Modulation of UDP-Glucuronosyltransferase Function by Cytochrome P450: Evidence for the Alteration of UGT2B7-Catalyzed Glucuronidation of Morphine by CYP3A4-Reference-Cited by-同舟云学术

Modulation of UDP-Glucuronosyltransferase Function by Cytochrome P450: Evidence for the Alteration of UGT2B7-Catalyzed Glucuronidation of Morphine by CYP3A4

Published:2004-12-20 Issue:3 Volume:67 Page:665-672
ISSN:0026-895X
Container-title:Molecular Pharmacology
language:en
Short-container-title:Mol Pharmacol

Author:

Takeda Shuso,Ishii Yuji,Iwanaga Megumi,Mackenzie Peter I.,Nagata Kiyoshi,Yamazoe Yasushi,Oguri Kazuta,Yamada Hideyuki

Publisher

American Society for Pharmacology & Experimental Therapeutics (ASPET)

Subject

Pharmacology,Molecular Medicine

Reference39 articles.

1. Interactions among cytochromes P-450 in the endoplasmic reticulum. Detection of chemically cross-linked complexes with monoclonal antibodies.

2. Membrane Insertion of Cytochrome P450 1A2 Promoted by Anionic Phospholipids

3. Participation of cytochrome P-450 isozymes in N-demethylation, N-hydroxylation and aromatic hydroxylation of methamphetamine

4. N-Glycosylation and Residue 96 Are Involved in the Functional Properties of UDP-Glucuronosyltransferase Enzymes,

5. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

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