메뉴 건너뛰기




Volumn 13, Issue 2, 2004, Pages 159-170

Mutant presenilins specifically elevate the levels of the 42 residue β-amyloid peptide in vivo: Evidence for augmentation of a 42-specific γ secretase

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN[1-40]; AMYLOID BETA PROTEIN[1-42]; AMYLOID PRECURSOR PROTEIN; BETA SECRETASE; BETA SECRETASE 1; GAMMA SECRETASE; PRESENILIN 1; PRESENILIN 2; UNCLASSIFIED DRUG;

EID: 1642555780     PISSN: 09646906     EISSN: None     Source Type: Journal    
DOI: 10.1093/hmg/ddh019     Document Type: Review
Times cited : (1249)

References (80)
  • 2
    • 0021207461 scopus 로고
    • Alzheimer's disease and Down's syndrome: Sharing of a unique cerebrovascular amyloid fibril protein
    • Glenner, G.G. and Wong, C.W. (1984) Alzheimer's disease and Down's syndrome: sharing of a unique cerebrovascular amyloid fibril protein. Biochem. Biophys. Res. Commun., 122, 1131-1135.
    • (1984) Biochem. Biophys. Res. Commun. , vol.122 , pp. 1131-1135
    • Glenner, G.G.1    Wong, C.W.2
  • 4
    • 0022550027 scopus 로고
    • Purification, ultrastructure, and chemical analysis of Alzheimer disease amyloid plaque core protein
    • Roher, A., Wolfe, D., Palutke, M. and KuKurga, D. (1986) Purification, ultrastructure, and chemical analysis of Alzheimer disease amyloid plaque core protein. Proc. Natl Acad. Sci. USA, 83, 2662-2666.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 2662-2666
    • Roher, A.1    Wolfe, D.2    Palutke, M.3    KuKurga, D.4
  • 7
    • 0027332081 scopus 로고
    • beta-Amyloid-(1-42) is a major component of cerebrovascular amyloid deposits: Implications for the pathology of Alzheimer disease
    • Roher, A.E., Lowenson, J.D., Clarke, S., Woods, A.S., Cotter, R.J., Gowing, E. and Ball, M.J. (1993) beta-Amyloid-(1-42) is a major component of cerebrovascular amyloid deposits: implications for the pathology of Alzheimer disease. Proc. Natl Acad. Sci. USA, 90, 10836-10840.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 10836-10840
    • Roher, A.E.1    Lowenson, J.D.2    Clarke, S.3    Woods, A.S.4    Cotter, R.J.5    Gowing, E.6    Ball, M.J.7
  • 9
    • 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
  • 10
    • 0028246308 scopus 로고
    • Mutations associated with a locus for familial Alzheimer's disease result in alternative processing of amyloid β-protein precursor
    • Haass, C., Hung, A.Y., Selkoe, D.J. and Teplow, D.B. (1994) Mutations associated with a locus for familial Alzheimer's disease result in alternative processing of amyloid β-protein precursor. J. Biol. Chem., 269, 17741-17748.
    • (1994) J. Biol. Chem. , vol.269 , pp. 17741-17748
    • Haass, C.1    Hung, A.Y.2    Selkoe, D.J.3    Teplow, D.B.4
  • 13
    • 0027195933 scopus 로고
    • Seeding 'one-dimensional crystallization' of amyloid: A pathogenic mechanism in Alzheimer's disease and scrapie?
    • Jarrett, J.T., Lansbury, P.T., Jr. (1993) Seeding 'one-dimensional crystallization' of amyloid: a pathogenic mechanism in Alzheimer's disease and scrapie? Cell, 73, 1055-1058.
