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Q28139174-372C5FA4-D2C7-4642-95A7-AC8E5B48C44C
Q28139174-372C5FA4-D2C7-4642-95A7-AC8E5B48C44C
BestRank
Statement
http://www.wikidata.org/entity/statement/Q28139174-372C5FA4-D2C7-4642-95A7-AC8E5B48C44C
Regulation of protein kinase D by multisite phosphorylation. Identification of phosphorylation sites by mass spectrometry and characterization by site-directed mutagenesis
P2860
Q28139174-372C5FA4-D2C7-4642-95A7-AC8E5B48C44C
BestRank
Statement
http://www.wikidata.org/entity/statement/Q28139174-372C5FA4-D2C7-4642-95A7-AC8E5B48C44C
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wasDerivedFrom
85ea481e6b08e05e6ca9fd108b9f5dabcfae32bc
P2860
The pleckstrin homology domain of protein kinase D interacts preferentially with the eta isoform of protein kinase C