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Titolo:
Sesquiterpene lactones, inhibitors of farnesyl protein transferase, isolated from the flower of Artemisia sylvatica
Autore:
Lee, SH; Kang, HM; Song, HC; Lee, H; Lee, UC; Son, KH; Kim, SH; Kwon, BM;
Indirizzi:
Korea Res Inst Biosci & Biotechnol, Taejon 305600, South Korea Korea Res Inst Biosci & Biotechnol Taejon South Korea 305600 South Korea Chungbuk Natl Univ, Coll Pharm, Chongju 360763, South Korea Chungbuk Natl Univ Chongju South Korea 360763 hongju 360763, South Korea Korea Res Inst Ginseng & Tobacco, Taejon 305, South Korea Korea Res Inst Ginseng & Tobacco Taejon South Korea 305 305, South Korea Kyunghee Univ, Grad Sch East West Med Sci, Seoul 130, South Korea KyungheeUniv Seoul South Korea 130 West Med Sci, Seoul 130, South Korea
Titolo Testata:
TETRAHEDRON
fascicolo: 27, volume: 56, anno: 2000,
pagine: 4711 - 4715
SICI:
0040-4020(20000630)56:27<4711:SLIOFP>2.0.ZU;2-D
Fonte:
ISI
Lingua:
ENG
Keywords:
sesquiterpene lactones; Artemisia sylvatica; farnesyl protein;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Physical, Chemical & Earth Sciences
Citazioni:
15
Recensione:
Indirizzi per estratti:
Indirizzo: Kwon, BM Korea Res Inst Biosci & Biotechnol, POB 115, Taejon 305600, SouthKorea Korea Res Inst Biosci & Biotechnol POB 115 Taejon South Korea 305600
Citazione:
S.H. Lee et al., "Sesquiterpene lactones, inhibitors of farnesyl protein transferase, isolated from the flower of Artemisia sylvatica", TETRAHEDRON, 56(27), 2000, pp. 4711-4715

Abstract

Five sesquiterpene lactones, 8-acetylarteminolide (1), artanomaloide (2), arteminones (3 and 4), and dehydromatricarin (5), were isolated from the methanolic extract of the flower of Artemisia sylvatica and characterized on the basis of their spectral data. New sesquiterpene lactone 1 was identified as a configurational isomer of artanomaloide (2), and the new arteminones3 and 4 are determined as stereoisomers. 8-Acetylarteminolide (1) stronglyinhibited FPTase with an IC50 of 1.8 mu M, however, the other sesquiterpene lactones mildly inhibited the transferase with an IC50 of 22-300 mu M. (C) 2000 Elsevier Science Ltd. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 13/07/20 alle ore 17:32:32