    • (1993) Cell , vol.73 , pp. 1055-1058
    • Jarrett, J.T.1    Lansbury Jr., P.T.2
  • 14
    • 0028169925 scopus 로고
    • Visualization of Aβ42(43)-positive and Aβ40-positive senile plaques with end-specific Aβ-monoclonal antibodies: Evidence that an initially deposited Aβ species is Aβ1-42(43)
    • Iwatsubo, T., Odaka, A., Suzuki, N., Mizusawa, H., Nukina, N. and Ihara, Y. (1994) Visualization of Aβ42(43)-positive and Aβ40-positive senile plaques with end-specific Aβ-monoclonal antibodies: evidence that an initially deposited Aβ species is Aβ1-42(43). Neuron, 13, 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
  • 15
    • 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, E.I., Sherrington, R., Rogaeva, E.A., Levesque, G., Ikeda, M., Liang, Y., Chi, H., Lin, C., Holman, K., Tsuda, T. et al. (1995) 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, 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    Holman, K.9    Tsuda, T.10
  • 18
  • 20
    • 0035204206 scopus 로고    scopus 로고
    • Nicastrin is required for Presenilin-mediated transmembrane cleavage in Drosophila
    • Chung, H.M. and Struhl, G. (2001) Nicastrin is required for Presenilin-mediated transmembrane cleavage in Drosophila. Nat. Cell Biol., 3, 1129-1132.
    • (2001) Nat. Cell Biol. , vol.3 , pp. 1129-1132
    • Chung, H.M.1    Struhl, G.2
  • 21
    • 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
  • 22
    • 0036007117 scopus 로고    scopus 로고
    • Nicastrin is required for γ-secretase cleavage of the Drosophila notch receptor
    • Hu, Y., Ye, Y. and Fortini, M.E. (2002) Nicastrin is required for γ-secretase cleavage of the Drosophila notch receptor. Dev. Cell, 2, 69-78.
    • (2002) Dev. Cell , vol.2 , pp. 69-78
    • Hu, Y.1    Ye, Y.2    Fortini, M.E.3
  • 23
    • 0037160063 scopus 로고    scopus 로고
    • Mammalian APH-1 interacts with presenilin and nicastrin, and is required for intramembrane proteolysis of APP and Notch
    • Lee, S.F., Shah, S., Li, H., Yu, C., Han, W. and Yu, G. (2002) Mammalian APH-1 interacts with presenilin and nicastrin, and is required for intramembrane proteolysis of APP and Notch. J. Biol. Chem., 277, 45013-45019.
    • (2002) J. Biol. Chem. , vol.277 , pp. 45013-45019
    • Lee, S.F.1    Shah, S.2    Li, H.3    Yu, C.4    Han, W.5    Yu, G.6
  • 24
    • 0036007118 scopus 로고    scopus 로고
    • Drosophila nicastrin is essential for the intramembranous cleavage of notch
    • Lopez-Schier, H. and St Johnston, D. (2002) Drosophila nicastrin is essential for the intramembranous cleavage of notch. Dev. Cell, 2, 79-89.
    • (2002) Dev. Cell , vol.2 , pp. 79-89
    • Lopez-Schier, H.1    St Johnston, D.2
  • 25
    • 0037131218 scopus 로고    scopus 로고
    • PEN-2 is an integral component of the gamma-secretase complex required for coordinated expression of presenilin and nicastrin
    • Steiner, H., Winkler, E., Edbauer, D., Prokop, S., Basset, G., Yamasaki, A., Kostka, M. and Haass, C. (2002) PEN-2 is an integral component of the gamma-secretase complex required for coordinated expression of presenilin and nicastrin. J. Biol. Chem., 277, 39062-39065.
    • (2002) J. Biol. Chem. , vol.277 , pp. 39062-39065
    • Steiner, H.1    Winkler, E.2    Edbauer, D.3    Prokop, S.4    Basset, G.5    Yamasaki, A.6    Kostka, M.7    Haass, C.8
  • 31
    • 0033535553 scopus 로고    scopus 로고
    • Two transmembrane aspartates in presenilin-1 required for presenilin endoproteolysis and gamma-secretase activity
    • Wolfe, M.S., Xia, W., Ostazewski, B.L., Diehl, T.S., Kimberly, W.T. and Selkoe, D.J. (1999) Two transmembrane aspartates in presenilin-1 required for presenilin endoproteolysis and gamma-secretase activity. Nature, 398, 513-517.
