Page last updated: 2024-08-24

kynostatin 272 and ritonavir

kynostatin 272 has been researched along with ritonavir in 7 studies

Research

Studies (7)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's3 (42.86)18.2507
2000's4 (57.14)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Blum, LE; Clemente, JC; Dunn, BM; Goodenow, MM; Hemrajani, R1
Ami, E; Hamada, Y; Hayashi, Y; Hidaka, K; Kimura, T; Kiso, Y; Nakahara, K; Nakatani, S; Nguyen, JT; Sato, A1
Ami, E; Hamada, Y; Hayashi, Y; Hidaka, K; Hori, Y; Kimura, T; Kiso, Y; Nagai, A; Nakahara, K; Nakatani, S; Nguyen, JT; Ohnishi, N; Sato, A1
Anderson, B; Erickson, JW; Gulnik, SV; Liu, B; Mitsuya, H; Suvorov, LI; Yu, B1
Maeda, Y; Mitsuya, H; Uchida, H1
Aquaro, S; CaliĆ², R; Davis, DA; Humphrey, RW; Newcomb, FM; Perno, CF; Yarchoan, R1
Lu, Y; Wang, S; Yang, CY1

Other Studies

7 other study(ies) available for kynostatin 272 and ritonavir

ArticleYear
Secondary mutations M36I and A71V in the human immunodeficiency virus type 1 protease can provide an advantage for the emergence of the primary mutation D30N.
    Biochemistry, 2003, Dec-30, Volume: 42, Issue:51

    Topics: Alanine; Anti-HIV Agents; Asparagine; Aspartic Acid; Binding Sites; Drug Resistance, Viral; HIV Protease; HIV Protease Inhibitors; HIV-1; Humans; Indinavir; Isoleucine; Kinetics; Methionine; Mutagenesis, Site-Directed; Nelfinavir; Ritonavir; Valine

2003
Synthesis and antiviral property of allophenylnorstatine-based HIV protease inhibitors incorporating D-cysteine derivatives as P2/P3 moieties.
    Bioorganic & medicinal chemistry letters, 2007, Aug-01, Volume: 17, Issue:15

    Topics: Amides; Cell Line; Cysteine; HIV; HIV Protease Inhibitors; Humans; Models, Molecular; Phenylbutyrates; Thiazoles

2007
Combination of non-natural D-amino acid derivatives and allophenylnorstatine-dimethylthioproline scaffold in HIV protease inhibitors have high efficacy in mutant HIV.
    Journal of medicinal chemistry, 2008, May-22, Volume: 51, Issue:10

    Topics: Amino Acids; Drug Resistance, Viral; HIV Protease; HIV Protease Inhibitors; HIV-1; Models, Molecular; Mutation; Phenylbutyrates; Stereoisomerism; Structure-Activity Relationship; Thiazoles

2008
Kinetic characterization and cross-resistance patterns of HIV-1 protease mutants selected under drug pressure.
    Biochemistry, 1995, Jul-25, Volume: 34, Issue:29

    Topics: Amino Acid Sequence; Binding Sites; Carbamates; Cloning, Molecular; Drug Resistance, Microbial; HIV Protease; HIV Protease Inhibitors; HIV-1; Indinavir; Isoquinolines; Kinetics; Methylurea Compounds; Mutagenesis, Site-Directed; Oligopeptides; Point Mutation; Pyridines; Quinolines; Recombinant Proteins; Saquinavir; Structure-Activity Relationship; Thiazoles; Valine

1995
HIV-1 protease does not play a critical role in the early stages of HIV-1 infection.
    Antiviral research, 1997, Volume: 36, Issue:2

    Topics: Chloramphenicol O-Acetyltransferase; HeLa Cells; HIV Infections; HIV Protease; HIV Protease Inhibitors; HIV-1; Humans; Oligopeptides; Ritonavir; Saquinavir

1997
Relative potency of protease inhibitors in monocytes/macrophages acutely and chronically infected with human immunodeficiency virus.
    The Journal of infectious diseases, 1998, Volume: 178, Issue:2

    Topics: Anti-HIV Agents; Cell Line; Cells, Cultured; HIV Core Protein p24; HIV Protease Inhibitors; HIV-1; Humans; Macrophages; Monocytes; Oligopeptides; Reverse Transcriptase Inhibitors; Ritonavir; Saquinavir; Zidovudine

1998
Binding free energy contributions of interfacial waters in HIV-1 protease/inhibitor complexes.
    Journal of the American Chemical Society, 2006, Sep-13, Volume: 128, Issue:36

    Topics: Binding Sites; Computer Simulation; Crystallization; HIV Protease; HIV Protease Inhibitors; Kinetics; Models, Chemical; Models, Molecular; Oligopeptides; Protein Binding; Protein Conformation; Ritonavir; Thermodynamics; Water

2006