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Q30175156-E64FBE9F-44E6-4A1F-954D-886E377BB228
Q30175156-E64FBE9F-44E6-4A1F-954D-886E377BB228
BestRank
Statement
http://www.wikidata.org/entity/statement/Q30175156-E64FBE9F-44E6-4A1F-954D-886E377BB228
Phosphorylation of dynamin I on Ser-795 by protein kinase C blocks its association with phospholipids.
P2860
Q30175156-E64FBE9F-44E6-4A1F-954D-886E377BB228
BestRank
Statement
http://www.wikidata.org/entity/statement/Q30175156-E64FBE9F-44E6-4A1F-954D-886E377BB228
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wasDerivedFrom
02d8f8fffd100d0f2293d35fb95a81f893202f29
P2860
The pleckstrin homology domain of protein kinase D interacts preferentially with the eta isoform of protein kinase C