The conserved domain in MORF proteins has distinct affinities to the PPR and E 
elements in PPR RNA editing factors

Bayer-Császár, Eszter; Haag, Sascha; Jörg, Anja; Glass, Franziska; Härtel, Barbara; Obata, T.; Meyer, E. H.; Brennicke, Axel; Takenaka, Mizuki

doi:https://doi.org/10.1016/j.bbagrm.2017.05.004

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The conserved domain in MORF proteins has distinct affinities to the PPR and E elements in PPR RNA editing factors

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Obata, T.
Central Metabolism, Department Willmitzer, Max Planck Institute of Molecular Plant Physiology, Max Planck Society;

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Meyer, E. H.
Organelle Biology and Biotechnology, Department Bock, Max Planck Institute of Molecular Plant Physiology, Max Planck Society;

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Bayer-Császár, E., Haag, S., Jörg, A., Glass, F., Härtel, B., Obata, T., et al. (2017). The conserved domain in MORF proteins has distinct affinities to the PPR and E elements in PPR RNA editing factors. Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms, 1860(8), 813-828. doi:https://doi.org/10.1016/j.bbagrm.2017.05.004.

Cite as: https://hdl.handle.net/11858/00-001M-0000-002D-6FC2-A

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