    • (1999) Nature , vol.398 , pp. 513-517
    • Wolfe, M.S.1    Xia, W.2    Ostazewski, B.L.3    Diehl, T.S.4    Kimberly, W.T.5    Selkoe, D.J.6
  • 32
    • 0033783140 scopus 로고    scopus 로고
    • Presenilin-1 differentially facilitates endoproteolysis of the β-amyloid precursor protein and Notch
    • Capell, A., Steiner, H., Romig, H., Keck, S., Baader, M., Grim, M.G., Baumeister, R. and Haass, C. (2000) Presenilin-1 differentially facilitates endoproteolysis of the β-amyloid precursor protein and Notch. Nat. Cell Biol., 2, 205-211.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 205-211
    • Capell, A.1    Steiner, H.2    Romig, H.3    Keck, S.4    Baader, M.5    Grim, M.G.6    Baumeister, R.7    Haass, C.8
  • 33
  • 34
    • 0033779635 scopus 로고    scopus 로고
    • Presenilins are required for gamma-secretase cleavage of beta-APP and transmembrane cleavage of Notch-1
    • Zhang, Z., Nadeau, P., Song, W., Donoviel, D., Yuan, M., Bernstein, A. and Yankner, B.A. (2000) Presenilins are required for gamma-secretase cleavage of beta-APP and transmembrane cleavage of Notch-1. Nat. Cell Biol., 2, 463-465.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 463-465
    • Zhang, Z.1    Nadeau, P.2    Song, W.3    Donoviel, D.4    Yuan, M.5    Bernstein, A.6    Yankner, B.A.7
  • 35
    • 0034774969 scopus 로고    scopus 로고
    • Presenilin-dependent γ-secretase processing of β-amyloid precursor protein at a site corresponding to the S3 cleavage of notch
    • Sastre, M., Steiner, H., Fuchs, K., Capell, A., Multhaup, G., Condron, M., Teplow, D. and Haass, C. (2001) Presenilin-dependent γ-secretase processing of β-amyloid precursor protein at a site corresponding to the S3 cleavage of notch. Sci. Rep., 2, 835-841.
    • (2001) Sci. Rep. , vol.2 , pp. 835-841
    • Sastre, M.1    Steiner, H.2    Fuchs, K.3    Capell, A.4    Multhaup, G.5    Condron, M.6    Teplow, D.7    Haass, C.8
  • 38
    • 16044373524 scopus 로고    scopus 로고
    • Secreted amyloid β-protein similar to that in the senile plaques of Alzheimer's disease is increased in vivo by the presenilin 1 and 2 and APP mutations linked to familial Alzheimer's disease
    • Scheuner, D., Eckman, C., Jensen, M., Song, X., Citron, M., Suzuki, N., Bird, T.D., Hardy, J., Hutton, M., Kukull, W. et al. (1996) Secreted amyloid β-protein similar to that in the senile plaques of Alzheimer's disease is increased in vivo by the presenilin 1 and 2 and APP mutations linked to familial Alzheimer's disease. Nat. Med., 2, 864-870.
    • (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
  • 40
    • 16944362157 scopus 로고    scopus 로고
    • Mutant presenilins of Alzheimer's disease increase production of 42-residue amyloid β-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. et al. (1997) Mutant presenilins of Alzheimer's disease increase production of 42-residue amyloid β-protein in both transfected cells and transgenic mice. Nat. Med., 3, 67-72.
    • (1997) 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
  • 42
    • 0033360402 scopus 로고    scopus 로고
    • Amyloid production and deposition in mutant amyloid precursor protein and presenilin-1 yeast artificial chromosome transgenic mice
    • Lamb, B.T., Bardel, K.A., Kulnane, L.S., Anderson, J.J., Holtz, G., Wagner, S.L., Sisodia, S.S. and Hoeger, E.J. (1999) Amyloid production and deposition in mutant amyloid precursor protein and presenilin-1 yeast artificial chromosome transgenic mice. Nat. Neurosci., 2, 695-697.
