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Volumn 920, Issue , 2000, Pages 158-164

Presenilin function in APP processing

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID PRECURSOR PROTEIN; PRESENILIN 1; PRESENILIN 2;

EID: 0034528008     PISSN: 00778923     EISSN: None     Source Type: Book Series    
DOI: 10.1111/j.1749-6632.2000.tb06917.x     Document Type: Conference Paper
Times cited : (23)

References (53)
  • 2
    • 0032211830 scopus 로고    scopus 로고
    • The cell biology of beta-amyloid precursor protein and presenilin in Alzheimer's disease
    • (1998) Trends Cell. Biol. , vol.8 , pp. 447-453
    • Selkoe, D.J.1
  • 8
    • 14444272986 scopus 로고    scopus 로고
    • Evidence that tumor necrosis factor alpha converting enzyme is involved in regulated alpha-secretase cleavage of the Alzheimer amyloid protein precursor
    • (1998) J. Biol. Chem. , vol.273 , pp. 27765-27767
    • Buxbaum, J.D.1    Liu, K.N.2    Luo, Y.3
  • 10
    • 0033569653 scopus 로고    scopus 로고
    • Membrane-anchored metalloprotease MDC9 has an alpha-secretase activity responsible for processing the amyloid precursor protein
    • (1999) Biochem. J. , vol.343 , Issue.PART 2 , pp. 371-375
    • Koike, H.1    Tomioka, S.2    Sorimachi, H.3
  • 11
    • 0343196671 scopus 로고    scopus 로고
    • Kuzbanian controls proteolytic processing of Notch and mediates lateral inhibition during Drosophila and vertebrate neurogenesis
    • (1997) Cell , vol.90 , pp. 271-280
    • Pan, D.1    Rubin, G.M.2
  • 14
    • 10544248594 scopus 로고    scopus 로고
    • Beta-secretase processing of the beta-amyloid precursor protein in transgenic mice is efficient in neurons but inefficient in astrocytes
    • (1996) J. Biol. Chem. , vol.271 , pp. 31407-31411
    • Zhao, J.1    Paganini, L.2    Mucke, L.3
  • 19
    • 0001050325 scopus 로고    scopus 로고
    • BACE maps to chromosome 11 and a BACE homolog, BACE2, reside in the obligate down syndrome region of chromosome 21
    • (1999) Science , vol.286
    • Saunders, A.J.1
  • 24
    • 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
    • (1998) J. Biol. Chem. , vol.273 , pp. 3205-3211
    • Capell, A.1    Grunberg, J.2    Pesold, B.3
  • 27
    • 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
    • (1996) Nat. Med. , vol.2 , pp. 864-870
    • Scheuner, D.1    Eckman, C.2    Jensen, M.3
  • 28
    • 16944362157 scopus 로고    scopus 로고
    • Mutant presenilins of Alzheimer's disease increase production of 42-residue amyloid beta-protein in both transfected cells and transgenic mice
    • (1997) Nat. Med. , vol.3 , pp. 67-72
    • Citron, M.1    Westaway, D.2    Xia, W.3
  • 35
    • 0032905727 scopus 로고    scopus 로고
    • Presenilin mutations associated with Alzheimer disease cause defective intracellular trafficking of beta-catenin, a component of the presenilin protein complex
    • (1999) Nat. Med. , vol.5 , pp. 164-169
    • Nishimura, M.1    Yu, G.2    Levesque, G.3
  • 38
    • 0032555718 scopus 로고    scopus 로고
    • Roles for proteolysis and trafficking in notch maturation and signal transduction
    • (1998) Cell , vol.94 , pp. 423-426
    • Chan, Y.M.1    Jan, Y.N.2
  • 39
    • 0030941803 scopus 로고    scopus 로고
    • The SREBP pathway: Regulation of cholesterol metabolism by proteolysis of a membrane-bound transcription factor
    • (1997) Cell , vol.89 , pp. 331-340
    • Brown, M.S.1    Goldstein, J.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.