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Volumn 3, Issue 4, 1997, Pages 325-337

Presenilin proteins undergo heterogeneous endoproteolysis between Thr291 and Ala299 and occur as stable N- and C-terminal fragments in normal and Alzheimer brain tissue

Author keywords

[No Author keywords available]

Indexed keywords

ALZHEIMER DISEASE; AMINO TERMINAL SEQUENCE; ANIMAL CELL; ANIMAL TISSUE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; HUMAN; HUMAN TISSUE; MISSENSE MUTATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION;

EID: 0030889220     PISSN: 09699961     EISSN: None     Source Type: Journal    
DOI: 10.1006/nbdi.1997.0129     Document Type: Article
Times cited : (279)

References (26)
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    • Iwatsubo T., Odaka A., Suzuki N., Mizusawa H., Nukina N., Ihara Y. Visualization of Aβ42(43) and Aβ40 in senile plaques with end-specific Aβ monoclonals: Evidence that an initially deposited species is Aβ42(43). Neuron. 13:1995b;45-53.
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    • Lemere, C.A.1    Blustzjan, J.K.2    Yamaguchi, H.3    Wisniewski, T.4    Saido, T.C.5    Selkoe, D.J.6
  • 13
    • 0030575338 scopus 로고    scopus 로고
    • Characterization of human presenilin 1 using N-terminal specific monoclonal antibodies: Evidence that Alzheimer mutations affect proteolytic processing
    • Mercken M., Takahashi H., Honda T., Sato K., Murayama M., Nakazato Y., Noguchi K., Imahori K., Takashima A. Characterization of human presenilin 1 using N-terminal specific monoclonal antibodies: Evidence that Alzheimer mutations affect proteolytic processing. FEBS Lett. 389:1996;297-303.
    • (1996) FEBS Lett. , vol.389 , pp. 297-303
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    • Homology of the amyloid β-protein precursor in monkey and human supports a primate model for β-amyloidosis in Alzheimer's disease
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* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.