    • (1999) Nat. Neurosci. , vol.2 , pp. 695-697
    • Lamb, B.T.1    Bardel, K.A.2    Kulnane, L.S.3    Anderson, J.J.4    Holtz, G.5    Wagner, S.L.6    Sisodia, S.S.7    Hoeger, E.J.8
  • 43
    • 0033784099 scopus 로고    scopus 로고
    • Modeling Alzheimer's disease in transgenic mice: Effect of age and presenilin 1 on amyloid biochemistry and pathology in APP/London mice
    • Dewachter, I., van Dorple, J., Spittaels, K., Tesseur, I., Van den Haute, C., Moechars, D. and Van Leuven, F. (2000) Modeling Alzheimer's disease in transgenic mice: effect of age and presenilin 1 on amyloid biochemistry and pathology in APP/London mice. Exp. Gerontol., 35, 831-841.
    • (2000) Exp. Gerontol. , vol.35 , pp. 831-841
    • Dewachter, I.1    van Dorple, J.2    Spittaels, K.3    Tesseur, I.4    Van den Haute, C.5    Moechars, D.6    Van Leuven, F.7
  • 45
    • 0030851335 scopus 로고    scopus 로고
    • Alzheimer transgenic mouse models come of age
    • Duff, K. (1997) Alzheimer transgenic mouse models come of age. Trends Neurosci., 20, 279-280.
    • (1997) Trends Neurosci. , vol.20 , pp. 279-280
    • Duff, K.1
  • 48
    • 0031914718 scopus 로고    scopus 로고
    • Accelerated Alzheimer-type phenotype in transgenic mice carrying both mutant amyloid precursor protein and presenilin 1 transgenes
    • Holcomb, L., Gordon, M.N., McGowan, E., Yu, X., Benkovic, S., Jantzen, P., Wright, K., Saad, I., Mueller, R., Morgan, D. et al. (1998) Accelerated Alzheimer-type phenotype in transgenic mice carrying both mutant amyloid precursor protein and presenilin 1 transgenes. Nat. Med., 4, 97-100.
    • (1998) Nat. Med. , vol.4 , pp. 97-100
    • Holcomb, L.1    Gordon, M.N.2    McGowan, E.3    Yu, X.4    Benkovic, S.5    Jantzen, P.6    Wright, K.7    Saad, I.8    Mueller, R.9    Morgan, D.10
  • 49
    • 0034711207 scopus 로고    scopus 로고
    • Carboxyl-terminal fragments of alzheimer beta-amyloid precursor protein accumulate in restricted and unpredicted intracellular compartments in presenilin 1-deficient cells
    • Chen, F., Yang, D.S., Petanceska, S., Yang, A., Tandon, A., Yu, G., Rozmahel, R., Ghiso, J., Nishimura, M., Zhang, D.M. et al. (2000) Carboxyl-terminal fragments of alzheimer beta-amyloid precursor protein accumulate in restricted and unpredicted intracellular compartments in presenilin 1-deficient cells. J. Biol. Chem., 275, 36794-36802.
    • (2000) J. Biol. Chem. , vol.275 , pp. 36794-36802
    • Chen, F.1    Yang, D.S.2    Petanceska, S.3    Yang, A.4    Tandon, A.5    Yu, G.6    Rozmahel, R.7    Ghiso, J.8    Nishimura, M.9    Zhang, D.M.10
  • 51
    • 0034523058 scopus 로고    scopus 로고
    • FAD mutations in presenilin-1 or amyloid precursor protein decrease the efficacy of a gamma-secretase inhibitor: Evidence for direct involvement of PS1 in the gamma-secretase cleavage complex
    • Xia, W., Ostaszewski, B.L., Kimberly, W.T., Rahmati, T., Moore, C.L., Wolfe, M.S. and Selkoe, D.J. (2000) FAD mutations in presenilin-1 or amyloid precursor protein decrease the efficacy of a gamma-secretase inhibitor: evidence for direct involvement of PS1 in the gamma-secretase cleavage complex. Neurobiol. Dis., 7, 673-681.
