Zobrazeno 1 - 10
of 17
pro vyhledávání: '"Ashley C. Campbell"'
Autor:
Alice-Roza Eruera, Alice M. McSweeney, Geena M. McKenzie-Goldsmith, Helen K. Opel-Reading, Simone X. Thomas, Ashley C. Campbell, Louise Stubbing, Andrew Siow, Jonathan G. Hubert, Margaret A. Brimble, Vernon K. Ward, Kurt L. Krause
Publikováno v:
Viruses, Vol 15, Iss 11, p 2202 (2023)
Norovirus is the leading cause of viral gastroenteritis worldwide, and there are no approved vaccines or therapeutic treatments for chronic or severe norovirus infections. The structural characterisation of the norovirus protease and drug development
Externí odkaz:
https://doaj.org/article/86ca3c78c4f045989589594a543e6b57
Publikováno v:
Viruses, Vol 13, Iss 10, p 1893 (2021)
Influenza virus is a highly contagious virus that causes significant human mortality and morbidity annually. The most effective drugs for treating influenza are the neuraminidase inhibitors, but resistance to these inhibitors has emerged, and additio
Externí odkaz:
https://doaj.org/article/bf364fc05993415b84fbc0e685dc5f1d
Autor:
Ashley C. Campbell, Thomas P. Quinn, Austin R. Prater, Alexandra N. Bogner, Kent S. Gates, Donald F. Becker, John J. Tanner
Publikováno v:
ACS Chem Biol
Proline dehydrogenase (PRODH) is a flavoenzyme that catalyzes the first step of proline catabolism, the oxidation of L-proline to Δ(1)-pyrroline-5-carboxylate. PRODH has emerged as a cancer therapy target because of its involvement in the metabolic
Autor:
Sophie LeBlanc, Jonathan P. Schuermann, Ashley C. Campbell, Han G. Nam, Hannah Valentino, Nazneen Sultana, Pablo Sobrado, John J. Tanner
Publikováno v:
J Biol Chem
Allicin is a component of the characteristic smell and flavor of garlic (Allium sativum). A flavin-containing monooxygenase (FMO) produced by A. sativum (AsFMO) was previously proposed to oxidize S-allyl-l-cysteine (SAC) to alliin, an allicin precurs
Publikováno v:
Arch Biochem Biophys
Proline utilization A (PutA) proteins are bifunctional proline catabolic enzymes that catalyze the 4-electron oxidation of L-proline to L-glutamate using spatially-separated proline dehydrogenase and L-glutamate-γ-semialdehyde dehydrogenase (GSALDH,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dd55e098f98ed0f5667be0c22fdb4546
https://europepmc.org/articles/PMC7856085/
https://europepmc.org/articles/PMC7856085/
The ornithine hydroxylase known as SidA is a class B flavin monooxygenase that catalyzes the first step in the biosynthesis of hydroxamate-containing siderophores in Aspergillus fumigatus. Crystallographic studies of SidA revealed that the FAD underg
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a3f674109addec67d0db17f8c9e1e237
https://hdl.handle.net/10919/107583
https://hdl.handle.net/10919/107583
Autor:
Ritcha Mehra-Chaudhary, Pablo Sobrado, Kyle M. Stiers, Julia S. Martin del Campo, John J. Tanner, Ashley C. Campbell
The siderophore biosynthetic enzyme A (SidA) ornithine hydroxylase fromAspergillus fumigatusis a fungal disease drug target involved in the production of hydroxamate-containing siderophores, which are used by the pathogen to sequester iron. SidA is a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5f4e759ca3d9260cff67d8f54bfcbeb9
https://hdl.handle.net/10919/102380
https://hdl.handle.net/10919/102380
Autor:
Ashley C, Campbell, Kyle M, Stiers, Julia S, Martin Del Campo, Ritcha, Mehra-Chaudhary, Pablo, Sobrado, John J, Tanner
Publikováno v:
J Biol Chem
The siderophore biosynthetic enzyme A (SidA) ornithine hydroxylase from Aspergillus fumigatus is a fungal disease drug target involved in the production of hydroxamate-containing siderophores, which are used by the pathogen to sequester iron. SidA is
Publikováno v:
ACS Chem Biol
Proline dehydrogenase (PRODH) catalyzes the first step of proline catabolism, the FAD-dependent 2-electron oxidation of l-proline to Δ(1)-pyrroline-5-carboxylate. PRODH has emerged as a possible cancer therapy target, and thus the inhibition of PROD
Autor:
Ashley C. Campbell, Pablo Sobrado, Yumin Dai, Karina Kizjakina, David A. Korasick, John J. Tanner
Publikováno v:
ChemBioChem. 19:53-57
The flavin-dependent enzyme 2-haloacrylate hydratase (2-HAH) catalyzes the conversion of 2-chloroacrylate, a major component in the manufacture of acrylic polymers, to pyruvate. The enzyme was expressed in Escherichia coli, purified, and characterize