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  Arabidopsis AtDGK7, the smallest member of plant diacylglycerol kinases (DGKs), displays unique biochemical features and saturates at low substrate concentration - The DGK inhibitor R59022 differentially affects AtDGK2 and AtDGK7 activity in vitro and alters plant growth and development

Gomez-Merino, F. C., Arana-Ceballos, F. A., Trejo-Tellez, L. I., Skirycz, A., Brearley, C. A., Doermann, P., et al. (2005). Arabidopsis AtDGK7, the smallest member of plant diacylglycerol kinases (DGKs), displays unique biochemical features and saturates at low substrate concentration - The DGK inhibitor R59022 differentially affects AtDGK2 and AtDGK7 activity in vitro and alters plant growth and development. Journal of Biological Chemistry, 280(41), 34888-34899. doi:10.1074/jbc.M506859200.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0014-2BC4-A Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0014-2BC5-8
Genre: Journal Article

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Gomez-Merino-2005-Arabidopsis AtDGK7.pdf (Any fulltext), 806KB
 
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 Creators:
Gomez-Merino, F. C.1, Author
Arana-Ceballos, F. A.1, Author
Trejo-Tellez, L. I.1, Author
Skirycz, A.1, Author
Brearley, C. A.1, Author
Doermann, P.2, Author              
Mueller-Roeber, B.3, Author              
Affiliations:
1External Organizations, ou_persistent22              
2Plant Lipids, Department Willmitzer, Max Planck Institute of Molecular Plant Physiology, Max Planck Society, ou_1753347              
3Plant Signalling, Cooperative Research Groups, Max Planck Institute of Molecular Plant Physiology, Max Planck Society, ou_1753311              

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Free keywords: pleckstrin homology domain phosphatidic-acid phospholipase-c plasma-membrane rich region cells protein phosphatidylinositol accumulation thaliana
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Language(s): eng - English
 Dates: 2005-08-062005
 Publication Status: Published in print
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 Table of Contents: -
 Rev. Type: -
 Identifiers: ISI: ISI:000232403900061
DOI: 10.1074/jbc.M506859200
ISSN: 0021-9258 (Print) 0021-9258 (Linking)
URI: ://000232403900061 http://www.jbc.org/content/280/41/34888.full.pdf
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Title: Journal of Biological Chemistry
Source Genre: Journal
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Pages: - Volume / Issue: 280 (41) Sequence Number: - Start / End Page: 34888 - 34899 Identifier: -