Primary Literature
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- Park Y, et al. (2022) Mutant phosphatidate phosphatase Pah1-W637A exhibits altered phosphorylation, membrane association, and enzyme function in yeast. J Biol Chem 298(2):101578 PMID: 35026226
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- Mirheydari M, et al. (2020) The Spo7 sequence LLI is required for Nem1-Spo7/Pah1 phosphatase cascade function in yeast lipid metabolism. J Biol Chem 295(33):11473-11485 PMID: 32527729
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- Hsieh LS, et al. (2015) Phosphorylation regulates the ubiquitin-independent degradation of yeast Pah1 phosphatidate phosphatase by the 20S proteasome. J Biol Chem 290(18):11467-78 PMID: 25809482
- Su WM, et al. (2014) Yeast Nem1-Spo7 protein phosphatase activity on Pah1 phosphatidate phosphatase is specific for the Pho85-Pho80 protein kinase phosphorylation sites. J Biol Chem 289(50):34699-708 PMID: 25359770
- Viner R, et al. (2012) Identification of two Legionella pneumophila effectors that manipulate host phospholipids biosynthesis. PLoS Pathog 8(11):e1002988 PMID: 23133385
- Siniossoglou S, et al. (1998) A novel complex of membrane proteins required for formation of a spherical nucleus. EMBO J 17(22):6449-64 PMID: 9822591