    • (2000) Neurobiol. Dis. , vol.7 , pp. 673-681
    • Xia, W.1    Ostaszewski, B.L.2    Kimberly, W.T.3    Rahmati, T.4    Moore, C.L.5    Wolfe, M.S.6    Selkoe, D.J.7
  • 52
    • 0032564388 scopus 로고    scopus 로고
    • Presenilin 1 regulates the processing of beta-amyloid precursor protein C-terminal fragments and the generation of amyloid beta-protein in endoplasmic reticulum and Golgi
    • Xia, W., Zhang, J., Ostaszewski, B.L., Kimberly, W.T., Seubert, P., Koo, E.H., Shen, J. and Selkoe, D.J. (1998) Presenilin 1 regulates the processing of beta-amyloid precursor protein C-terminal fragments and the generation of amyloid beta-protein in endoplasmic reticulum and Golgi. Biochemistry, 37, 16465-16471.
    • (1998) Biochemistry , vol.37 , pp. 16465-16471
    • Xia, W.1    Zhang, J.2    Ostaszewski, B.L.3    Kimberly, W.T.4    Seubert, P.5    Koo, E.H.6    Shen, J.7    Selkoe, D.J.8
  • 58
    • 0035863055 scopus 로고    scopus 로고
    • Age-dependent changes in brain, CSF, and plasma amyloid (beta) protein in the Tg2576 transgenic mouse model of Alzheimer's disease
    • Kawarabayashi, T., Younkin, L.H., Saido, T.C., Shoji, M., Ashe, K.H. and Younkin, S.G. (2001) Age-dependent changes in brain, CSF, and plasma amyloid (beta) protein in the Tg2576 transgenic mouse model of Alzheimer's disease. J. Neurosci., 21, 372-381.
    • (2001) J. Neurosci. , vol.21 , pp. 372-381
    • Kawarabayashi, T.1    Younkin, L.H.2    Saido, T.C.3    Shoji, M.4    Ashe, K.H.5    Younkin, S.G.6
  • 61
    • 0344642405 scopus 로고    scopus 로고
    • A variant of Alzheimer's disease wtih spastic paraparaesis and unusual plaques due to deletion of exon 9 of presenilin 1
    • Crook, R., Chen, L.S., Bende, S.M. and LaFerla, F.M. (1998) A variant of Alzheimer's disease wtih spastic paraparaesis and unusual plaques due to deletion of exon 9 of presenilin 1. Nat. Med., 4, 1-4.
    • (1998) Nat. Med. , vol.4 , pp. 1-4
    • Crook, R.1    Chen, L.S.2    Bende, S.M.3    LaFerla, F.M.4
  • 62
    • 0034076439 scopus 로고    scopus 로고
    • Identification of a novel 4.6-kb genomic deletion in presenilin-1 gene which results in exclusion of exon 9 in a Finnish early onset Alzheimer's disease family: An Alu core sequence-stimulated recombination?
    • Hiltunen, M., Helisalmi, S., Mannermaa, A., Alafuzoff, I., Koivisto, A.M., Lehtovirta, M., Pirskanen, M., Sulkava, R., Verkkoniemi, A. and Soininen, H. (2000) Identification of a novel 4.6-kb genomic deletion in presenilin-1 gene which results in exclusion of exon 9 in a Finnish early onset Alzheimer's disease family: an Alu core sequence-stimulated recombination? Eur. J. Hum. Genet., 8, 259-266.
    • (2000) Eur. J. Hum. Genet. , vol.8 , pp. 259-266
    • Hiltunen, M.1    Helisalmi, S.2    Mannermaa, A.3    Alafuzoff, I.4    Koivisto, A.M.5    Lehtovirta, M.6    Pirskanen, M.7    Sulkava, R.8    Verkkoniemi, A.9    Soininen, H.10
  • 63
    • 0034917266 scopus 로고    scopus 로고
    • Cases of Alzheimer's disease due to deletion of exon 9 of the presenilin-1 gene show an unusual but characteristic beta-amyloid pathology known as 'cotton wool' plaques
    • Mann, D.M., Takeuchi, A., Sato, S., Cairns, N.J., Lantos, P.L., Rossor, M.N., Haltia, M., Kalimo, H. and Iwatsubo, T. (2001) Cases of Alzheimer's disease due to deletion of exon 9 of the presenilin-1 gene show an unusual but characteristic beta-amyloid pathology known as 'cotton wool' plaques. Neuropathol. Appl. Neurobiol., 27, 189-196.
