| Year |
Citation |
Score |
| 2019 |
Hassaninasab A, Hsieh LS, Su WM, Han GS, Carman GM. Yck1 casein kinase I regulates the activity and phosphorylation of Pah1 phosphatidate phosphatase from . The Journal of Biological Chemistry. PMID 31645435 DOI: 10.1074/Jbc.Ra119.011314 |
0.785 |
|
| 2019 |
Dey P, Su WM, Mirheydari M, Han GS, Carman GM. Protein kinase C mediates the phosphorylation of the Nem1-Spo7 protein phosphatase complex in yeast. The Journal of Biological Chemistry. PMID 31501244 DOI: 10.1074/Jbc.Ra119.010592 |
0.795 |
|
| 2018 |
Su WM, Han GS, Dey P, Carman GM. Protein kinase A phosphorylates the Nem1-Spo7 protein phosphatase complex that regulates the phosphorylation state of the phosphatidate phosphatase Pah1 in yeast. The Journal of Biological Chemistry. PMID 30201607 DOI: 10.1074/Jbc.Ra118.005348 |
0.799 |
|
| 2017 |
Dey P, Su WM, Han GS, Carman GM. Phosphorylation of lipid metabolic enzymes by yeast Pkc1 protein kinase C requires phosphatidylserine and diacylglycerol. Journal of Lipid Research. PMID 28154205 DOI: 10.1194/Jlr.M075036 |
0.73 |
|
| 2016 |
Hsieh LS, Su WM, Han GS, Carman GM. Phosphorylation of Yeast Pah1 Phosphatidate Phosphatase by Casein Kinase II Regulates Its Function in Lipid Metabolism. The Journal of Biological Chemistry. PMID 27044741 DOI: 10.1074/Jbc.M116.726588 |
0.787 |
|
| 2015 |
Barbosa AD, Sembongi H, Su WM, Abreu S, Reggiori F, Carman GM, Siniossoglou S. Lipid partitioning at the nuclear envelope controls membrane biogenesis. Molecular Biology of the Cell. 26: 3641-57. PMID 26269581 DOI: 10.1091/Mbc.E15-03-0173 |
0.552 |
|
| 2015 |
Hsieh LS, Su WM, Han GS, Carman GM. Phosphorylation regulates the ubiquitin-independent degradation of yeast Pah1 phosphatidate phosphatase by the 20S proteasome. The Journal of Biological Chemistry. 290: 11467-78. PMID 25809482 DOI: 10.1074/Jbc.M115.648659 |
0.671 |
|
| 2014 |
Su WM, Han GS, Carman GM. Yeast Nem1-Spo7 protein phosphatase activity on Pah1 phosphatidate phosphatase is specific for the Pho85-Pho80 protein kinase phosphorylation sites. The Journal of Biological Chemistry. 289: 34699-708. PMID 25359770 DOI: 10.1074/Jbc.M114.614883 |
0.761 |
|
| 2014 |
Su WM, Han GS, Carman GM. Cross-talk phosphorylations by protein kinase C and Pho85p-Pho80p protein kinase regulate Pah1p phosphatidate phosphatase abundance in Saccharomyces cerevisiae. The Journal of Biological Chemistry. 289: 18818-30. PMID 24876385 DOI: 10.1074/Jbc.M114.581462 |
0.771 |
|
| 2014 |
Cui Y, Sun YW, Lin HS, Su WM, Fang Y, Zhao Y, Wei XQ, Qin YH, Kohama K, Gao Y. Platelet-derived growth factor-BB induces matrix metalloproteinase-2 expression and rat vascular smooth muscle cell migration via ROCK and ERK/p38 MAPK pathways. Molecular and Cellular Biochemistry. 393: 255-63. PMID 24792035 DOI: 10.1007/s11010-014-2068-5 |
0.388 |
|
| 2012 |
Su WM, Han GS, Casciano J, Carman GM. Protein kinase A-mediated phosphorylation of Pah1p phosphatidate phosphatase functions in conjunction with the Pho85p-Pho80p and Cdc28p-cyclin B kinases to regulate lipid synthesis in yeast. The Journal of Biological Chemistry. 287: 33364-76. PMID 22865862 DOI: 10.1074/Jbc.M112.402339 |
0.768 |
|
| 2012 |
Choi HS, Su WM, Han GS, Plote D, Xu Z, Carman GM. Pho85p-Pho80p phosphorylation of yeast Pah1p phosphatidate phosphatase regulates its activity, location, abundance, and function in lipid metabolism. The Journal of Biological Chemistry. 287: 11290-301. PMID 22334681 DOI: 10.1074/Jbc.M112.346023 |
0.772 |
|
| 2012 |
Xu Z, Su WM, Carman GM. Fluorescence spectroscopy measures yeast PAH1-encoded phosphatidate phosphatase interaction with liposome membranes. Journal of Lipid Research. 53: 522-8. PMID 22180632 DOI: 10.1194/Jlr.M022798 |
0.621 |
|
| 2011 |
Choi HS, Su WM, Morgan JM, Han GS, Xu Z, Karanasios E, Siniossoglou S, Carman GM. Phosphorylation of phosphatidate phosphatase regulates its membrane association and physiological functions in Saccharomyces cerevisiae: identification of SER(602), THR(723), AND SER(744) as the sites phosphorylated by CDC28 (CDK1)-encoded cyclin-dependent kinase. The Journal of Biological Chemistry. 286: 1486-98. PMID 21081492 DOI: 10.1074/Jbc.M110.155598 |
0.756 |
|
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