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Volumn 56, Issue 3, 2001, Pages 395-399

Does an inhibition of the ubiquitin/26S proteasome pathway of protein degradation underlie the pathogenesis of non-familial Alzheimer's disease?

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA SYNUCLEIN; AMYLOID PRECURSOR PROTEIN; PRESENILIN 1; PROTEASOME; REGULATOR PROTEIN; TAU PROTEIN; UBIQUITIN;

EID: 0035037689     PISSN: 03069877     EISSN: None     Source Type: Journal    
DOI: 10.1054/mehy.2000.1198     Document Type: Article
Times cited : (12)

References (22)
  • 4
    • 0025326719 scopus 로고
    • Ubiquitin carboxyl-terminal hydrolase (PGP9.5) is selectively present in ubiquitinated inclusion bodies characteristic of human neurodegenerative diseases
    • (1990) J Pathol , vol.161 , pp. 153-160
    • Lowe, J.1    McDermott, H.2    Landon, M.3
  • 11
    • 0030606288 scopus 로고    scopus 로고
    • Pathological lesions of Alzheimer's disease and dementia with Lewy bodies exhibit immunoreactivity to an ATPast that is a regulatory subunit of the 26S proteasome
    • (1996) Neurosci Lett , vol.219 , pp. 167-170
    • Fergusson, J.1    Landon, M.2    Lowe, J.3
  • 20
  • 21
    • 0032127320 scopus 로고    scopus 로고
    • Both N-terminal and C-terminal fragments of presenilin-1 colocalize with neurofibrillary tangles in neurons and dystrophic neurites of senile plaques in Alzheimer's disease
    • (1998) J Neurosci Res , vol.53 , pp. 99-106
    • Chui, D.H.1    Shirotani, K.2    Tanahashi, H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.