메뉴 건너뛰기




Volumn 405, Issue 6787, 2000, Pages 689-694

Photoactivated γ-secretase inhibitors directed to the active site covalently label presenilin 1

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID PRECURSOR PROTEIN; ASPARTIC ACID; ASPARTIC PROTEINASE; BENZOPHENONE; ENZYME INHIBITOR; ENZYME PRECURSOR; GAMMA SECRETASE; PRESENILIN 1; PRESENILIN 2;

EID: 0034621824     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/35015085     Document Type: Article
Times cited : (877)

References (23)
  • 1
    • 0032211830 scopus 로고    scopus 로고
    • The cell biology of β-amyloid precursor protein and presenilin in Alzheimer's disease
    • Selkoe, D. J. The cell biology of β-amyloid precursor protein and presenilin in Alzheimer's disease. Trends Cell Biol. 8, 447-453 (1998).
    • (1998) Trends Cell Biol. , vol.8 , pp. 447-453
    • Selkoe, D.J.1
  • 2
    • 0029004341 scopus 로고
    • Cloning of a gene bearing missense mulations in early-onset familial Alzheimer's disease
    • Sherrington, R. et al. Cloning of a gene bearing missense mulations in early-onset familial Alzheimer's disease. Nature 375, 734-760 (1995).
    • (1995) Nature , vol.375 , pp. 734-760
    • Sherrington, R.1
  • 3
    • 0029150716 scopus 로고
    • A familial Alzheimer's disease locus on chromosome 1
    • Levy-Lahad, E. et al. A familial Alzheimer's disease locus on chromosome 1. Science 269, 970-973 (1995).
    • (1995) Science , vol.269 , pp. 970-973
    • Levy-Lahad, E.1
  • 4
    • 16044373524 scopus 로고    scopus 로고
    • Secreted amyloid beta-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 beta-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
  • 5
    • 16044366039 scopus 로고    scopus 로고
    • Increased amyloid-beta42(43) in brains of mice expressing mutant presenilin 1
    • Duff, K. et al. Increased amyloid-beta42(43) in brains of mice expressing mutant presenilin 1 Nature 383, 710-713 (1996).
    • (1996) Nature , vol.383 , pp. 710-713
    • Duff, K.1
  • 6
    • 0030293676 scopus 로고    scopus 로고
    • Familial Alzheimer's disease-linked presenilin 1 variants elevate Abetal-42,1-40 ratio in vitro and in vivo
    • Borchelt, D. R. et al. Familial Alzheimer's disease-linked presenilin 1 variants elevate Abetal-42,1-40 ratio in vitro and in vivo. Neuron 17, 1005-1013 (1996).
    • (1996) Neuron , vol.17 , pp. 1005-1013
    • Borchelt, D.R.1
  • 7
    • 0032556859 scopus 로고    scopus 로고
    • Deficiency of presenilin-1 inhibits the normal cleavage of amyloid precursor protein
    • De Strooper, B. et al. Deficiency of presenilin-1 inhibits the normal cleavage of amyloid precursor protein. Nature 391, 387-390 (1998).
    • (1998) Nature , vol.391 , pp. 387-390
    • De Strooper, B.1
  • 8
    • 0033535553 scopus 로고    scopus 로고
    • Two transmembrane aspartates in presenilin-1 required for presenilin endoproteolysis and γ-secretase activity
    • Wolfe, M. S. et al. Two transmembrane aspartates in presenilin-1 required for presenilin endoproteolysis and γ-secretase activity. Nature 398, 513-517 (1999).
    • (1999) Nature , vol.398 , pp. 513-517
    • Wolfe, M.S.1
  • 9
    • 0343891435 scopus 로고    scopus 로고
    • L-685,458, an aspartic protease transition state mimic, is a potent inhibitor of APP γ-secretase activity
    • in the press
    • Shearman, M. S. et al. L-685,458, an aspartic protease transition state mimic, is a potent inhibitor of APP γ-secretase activity. Biochemistry, in the press.
    • Biochemistry
    • Shearman, M.S.1
  • 10
    • 0002903441 scopus 로고
    • Analog approaches to the structure of the transition state in enzyme reactions
    • Wolfenden, R. Analog approaches to the structure of the transition state in enzyme reactions. Accts. Chem. Res. 5, 10-18 (1972).
    • (1972) Accts. Chem. Res. , vol.5 , pp. 10-18
    • Wolfenden, R.1
  • 11
    • 0001172518 scopus 로고
    • eds. Barrett, A. J. & Salvesen, G. Elsevier Science
    • Rich, D. H. Inhibitors of Aspartic Proteinases. (eds. Barrett, A. J. & Salvesen, G.) 179-217 (Elsevier Science, 1986).
    • (1986) Inhibitors of Aspartic Proteinases , pp. 179-217
    • Rich, D.H.1
  • 12
    • 25744457539 scopus 로고    scopus 로고
    • Presenilin-1 is linked with γ-secretase activity in the detergent solubilized state
    • in the press
    • Li, Y.-M. et al. Presenilin-1 is linked with γ-secretase activity in the detergent solubilized state. Proc. Natl Acad. Sci. USA (in the press).
    • Proc. Natl Acad. Sci. USA
    • Li, Y.-M.1
  • 13
    • 0033551099 scopus 로고    scopus 로고
    • Peptidomimetic probes and molecular modeling suggest that Alzheimer's γ-secretase is an intramembrane-cleaving aspartyl protease
