ArticleMethods in molecular biology (Clifton, N.J.)2017
Characterizing PKA-Mediated Phosphorylation of Plexin Using Purified Proteins.
Article in Methods in molecular biology (Clifton, N.J.), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
2 citing papers in PubMed, 4 citations in OpenAlex.
- Effects of whole nutritional formula foods on nutritional improvement and intestinal flora in malnourished rats.Food science & nutrition · 2024Article
- Assaying Protein Kinase Activity with Radiolabeled ATP.Journal of visualized experiments : JoVE · 2017Article
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2 authors at 1 institution in 1 country.
Funding
Abstract
Protein phosphorylation is one of the widely used posttranslational modifications that alter protein function in vivo. We recently showed phosphorylation of Drosophila Plexin A by cyclic adenosine monophosphate (cAMP)-dependent protein kinase (PKA) and subsequent inhibition of plexin-mediated repulsive guidance. This phosphorylation occurs in the active site of the plexin GTPase-activating protein (GAP) domain, which in turn inhibits endogenous GAP activity toward Ras/Rap family small GTP-binding proteins by recruiting the phospho-serine/threonine-binding protein 14-3-3ε. Here we describe how phosphorylation of Plexin A can be detected and quantitated using an in vitro kinase assay and radioactive [γ-P
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