JMJD5 is a human arginyl C-3 hydroxylase.

Wilkins, Sarah E; Islam, Saif; Gannon, Joan M; Markolovic, Suzana; Hopkinson, Richard J; Ge, Wei; Schofield, Christopher J; Chowdhury, Rasheduzzaman

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Authors

Wilkins, Sarah E

Islam, Saif

Gannon, Joan M

Markolovic, Suzana

Hopkinson, Richard J

Ge, Wei

Schofield, Christopher J

Publication Date

2018-03-21

Journal Title

Nature communications

ISSN

2041-1723

Volume

Issue

Pages

1180

Language

eng

Type

Article

This Version

VoR

Physical Medium

Electronic

Metadata

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Citation

Wilkins, S. E., Islam, S., Gannon, J. M., Markolovic, S., Hopkinson, R. J., Ge, W., Schofield, C. J., & et al. (2018). JMJD5 is a human arginyl C-3 hydroxylase.. Nature communications, 9 (1), 1180. https://doi.org/10.1038/s41467-018-03410-w

Keywords

Humans, Escherichia coli, Arginine, Lysine, Carrier Proteins, Membrane Proteins, Recombinant Proteins, Ribosomal Protein S6, Crystallography, X-Ray, Cloning, Molecular, Gene Expression, Catalytic Domain, Protein Binding, Protein Folding, Substrate Specificity, Hydroxylation, Kinetics, Genetic Vectors, Stereoisomerism, Thermodynamics, Models, Molecular, Protein Interaction Domains and Motifs, Histone Demethylases, Protein Conformation, alpha-Helical, Protein Conformation, beta-Strand

Identifiers

External DOI: https://doi.org/10.1038/s41467-018-03410-w

This record's URL: https://www.repository.cam.ac.uk/handle/1810/307333

Rights

Attribution 4.0 International

Licence URL: https://creativecommons.org/licenses/by/4.0/

Except where otherwise noted, this item's licence is described as Attribution 4.0 International