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Volumn 3, Issue 1, 1997, Pages 67-72

Mutant presenilins of Alzheimer's disease increase production of 42-residue amyloid β-protein in both transfected cells and transgenic mice

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID BETA PROTEIN; PRESENILIN 1; PRESENILIN 2;

EID: 16944362157     PISSN: 10788956     EISSN: None     Source Type: Journal    
DOI: 10.1038/nm0197-67     Document Type: Article
Times cited : (1187)

References (28)
  • 1
    • 0029784838 scopus 로고    scopus 로고
    • Amyloid β-protein and the genetics of Alzheimer's disease
    • Selkoe, D.J. Amyloid β-protein and the genetics of Alzheimer's disease. J. Biol. Chem. 271, 18295-18296 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 18295-18296
    • Selkoe, D.J.1
  • 2
    • 0027258525 scopus 로고
    • The carboxy terminus of the beta amyloid protein is critical for the seeding of amyloid formation: Implications for the pathogenesis of Alzheimer's disease
    • Jarrett, J.T., Berger, E.P. & Lansbury P.T., Jr. The carboxy terminus of the beta amyloid protein is critical for the seeding of amyloid formation: Implications for the pathogenesis of Alzheimer's disease. Biochemistry 32, 4693-4697 (1993).
    • (1993) Biochemistry , vol.32 , pp. 4693-4697
    • Jarrett, J.T.1    Berger, E.P.2    Lansbury Jr., P.T.3
  • 3
    • 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. et al. 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. Nature Med. 2, 864-870 (1996).
    • (1996) Nature Med. , vol.2 , pp. 864-870
    • Scheuner, D.1
  • 4
    • 0029792928 scopus 로고    scopus 로고
    • New clues to Alzheimer's disease: Unraveling the roles of amyloid and tau
    • Yankner, B.A. New clues to Alzheimer's disease: Unraveling the roles of amyloid and tau. Nature Med. 2, 850-852 (1996).
    • (1996) Nature Med. , vol.2 , pp. 850-852
    • Yankner, B.A.1
  • 5
    • 0030199986 scopus 로고    scopus 로고
    • Inhibition of amyloid β-protein production in neural cells by the serine protease inhibitor AEBSF
    • Citron, M. et al. Inhibition of amyloid β-protein production in neural cells by the serine protease inhibitor AEBSF. Neuron 17, 171-179 (1996).
    • (1996) Neuron , vol.17 , pp. 171-179
    • Citron, M.1
  • 6
    • 0028924248 scopus 로고
    • Generation of amyloid β-protein from its precursor is sequence specific
    • Citron, M., Teplow, D.B. & Selkoe, D.J. Generation of amyloid β-protein from its precursor is sequence specific. Neuron 14, 661-670 (1995).
    • (1995) Neuron , vol.14 , pp. 661-670
    • Citron, M.1    Teplow, D.B.2    Selkoe, D.J.3
  • 7
    • 0028817351 scopus 로고
    • Cell-type and amyloid precursor protein-type specific inhibition of Aβ release by Bafilomycin A1, a selective inhibitor of vacuolar ATPases
    • Knops, J. et al. Cell-type and amyloid precursor protein-type specific inhibition of Aβ release by Bafilomycin A1, a selective inhibitor of vacuolar ATPases. J. Biol. Chem. 270, 2419-2422 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 2419-2422
    • Knops, J.1
  • 8
    • 0028866435 scopus 로고
    • The Swedish mutation causes early-onset alzheimer's disease by β-secretase cleavage within the secretory pathway
    • Haass, C. et al. The Swedish mutation causes early-onset alzheimer's disease by β-secretase cleavage within the secretory pathway. Nature Med. 1, 1291-1296 (1995).
    • (1995) Nature Med. , vol.1 , pp. 1291-1296
    • Haass, C.1
  • 9
    • 15844425969 scopus 로고    scopus 로고
    • Endoproteolysis of presenilin 1 and accumulation of processed derivatives in vivo
    • Thinakaran, G. et al. Endoproteolysis of presenilin 1 and accumulation of processed derivatives in vivo. Neuron 17, 181-190 (1996).
