𝔖 Bobbio Scriptorium
✦   LIBER   ✦

Protein kinase Cα-dependent phosphorylation of Golgi proteins

✍ Scribed by Boris Radau; Albrecht Otto; Eva-Christina Müller; Peter Westermann

Publisher
John Wiley and Sons
Year
2000
Tongue
English
Weight
186 KB
Volume
21
Category
Article
ISSN
0173-0835

No coin nor oath required. For personal study only.

📜 SIMILAR VOLUMES

Phosphorylation-dependent protein kinase
Phosphorylation-dependent protein kinase Dactivation
✍ Richard T. Waldron; Teresa Iglesias; Enrique Rozengurt 📂 Article 📅 1999 🏛 John Wiley and Sons 🌐 English ⚖ 134 KB

The novel mouse serine-threonine kinase protein kinase D (PKD) is activated in intact Swiss 3T3 cells stimulated by phorbol esters, cell permeant diacylglycerols, bryostatin, neuropeptides and growth factors via a phosphorylation-dependent mechanism requiring protein kinase C (PKC) activity. Structu

Inhibition of protein kinase C-dependent
Inhibition of protein kinase C-dependent protein phosphorylation correlates with increased polarity and locomotion in Walker 256 carcinosarcoma cells
✍ Verena Niggli; Arthur Zimmermann; Hansuli Keller 📂 Article 📅 1996 🏛 John Wiley and Sons 🌐 French ⚖ 746 KB

Signal transduction pathways controlling tumor cell locomotion are not yet well understood. We have studied the role of protein kinase C (PKC)-dependent protein phosphorylation associated with changes in cell shape and locomotor activity of Walker carcinosarcoma cells in culture. We show that the in

Protein kinase C and cAMP-dependent prot
Protein kinase C and cAMP-dependent protein kinase regulate the neuronal differentiation of immortalized raphe neurons
✍ Howard B. Rind; Scott R. Whittemore 📂 Article 📅 1999 🏛 John Wiley and Sons 🌐 English ⚖ 185 KB 👁 2 views

These studies examined the extent to which protein kinase C (PKC) and cAMP-dependent protein kinase (PKA) regulate the neuronal differentiation of the raphe-derived neuronal cell line, RN33B. A differentiation-specific 2.25-fold increase in soluble PKA activity was observed. Neither membrane-associa

Phosphorylation of tyrosine 256 facilita
Phosphorylation of tyrosine 256 facilitates nuclear import of atypical protein kinase C
✍ Wendy O. White; M. Lamar Seibenhener; Marie W. Wooten 📂 Article 📅 2002 🏛 John Wiley and Sons 🌐 English ⚖ 319 KB

## Abstract Herein, we employed a combined approach of molecular modeling and site‐directed mutagenesis to address the role of tyrosine phosphorylation in transport of atypical protein kinase C (aPKC) into the nucleus. Computer modeling of the three‐dimensional structure of the aPKC catalytic core,