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Titolo:
Mechanism-based inhibition of zinc proteases
Autore:
Kim, DH; Mobashery, S;
Indirizzi:
Wayne State Univ, Dept Chem, Detroit, MI 48202 USA Wayne State Univ Detroit MI USA 48202 v, Dept Chem, Detroit, MI 48202 USA Pohang Univ Sci & Technol, Dept Chem, Pohang, South Korea Pohang Univ Sci & Technol Pohang South Korea Chem, Pohang, South Korea
Titolo Testata:
CURRENT MEDICINAL CHEMISTRY
fascicolo: 8, volume: 8, anno: 2001,
pagine: 959 - 965
SICI:
0929-8673(200107)8:8<959:MIOZP>2.0.ZU;2-V
Fonte:
ISI
Lingua:
ENG
Soggetto:
KETONE SUBSTRATE-ANALOGS; CARBOXYPEPTIDASE-A; AMIDE HYDROLYSIS; FORMULA <(ETA-5-C5H5)RE(NO)(PPH3)(IR)>+BF4; ANHYDRIDE INTERMEDIATE; INACTIVATION CHEMISTRY; RENAL DIPEPTIDASE; ESTER HYDROLYSIS; TRANSITION-STATE; HALIDE-COMPLEXES;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
71
Recensione:
Indirizzi per estratti:
Indirizzo: Mobashery, S Wayne State Univ, Dept Chem, Detroit, MI 48202 USA Wayne State Univ Detroit MI USA 48202 Detroit, MI 48202 USA
Citazione:
D.H. Kim e S. Mobashery, "Mechanism-based inhibition of zinc proteases", CURR MED CH, 8(8), 2001, pp. 959-965

Abstract

The functions of zinc proteases have been implicated in a host of physiological and pathological processes in living organisms. Mechanism-based inhibitors are highly sought as biologically active molecules that afford high selectivity in targeting specific enzymes. Mechanism-based inhibitors for zinc-dependent proteases have been developed in the past several years. Theseinhibitors exploit the chemistry inherent to transition metals in their mechanisms of enzyme inhibition. These efforts have been reviewed in this manuscript.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 29/11/20 alle ore 09:35:47