Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Ingrid C. Northwood"'
Publikováno v:
Trends in Biochemical Sciences. 25:441-447
Phosphatidylcholine (PC) synthesis in animal cells is generally controlled by cytidine 5'-triphosphate (CTP):phosphocholine cytidylyltransferase (CCT). This enzyme is amphitropic, that is, it can interconvert between a soluble inactive form and a mem
Autor:
Adrienne E. Drobnies, Bryan Crawford, Ingrid C. Northwood, Amy H.Y. Tong, Rosemary B. Cornell
Publikováno v:
Journal of Biological Chemistry. 274:26240-26248
The transition from quiescence (G(0)) into the cell division cycle is marked by accelerated phospholipid turnover. We examined the rates of phosphatidylcholine (PC) synthesis and the activity, membrane affinity, and intracellular localization of the
Autor:
Tom Curran, Alpna Seth, Debra A. Latour, Cory Abate, Roger J. Davis, Ingrid C. Northwood, Elvira Alvarez, Fernando A. Gonzalez
Publikováno v:
Journal of Biological Chemistry. 266:15277-15285
A growth factor-stimulated (MAP2-related) protein kinase, ERT, that phosphorylates the epidermal growth factor receptor at Thr669 has been purified from KB human tumor cells by Northwood and co-workers (Northwood, I. C., Gonzalez, F. A., Wartmann, M.
Publikováno v:
Journal of Biological Chemistry. 266:15266-15276
A growth factor-stimulated protein kinase activity that phosphorylates the epidermal growth factor (EGF) receptor at Thr669 has been described (Countaway, J. L., Northwood, I. C., and Davis, R. J. (1989) J. Biol. Chem. 264, 10828-10835). Anion-exchan
Autor:
Ingrid C. Northwood, Roger J. Davis
Publikováno v:
Journal of Biological Chemistry. 263:7450-7453
The epidermal growth factor (EGF) receptor exists in a monomeric (170 kDa) form and in several aggregated states (360 kDa, greater than 500 kDa). The hypothesis that the oligomerization of the receptor is required for the stimulation of the kinase wa
Publikováno v:
Journal of Biological Chemistry. 264:10828-10835
The major site of phosphorylation of the epidermal growth factor (EGF) receptor after treatment of cells with EGF is threonine 669. Phosphorylation of this site is also associated with the transmodulation of the EGF receptor caused by platelet-derive
Autor:
Roger J. Davis, Ingrid C. Northwood
Publikováno v:
Journal of Biological Chemistry. 264:5746-5750
Treatment of A431 human epidermoid carcinoma cells with 4-phorbol 12-myristate 13-acetate (PMA) causes an inhibition of the high affinity binding of epidermal growth factor (EGF) to cell surface receptors and an inhibition of the EGF receptor tyrosin