    • Wolfe, M. S. et al. Peptidomimetic probes and molecular modeling suggest that Alzheimer's γ-secretase is an intramembrane-cleaving aspartyl protease. Biochemistry 38, 4720-4727 (1999).
    • (1999) Biochemistry , vol.38 , pp. 4720-4727
    • Wolfe, M.S.1
  • 14
    • 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
  • 15
    • 12644290265 scopus 로고    scopus 로고
    • Evidence for phosphorylation of oligomeric assembly of presenilin 1
    • Seeger, M. et al. Evidence for phosphorylation of oligomeric assembly of presenilin 1. Proc. Natl Acad. Sci. USA 94, 5090-5094 (1997).
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 5090-5094
    • Seeger, M.1
  • 16
    • 0032488995 scopus 로고    scopus 로고
    • The proteolytic fragments of the Alzheimer's disease-associated presenilin-1 form heterodimers and occur as a 100-150-kDa molecular mass complex
    • Capell, A. et al. The proteolytic fragments of the Alzheimer's disease-associated presenilin-1 form heterodimers and occur as a 100-150-kDa molecular mass complex. J. Biol. Chem. 273, 3205-3211 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 3205-3211
    • Capell, A.1
  • 17
    • 0029554875 scopus 로고
    • A mutation in Alzheimer's disease destroying a splice acceptor site in the presenilin-1 gene
    • Perez-Tur, J. et al. A mutation in Alzheimer's disease destroying a splice acceptor site in the presenilin-1 gene. Neuroreport 7, 297-301 (1995).
    • (1995) Neuroreport , vol.7 , pp. 297-301
    • Perez-Tur, J.1
  • 18
    • 0030667426 scopus 로고    scopus 로고
    • Evidence that levels of presenilins (PS1 and PS2) are coordinately regulated by competition for limiting cellular factors
    • Thinakaran, G. et al. Evidence that levels of presenilins (PS1 and PS2) are coordinately regulated by competition for limiting cellular factors. J. Biol. Chem. 272, 28415-28422 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 28415-28422
    • Thinakaran, G.1
  • 19
    • 0000273282 scopus 로고
    • A stereocontrolled synthesis of hydroxyethylene dipeptide isosteres using novel, chiral aminoalkyl epoxides and γ-(aminoalkyl) γ-lactones
    • Evans, B. E. et al. A stereocontrolled synthesis of hydroxyethylene dipeptide isosteres using novel, chiral aminoalkyl epoxides and γ-(aminoalkyl) γ-lactones. J. Org. Chem. 50, 4635-4625 (1985).
    • (1985) J. Org. Chem. , vol.50 , pp. 4635-14625
    • Evans, B.E.1
  • 20
    • 14744295939 scopus 로고
    • Electrochemiluminescence: A new diagnostic and research tool
    • Yang, H., Leland, J. K., Yost, D. & Massey, R. J. Electrochemiluminescence: A new diagnostic and research tool. Biol/Technology 12, 193-194 (1994).
    • (1994) Biol/Technology , vol.12 , pp. 193-194
    • Yang, H.1    Leland, J.K.2    Yost, D.3    Massey, R.J.4
  • 21
    • 0032145289 scopus 로고    scopus 로고
    • Modulation of amyloid precursor protein processing by compounds with various mechanisms of action: Detection by liquid phase electrochemiluminescent system
    • Khorkova, O. E., Patel, K., Heroux, J. & Sahasrabudhe, S. Modulation of amyloid precursor protein processing by compounds with various mechanisms of action: detection by liquid phase electrochemiluminescent system. J. Neurosci. Methods 82, 159-166 (1998).
    • (1998) J. Neurosci. Methods , vol.82 , pp. 159-166
    • Khorkova, O.E.1    Patel, K.2    Heroux, J.3    Sahasrabudhe, S.4
  • 22
    • 0029661424 scopus 로고    scopus 로고
    • Analysis of heterogeneous βA4 peptides in human cerebrospinal fluid and blood by a newly developed sensitive western blot analysis
    • Ida, N. et al. Analysis of heterogeneous βA4 peptides in human cerebrospinal fluid and blood by a newly developed sensitive western blot analysis. J. Biol. Chem. 271, 22908-22914 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 22908-22914
    • Ida, N.1
  • 23
    • 14444267540 scopus 로고    scopus 로고
    • Characterization of new polyclonal antibodies specific for 40 and 42 amino acid-long amyloid β-peptides: Their use to examine the cell biology of presenilins and the immunohistochemistry of sporadic Azcheimer's desease and cerebral amyloid angiopathy cases
    • Barelli, H. L. et al. Characterization of new polyclonal antibodies specific for 40 and 42 amino acid-long amyloid β-peptides: Their use to examine the cell biology of presenilins and the immunohistochemistry of sporadic Azcheimer's desease and cerebral amyloid angiopathy cases. Mol. Med. 3, 695-707 (1997).
    • (1997) Mol. Med. , vol.3 , pp. 695-707
    • Barelli, H.L.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.