HIV protease

Human Immunodeficiency Virus Type 1 Reverse Transcriptase Dimer Destabilization by 1-{Spiro[4‘ ‘-amino-2‘ ‘,2‘ ‘-dioxo-1‘ ‘,2‘ ‘-oxathiole-5‘ ‘,3‘- [2‘,5‘-bis- O -( tert -butyldimethylsilyl)-β- d -ribofuranosyl]]}-3-ethylthymine †

Biochemistry / Microbiology / Medical Microbiology / HIV / Software / Humans / Sequence alignment / Mutation / HIV protease / Urea / High Pressure Liquid Chromatography / Information Storage and Retrieval / Amino Acid Sequence / Protein Denaturation / Furans / Biochemistry and cell biology / Reading Frames / Dimerization / Nevirapine / Thymidine / Molecular Sequence Data / Humans / Sequence alignment / Mutation / HIV protease / Urea / High Pressure Liquid Chromatography / Information Storage and Retrieval / Amino Acid Sequence / Protein Denaturation / Furans / Biochemistry and cell biology / Reading Frames / Dimerization / Nevirapine / Thymidine / Molecular Sequence Data

A Novel Bis-Tetrahydrofuranylurethane-Containing Nonpeptidic Protease Inhibitor (PI), GRL-98065, Is Potent against Multiple-PI-Resistant Human Immunodeficiency Virus In Vitro

Microbiology / Medical Microbiology / HIV / Humans / HIV protease / Drug Design / Human immunodeficiency virus / Spectrum / Active site / Antimicrobial agents / Microbial Sensitivity Tests / Amino Acid Profile / Amino Acid Sequence / Antiviral Activity / Binding Site / Furans / Drug Design / Human immunodeficiency virus / Spectrum / Active site / Antimicrobial agents / Microbial Sensitivity Tests / Amino Acid Profile / Amino Acid Sequence / Antiviral Activity / Binding Site / Furans

Oximinoarylsulfonamides as potent HIV protease inhibitors

Organic Chemistry / Kinetics / HIV protease / Drug Design / Molecular Conformation / Bioorganic and medicinal Chemistry / Structure activity Relationship / Carbamates / Bioorganic and medicinal Chemistry / Structure activity Relationship / Carbamates

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