about
Cardiac myosin binding protein C: its role in physiology and diseaseEvidence for the slow reaction of hypoxia-inducible factor prolyl hydroxylase 2 with oxygenStudies on the reaction of nitric oxide with the hypoxia-inducible factor prolyl hydroxylase domain 2 (EGLN1)Support for a trimeric collar of myosin binding protein C in cardiac and fast skeletal muscle, but not in slow skeletal muscleOGFOD1 catalyzes prolyl hydroxylation of RPS23 and is involved in translation control and stress granule formationCellular oxygen sensing: Crystal structure of hypoxia-inducible factor prolyl hydroxylase (PHD2)Studies on the activity of the hypoxia-inducible-factor hydroxylases using an oxygen consumption assayLocalization of the binding site of the C-terminal domain of cardiac myosin-binding protein-C on the myosin rodCatalytic strategies of the non-heme iron dependent oxygenases and their roles in plant biologyEpigenetic regulation by histone demethylases in hypoxiaCrystal structure of the C1 domain of cardiac myosin binding protein-C: implications for hypertrophic cardiomyopathyStructural basis for binding of hypoxia-inducible factor to the oxygen-sensing prolyl hydroxylasesInvestigating the contribution of the active site environment to the slow reaction of hypoxia-inducible factor prolyl hydroxylase domain 2 with oxygenUse of ferrous iron by metallo-β-lactamasesHypoxia-inducible factor prolyl hydroxylase 2 has a high affinity for ferrous iron and 2-oxoglutaratePlant cysteine oxidases are dioxygenases that directly enable arginyl transferase-catalysed arginylation of N-end rule targets.Application of a proteolysis/mass spectrometry method for investigating the effects of inhibitors on hydroxylase structure.Identification of novel interactions between domains of Myosin binding protein-C that are modulated by hypertrophic cardiomyopathy missense mutations.Kinetic rationale for selectivity toward N- and C-terminal oxygen-dependent degradation domain substrates mediated by a loop region of hypoxia-inducible factor prolyl hydroxylases.Evidence for a stereoelectronic effect in human oxygen sensing.Direct analysis of enzyme-catalyzed DNA demethylation.Use of mass spectrometry to probe the nucleophilicity of cysteinyl residues of prolyl hydroxylase domain 2.Using NMR solvent water relaxation to investigate metalloenzyme-ligand binding interactions.Investigating the dependence of the hypoxia-inducible factor hydroxylases (factor inhibiting HIF and prolyl hydroxylase domain 2) on ascorbate and other reducing agents.Ribonucleotide Reductase Requires Subunit Switching in Hypoxia to Maintain DNA ReplicationBiochemical characterization of New Delhi metallo-β-lactamase variants reveals differences in protein stability.Kinetic Investigations of the Role of Factor Inhibiting Hypoxia-inducible Factor (FIH) as an Oxygen Sensor.OS-9: another piece in the HIF complex story.Structure and Mechanism of a Viral Collagen Prolyl HydroxylaseSecondary binding sites for triplex-forming oligonucleotides containing bulges, loops, and mismatches in the third strand.Non-enzymatic chemistry enables 2-hydroxyglutarate-mediated activation of 2-oxoglutarate oxygenases.The Activity of JmjC Histone Lysine Demethylase KDM4A is Highly Sensitive to Oxygen Concentrations.Dynamic states of the DNA repair enzyme AlkB regulate product release.Studying the active-site loop movement of the São Paolo metallo-β-lactamase-1†Electronic supplementary information (ESI) available: Procedures for protein expression and purification, 19F-labelling, crystallisation, data collection, and structure deStudies on the Interaction of the Histone Demethylase KDM5B with Tricarboxylic Acid Cycle Intermediates.Investigations on the oxygen dependence of a 2-oxoglutarate histone demethylase.ESI-MS studies on prolyl hydroxylase domain 2 reveal a new metal binding site.Lysine-241 has a role in coupling 2OG turnover with substrate oxidation during KDM4-catalysed histone demethylation.Molecular and cellular mechanisms of HIF prolyl hydroxylase inhibitors in clinical trials.YcfDRM is a thermophilic oxygen-dependent ribosomal protein uL16 oxygenase.
P50
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P50
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chemist
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Emily Flashman
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Emily Flashman
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Emily Flashman
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Emily Flashman
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Emily Flashman
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Emily Flashman
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Emily Flashman
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Emily Flashman
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Emily Flashman
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Emily Flashman
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Emily G. Flashman
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Emily Gudrun Flashman
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Emily Flashman
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Emily Flashman
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Emily Flashman
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Emily Flashman
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0000 0001 3468 4015
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P496
0000-0002-4169-4278