    • (1996) Neuron , vol.17 , pp. 181-190
    • Thinakaran, G.1
  • 10
    • 85086348152 scopus 로고    scopus 로고
    • The Alzheimer's disease associated presenilins are differentially phosphorylated proteins located predominantly within the endoplasmic reticulum
    • in the press
    • Walter, J. et al. The Alzheimer's disease associated presenilins are differentially phosphorylated proteins located predominantly within the endoplasmic reticulum. Mol. Med. (in the press).
    • Mol. Med.
    • Walter, J.1
  • 11
    • 0026176190 scopus 로고
    • Homology of the amyloid β-protein precursor in monkey and human supports a primate model for β-amyloidosis in Alzheimer's disease
    • Podlisny, MB., Tolan, D. & Selkoe, D.J. Homology of the amyloid β-protein precursor in monkey and human supports a primate model for β-amyloidosis in Alzheimer's disease. Am. J. Pathol. 138, 1423-1435(1991).
    • (1991) Am. J. Pathol. , vol.138 , pp. 1423-1435
    • Podlisny, M.B.1    Tolan, D.2    Selkoe, D.J.3
  • 12
    • 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. & Teplow, D.B. 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).
    • (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
    • 0026646604 scopus 로고
    • Amyloid β-peptide is produced by cultured cells during normal metabolism
    • Haass, C. et al. Amyloid β-peptide is produced by cultured cells during normal metabolism. Nature 359, 322-325 (1992).
    • (1992) Nature , vol.359 , pp. 322-325
    • Haass, C.1
  • 14
    • 0029803744 scopus 로고    scopus 로고
    • Evidence that Aβ42 and Aβ40 are generated from the β-amyloid precursor protein by different protease activities
    • Citron, M. et al. Evidence that Aβ42 and Aβ40 are generated from the β-amyloid precursor protein by different protease activities. Proc. Natl. Acad. Sci. USA 93, 13170-13175 (1996).
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 13170-13175
    • Citron, M.1
  • 15
    • 0027086835 scopus 로고
    • Chimeric prion protein expression in cultured cells and transgenic mice
    • Scott, M.R., Kohler, R., Foster, D. & Prusiner, S.B. Chimeric prion protein expression in cultured cells and transgenic mice. Protein Sci. 1, 986-997 (1992).
    • (1992) Protein Sci. , vol.1 , pp. 986-997
    • Scott, M.R.1    Kohler, R.2    Foster, D.3    Prusiner, S.B.4
  • 16
    • 0025244011 scopus 로고
    • Transgenetic studies implicate interactions between homologous PrP isoforms in scrapie prion replication
    • Prusiner, S., Scott, M., Foster, D., Westaway, D. & DeArmond, S. Transgenetic studies implicate interactions between homologous PrP isoforms in scrapie prion replication. Cell 63, 673-686 (1990).
    • (1990) Cell , vol.63 , pp. 673-686
    • Prusiner, S.1    Scott, M.2    Foster, D.3    Westaway, D.4    DeArmond, S.5
  • 17
    • 0028902465 scopus 로고
    • Developmental expression of the PrP gene in glial cells
    • Moser, M., Colello, R.J., Pott, U. & Oesch, B. Developmental expression of the PrP gene in glial cells. Neuron 14, 509-517 (1995).
    • (1995) Neuron , vol.14 , pp. 509-517
    • Moser, M.1    Colello, R.J.2    Pott, U.3    Oesch, B.4
  • 18
    • 0028810244 scopus 로고
    • Age-related CNS disorder and early death in transgenic FVB/N mice overexpressing Alzheimer amyloid precursor proteins
    • Hsiao, K.K. et al. Age-related CNS disorder and early death in transgenic FVB/N mice overexpressing Alzheimer amyloid precursor proteins. Neuron 15, 1203-1218 (1995).
