The Role of the FMN-Domain of Human Cytochrome P450 Oxidoreductase in Its Promiscuous Interactions With Structurally Diverse Redox Partners-Reference-Cited by-同舟云学术

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The Role of the FMN-Domain of Human Cytochrome P450 Oxidoreductase in Its Promiscuous Interactions With Structurally Diverse Redox Partners

Published:2020-03-18 Issue: Volume:11 Page:
ISSN:1663-9812
Container-title:Frontiers in Pharmacology
language:
Short-container-title:Front. Pharmacol.

Author:

Esteves Francisco,Campelo Diana,Gomes Bruno Costa,Urban Philippe,Bozonnet Sophie,Lautier Thomas,Rueff José,Truan Gilles,Kranendonk Michel

Funder

Fundação para a Ciência e a Tecnologia

Agence Nationale de la Recherche

Publisher

Frontiers Media SA

Subject

Pharmacology (medical),Pharmacology

Reference65 articles.

1. Structure of the open conformation of a functional chimeric NADPH cytochrome P450 reductase.;Aigrain;EMBO Rep.,2009

2. The catalytic function of cytochrome P450 is entwined with its membrane-bound nature.;Barnaba;F1000Res,2017

3. Picturing the membrane-assisted choreography of cytochrome P450 with lipid nanodiscs.;Barnaba;Chemphyschem,2018

4. Structural and functional effects of cytochrome b5 interactions with human cytochrome P450 enzymes.;Bart;J. Biol. Chem.,2017

5. Structures of human cytochrome P450 1A1 with bergamottin and erlotinib reveal active-site modifications for binding of diverse ligands.;Bart;J. Biol. Chem.,2018

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