Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Filippo Fiorentini"'
Publikováno v:
Biochemical Society Transactions
TRIM proteins form a protein family that is characterized by a conserved tripartite motif domain comprising a RING domain, one or two B-box domains and a coiled-coil region. Members of this large protein family are important regulators of numerous ce
Publikováno v:
Biochemistry. 60:3419-3421
Autor:
Andrea Mattevi, Filippo Fiorentini, Gautier Bailleul, Callum R. Nicoll, María Laura Mascotti, Marco W. Fraaije
Publikováno v:
Nature Structural & Molecular Biology, 27(1), 14-24. Nature Publishing Group
Nature Structural & Molecular Biology
Nature Structural & Molecular Biology
Flavin-containing monooxygenases (FMOs) are ubiquitous in all domains of life and metabolize a myriad of xenobiotics, including toxins, pesticides and drugs. However, despite their pharmacological importance, structural information remains bereft. To
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6ceb66ab202505c6149dc08967d70dec
https://research.rug.nl/en/publications/3511387e-222d-4e47-8515-4b8bac4f4995
https://research.rug.nl/en/publications/3511387e-222d-4e47-8515-4b8bac4f4995
Autor:
Elvira Romero, Andrea Mattevi, Gautier Bailleul, Simone Savino, Nikola Lončar, Filippo Fiorentini, Marco W. Fraaije
Publikováno v:
Applied Microbiology and Biotechnology, 103(4), 1755-1764. SPRINGER
Applied Microbiology and Biotechnology
Applied Microbiology and Biotechnology
The flavin-containing monooxygenases (FMOs) play an important role in drug metabolism but they also have a high potential in industrial biotransformations. Among the hitherto characterized FMOs, there was no thermostable representative, while such bi
Autor:
Andrea Mattevi, María Laura Mascotti, Callum R. Nicoll, Gautier Bailleul, Filippo Fiorentini, Marco W. Fraaije
Publikováno v:
Nature Structural & Molecular Biology. 27:222-222
In the print and PDF versions of this article initially published, panel e was missing from Fig. 6. The error has been corrected in the PDF version of the article.(Figure presented.).
Autor:
Kurt Faber, Mélanie Hall, Martina Geier, Andrea Mattevi, Claudia Binda, Margit Winkler, Filippo Fiorentini
Publikováno v:
ACS chemical biology. 11(4)
Flavin-containing mono-oxygenases are known as potent drug-metabolizing enzymes, providing complementary functions to the well-investigated cytochrome P450 mono-oxygenases. While human FMO isoforms are typically involved in the oxidation of soft nucl
Publikováno v:
Current Opinion in Structural Biology
Current Opinion in Structural Biology, 59, 29-37
Current Opinion in Structural Biology, 59, 29-37
Monooxygenases (MOs) face the challenging reaction of an organic target, oxygen and a cofactor – most commonly heme or flavin. To correctly choreograph the substrates spatially and temporally, MOs evolved a variety of strategies, which involve stru