, R. A. and Butterfield, D. A. (1994) Amodel for beta-amyloid aggregation and neurotoxicity based on free radical generation by the peptide: relevance to Alzheimer disease. Proc. Natl. Acad. Sci. USA 91, 3270-3274.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 3270-3274
    • Hensley, K.1    Carney, J.M.2    Mattson, M.P.3    Aksenova, M.4    Harris, M.5    Wu, J.F.6    Floyd, R.A.7    Butterfield, D.A.8
  • 44
    • 0036751954 scopus 로고    scopus 로고
    • Oxidative stress in brain aging. Implications for therapeutics of neurodegenerative diseases
    • Floyd, R. A. and Hensley, K. (2002) Oxidative stress in brain aging. Implications for therapeutics of neurodegenerative diseases. Neurobiol. Aging 23, 795-807.
    • (2002) Neurobiol. Aging , vol.23 , pp. 795-807
    • Floyd, R.A.1    Hensley, K.2
  • 45
    • 0031020476 scopus 로고    scopus 로고
    • A role for 4-hydroxynonenal, an aldehydic product of lipid peroxidation, in disruption of ion homeostasis and neuronal death induced by amyloid betapeptide
    • Mark, R. J., Lovell, M. A., Markesbery, W. R., Uchida, K. and Mattson, M. P. (1997) A role for 4-hydroxynonenal, an aldehydic product of lipid peroxidation, in disruption of ion homeostasis and neuronal death induced by amyloid betapeptide. J. Neurochem. 68, 255-264.
    • (1997) J. Neurochem , vol.68 , pp. 255-264
    • Mark, R.J.1    Lovell, M.A.2    Markesbery, W.R.3    Uchida, K.4    Mattson, M.P.5
  • 46
    • 27744542593 scopus 로고    scopus 로고
    • Hydrogen peroxide is generated during the very early stages of aggregation of the amyloid peptides implicated in Alzheimer's disease and familial British dementia
    • Tabner, B. J., El-Agnaf, O. M., Turnbull, S., German, M. J., Paleologou, K. E., Hayashi, Y., Cooper, L. J., Fullwood, N. J. and Allsop D (2005) Hydrogen peroxide is generated during the very early stages of aggregation of the amyloid peptides implicated in Alzheimer's disease and familial British dementia. J. Biol. Chem. 280, 35789-35792.
    • (2005) J. Biol. Chem , vol.280 , pp. 35789-35792
    • Tabner, B.J.1    El-Agnaf, O.M.2    Turnbull, S.3    German, M.J.4    Paleologou, K.E.5    Hayashi, Y.6    Cooper, L.J.7    Fullwood, N.J.8    Allsop, D.9
  • 47
    • 27544511750 scopus 로고    scopus 로고
    • Formation and stabilization model of the 42-mer Abeta radical: Implications for the long-lasting oxidative stress in Alzheimer's disease
    • Murakami, K., Irie, K., Ohigashi, H., Hara, H., Nagao, M., Shimizu, T. and Shirasawa T(2005) Formation and stabilization model of the 42-mer Abeta radical: implications for the long-lasting oxidative stress in Alzheimer's disease. J. Am. Chem. Soc. 127, 15168-15174.
    • (2005) J. Am. Chem. Soc , vol.127 , pp. 15168-15174
    • Murakami, K.1    Irie, K.2    Ohigashi, H.3    Hara, H.4    Nagao, M.5    Shimizu, T.6    Shirasawa, T.7
  • 53
    • 0030917601 scopus 로고    scopus 로고
    • Alzheimer's presenilin mutation sensitizes neural cells to apoptosis induced by trophic factor withdrawal and amyloid beta-peptide: Involvement of calcium and oxyradicals
    • Guo, Q., Sopher, B. L., Furukawa, K., Pham, D. G., Robinson, N., Martin, G. M. and Mattson, M. P. (1997) Alzheimer's presenilin mutation sensitizes neural cells to apoptosis induced by trophic factor withdrawal and amyloid beta-peptide: involvement of calcium and oxyradicals. J. Neurosci. 17, 4212-4222.
