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Titolo:
The biochemistry of Alzheimer disease
Autore:
Fine, RE;
Indirizzi:
Boston Univ, Sch Med, Dept Biochem, Boston, MA 02118 USA Boston Univ Boston MA USA 02118 h Med, Dept Biochem, Boston, MA 02118 USA Edith Nourse Rogers Mem Vet Adm Hosp, Geriatr Res Educ & Clin Ctr, Bedford, MA 01730 USA Edith Nourse Rogers Mem Vet Adm Hosp Bedford MA USA 01730 d, MA 01730 USA
Titolo Testata:
ALZHEIMER DISEASE & ASSOCIATED DISORDERS
, volume: 13, anno: 1999, supplemento:, 1
pagine: S82 - S87
SICI:
0893-0341(199904/06)13:<S82:TBOAD>2.0.ZU;2-O
Fonte:
ISI
Lingua:
ENG
Soggetto:
AMYLOID PRECURSOR PROTEIN; BETA-PROTEIN; APOLIPOPROTEIN-E; TRANSGENIC MICE; ENDOPLASMIC-RETICULUM; MUTANT PRESENILIN-1; PARKINSONS-DISEASE; ALPHA-SYNUCLEIN; IN-VIVO; GENE;
Keywords:
Alzheimer disease; biochemistry; apolipoprotein E; beta-amyloid precursor protein; presenilin;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Clinical Medicine
Life Sciences
Citazioni:
49
Recensione:
Indirizzi per estratti:
Indirizzo: Fine, RE Boston Univ, Sch Med, Dept Biochem, 715 Albany St K-124-C, Boston, MA 02118 USA Boston Univ 715 Albany St K-124-C Boston MA USA 02118 A 02118 USA
Citazione:
R.E. Fine, "The biochemistry of Alzheimer disease", ALZ DIS A D, 13, 1999, pp. S82-S87

Abstract

Biochemical and genetic investigations have identified four key proteins, mutations in which either cause Alzheimer disease (AD) (beta-amyloid precursor protein, presenilin 1 and 2) or confer a higher risk of developing AD (apolipoprotein E). This paper discusses the biochemical evidence that linkseach protein to AD, various animal and cell models that have been used in these investigations, and the putative interactions between these proteins that lead to AD. Areas that are especially fertile for novel research are noted as are gaps in our present understanding of the etiology of AD.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 02/04/20 alle ore 21:03:43