Amelia R. Brasnett

Oxford, ENG, United Kingdom

Last Updated: 09/26/2026

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Found 8 publications

Structural basis of the promiscuity of the unusual Fe(II) and 2-oxoglutarate dependent human aspartate/asparagine-β-hydroxylase.

Structural basis of the promiscuity of the unusual Fe(II) and 2-oxoglutarate dependent human aspartate/asparagine-β-hydroxylase.

Journal: Nature communications

Published: August 30, 2025

Structural and functional consequences of aspartate/asparagine-β-hydroxylase variants causing Traboulsi syndrome.

Structural and functional consequences of aspartate/asparagine-β-hydroxylase variants causing Traboulsi syndrome.

Journal: The Journal of biological chemistry

Published: June 19, 2025

Methods for production and assaying catalysis of isolated recombinant human aspartate/asparagine-β-hydroxylase.

Methods for production and assaying catalysis of isolated recombinant human aspartate/asparagine-β-hydroxylase.

Journal: Methods in enzymology

Published: September 20, 2024

Structure-guided optimisation of N-hydroxythiazole-derived inhibitors of factor inhibiting hypoxia-inducible factor-α.

Structure-guided optimisation of N-hydroxythiazole-derived inhibitors of factor inhibiting hypoxia-inducible factor-α.

Journal: Chemical science

Published: August 14, 2023

The crystalline state as a dynamic system: IR microspectroscopy under electrochemical control for a [NiFe] hydrogenase.

The crystalline state as a dynamic system: IR microspectroscopy under electrochemical control for a [NiFe] hydrogenase.

Journal: Chemical science

Published: March 26, 2021

Rubisco Adaptation Is More Limited by Phylogenetic Constraint Than by Catalytic Trade-off.

Rubisco Adaptation Is More Limited by Phylogenetic Constraint Than by Catalytic Trade-off.

Journal: Molecular biology and evolution

Published: March 19, 2021

Human Oxygenase Variants Employing a Single Protein FeII Ligand Are Catalytically Active.

Human Oxygenase Variants Employing a Single Protein FeII Ligand Are Catalytically Active.

Journal: Angewandte Chemie (International ed. in English)

Published: March 15, 2021

Human Oxygenase Variants Employing a Single Protein FeII Ligand Are Catalytically Active.

Human Oxygenase Variants Employing a Single Protein FeII Ligand Are Catalytically Active.

Journal: Angewandte Chemie (Weinheim an der Bergstrasse, Germany)

Published: March 15, 2021

Showing 1-8 of 8

Last Updated: 09/26/2026