Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
Chaperone-like activity of synucleins
Autore:
Souza, JM; Giasson, BI; Lee, VMY; Ischiropoulos, H;
Indirizzi:
Univ Penn, Childrens Hosp Philadelphia, Med Ctr, Stokes Res Inst, Philadelphia, PA 19104 USA Univ Penn Philadelphia PA USA 19104 Res Inst, Philadelphia, PA 19104 USA Univ Penn, Med Ctr, Abramson Ctr 416D, Dept Biochem & Biophys, Philadelphia, PA 19104 USA Univ Penn Philadelphia PA USA 19104 & Biophys, Philadelphia, PA 19104 USA Univ Penn, Med Ctr, Ctr Neurodegenerat Dis Res, Philadelphia, PA 19104 USAUniv Penn Philadelphia PA USA 19104 t Dis Res, Philadelphia, PA 19104 USA Univ Penn, Med Ctr, Dept Pathol & Lab Med, Philadelphia, PA 19104 USA UnivPenn Philadelphia PA USA 19104 & Lab Med, Philadelphia, PA 19104 USA Univ Republ, Fac Med, Dept Bioquim, Montevideo 11800, Uruguay Univ RepublMontevideo Uruguay 11800 Bioquim, Montevideo 11800, Uruguay
Titolo Testata:
FEBS LETTERS
fascicolo: 1, volume: 474, anno: 2000,
pagine: 116 - 119
SICI:
0014-5793(20000526)474:1<116:CAOS>2.0.ZU;2-P
Fonte:
ISI
Lingua:
ENG
Soggetto:
LEWY BODY DEMENTIA; A-BETA COMPONENT; ALPHA-SYNUCLEIN; PARKINSONS-DISEASE; MOLECULAR CHAPERONE; ALZHEIMERS-DISEASE; PRECURSOR PROTEIN; NERVOUS-SYSTEM; IN-VITRO; AGGREGATION;
Keywords:
Parkinson's disease; lewy body; neurodegenerative disorder;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
32
Recensione:
Indirizzi per estratti:
Indirizzo: Ischiropoulos, H Univ Penn, Childrens Hosp Philadelphia, Med Ctr, Stokes Res Inst, 34th St & Civic Ctr Bldg, Philadelphia, PA 19104 USA Univ Penn 34th St & Civic Ctr Bldg Philadelphia PA USA 19104
Citazione:
J.M. Souza et al., "Chaperone-like activity of synucleins", FEBS LETTER, 474(1), 2000, pp. 116-119

Abstract

Synucleins are a family of small proteins that are predominantly expressedin neurons. The functions of the synucleins are not entirely understood, but they have been implicated in the pathogenesis of several neurodegenerative diseases. Our data show that alpha-, beta- or gamma-synuclein suppressesthe aggregation of thermally denatured alcohol dehydrogenase and chemically denatured insulin. The A53T but not the A30P mutant alpha-synuclein was able to inhibit the aggregation of insulin and the chaperone-like activity of alpha-synuclein was lost upon removal of its C-terminal residues 98-140, These results demonstrate that synucleins with the exception of the A30P mutant possess chaperone-like activity. (C) 2000 Federation of European Biochemical Societies.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 07/07/20 alle ore 15:40:18