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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 kinase

International Journal of Biochemistry and Cell Biology, 1997
Fumio Sakane, Hideo Kanoh
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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, phosphatidic acid, and the converting enzyme, diacylglycerol kinase, in the nucleus

Biochimica Et Biophysica Acta - Molecular and Cell Biology of Lipids, 2006
There exists phosphoinositide (PI) cycle in the nucleus, which is operated differentially from the classical PI cycle at the plasma membrane. Evidence has been accumulated that nuclear PIs and the related enzymes are closely involved in a variety of nuclear processes, although the details remain to be elucidated. In this mini review, some components of
Kaoru Gotō, Yasukazu Hozumi
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Properties and functions of diacylglycerol kinases

Cellular Signalling, 2000
Diacylglycerol kinases (DGKs) phosphorylate the second-messenger diacylglycerol (DAG) to phosphatidic acid (PA). The family of DGKs is well conserved among most species. Nine mammalian isotypes have been identified, and are classified into five subgroups based on their primary structure.
W J, van Blitterswijk, B, Houssa
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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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An endogenous regulator of diacylglycerol kinase

Biochemical and Biophysical Research Communications, 1988
During the initial steps of the subcellular fractionation of rat brain homogenate, we recovered more than 100% of diacylglycerol kinase activity. The unusually high yields prompted us to examine the possibility that we had removed an endogenous inhibitor from diacylglycerol kinase during those steps.
I M, Jeng, N, Klemm, C Z, Wu
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Diacylglycerol kinase

1996
Abstract Diacylglycerol kinase (DGK) reverses the normal flow of phospholipid biosynthesis by phosphory/ating diacylglycerol back to phosphatidic acid. DGK consists of a number of isozymes with different enzymological properties. The three isozymes so far sequenced, however, share highly conserved regions including two sets each of EF-
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