Results 251 to 260 of about 76,688 (279)

Design and synthesis of protein kinase C epsilon selective diacylglycerol lactones (DAG-lactones)

, 2014
Jihyae Ann, Suyoung Yoon, Jisoo Baek, Da Hye Kim, Nancy E. Lewin, Colin Hill, Peter M. Blumberg, Jeewoo Lee   +7 more
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Evidence for discrete diacylglycerol and phorbol ester activator sites on protein kinase C. Differences in effects of 1-alkanol inhibition, activation by phosphatidylethanolamine and calcium chelation.

, 1994
Simon J. Slater, Mary Beth Kelly, Frank J. Taddeo, Emanuel Rubin, Christopher D. Stubbs   +4 more
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Immunological characterization of sn-1,2-diacylglycerol and sn-2-monoacylglycerol kinase from pig brain.

, 1986
Hideo Kanoh, Tomoko Iwata, Takashi Ono, Toshihiko Suzuki   +3 more
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Stereoselective Degradation of Diacylglycerol Kinases Potentiate T cell Activation and Tumor Cell Cytotoxicity

Minhaj Shaikh, Saktipada Mookherjee, Claire C. Weckerly, Adam H. Libby, Aizhen Xiao, Yunge Zhao, Shailja Vaidya, AeRyon Kim, Zhihong Li, Madeleine L. Ware, Michelle Marants, Olivia Murtagh, Wesley J Wolfe, Timothy N. J. Bullock, Benjamin Purow, Gerald Hammond, Ken Y. Hsu   +16 more
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Referee report. For: Amodiaquine drug pressure selects nonsynonymous mutations in pantothenate kinase 1, diacylglycerol kinase, and phosphatidylinositol-4 kinase in Plasmodium berghei ANKA [version 3; peer review: 1 approved, 1 approved with reservations, 1 not approved]

Dina Coertzen
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Diacylglycerol kinases

Cellular Signalling, 2004
Diacylglycerol kinases (DGKs) phosphorylate diacylglycerol to form phosphatidic acid. In most cases, members of this large family of enzymes appear to bind and regulate proteins activated by either diacylglycerol or phosphatidic acid. Proteins that appear to be regulated, in part, by DGKs include protein kinase Cs, RasGRPs, and phosphatidylinositol ...
Bai, Luo, Debra S, Regier, Stephen M, Prescott, Matthew K, Topham   +3 more
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Diacylglycerol kinases in cancer

Advances in Biological Regulation, 2017
Diacylglycerol kinases (DGK) are a family of enzymes that catalyze the transformation of diacylglycerol into phosphatidic acid. In T lymphocytes, DGKα and ζ limit the activation of the PLCγ/Ras/ERK axis, providing a critical checkpoint to inhibit T cell responses. Upregulation of these isoforms limits Ras activation, leading to hypo-responsive, anergic
Isabel Mérida, Pedro Torres-Ayuso, Antonia Ávila-Flores, Javier Arranz-Nicolás, Elena Andrada, María Tello-Lafoz, Rosa Liébana, Raquel Arcos   +7 more
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Diacylglycerol Kinase

2009
Diacylglycerol kinase (DGK, EC 2.7.1.107) is a lipid kinase that phosphorylates diacylglycerol (DAG) to generate phosphatidic acid (PA). DGK belongs to a well-conserved family of proteins found in diverse species, such as Saccharomyces cerevisiae, Drosophila melanogaster, Caenorhabditis elegans, mammals, plants, and bacteria (Merida et al.
Arisz, S.A., Munnik, T.
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Diacylglycerol kinases in signal transduction

Chemistry and Physics of Lipids, 1999
Diacylglycerol kinase (DGK) phosphorylates the second messenger diacylglycerol (DAG) to phosphatidic acid. A family of nine mammalian isotypes have been identified. Their primary structure shows a diverse array of conserved domains, such as a catalytic domain, zinc fingers, pleckstrin homology domains and EF-hand structures, known to interact with ...
W J, van Blitterswijk, B, Houssa
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