Zobrazeno 1 - 10
of 14
pro vyhledávání: '"John de Widt"'
Autor:
Ila van Kruijsbergen, Monique P. C. Mulder, Michael Uckelmann, Tibor van Welsem, John de Widt, Aldo Spanjaard, Heinz Jacobs, Farid El Oualid, Huib Ovaa, Fred van Leeuwen
Publikováno v:
Frontiers in Chemistry, Vol 8 (2020)
Protein ubiquitination is a key post-translational modification regulating a wide range of biological processes. Ubiquitination involves the covalent attachment of the small protein ubiquitin to a lysine of a protein substrate. In addition to its wel
Externí odkaz:
https://doaj.org/article/96f73bcacfac4bcd927a6cd4d515cee0
Autor:
Nullin Divecha, Fabian P. Vinke, John de Widt, Alrik P. Los, Wim J. van Blitterswijk, Matthew K. Topham
Publikováno v:
Journal of Biological Chemistry. 281:858-866
The retinoblastoma protein (pRB) is a tumor suppressor and key regulator of the cell cycle. We have previously shown that pRB interacts with phosphatidylinositol-4-phosphate 5-kinases, lipid kinases that can regulate phosphatidylinositol 4,5-bisphosp
Publikováno v:
Journal of Biological Chemistry. 280:9870-9878
Diacylglycerol kinase (DGK) phosphorylates the second messenger diacylglycerol (DAG) to phosphatidic acid. We previously identified DGK as one of nine mammalian DGK isoforms and reported on its regulation by interaction with RhoA and by translocation
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids. 1636:169-174
Diacylglycerol kinase (DGK) phosphorylates the second messenger diacylglycerol (DAG) to phosphatidic acid (PA). Among the nine mammalian isotypes identified, DGKtheta is the only one with three cysteine-rich domains (CRDs) (instead of two) in its N-t
Publikováno v:
International Journal of Biochemistry and Cell Biology 44 (2012) 11
International Journal of Biochemistry and Cell Biology, 44(11), 1791-1799
International Journal of Biochemistry and Cell Biology, 44(11), 1791-1799
Epidermal growth factor receptor (EGFR) activation is negatively regulated by protein kinase C (PKC) signaling. Stimulation of A431 cells with EGF, bradykinin or UTP increased EGFR phosphorylation at Thr654 in a PKC-dependent manner. Inhibition of PK
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ec3b1924ec98e43fa1873dae6dcdde9e
https://research.wur.nl/en/publications/diacylglycerol-kinase-counteracts-protein-kinase-c-mediated-inact
https://research.wur.nl/en/publications/diacylglycerol-kinase-counteracts-protein-kinase-c-mediated-inact
Publikováno v:
Journal of Biological Chemistry. 274:6820-6822
Diacylglycerol kinase (DGK) phosphorylates the second messenger diacylglycerol to yield phosphatidic acid. To date, very little is known about the regulation of DGK activity. We have previously identified the DGKtheta isotype, which is predominantly
Publikováno v:
Advances in enzyme regulation. 48
Autor:
Rob van der Bend, Jose van Damme, Hidde L. Ploegh, Jose van der Wal, Dick Schaap, Joël Vandekerckhove, Detlef Gussow, John de Widt, Whim J. van Blitterswijk
Publikováno v:
FEBS Letters. 275:151-158
Diacylglycerol (DG) kinase attenuates the level of the second messenger DG in signal transduction, and therefore possibly modulates protein kinase C (PKC). DG kinase was purified to homogeneity from human white blood cells, showing an M1 of 86 kDa as
Publikováno v:
Biochimica et biophysica acta. 1773(3)
We previously showed that the retinoblastoma protein (pRB), a key regulator of G1 to S-phase transition of the cell cycle, binds to and stimulates diacylglycerol kinase-zeta (DGKzeta) to phosphorylate the lipid second messenger diacylglycerol into ph
Autor:
Francisco J.G. Muriana, Marc C.M. van Dijk, John de Widt, Henk Hilkmann, Wim J. van Blitterswijk
Publikováno v:
The Journal of biological chemistry. 272(17)
The role of phosphatidylcholine (PC) hydrolysis in activation of the mitogen-activated protein kinase (MAPK) pathway by platelet-derived growth factor (PDGF) was studied in Rat-1 fibroblasts. PDGF induced the transient formation of phosphatidic acid,