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- August 14, 2016.
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Author Information
- Mark D. White1,
- Maria Klecker2,3,
- Richard J. Hopkinson1,
- Daan Weits4,
- Carolin Mueller5,6,
- Christin Naumann2,3,
- Rebecca O’Neill1,
- James Wickens1,
- Tom N. Grossmann5,6,
- Nico Dissmeyer2,3,* and
- Emily Flashman1,*
- 1Chemistry Research Laboratory, University of Oxford, 12 Mansfield Road, Oxford, OX1 3TA, United Kingdom
- 2Independent Junior Research Group on Protein Recognition and Degradation, Leibniz Institute of Plant Biochemistry (IPB), Weinberg 3, D-06120 Halle (Saale), Germany
- 3ScienceCampus Halle – Plant-based Bioeconomy, Betty-Heimann-Str. 3, D-06120 Halle (Saale), Germany
- 4Institute of Biology I, RWTH Aachen University, Worringerweg 1, D-52074 Aachen, Germany
- 5Chemical Genomics Centre of the Max Planck Society, Department of Chemistry and Chemical Biology, Technische Universität Dortmund, Otto-Hahn-Str. 15, D-44227 Dortmund, Germany
- 6VU University Amsterdam, De Boelelaan 1083, 1081 HV Amsterdam, The Netherlands
- ↵*Corresponding authors: emily.flashman{at}chem.ox.ac.uk, +44(0)1865 275920 nico.dissmeyer{at}ipb-halle.de, ++49 (0) 345 5582 1710
Posted August 14, 2016.
Plant Cysteine Oxidases are Dioxygenases that Directly Enable Arginyl Transferase-Catalyzed Arginylation of N-End Rule Targets