    • (1997) J. Neurosci , vol.17 , pp. 4212-4222
    • Guo, Q.1    Sopher, B.L.2    Furukawa, K.3    Pham, D.G.4    Robinson, N.5    Martin, G.M.6    Mattson, M.P.7
  • 55
    • 18444391830 scopus 로고    scopus 로고
    • Presenilin-1 mutations of leucine 166 equally affect the generation of the Notch and APP intracellular domains independent of their effect on Abeta 42 production
    • Moehlmann, T., Winkler, E., Xia, X., Edbauer, D., Murrell, J., Capell, A., Kaether, C., Zheng, H., Ghetti, B., Haass, C. et al. (2002) Presenilin-1 mutations of leucine 166 equally affect the generation of the Notch and APP intracellular domains independent of their effect on Abeta 42 production. Proc. Natl. Acad. Sci. USA 99, 8025-8030.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 8025-8030
    • Moehlmann, T.1    Winkler, E.2    Xia, X.3    Edbauer, D.4    Murrell, J.5    Capell, A.6    Kaether, C.7    Zheng, H.8    Ghetti, B.9    Haass, C.10
  • 56
    • 33749521100 scopus 로고    scopus 로고
    • Intraneuronal beta-amyloid aggregates, neurodegeneration, and neuron loss in transgenic mice with five familial Alzheimer's disease mutations: Potential factors in amyloid plaque formation
    • Oakley, H., Cole, S. L., Logan, S., Maus, E., Shao, P., Craft, J., Guillozet-Bongaarts, A., Ohno, M., Disterhoft, J., Van Eldik, L. et al. (2006) Intraneuronal beta-amyloid aggregates, neurodegeneration, and neuron loss in transgenic mice with five familial Alzheimer's disease mutations: potential factors in amyloid plaque formation. J. Neurosci. 26, 10129-10140.
    • (2006) J. Neurosci , vol.26 , pp. 10129-10140
    • Oakley, H.1    Cole, S.L.2    Logan, S.3    Maus, E.4    Shao, P.5    Craft, J.6    Guillozet-Bongaarts, A.7    Ohno, M.8    Disterhoft, J.9    Van Eldik, L.10
  • 58
    • 0029803744 scopus 로고    scopus 로고
    • Evidence that the 42- and 40-amino acid forms of amyloid beta protein are generated from the beta-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 beta protein are generated from the beta-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
  • 60
    • 0032972922 scopus 로고    scopus 로고
    • Altered calcium homeostasis and mitochondrial dysfunction in cortical synaptic compartments of presenilin-1 mutant mice
    • Begley, J. G., Duan, W., Chan, S., Duff, K. and Mattson, M. P. (1999) Altered calcium homeostasis and mitochondrial dysfunction in cortical synaptic compartments of presenilin-1 mutant mice. J. Neurochem. 72, 1030-1039.
    • (1999) J. Neurochem , vol.72 , pp. 1030-1039
    • Begley, J.G.1    Duan, W.2    Chan, S.3    Duff, K.4    Mattson, M.P.5
  • 61
    • 4444304720 scopus 로고    scopus 로고
    • APP and PS-1 mutations induce brain oxidative stress independent of dietary cholesterol: Implications for Alzheimer's disease
    • Mohmmad Abdul, H., Wenk, G. L., Gramling, M., Hauss-Wegrzyniak, B. and Butterfield, D. A. (2004) APP and PS-1 mutations induce brain oxidative stress independent of dietary cholesterol: implications for Alzheimer's disease. Neurosci. Lett. 368, 148-150
    • (2004) Neurosci. Lett , vol.368 , pp. 148-150
    • Mohmmad Abdul, H.1    Wenk, G.L.2    Gramling, M.3    Hauss-Wegrzyniak, B.4    Butterfield, D.A.5
  • 63
  • 64
    • 8244260610 scopus 로고    scopus 로고
    • Kwok, J. B., Taddei, K., Hallupp, M., Fisher, C., Brooks, W. S., Broe, G. A., Hardy, J., Fulham, M. J., Nicholson, G. A., Stell, R. et al. (1997) Two novel (M233T and R278T) presenilin-1 mutations in early-onset Alzheimer's disease pedigrees and preliminary evidence for association of presenilin-1 mutations with a novel phenotype. Neuroreport 8, 1537-1542.
    • Kwok, J. B., Taddei, K., Hallupp, M., Fisher, C., Brooks, W. S., Broe, G. A., Hardy, J., Fulham, M. J., Nicholson, G. A., Stell, R. et al. (1997) Two novel (M233T and R278T) presenilin-1 mutations in early-onset Alzheimer's disease pedigrees and preliminary evidence for association of presenilin-1 mutations with a novel phenotype. Neuroreport 8, 1537-1542.
  • 65
    • 0034813045 scopus 로고    scopus 로고
    • Sodeyama, N., Iwata, T., Ishikawa, K., Mizusawa, H., Yamada, M., Itoh, Y., Otomo, E., Matsushita, M. and Komatsuzaki, Y. (2001) Very early onset Alzheimer's disease with spastic paraparesis associated with a novel presenilin 1 mutation (Phe237Ile). J. Neurol. Neurosurg. Psychiatry 71, 556-557.
