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Rapamycin sensitivity in Saccharomyces cerevisiae is mediated by a peptidyl-prolyl cis-trans isomerase related to human FK506-binding protein

Autor: R Cafferkey, Y Koltin, D J Bergsma, L Faucette, M A Levy, R K Johnson, George P. Livi, P L Koser

Publikováno v: Molecular and Cellular Biology. 11:1718-1723

Rapamycin is a macrolide antifungal agent with structural similarity to FK506. It exhibits potent immunosuppressive properties analogous to those of both FK506 and cyclosporin A (CsA). Unlike FK506 and CsA, however, rapamycin does not inhibit the tra

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c8fe3e49c8471890866c1965808a54ed
https://doi.org/10.1128/mcb.11.3.1718

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Cytochrome P3-450 cDNA encodes aflatoxin B1-4-hydroxylase

Autor: H. V. Gelboin, Narayana Battula, Alexander E. Maccubbin, G. K. Townsend, Hira L. Gurtoo, P. L. Koser, M. B. Faletto

Publikováno v: Journal of Biological Chemistry. 263:12187-12189

Aflatoxin B1 (AFB1), a potent hepatocarcinogen and ubiquitous dietary contaminant in some countries, is detoxified to aflatoxin M1 (AFM1) via cytochrome P-450-mediated AFB1-4-hydroxylase. Genetic studies in mice have demonstrated that the expression

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::75240ae660abff558e6eac9da564ef68
https://doi.org/10.1016/s0021-9258(18)37736-6

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Induction of aryl hydrocarbon hydroxylase and DNA adduct formation in parental and carcinogen transformed C3H/10T1/2 clone 8 cells by benzo[a]pyrene

Autor: M B, Faletto, A E, Maccubbin, P L, Koser, J A, Vangalio, H L, Gurtoo

Publikováno v: Cancer biochemistry biophysics. 10(3)

C3H/10T1/2 clone 8 (10T1/2) cells possess aryl hydrocarbon hydroxylase (AHH) activity capable of metabolizing polycyclic aromatic hydrocarbons to ultimate carcinogenic forms. AHH activity in 10T1/2 cells was measured before and after culturing in the

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::1faaba6eb61ffdfe5bc8f01c409f3827
https://pubmed.ncbi.nlm.nih.gov/2505924

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Metabolism and binding of cyclophosphamide and its metabolite acrolein to rat hepatic microsomal cytochrome P-450

Autor: A J, Marinello, S K, Bansal, B, Paul, P L, Koser, J, Love, R F, Struck, H L, Gurtoo

Publikováno v: Cancer research. 44(10)

The hepatic cytochrome P-450-mediated metabolism and metabolic activation of [chloroethyl-3H]cyclophosphamide [( chloroethyl-3H]CP) and [4-14C]cyclophosphamide [( 4-14C]CP) were investigated in vitro in the reconstituted system containing cytochrome

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::62d71e55598c4daa67a15ad5c1ac46d6
https://pubmed.ncbi.nlm.nih.gov/6380709

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Cytochrome P3-450 cDNA encodes aflatoxin B1-4-hydroxylase

Autor: M B, Faletto, P L, Koser, N, Battula, G K, Townsend, A E, Maccubbin, H V, Gelboin, H L, Gurtoo

Publikováno v: The Journal of biological chemistry. 263(25)

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::df9aa24b2c2c65888b0415f8f9aad96f
https://pubmed.ncbi.nlm.nih.gov/3137222

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The genetics of aflatoxin B1 metabolism. Association of the induction of aflatoxin B1-4-hydroxylase with the transcriptional activation of cytochrome P3-450 gene

Autor: P L, Koser, M B, Faletto, A E, Maccubbin, H L, Gurtoo

Publikováno v: The Journal of biological chemistry. 263(25)

The association between murine cytochrome P3-450 and hepatic aflatoxin B1-4-hydroxylase, a cytochrome P-450-dependent enzyme which converts aflatoxin B1 (AFB1) to aflatoxin M1 (AFM1), was examined by (a) purification of the cytochrome P-450 which pre

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::d447d8f612e17bff19dca80e5931a6cd
https://pubmed.ncbi.nlm.nih.gov/3137229

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