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Titolo:
Presenilin structure, function and role in Alzheimer disease
Autore:
Fraser, PE; Yang, DS; Yu, G; Levesque, L; Nishimura, M; Arawaka, S; Serpell, LC; Rogaeva, E; St George-Hyslop, P;
Indirizzi:
Univ Toronto, Ctr Res Neurodegenerat Dis, Toronto, ON M5S 3H2, Canada UnivToronto Toronto ON Canada M5S 3H2 t Dis, Toronto, ON M5S 3H2, Canada Univ Toronto, Dept Med Biophys, Toronto, ON, Canada Univ Toronto Toronto ON Canada to, Dept Med Biophys, Toronto, ON, Canada MRC Ctr, Neurobiol Unit, Cambridge, England MRC Ctr Cambridge EnglandMRC Ctr, Neurobiol Unit, Cambridge, England
Titolo Testata:
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR BASIS OF DISEASE
fascicolo: 1, volume: 1502, anno: 2000,
pagine: 1 - 15
SICI:
0925-4439(20000726)1502:1<1:PSFARI>2.0.ZU;2-U
Fonte:
ISI
Lingua:
ENG
Soggetto:
AMYLOID-BETA-PROTEIN; GRADIENT GEL-ELECTROPHORESIS; C-TERMINAL FRAGMENTS; MISSENSE MUTATIONS; IN-VIVO; CAENORHABDITIS-ELEGANS; MUTANT PRESENILIN-1; PRECURSOR PROTEIN; PROTEOLYTIC FRAGMENTS; MEMBRANE-PROTEIN;
Keywords:
Alzheimer disease; presenilin; beta-amyloid precursor protein; notch 1; beta-catenin; armadillo; secretase; amyloid-beta peptide; tau;
Tipo documento:
Review
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
102
Recensione:
Indirizzi per estratti:
Indirizzo: Fraser, PE Univ Toronto, Ctr Res Neurodegenerat Dis, Tanz Neurosci Bldg,6 Queens Pk Crescent W, Toronto, ON M5S 3H2, Canada Univ Toronto Tanz Neurosci Bldg,6 Queens Pk Crescent W Toronto ON Canada M5S 3H2
Citazione:
P.E. Fraser et al., "Presenilin structure, function and role in Alzheimer disease", BBA-MOL BAS, 1502(1), 2000, pp. 1-15

Abstract

Numerous missense mutations in the presenilins are associated with the autosomal dominant form of familial Alzheimer disease. Presenilin genes encodepolytopic transmembrane proteins, which are processed by proteolytic cleavage and form high-molecular-weight complexes under physiological conditions. The presenilins have been suggested to be functionally involved in developmental morphogenesis, unfolded protein responses and processing of selected proteins including the beta-amyloid precursor protein. Although the underlying mechanism by which presenilin mutations lead to development of Alzheimer disease remains elusive, one consistent mutational effect is an overproduction of long-tailed amyloid beta-peptides. Furthermore, presenilins interact with beta-catenin to form presenilin complexes, and the physiological and mutational effects are also observed in the catenin signal transductionpathway. (C) 2000 Elsevier Science B.V. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 03/06/20 alle ore 23:25:53