    • (2001) Neuropathol. Appl. Neurobiol. , vol.27 , pp. 189-196
    • Mann, D.M.1    Takeuchi, A.2    Sato, S.3    Cairns, N.J.4    Lantos, P.L.5    Rossor, M.N.6    Haltia, M.7    Kalimo, H.8    Iwatsubo, T.9
  • 64
    • 0030857182 scopus 로고    scopus 로고
    • Increased Aβ 42(43)-plaque depostion in early-onset familial Alzheimer's disease brains with the deletion of exon 9 and the missense point mutation (H163R) in the PS-1 gene
    • Ishii, K., Ii, K., Hasegawa, T., Shoji, S., Doi, A. and Mori, H. (1997) Increased Aβ 42(43)-plaque depostion in early-onset familial Alzheimer's disease brains with the deletion of exon 9 and the missense point mutation (H163R) in the PS-1 gene. Neurosci. Lett., 228, 17-20.
    • (1997) Neurosci. Lett. , vol.228 , pp. 17-20
    • Ishii, K.1    Ii, K.2    Hasegawa, T.3    Shoji, S.4    Doi, A.5    Mori, H.6
  • 65
    • 0027258525 scopus 로고
    • The carboxy terminus of the β amyloid protein is critical for the seeding of amyloid formation: Implications for the pathogenesis of Alzheimer's disease
    • Jarrett, J.T., Berger, E.P. and Lansbury, P.T. Jr (1993) The carboxy terminus of the β amyloid protein is critical for the seeding of amyloid formation: implications for the pathogenesis of Alzheimer's disease. Biochemistry, 32, 4693-4697.
    • (1993) Biochemistry , vol.32 , pp. 4693-4697
    • Jarrett, J.T.1    Berger, E.P.2    Lansbury Jr., P.T.3
  • 66
    • 0027006436 scopus 로고
    • Amyloid fibril formation requires a chemically discriminating nucleation event: Studies of an amyloidogenic sequence from the bacterial protein OsmB
    • Jarrett, J.T. and Lansbury, P.T., Jr (1992) Amyloid fibril formation requires a chemically discriminating nucleation event: studies of an amyloidogenic sequence from the bacterial protein OsmB. Biochemistry, 31, 12345-12352.
    • (1992) Biochemistry , vol.31 , pp. 12345-12352
    • Jarrett, J.T.1    Lansbury Jr., P.T.2
  • 67
    • 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
  • 68
    • 0031915681 scopus 로고    scopus 로고
    • A substrate-based difluoro ketone selectively inhibits Alzheimer's -secretase activity
    • Wolfe, M.S., Citron, M., Diehl, T.S., Xia, W., Donkor, I.O. and Selkoe, D.J. (2000) A substrate-based difluoro ketone selectively inhibits Alzheimer's -secretase activity. J. Med. Chem., 41, 6-9.
    • (2000) J. Med. Chem. , vol.41 , pp. 6-9
    • Wolfe, M.S.1    Citron, M.2    Diehl, T.S.3    Xia, W.4    Donkor, I.O.5    Selkoe, D.J.6
  • 72
    • 0028276801 scopus 로고
    • Evidence that production and release of amyloid β-protein involves the endocytic pathway
    • Koo, E.H. and Squazzo, S.L. (1994) Evidence that production and release of amyloid β-protein involves the endocytic pathway. J. Biol. Chem., 269, 17386-17389.
    • (1994) J. Biol. Chem. , vol.269 , pp. 17386-17389
    • Koo, E.H.1    Squazzo, S.L.2
  • 73
    • 0035900686 scopus 로고    scopus 로고
    • Multiple effects of aspartate mutant presenilin 1 on the processing and trafficking of amyloid precursor protein
    • Kim, S.H., Leem, J.Y., Lah, J.J., Slunt, H.H., Levey, A.I., Thinakaran, G. and Sisodia, S.S. (2001) Multiple effects of aspartate mutant presenilin 1 on the processing and trafficking of amyloid precursor protein. J. Biol. Chem., 276, 43343-43350.
