Results 271 to 280 of about 136,889 (307)
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The active site of HIV‐1 protease
Medicinal Research Reviews, 2001AbstractThe active site of the homodimeric HIV‐1 protease includes six amino acids (triads AspThrGly found in each monomer) in amino acid positions 25 to 27 and 25′ to 27′. Up to now, the role of Thr26 and Thr26′, and Gly27 and Gly27′, is unknown. It is hypothesized that strong hydrogen‐bonding forces between the Thr26 and Thr26′ residues stabilize the
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Peptide substrates and inhibitors of the HIV-1 protease
Biochemical and Biophysical Research Communications, 1989Oligopeptides containing the consensus retroviral protease cleavage sequence Ser/Thr-X-Y-Tyr/Phe-Pro are substrates for purified recombinant HIV-1 protease with Km's in the millimolar range. The minimum sequence containing the consensus pentapeptide which serves as a good substrate is a heptapeptide spanning the P4-P3' residues. Substitution of reduced
Michael L. Moore +12 more
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An electrochemical approach for the detection of HIV-1 protease
Chemical Communications, 2007An electrochemical biosensor with a new bioorganometallic approach for the detection of human immunodeficiency virus (HIV) type 1 protease (HIV-1 PR) using surface-bound ferrocenoyl (Fc)-pepstatin conjugates is presented.
Kagan, Kerman +2 more
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Defining HIV-1 Protease Substrate Selectivity
Current Drug Target -Infectious Disorders, 2002The Aspartyl protease of HIV-1 offers an excellent target for the development of specific drugs against the virus. Drugs against protease and reverse transcriptase form the basis for Highly Active Anti-Retroviral Therapy (HAART) that has been successful in improving survival rates and quality of life for HIV infected individuals.
Zachary Q, Beck +2 more
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Errors in prescribing HIV-1 protease inhibitors
Journal of the Association of Nurses in AIDS Care, 1997The purpose of this study was to describe and quantify errors in dosage frequency associated with written medical orders, compared to manufacturer's recommendations and current therapeutic recommendations for protease inhibitors, for persons living with HIV disease/AIDS who were receiving home care services.A convenience sample was used for a ...
P J, Ungvarski, J E, Rottner
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A Microtiter Colorimetric Assay for the HIV-1 Protease
Analytical Biochemistry, 1997We have developed a novel colorimetric assay for the HIV-1 protease that is suitable for high-throughput screening of inhibitors. This assay utilizes two nonenzymatic reaction steps, which are carried out in succession following enzymatic hydrolysis of a synthetic peptide. The first step involves a carbamylation reaction between cyanate and the nascent
J, Stebbins, C, Debouck
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Optimization of a Macromolecular Inhibitor of HIV-1 Protease
1998HIV protease (HIV PR) has been identified as a key target in the treatment of HIV infection, and antiviral drugs that block its proteolytic activity have been developed. However, there are numerous ways in which a drug can lose effectiveness during long-term therapy.
D S, Dauber +3 more
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The Triple Threat of HIV-1 Protease Inhibitors
2015Newly released human immunodeficiency virus type 1 (HIV-1) particles obligatorily undergo a maturation process to become infectious. The HIV-1 protease (PR) initiates this step, catalyzing the cleavage of the Gag and Gag-Pro-Pol structural polyproteins.
Marc, Potempa +3 more
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The HIV-1 Protease as a Therapeutic Target for AIDS
AIDS Research and Human Retroviruses, 1992HIV produces a small, dimeric aspartyl protease which specifically cleaves the polyprotein precursors encoding the structural proteins and enzymes of the virus. This proteolytic activity is absolutely required for the production of mature, infectious virions and is therefore an attractive target for therapeutic intervention.
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