    • Sodeyama, N., Iwata, T., Ishikawa, K., Mizusawa, H., Yamada, M., Itoh, Y., Otomo, E., Matsushita, M. and Komatsuzaki, Y. (2001) Very early onset Alzheimer's disease with spastic paraparesis associated with a novel presenilin 1 mutation (Phe237Ile). J. Neurol. Neurosurg. Psychiatry 71, 556-557.
  • 66
    • 0033762710 scopus 로고    scopus 로고
    • Variant Alzheimer's disease with spastic paraparesis and cotton wool plaques is caused by PS-1 mutations that lead to exceptionally high amyloid-beta concentrations
    • Houlden, H., Baker, M., McGowan, E., Lewis, P., Hutton, M., Crook, R., Wood, N. W., Kumar-Singh, S., Geddes, J., Swash, M. et al. (2000) Variant Alzheimer's disease with spastic paraparesis and cotton wool plaques is caused by PS-1 mutations that lead to exceptionally high amyloid-beta concentrations. Ann. Neurol. 48, 806-808.
    • (2000) Ann. Neurol , vol.48 , pp. 806-808
    • Houlden, H.1    Baker, M.2    McGowan, E.3    Lewis, P.4    Hutton, M.5    Crook, R.6    Wood, N.W.7    Kumar-Singh, S.8    Geddes, J.9    Swash, M.10
  • 69
    • 0038751845 scopus 로고    scopus 로고
    • Secretion and intracellular generated of truncated Abeta in beta-site amyloid-beta precursors protein-cleaving enzyme expressing human neurons
    • Lee, E. B., Skovronsky, D. M., Abtahian, F., Doms, R. W. and Lee, V. M. (2003) Secretion and intracellular generated of truncated Abeta in beta-site amyloid-beta precursors protein-cleaving enzyme expressing human neurons. J. Biol. Chem. 278, 4458-4466.
    • (2003) J. Biol. Chem , vol.278 , pp. 4458-4466
    • Lee, E.B.1    Skovronsky, D.M.2    Abtahian, F.3    Doms, R.W.4    Lee, V.M.5
  • 70
    • 0035818998 scopus 로고    scopus 로고
    • Kinesin-mediated axonal transport of a membrane compartment containing beta-secretase and presenilin-1 requires APP
    • Kamal, A., Almenar-Queralt, A., LeBlanc, J. F., Roberts, E. A. and Goldstein, L. S. (2001) Kinesin-mediated axonal transport of a membrane compartment containing beta-secretase and presenilin-1 requires APP. Nature 414, 643-648.
    • (2001) Nature , vol.414 , pp. 643-648
    • Kamal, A.1    Almenar-Queralt, A.2    LeBlanc, J.F.3    Roberts, E.A.4    Goldstein, L.S.5
  • 74
    • 33745228920 scopus 로고    scopus 로고
    • The various aggregation states of beta-amyloid 1-42 mediate different effects on oxidative stress, neurodegeneration, and BACE-1 expression
    • Tamagno, E., Bardini, P., Guglielmotto, M., Danni, O. and Tabaton, M. (2006) The various aggregation states of beta-amyloid 1-42 mediate different effects on oxidative stress, neurodegeneration, and BACE-1 expression. Free Radic. Biol. Med. 41, 202-212.
    • (2006) Free Radic. Biol. Med , vol.41 , pp. 202-212
    • Tamagno, E.1    Bardini, P.2    Guglielmotto, M.3    Danni, O.4    Tabaton, M.5
  • 75
    • 0034763569 scopus 로고    scopus 로고
    • Differential effects of unaggregated and aggregated amyloid beta protein (1-40) on K(+) channel currents in primary cultures of rat cerebellar granule and cortical neurones
    • Ramsden, M., Plant, L. D., Webster, N. J., Vaughan, P. F., Henderson, Z. and Pearson, H. A. (2001) Differential effects of unaggregated and aggregated amyloid beta protein (1-40) on K(+) channel currents in primary cultures of rat cerebellar granule and cortical neurones. J. Neurochem. 79, 699-712.
    • (2001) J. Neurochem , vol.79 , pp. 699-712
    • Ramsden, M.1    Plant, L.D.2    Webster, N.J.3    Vaughan, P.F.4    Henderson, Z.5    Pearson, H.A.6
  • 76
    • 0038045587 scopus 로고    scopus 로고
    • The production of amyloid beta peptide is a critical requirement for the viability of central neurons
    • Plant, L. D., Boyle, J. P., Smith, I. F., Peers, C. and Pearson, H. A. (2003) The production of amyloid beta peptide is a critical requirement for the viability of central neurons. J. Neurosci. 23, 5531-5535.
    • (2003) J. Neurosci , vol.23 , pp. 5531-5535
    • Plant, L.D.1    Boyle, J.P.2    Smith, I.F.3    Peers, C.4    Pearson, H.A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.