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Titolo:
Reversible conversion of monomeric human prion protein between native and fibrilogenic conformations
Autore:
Jackson, GS; Hosszu, LLP; Power, A; Hill, AF; Kenney, J; Saibil, H; Craven, CJ; Waltho, JP; Clarke, AR; Collinge, J;
Indirizzi:
Univenet,Prionperial Coll Sci Technol & Med, St Marys, Sch Med, Dept Neurog Univ London Imperial Coll Sci Technol & Med London England W2 1NY Neurog Univshire,ield, Krebs Inst Mol Biol & Biotechnol, Sheffield S10 2TN, S York Univ Sheffield Sheffield S Yorkshire England S10 2TN ield S10 2TN, S York Univ London Birkbeck Coll, Dept Crystallog, London WC1E 7HX, England Univ London Birkbeck Coll London England WC1E 7HX ndon WC1E 7HX, England Univ Bristol, Sch Med Sci, Dept Biochem, Bristol BS8 1TD, Avon, England Univ Bristol Bristol Avon England BS8 1TD Bristol BS8 1TD, Avon, England
Titolo Testata:
SCIENCE
fascicolo: 5409, volume: 283, anno: 1999,
pagine: 1935 - 1937
SICI:
0036-8075(19990319)283:5409<1935:RCOMHP>2.0.ZU;2-K
Fonte:
ISI
Lingua:
ENG
Soggetto:
CREUTZFELDT-JAKOB DISEASE; MOLTEN GLOBULE STATE; ALPHA-LACTALBUMIN; SCRAPIE; ORGANELLES; STABILITY; LYSOSOMES; ISOFORM; DOMAIN; CELLS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Life Sciences
Physical, Chemical & Earth Sciences
Citazioni:
23
Recensione:
Indirizzi per estratti:
Indirizzo: Collinge, J Univenet,Prionperial Coll Sci Technol & Med, St Marys, Sch Med, Dept Neurog Univ London Imperial Coll Sci Technol & Med London England W2 1NY
Citazione:
G.S. Jackson et al., "Reversible conversion of monomeric human prion protein between native and fibrilogenic conformations", SCIENCE, 283(5409), 1999, pp. 1935-1937

Abstract

Prion propagation involves the conversion of cellular prion protein (PrPc)into a disease-specific isomer, PrPSc, shifting from a predominantly alpha-helical to beta-sheet structure. Here, conditions were established in which recombinant human PrP could switch between the native a conformation, characteristic of PrPc, and a compact, highly soluble, monomeric form rich in beta structure. The soluble beta form (beta-PrP) exhibited partial resistance to proteinase kappa digestion, characteristic of PrPSc, and was a directprecursor of fibrillar structures closely similar to those isolated from diseased brains. The conversion of PrPc to beta-PrP in suitable cellular compartments, and its subsequent stabilization by intermolecular association, provide a molecular mechanism for prion propagation.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 14/07/20 alle ore 07:05:29