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Titolo:
ALLOSTERIC INHIBITORS AGAINST HIV-1 REVERSE-TRANSCRIPTASE - DESIGN AND SYNTHESIS OF MKC-442 ANALOGS HAVING AN OMEGA-FUNCTIONALIZED ACYCLIC STRUCTURE
Autore:
TANAKA H; WALKER RT; HOPKINS AL; REN J; JONES EY; FUJIMOTO K; HAYASHI M; MIYASAKA T; BABA M; STAMMERS DK; STUART DI;
Indirizzi:
SHOWA UNIV,SCH PHARMACEUT SCI,SHINAGAWA KU,1-5-8 HATANODAI TOKYO 142 JAPAN UNIV BIRMINGHAM,SCH CHEM BIRMINGHAM B15 2TT W MIDLANDS ENGLAND UNIV OXFORD,MOL BIOPHYS LAB OXFORD OX1 3QU ENGLAND OXFORD CTR MOL SCI OXFORD OX1 3QT ENGLAND KAGOSHIMA UNIV,FAC MED,CTR CHRON VIRAL DIS,DIV HUMAN RETROVIRUSES KAGOSHIMA 890 JAPAN
Titolo Testata:
Antiviral chemistry & chemotherapy
fascicolo: 4, volume: 9, anno: 1998,
pagine: 325 - 332
SICI:
0956-3202(1998)9:4<325:AIAHR->2.0.ZU;2-L
Fonte:
ISI
Lingua:
ENG
Soggetto:
IMMUNODEFICIENCY-VIRUS TYPE-1; ANTI-HIV-1 AGENTS; IN-VITRO; POTENT; 1-)(2-HYDROXYETHOXY)METHYL>-6-(PHENYLTHIO)THYMINE; REPLICATION; SERIES; ASSAY; HEPT;
Keywords:
HEPT; MKC-442; NNRTIS; REVERSE TRANSCRIPTASE; HYDROGEN BONDING; ANTI-HIV ACTIVITY;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
18
Recensione:
Indirizzi per estratti:
Citazione:
H. Tanaka et al., "ALLOSTERIC INHIBITORS AGAINST HIV-1 REVERSE-TRANSCRIPTASE - DESIGN AND SYNTHESIS OF MKC-442 ANALOGS HAVING AN OMEGA-FUNCTIONALIZED ACYCLIC STRUCTURE", Antiviral chemistry & chemotherapy, 9(4), 1998, pp. 325-332

Abstract

Based on X-ray crystallographic analysis of MKC-442/human immunodeficiency virus type 1 reverse transcriptase (HIV-1 RT) complex, analoguesin which the N1-substituent is replaced with omega-functionalized alkyl groups were designed to improve the affinity for the enzyme. Synthesis of these compounds was carried out starting from MKC-442 by a sequence of reactions (N3-protection, removal of N1-ethoxymethyl group, alkylation, and N3-deprotection). The compounds were evaluated for anti-HIV activity. Structure-activity relationships are discussed in terms of the possible interaction with the enzyme.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 30/09/20 alle ore 08:40:58