Becky Tu-Sekine, Ph.D.
Affiliations: | 2006 | Johns Hopkins University, Baltimore, MD |
Area:
Biochemistry, Molecular Biology, Cell BiologyGoogle:
"Becky Tu-Sekine"Mean distance: (not calculated yet)
Parents
Sign in to add mentorDaniel M. Raben | grad student | 2006 | Johns Hopkins | |
(Investigation into the regulation and function of diacylglycerol kinase theta.) |
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Publications
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Tu-Sekine B, Goldschmidt HL, Raben DM. (2016) DGK-θ: Structure, Enzymology, and Physiological Roles. Frontiers in Cell and Developmental Biology. 4: 101 |
Sangster-Guity N, Tu-Sekine B, Raben DM, et al. (2016) Mutational analysis of prostate-specific antigen defines the intrinsic proteolytic activity of the proPSA zymogen. The Prostate |
Goldschmidt HL, Tu-Sekine B, Volk L, et al. (2015) DGKθ Catalytic Activity Is Required for Efficient Recycling of Presynaptic Vesicles at Excitatory Synapses. Cell Reports |
Tu-Sekine B, Goldschmidt H, Raben DM. (2015) Diacylglycerol, phosphatidic acid, and their metabolic enzymes in synaptic vesicle recycling. Advances in Biological Regulation. 57: 147-52 |
Ueda S, Tu-Sekine B, Yamanoue M, et al. (2013) The expression of diacylglycerol kinase theta during the organogenesis of mouse embryos. Bmc Developmental Biology. 13: 35 |
Bolduc D, Rahdar M, Tu-Sekine B, et al. (2013) Phosphorylation-mediated PTEN conformational closure and deactivation revealed with protein semisynthesis. Elife. 2: e00691 |
Tu-Sekine B, Goldschmidt H, Petro E, et al. (2013) Diacylglycerol kinase θ: regulation and stability. Advances in Biological Regulation. 53: 118-26 |
Bolduc D, Rahdar M, Tu-Sekine B, et al. (2013) Author response: Phosphorylation-mediated PTEN conformational closure and deactivation revealed with protein semisynthesis Elife |
Tu-Sekine B, Raben DM. (2012) Dual regulation of diacylglycerol kinase (DGK)-θ: polybasic proteins promote activation by phospholipids and increase substrate affinity. The Journal of Biological Chemistry. 287: 41619-27 |
Tu-Sekine B, Raben DM. (2011) Regulation and roles of neuronal diacylglycerol kinases: a lipid perspective. Critical Reviews in Biochemistry and Molecular Biology. 46: 353-64 |