M. Wieprecht

Evidence for Phosphorylation of CTP:Phosphocholine Cytidylyltransferase by Multiple Proline-directed Protein Kinases (*)

T. Wieder, C. Orfanos, M. Wieprecht, 1996, The Journal of Biological Chemistry.

c-Ha-ras oncogene expression increases choline uptake, CTP: phosphocholine cytidylyltransferase activity and phosphatidylcholine biosynthesis in the immortalized human keratinocyte cell line HaCaT.

T. Wieder, C. Orfanos, M. Wieprecht, 1996, Biochimica et biophysica acta.

Identification of a putative membrane‐interacting domain of CTP: Phosphocholine cytidylyltransferase from rat liver

A. Becker, T. Wieder, C. Orfanos, 1994, FEBS letters.

The mitogen-activated protein kinases system (MAP kinase cascade): its role in skin signal transduction. A review.

C. Orfanos, M. Wieprecht, C. Geilen, 1996, Journal of dermatological science.

A selective inhibitor of cyclic AMP‐dependent protein kinase, N‐[2‐bromocinnamyl(amino)ethyl]‐5‐isoquinolinesulfonamide (H‐89), inhibits phosphatidylcholine biosynthesis in HeLa cells

W. Reutter, T. Wieder, M. Wieprecht, 1992, FEBS letters.

Growth factors stimulate phosphorylation of CTP:Phosphocholine cytidylyltransferase in HeLa cells

T. Wieder, C. Orfanos, M. Wieprecht, 1994, FEBS letters.

N-[2-bromocinnamyl(amino)ethyl]-5-isoquinolinesulphonamide (H-89) inhibits incorporation of choline into phosphatidylcholine via inhibition of choline kinase and has no effect on the phosphorylation of CTP:phosphocholine cytidylyltransferase.

T. Wieder, M. Wieprecht, C. Geilen, 1994, The Biochemical journal.