4 documents found, page 1 of 1
The Role of the FMN-Domain of Human Cytochrome P450 Oxidoreductase in Its Promi...
Esteves, Francisco; Campelo, Diana; Gomes, Bruno Costa; Urban, Philippe; Bozonnet, Sophie; Lautier, Thomas; Rueff, Jose; Truan, GillesNADPH cytochrome P450 oxidoreductase (CPR) is the obligatory electron supplier that sustains the activity of microsomal cytochrome P450 (CYP) enzymes. The variant nature of the isoform-specific proximal interface of microsomal CYPs indicates that CPR is capable of multiple degenerated interactions with CYPs for electron transfer, through different binding mechanisms, and which are still not well-understood. Rec...
Corrigendum
Esteves, Francisco; Campelo, Diana; Gomes, Bruno Costa; Urban, Philippe; Bozonnet, Sophie; Lautier, Thomas; Rueff, Jose; Truan, Gilles[This corrects the article DOI: 10.3389/fphar.2020.00299.].
Correction
Campelo, Diana; Lautier, Thomas; Urban, Philippe; Esteves, Francisco; Bozonnet, Sophie; Truan, Gilles; Kranendonk, Michel[This corrects the article on p. 755 in vol. 8, PMID: 29163152.].
The hinge segment of human NADPH-cytochrome P450 reductase in conformational sw...
Campelo, Diana; Lautier, Thomas; Urban, Philippe; Esteves, Francisco; Bozonnet, Sophie; Truan, Gilles; Kranendonk, MichelThis work was in part funded by a joint ANR/FCT program; France: ANR-13-ISV5-0001 (DODYCOEL), and Portuguese national funds, through the Fundacao para a Ciencia e a Tecnologia (Project FCT-ANR/BEX-BCM/0002/2013).; NADPH-cytochrome P450 reductase (CPR) is a redox partner of microsomal cytochromes P450 and is a prototype of the diflavin reductase family. CPR contains 3 distinct functional domains: a FMN-binding d...