    • (1995) Neuron , vol.15 , pp. 1203-1218
    • Hsiao, K.K.1
  • 19
    • 0029004341 scopus 로고
    • Cloning of a novel gene bearing missense mutations in early onset familial Alzheimer disease
    • Sherrington, R. et al. Cloning of a novel gene bearing missense mutations in early onset familial Alzheimer disease. Nature 375, 754-760 (1995).
    • (1995) Nature , vol.375 , pp. 754-760
    • Sherrington, R.1
  • 20
    • 0031569390 scopus 로고    scopus 로고
    • Analysis of the 5′ sequence, genomic structure and alternative splicing of the presenilin 1 gene associated with early onset alzheimer's disease
    • in the press
    • Rogaev, E.I. et al. Analysis of the 5′ sequence, genomic structure and alternative splicing of the presenilin 1 gene associated with early onset alzheimer's disease. Genomics (in the press).
    • Genomics
    • Rogaev, E.I.1
  • 21
    • 0021803192 scopus 로고
    • Alzheimer's presenile dementia transmitted in an extended kindred
    • Foncin, J.F. et al. Alzheimer's presenile dementia transmitted in an extended kindred. Rev. Neurol. (Paris) 141, 194-202 (1985).
    • (1985) Rev. Neurol. (Paris) , vol.141 , pp. 194-202
    • Foncin, J.F.1
  • 23
    • 0027459686 scopus 로고
    • Secretion of β-amyloid precursor protein cleaved at the amino-terminus of the β-amyloid peptide
    • Seubert, P. et al. Secretion of β-amyloid precursor protein cleaved at the amino-terminus of the β-amyloid peptide. Nature 361, 260-263 (1993).
    • (1993) Nature , vol.361 , pp. 260-263
    • Seubert, P.1
  • 24
    • 33845280446 scopus 로고
    • Comparing the polarities of the amino acids: Side-chain distribution coefficients between the vapor phase, cyclohexane, 1-octanol, and neutral aqueous solution
    • Radzicka, A. & Wolfenden, R. Comparing the polarities of the amino acids: Side-chain distribution coefficients between the vapor phase, cyclohexane, 1-octanol, and neutral aqueous solution. Biochemistry 27, 1664-1670 (1988).
    • (1988) Biochemistry , vol.27 , pp. 1664-1670
    • Radzicka, A.1    Wolfenden, R.2
  • 25
    • 8944241774 scopus 로고    scopus 로고
    • Alzheimer's disease associated with mutations in presenilin 2 is rare and variably penetrant
    • Sherrington, R. et al. Alzheimer's disease associated with mutations in presenilin 2 is rare and variably penetrant. Hum. Mol. Genetics 5, 985-988 (1996).
    • (1996) Hum. Mol. Genetics , vol.5 , pp. 985-988
    • Sherrington, R.1
  • 26
    • 16044365171 scopus 로고    scopus 로고
    • The E280A presenilin 1 Alzheimer mutation produces increased Aβ42 deposition and severe cerebellar pathology
    • Lemere, C.A. et al. The E280A presenilin 1 Alzheimer mutation produces increased Aβ42 deposition and severe cerebellar pathology. Nature Med. 2, 1146-1150 (1996).
    • (1996) Nature Med. , vol.2 , pp. 1146-1150
    • Lemere, C.A.1
  • 27
    • 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. 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 376, 775-778 (1995).
    • (1995) Nature , vol.376 , pp. 775-778
    • Rogaev, E.I.1
  • 28
    • 0026646605 scopus 로고
    • Isolation and quantitation of soluble Alzheimer's β-peptide from biological fluids
    • Seubert, P. et al. Isolation and quantitation of soluble Alzheimer's β-peptide from biological fluids. Nature 359, 325-327 (1992).
    • (1992) Nature , vol.359 , pp. 325-327
    • Seubert, P.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.