Results 311 to 320 of about 260,498 (362)
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AIDS, 1996
The protease encoded by the human immunodeficiency virus (HIV protease) mediates the maturation of newly formed HIV particles through proteolytic processing of the gag and gag-pol gene products. Because of its essential role in the HIV replication cycle, this enzyme represents a logical target for the treatment of HIV infection.
A, Carr, D A, Cooper
semanticscholar +7 more sources
The protease encoded by the human immunodeficiency virus (HIV protease) mediates the maturation of newly formed HIV particles through proteolytic processing of the gag and gag-pol gene products. Because of its essential role in the HIV replication cycle, this enzyme represents a logical target for the treatment of HIV infection.
A, Carr, D A, Cooper
semanticscholar +7 more sources
Heterocyclic HIV-Protease Inhibitors
Current Medicinal Chemistry, 2013In the panorama of HIV protease inhibitors (HIV PIs), many efforts have been devoted to the development of new compounds with reduced peptidic nature in order to improve pharmacokinetics and pharmacodynamics features. The introduction of cyclic scaffolds in the design of new chemical entities reduces flexibility and affords more rigid inhibitors ...
CALUGI, CHIARA +2 more
openaire +3 more sources
HIV Protease Inhibitor Resistance
2014HIV protease is pivotal in the viral replication cycle and directs the formation of mature infectious virus particles. The development of highly specific HIV protease inhibitors (PIs), based on thorough understanding of the structure of HIV protease and its substrate, serves as a prime example of structure-based drug design.
Wensing, Annemarie M.J. +2 more
openaire +2 more sources
Enamino-oxindole HIV protease inhibitors
Bioorganic & Medicinal Chemistry Letters, 2012We have designed and synthesized a series of HIV protease inhibitors (PIs) with enamino-oxindole substituents optimized to interact with the S2' subsite of the HIV protease binding pocket. Several of these inhibitors have sub-nanomolar K(i) and antiviral IC(50) in the low nM range against WT HIV and against a panel of multi-drug resistant (MDR) strains.
Michael, Eissenstat +8 more
openaire +2 more sources
Prodrugs of HIV Protease Inhibitors
Current Pharmaceutical Design, 2003Despite the efficiency of the present polytherapies against AIDS, HIV replication continues indicating difficulties in drug adherence, drug-drug interactions, resistance issues, and the existence of reservoirs or sanctuaries for the virus. Moreover, most of the current FDA-approved HIV protease inhibitors (PIs) display disadvantageous physicochemical ...
Pierre, Vierling, Jacques, Greiner
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Protease Inhibitors for the Treatment of HIV/AIDS: Recent Advances and Future Challenges.
Current Topics in Medicinal Chemistry, 2019Acquired Immunodeficiency Syndrome (AIDS) is a chronic disease characterized by multiple life-threatening illnesses caused by a retro-virus, Human Immunodeficiency Virus (HIV).
Chandrashekhar Voshavar
semanticscholar +1 more source
Peptidomimetic Inhibitors of HIV Protease
Current Topics in Medicinal Chemistry, 2004There are currently (July, 2002) six protease inhibitors approved for the treatment of HIV infection, each of which can be classified as peptidomimetic in structure. These agents, when used in combination with other antiretroviral agents, produce a sustained decrease in viral load, often to levels below the limits of quantifiable detection, and a ...
John T, Randolph, David A, DeGoey
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Resistance to HIV protease inhibitors
Haemophilia, 1998Summary. Resistance to the HIV‐1 protease inhibitor indinavir involves the accumulation of multiple amino acid substitutions in the viral protease. A minimum of 11 amino acid positions have been identified as potential contributors to phenotypic resistance.
C. A. Lee +5 more
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Non-Peptidic HIV Protease Inhibitors
Current Topics in Medicinal Chemistry, 2004The past decade has seen many exciting achievements and advances in the treatment of HIV infection. One of the key components in this ever-evolving remedial strategy has been medicinally efficacious enzymatic inhibitors targeting the essential viral aspartyl protease.
R Alan, Chrusciel, Joseph W, Strohbach
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