    • (2001) J. Biol. Chem. , vol.276 , pp. 43343-43350
    • Kim, S.H.1    Leem, J.Y.2    Lah, J.J.3    Slunt, H.H.4    Levey, A.I.5    Thinakaran, G.6    Sisodia, S.S.7
  • 74
    • 0036327098 scopus 로고    scopus 로고
    • Presenilin-1 affects trafficking and processing of betaAPP and is targeted in a complex with nicastrin to the plasma membrane
    • Kaether, C., Lammich, S., Edbauer, D., Ertl, M., Rietdorf, J., Capell, A., Steiner, H. and Haass, C. (2002) Presenilin-1 affects trafficking and processing of betaAPP and is targeted in a complex with nicastrin to the plasma membrane. J. Cell Biol., 158, 551-561.
    • (2002) J. Cell Biol. , vol.158 , pp. 551-561
    • Kaether, C.1    Lammich, S.2    Edbauer, D.3    Ertl, M.4    Rietdorf, J.5    Capell, A.6    Steiner, H.7    Haass, C.8
  • 77
    • 0022652923 scopus 로고
    • A comparative study of modified Bielschowsky, Bodian and thioflavin S stains on Alzheimer's neurofibrillary tangles
    • Yamamoto, T. and Hirano, A. (1986) A comparative study of modified Bielschowsky, Bodian and thioflavin S stains on Alzheimer's neurofibrillary tangles. Neuropathol. Appl. Neurobiol., 12, 3-9.
    • (1986) Neuropathol. Appl. Neurobiol. , vol.12 , pp. 3-9
    • Yamamoto, T.1    Hirano, A.2
  • 78
    • 0001468351 scopus 로고
    • Alzheimer's neurofibrillary changes. A topographic study
    • Hirano, A. and Zimmerman, H.M. (1962) Alzheimer's neurofibrillary changes. A topographic study. Arch. Neurol., 7, 227-242.
    • (1962) Arch. Neurol. , vol.7 , pp. 227-242
    • Hirano, A.1    Zimmerman, H.M.2
  • 79
    • 0029788661 scopus 로고    scopus 로고
    • Enhanced amyloidogenic processing of the β-amyloid precursor protein in gene-targeted mice bearing the Swedish familial Alzheimer's disease mutations and a "humanized" Aβ sequence
    • Reaume, A.G., Howland, D.S., Trusko, S.P., Savage, M.J., Lang, D.M., Greenberg, B.D., Siman, R. and Scott, R.W. (1996) Enhanced amyloidogenic processing of the β-amyloid precursor protein in gene-targeted mice bearing the Swedish familial Alzheimer's disease mutations and a "humanized" Aβ sequence. J. Biol. Chem., 271, 23380-23388.
    • (1996) J. Biol. Chem. , vol.271 , pp. 23380-23388
    • Reaume, A.G.1    Howland, D.S.2    Trusko, S.P.3    Savage, M.J.4    Lang, D.M.5    Greenberg, B.D.6    Siman, R.7    Scott, R.W.8
  • 80
    • 0028059841 scopus 로고
    • Expression of a ubiquitous, cross-reactive homologue of the mouse β-amyloid precursor protein (APP)
    • Slunt, H.H., Thinakaran, G., von Koch, C., Lo, A.C.Y., Tanzi, R.E. and Sisodia, S.S. (1994) Expression of a ubiquitous, cross-reactive homologue of the mouse β-amyloid precursor protein (APP). J. Biol. Chem., 269, 2637-2644.
    • (1994) J. Biol. Chem. , vol.269 , pp. 2637-2644
    • Slunt, H.H.1    Thinakaran, G.2    von Koch, C.3    Lo, A.C.Y.4    Tanzi, R.E.5    Sisodia, S.S.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.