JMJD5 is a human arginyl C-3 hydroxylase.
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Authors
Wilkins, Sarah E
Gannon, Joan M
Markolovic, Suzana
Schofield, Christopher J
Publication Date
2018-03-21Journal Title
Nature communications
ISSN
2041-1723
Volume
9
Issue
1
Pages
1180
Language
eng
Type
Article
This Version
VoR
Physical Medium
Electronic
Metadata
Show full item recordCitation
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