Derivatives of 5-Nitro-furan-2-carboxylic Acid Carbamoylmethyl Ester Inhibit RNase H Activity Associated with HIV-1 Reverse Transcriptase

The RNase H activity associated with human immunodeficiency virus type 1 (HIV-1) is an attractive target for an antiretroviral drug development. We screened 20000 small-molecular-weight compounds for RNase H inhibitors and identified a novel RNase H-inhibiting structure characterized by a 5-nitro-fu...

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Veröffentlicht in:	Journal of medicinal chemistry 2009-03, Vol.52 (5), p.1380-1387
Hauptverfasser:	Fuji, Hideyoshi, Urano, Emiko, Futahashi, Yuko, Hamatake, Makiko, Tatsumi, Junko, Hoshino, Tyuji, Morikawa, Yuko, Yamamoto, Naoki, Komano, Jun
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Anti-HIV Agents - chemical synthesis Anti-HIV Agents - chemistry Anti-HIV Agents - pharmacology Antibiotics. Antiinfectious agents. Antiparasitic agents Antiviral agents Biological and medical sciences Cell Line Crystallography, X-Ray Databases, Factual Furans - chemical synthesis Furans - chemistry Furans - pharmacology HIV-1 - drug effects HIV-1 - enzymology Humans Hydrophobic and Hydrophilic Interactions Medical sciences Models, Molecular Pharmacology. Drug treatments Protein Conformation Reverse Transcriptase Inhibitors - chemical synthesis Reverse Transcriptase Inhibitors - chemistry Reverse Transcriptase Inhibitors - pharmacology Ribonuclease H, Human Immunodeficiency Virus - antagonists & inhibitors Ribonuclease H, Human Immunodeficiency Virus - chemistry Structure-Activity Relationship Virus Replication - drug effects
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