Results 141 to 150 of about 183,390 (190)
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Current Protocols in Pharmacology, 1998
AbstractThe fluorescence‐based assay described in this unit is used not only to screen large numbers of compounds in a 96‐well format for the ability to inhibit human immunodeficiency virus‐1 (HIV) protease, but also to determine accurately the affinity of inhibitors for the enzyme.
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AbstractThe fluorescence‐based assay described in this unit is used not only to screen large numbers of compounds in a 96‐well format for the ability to inhibit human immunodeficiency virus‐1 (HIV) protease, but also to determine accurately the affinity of inhibitors for the enzyme.
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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
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1995
Abstract The retroviral protease, which plays an essential role in virion maturation (1), has been subjected to intensive studies and drug discovery efforts. The HIV-1 protease has a unique cleavage specificity and belongs to the family of aspartyl proteases.
C Debouck +3 more
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Abstract The retroviral protease, which plays an essential role in virion maturation (1), has been subjected to intensive studies and drug discovery efforts. The HIV-1 protease has a unique cleavage specificity and belongs to the family of aspartyl proteases.
C Debouck +3 more
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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
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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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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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Applied Biochemistry and Biotechnology, 1996
A new method for obtaining HIV-I protease was suggested. Fusion proteins composed of the N-terminal fragment of human gamma-interferon and HIV-I protease connected with (Asp)4Lys (protein I) or Asp-Pro (protein II) linkers were expressed in Escherichia coli cells. The fusion proteins were produced as insoluble inclusion bodies in the 20% yield of total
N I, Dergousova +3 more
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A new method for obtaining HIV-I protease was suggested. Fusion proteins composed of the N-terminal fragment of human gamma-interferon and HIV-I protease connected with (Asp)4Lys (protein I) or Asp-Pro (protein II) linkers were expressed in Escherichia coli cells. The fusion proteins were produced as insoluble inclusion bodies in the 20% yield of total
N I, Dergousova +3 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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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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Journal of Enzyme Inhibition, 1992
The human immunodeficiency virus (HIV), the etiological agent for the acquired immune deficiency syndrome (AIDS), is a retrovirus which makes use of a virally-encoded aspartic protease to perform specific proteolytic processing of two of its gene products in order to form active enzymes and structural proteins within the mature virion.
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The human immunodeficiency virus (HIV), the etiological agent for the acquired immune deficiency syndrome (AIDS), is a retrovirus which makes use of a virally-encoded aspartic protease to perform specific proteolytic processing of two of its gene products in order to form active enzymes and structural proteins within the mature virion.
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