Výsledky vyhledávání - "E F, JOHNSON"

[Computer model of 3D structure of cytochrome P450 2B4]

Autor: A A, Sechenykh, A V, Dubanov, V S, Skvortsov, A S, Ivanov, A I, Archakov, P, Williams, J, Cosme, E F, Johnson, D E, McRee

Publikováno v: Voprosy meditsinskoi khimii. 48(5)

Cytochromes P450 (CYPs) play an important role in the oxidative metabolism of xenobiotics. Three-dimensional structures of CYPs are needed to study structure-function relationships in their molecules and interaction with partner proteins. Experimenta

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::7510231ed8abb2fdf9f6152e1f5b5cb3
https://pubmed.ncbi.nlm.nih.gov/12498097

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Insights into the HER-2 receptor tyrosine kinase mechanism and substrate specificity using a transient kinetic analysis

Autor: A. J. Diamonti, E. F. Johnson, A. Y. Jan, Kermit L. Carraway, Karen S. Anderson

Publikováno v: Biochemistry. 39(32)

The HER-2/erbB-2/c-neu proto-oncogene encodes for an EGF receptor-like protein which has been implicated in the pathogenesis of several human malignancies. Although much has been learned about the physiological significance of this receptor tyrosine

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a0949869287419fc784c5783b2a914a8
https://pubmed.ncbi.nlm.nih.gov/10933796

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Rabbit pregnane X receptor is activated by rifampicin

Autor: U, Savas, M R, Wester, K J, Griffin, E F, Johnson

Publikováno v: Drug metabolism and disposition: the biological fate of chemicals. 28(5)

Reverse transcriptase-polymerase chain reaction was used to amplify a partial cDNA from rabbit lung mRNA that shared 77% protein sequence identity with the mouse pregnane X receptor (PXR). Rapid amplification of cDNA ends from a rabbit kidney lambdaZ

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::fac218462d853407856a8ba4934628c0
https://pubmed.ncbi.nlm.nih.gov/10772631

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Mammalian microsomal cytochrome P450 monooxygenase: structural adaptations for membrane binding and functional diversity

Autor: P A, Williams, J, Cosme, V, Sridhar, E F, Johnson, D E, McRee

Publikováno v: Molecular cell. 5(1)

Microsomal cytochrome P450s participate in xenobiotic detoxification, procarcinogen activation, and steroid hormone synthesis. The first structure of a mammalian microsomal P450 suggests that the association of P450s with the endoplasmic reticulum in

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::f3a5f05af4b21af669954226ee6960c7
https://pubmed.ncbi.nlm.nih.gov/10678174

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CYP2C19 participates in tolbutamide hydroxylation by human liver microsomes

Autor: M R, Wester, J M, Lasker, E F, Johnson, J L, Raucy

Publikováno v: Drug metabolism and disposition: the biological fate of chemicals. 28(3)

Tolbutamide is a sulfonylurea-type oral hypoglycemic agent whose action is terminated by hydroxylation of the tolylsulfonyl methyl moiety catalyzed by cytochrome P-450 (CYP) enzymes of the human CYP2C subfamily. Although most studies have implicated

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::c9d758d2ac920dc4a83dd659fd07b38a
https://pubmed.ncbi.nlm.nih.gov/10681382

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Engineering microsomal cytochrome P450 2C5 to be a soluble, monomeric enzyme. Mutations that alter aggregation, phospholipid dependence of catalysis, and membrane binding

Autor: J, Cosme, E F, Johnson

Publikováno v: The Journal of biological chemistry. 275(4)

Deletion of the N-terminal membrane-spanning domain from microsomal P450s 2C5 and 2C3 generates the enzymes, 2C5dH and 2C3dH, that exhibit a salt-dependent association with membranes indicating that they retain a monofacial membrane interaction domai

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::2abd56616bdf03caf4e76bff594b2b72
https://pubmed.ncbi.nlm.nih.gov/10644712

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Structure-function of cytochromes P450 and flavin-containing monooxygenases: implications for drug metabolism

Autor: J R, Halpert, T L, Domanski, O, Adali, C P, Biagini, J, Cosme, E A, Dierks, E F, Johnson, J P, Jones, P, Ortiz de Montellano, R M, Philpot, O, Sibbesen, W K, Wyatt, Z, Zheng

Publikováno v: Drug metabolism and disposition: the biological fate of chemicals. 26(12)

This article is a report on a symposium held at Experimental Biology '98 in San Francisco, California. Recent developments in site-directed mutagenesis, computer-modeling, and mechanistic analysis of cytochromes P450 and flavin-containing monooxygena

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::1f3f43f7c320a9586f1387fd6bbf8a6c
https://pubmed.ncbi.nlm.nih.gov/9860932

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Peroxisome proliferator activated receptor-alpha expression in human liver

Autor: C N, Palmer, M H, Hsu, K J, Griffin, J L, Raucy, E F, Johnson

Publikováno v: Molecular pharmacology. 53(1)

The peroxisome proliferator activated receptor alpha (PPAR) is a member of the steroid/hormone receptor superfamily that mediates the peroxisome proliferator-dependent transcriptional activation of genes encoding several peroxisomal and microsomal en

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::6623cefbdf6cf7b97b85bc3bf3cf602f
https://pubmed.ncbi.nlm.nih.gov/9443928

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