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The FEBS Journal|January 27, 2015
Rationally engineered flavin-dependent oxidase reveals steric control of dioxygen reductionDomen Zafred, Barbara Steiner, Andrea R Teufelberger, et al.
Science (New York, N.Y.)|July 6, 2019
Conserved N-terminal cysteine dioxygenases transduce responses to hypoxia in animals and plantsNorma Masson, Thomas P Keeley, Beatrice Giuntoli, et al.
RSC Medicinal Chemistry|January 22, 2021
Monitoring protein-metal binding by 19F NMR - a case study with the New Delhi metallo-β-lactamase 1Anna M Rydzik, Jürgen Brem, Shane A Chandler, et al.
Hypoxia (Auckland, N.Z.)|December 7, 2018
Born to sense: biophysical analyses of the oxygen sensing prolyl hydroxylase from the simplest animal Trichoplax adhaerensKerstin Lippl, Anna Boleininger, Michael A McDonough, et al.
Chemical Science|December 19, 2015
Modulating carnitine levels by targeting its biosynthesis pathway - selective inhibition of γ-butyrobetaine hydroxylaseAnna M Rydzik, Rasheduzzaman Chowdhury, Grazyna T Kochan, et al.
FEBS Letters|August 30, 2018
Mechanistic and structural studies of KDM-catalysed demethylation of histone 1 isotype 4 at lysine 26Louise J Walport, Richard J Hopkinson, Rasheduzzaman Chowdhury, et al.
ACS Infectious Diseases|May 18, 2021
Structural Basis of Metallo-β-lactamase Inhibition by N-Sulfamoylpyrrole-2-carboxylatesAlistair J M Farley, Yuri Ermolovich, Karina Calvopiña, et al.
ACS Bio & Med Chem Au|October 25, 2022
Plant Cysteine Oxidase Oxygen-Sensing Function Is Conserved in Early Land Plants and AlgaeLeah J Taylor-Kearney, Samuel Madden, Jack Wilson, et al.
Proceedings of the National Academy of Sciences of the United States of America|September 2, 2020
Structures of Arabidopsis thaliana oxygen-sensing plant cysteine oxidases 4 and 5 enable targeted manipulation of their activityMark D White, Laura Dalle Carbonare, Mikel Lavilla Puerta, et al.
Bioorganic & Medicinal Chemistry Letters|July 23, 2003
2-oxoglutarate analogue inhibitors of HIF prolyl hydroxylaseDavid R Mole, Imre Schlemminger, Luke A McNeill, et al.
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