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

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:10.1016/j.bbagrm.2017.05.004.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002D-6FC2-A Version Permalink: http://hdl.handle.net/21.11116/0000-0004-46A7-1
Genre: Journal Article

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Bayer-Császár, Eszter1, Author
Haag, Sascha1, Author
Jörg, Anja1, Author
Glass, Franziska1, Author
Härtel, Barbara1, Author
Obata, T.2, Author              
Meyer, E. H.3, Author              
Brennicke, Axel1, Author
Takenaka, Mizuki1, Author
Affiliations:
1External Organizations, ou_persistent22              
2Central Metabolism, Department Willmitzer, Max Planck Institute of Molecular Plant Physiology, Max Planck Society, ou_1753339              
3Organelle Biology and Biotechnology, Department Bock, Max Planck Institute of Molecular Plant Physiology, Max Planck Society, ou_1753326              

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Free keywords: RNA editing
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Language(s): eng - English
 Dates: 2017
 Publication Status: Published in print
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 Rev. Method: -
 Identifiers: DOI: 10.1016/j.bbagrm.2017.05.004
BibTex Citekey: BayerCsászár2017813
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Title: Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms
Source Genre: Journal
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Pages: - Volume / Issue: 1860 (8) Sequence Number: - Start / End Page: 813 - 828 Identifier: ISSN: 1874-9399