Výsledky vyhledávání - "J R, Palamanda"

Mechanism-based inactivation of CYP2D6 by 5-fluoro-2-[4-[(2-phenyl-1H-imidazol-5-yl)methyl]-1-piperazinyl]pyrimidine

Autor: J R, Palamanda, C N, Casciano, L A, Norton, R P, Clement, L V, Favreau, C, Lin, A A, Nomeir

Publikováno v: Drug metabolism and disposition: the biological fate of chemicals. 29(6)

SCH 66712 [5-fluoro-2-[4-[(2-phenyl-1H-imidazol-5-yl)methyl]-1-piperazinyl]pyrimidine] caused a time- and NADPH-dependent loss of CYP2D6 activity. The inactivation of human liver (HL) microsomal dextromethorphan O-demethylase activity, a prototype ma

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::ac2f0d04fc0485be3ad4394d62a415a0
https://pubmed.ncbi.nlm.nih.gov/11353755

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Inhibition of CYP3A4 in a rapid microtiter plate assay using recombinant enzyme and in human liver microsomes using conventional substrates

Autor: A A, Nomeir, C, Ruegg, M, Shoemaker, L V, Favreau, J R, Palamanda, P, Silber, C C, Lin

Publikováno v: Drug metabolism and disposition: the biological fate of chemicals. 29(5)

Cytochrome P450 inhibition studies are performed in the pharmaceutical industry in the discovery stage to screen candidates that may have the potential for clinical drug-drug interactions. A 96-well microtiter plate assay using recombinant cytochrome

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::9033c517bafc5b2fe975acc299619303
https://pubmed.ncbi.nlm.nih.gov/11302943

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Improved reliability of the rapid microtiter plate assay using recombinant enzyme in predicting CYP2D6 inhibition in human liver microsomes

Autor: L V, Favreau, J R, Palamanda, C C, Lin, A A, Nomeir

Publikováno v: Drug metabolism and disposition: the biological fate of chemicals. 27(4)

A higher throughput method of screening for the inhibition of recombinant CYP2D6 using a microtiter plate (MTP) assay was evaluated using 62 new chemical entities and compared to data from the dextromethorphan O-demethylase assay in human liver micro

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::bcc01bede7dbb874d2c75308388ef7a5
https://pubmed.ncbi.nlm.nih.gov/10101136

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Dapsone acetylation by human liver arylamine N-acetyltransferases and interaction with antiopportunistic infection drugs

Autor: J R, Palamanda, D, Hickman, A, Ward, E, Sim, M, Romkes-Sparks, J D, Unadkat

Publikováno v: Drug metabolism and disposition: the biological fate of chemicals. 23(4)

Dapsone is used in the treatment of Pneumocystis carinii pneumonia, an opportunistic infection that afflicts acquired immunodeficiency syndrome (AIDS) patients. Inhibition of N-acetyltransferase (NAT)-dependent acetylation of dapsone could increase p

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::1e9ab2c7cab158229b83726275f9f9cd
https://pubmed.ncbi.nlm.nih.gov/7600914

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