Zobrazeno 1 - 10 of 22 pro vyhledávání: '"D J Kempf"'
1
Human serum alpha 1 acid glycoprotein reduces uptake, intracellular concentration, and antiviral activity of A-80987, an inhibitor of the human immunodeficiency virus type 1 protease
Autor: Kathleen A. Stellrecht, J. Leonard, P. A. Bilello, D W Norbeck, John A. Bilello, George L. Drusano, T. Robins, D J Kempf
Publikováno v: Antimicrobial Agents and Chemotherapy. 40:1491-1497
The therapeutic utility of a human immunodeficiency virus type 1 (HIV-1) protease inhibitor may depend on its intracellular concentration, which is a property of its uptake, metabolism, and/or efflux. Previous studies in our laboratory indicated that
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5f28ff6ac2a9944f3acf219f16cd3a5a
https://doi.org/10.1128/aac.40.6.1491
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2
HIV Protease Inhibitors
Autor: D. J. Kempf, H. L. Sham
Publikováno v: Current Pharmaceutical Design. 2:225-246
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 cy
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::8f7237dbbddedb755a74cf24a8816111
https://doi.org/10.2174/1381612802666220921175941
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3
Human immunodeficiency virus type 1 virions composed of unprocessed Gag and Gag-Pol precursors are capable of reverse transcribing viral genomic RNA
Autor: D W Norbeck, R Swanstrom, Paul Krogstad, Andrew H. Kaplan, D J Kempf
Publikováno v: Antimicrobial Agents and Chemotherapy. 38:2929-2933
The structural proteins and enzymes of the human immunodeficiency virus type 1 core are translated as part of two polyprotein precursors, Gag and Gag-Pol, which are cleaved by a virally encoded protease. Viruses grown in the presence of inhibitors of
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e26d58d1a26d61449e5c5c7d9aaffc27
https://doi.org/10.1128/aac.38.12.2929
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4
Characterization of human immunodeficiency virus type 1 variants with increased resistance to a C2-symmetric protease inhibitor
Autor: M. K. Singh, T. Toyoshima, D. J. Kempf, David D. Ho, Chih-Ming Chen, S. K. Burt, N. E. Wideburg, Hongmei Mo, D. W. Norbeck, J. W. Erickson
Publikováno v: Journal of Virology. 68:2016-2020
Inhibitors of the human immunodeficiency virus type 1 protease represent a promising class of antiviral drugs for the treatment of AIDS, and several are now in clinical trials. Here, we report the in vitro selection of viral variants with decreased s
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::68f6c03706e8f6a1dbab9e4fbbf5356d
https://doi.org/10.1128/jvi.68.3.2016-2020.1994
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7
In vitro inhibition of human immunodeficiency virus (HIV) type 1 replication by C2 symmetry-based HIV protease inhibitors as single agents or in combinations
Autor: J N Weinstein, D W Norbeck, Hiroaki Mitsuya, John W. Erickson, D J Kempf, J J Plattner, Takuma Shirasaka, Seiji Kageyama
Publikováno v: Antimicrobial Agents and Chemotherapy. 36:926-933
C2 symmetry-based human immunodeficiency virus (HIV) protease inhibitors were examined in vitro as single agents or in combination with 3'-azido-2',3'-dideoxythymidine (AZT) or 2',3'-dideoxyinosine for activity against HIV type 1 (HIV-1). Ten C2 symm
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d90f584e2656ecd3168714db6367d3a6
https://doi.org/10.1128/aac.36.5.926
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8
In vitro metabolism of the HIV-1 protease inhibitor ABT-378: species comparison and metabolite identification
Autor: G N, Kumar, V, Jayanti, R D, Lee, D N, Whittern, J, Uchic, S, Thomas, P, Johnson, B, Grabowski, H, Sham, D, Betebenner, D J, Kempf, J F, Denissen
Publikováno v: Drug metabolism and disposition: the biological fate of chemicals. 27(1)
HIV protease inhibitor ABT-378 (ABT-378) was metabolized very extensively and rapidly by liver microsomes from mouse, rat, dog, monkey, and humans. The rates of NADPH-dependent metabolism of ABT-378 ranged from 2.39 to 9.80 nmol.mg microsomal protein
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::7c6f6181a104e68c5d9f610c175157dc
https://pubmed.ncbi.nlm.nih.gov/9884314
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9
Metabolism and disposition of the HIV-1 protease inhibitor ritonavir (ABT-538) in rats, dogs, and humans
Autor: J F, Denissen, B A, Grabowski, M K, Johnson, A M, Buko, D J, Kempf, S B, Thomas, B W, Surber
Publikováno v: Drug metabolism and disposition: the biological fate of chemicals. 25(4)
The metabolism and disposition of [14C]ritonavir (ABT-538, NOR-VIR), a potent, orally active HIV-1 protease inhibitor, were investigated in male and female Sprague-Dawley rats, beagle dogs, and HIV-negative male human volunteers. Rats and dogs receiv
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::5a9ff870dc1282e587403c00d33b2742
https://pubmed.ncbi.nlm.nih.gov/9107549
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10
Selection and analysis of human immunodeficiency virus type 1 variants with increased resistance to ABT-538, a novel protease inhibitor
Autor: David D. Ho, J. W. Erickson, D. J. Kempf, Hongmei Mo, Talapady N. Bhat, M. Markowitz, D. W. Norbeck
Publikováno v: Journal of virology. 69(2)
Inhibitors of the human immunodeficiency virus protease represent a promising new class of antiretroviral drugs for the treatment of AIDS. We now report the in vitro selection of viral variants with decreased sensitivity to a symmetry-based protease
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c04d1ddefe1663f3784bcc5f2f8fc948
https://pubmed.ncbi.nlm.nih.gov/7815532
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