Zobrazeno 1 - 10
of 111
pro vyhledávání: '"Philippe Urban"'
Autor:
Philippe Urban, Denis Pompon
Publikováno v:
Scientific Reports, Vol 12, Iss 1, Pp 1-13 (2022)
Abstract Conformational dynamics plays a critical role for the function of multidomain electron transfer complexes. While crystallographic or NMR approaches allow detailed insight into structures, lower resolution methods like cryo-electron microscop
Externí odkaz:
https://doaj.org/article/b97a4f31a5714b3bb1427fa757934d4f
Autor:
Francisco Esteves, Cristina M. M. Almeida, Sofia Silva, Inês Saldanha, Philippe Urban, José Rueff, Denis Pompon, Gilles Truan, Michel Kranendonk
Publikováno v:
Biomolecules, Vol 13, Iss 7, p 1083 (2023)
A unique cytochrome P450 (CYP) oxidoreductase (CPR) sustains activities of human microsomal CYPs. Its function requires toggling between a closed conformation enabling electron transfers from NADPH to FAD and then FMN cofactors and open conformations
Externí odkaz:
https://doaj.org/article/f62d15d3be7b4883af44a3ed7f77817f
Autor:
Francisco Esteves, Diana Campelo, Bruno Costa Gomes, Philippe Urban, Sophie Bozonnet, Thomas Lautier, José Rueff, Gilles Truan, Michel Kranendonk
Publikováno v:
Frontiers in Pharmacology, Vol 11 (2020)
Externí odkaz:
https://doaj.org/article/4feb1c7e46344f58a5e4ad60ebee8dd1
Autor:
Francisco Esteves, Diana Campelo, Bruno Costa Gomes, Philippe Urban, Sophie Bozonnet, Thomas Lautier, José Rueff, Gilles Truan, Michel Kranendonk
Publikováno v:
Frontiers in Pharmacology, Vol 11 (2020)
NADPH 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
Externí odkaz:
https://doaj.org/article/78cc9bf1507040fe9210808633b8f4ef
Publikováno v:
Frontiers in Bioengineering and Biotechnology, Vol 7 (2020)
4-hydroxybenzoic acid (pHBA) is an important industrial precursor of muconic acid and liquid crystal polymers whose production is based on the petrochemical industry. In order to decrease our dependency on fossil fuels and improve sustainability, mic
Externí odkaz:
https://doaj.org/article/baca3b1f6ed8409ba0bd38bc2b02dada
Publikováno v:
International Journal of Molecular Sciences, Vol 21, Iss 18, p 6669 (2020)
The activity of microsomal cytochromes P450 (CYP) is strictly dependent on the supply of electrons provided by NADPH cytochrome P450 oxidoreductase (CPR). The variant nature of the isoform-specific proximal interface of microsomal CYPs implies that t
Externí odkaz:
https://doaj.org/article/f38de3b62093425fb82ae6afc0e85982
Autor:
Diana Campelo, Thomas Lautier, Philippe Urban, Francisco Esteves, Sophie Bozonnet, Gilles Truan, Michel Kranendonk
Publikováno v:
Frontiers in Pharmacology, Vol 9 (2018)
Externí odkaz:
https://doaj.org/article/d0cd274b52a4418d9e0aa7aee26dcca0
Autor:
Diana Campelo, Thomas Lautier, Philippe Urban, Francisco Esteves, Sophie Bozonnet, Gilles Truan, Michel Kranendonk
Publikováno v:
Frontiers in Pharmacology, Vol 8 (2017)
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 domain (acceptor reduction), a linker (hinge), and
Externí odkaz:
https://doaj.org/article/f1ca40c81625441f975697aa2d133102
Autor:
Diana Campelo, Francisco Esteves, Bernardo Brito Palma, Bruno Costa Gomes, José Rueff, Thomas Lautier, Philippe Urban, Gilles Truan, Michel Kranendonk
Publikováno v:
International Journal of Molecular Sciences, Vol 19, Iss 12, p 3914 (2018)
NADPH-cytochrome P450 reductase (CPR) is the unique redox partner of microsomal cytochrome P450s (CYPs). CPR exists in a conformational equilibrium between open and closed conformations throughout its electron transfer (ET) function. Previously, we h
Externí odkaz:
https://doaj.org/article/58d027accb66413d9058ceea5e4463bd
Publikováno v:
International Journal of Molecular Sciences, Vol 19, Iss 6, p 1617 (2018)
Quantitative structure-activity relationships may bring invaluable information on structural elements of both enzymes and substrates that, together, govern substrate specificity. Buried active sites in cytochrome P450 enzymes are connected to the sol
Externí odkaz:
https://doaj.org/article/00245c6d415a487c88643e3d8bf97686