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| - vědecký článek publikovaný v roce 1995 (cs)
- artículu científicu espublizáu en 1995 (ast)
- 1995 թվականի սեպտեմբերին հրատարակված գիտական հոդված (hy)
- наукова стаття, опублікована у вересні 1995 (uk)
- 1995 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած (hyw)
- vedecký článok (publikovaný 1995/09/22) (sk)
- مقالة علمية (نشرت في 22-9-1995) (ar)
- article publié dans la revue scientifique Journal of Biological Chemistry (fr)
- wetenschappelijk artikel (gepubliceerd op 1995/09/22) (nl)
- scientific journal article (en)
- im September 1995 veröffentlichter wissenschaftlicher Artikel (de)
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| - J. A. Le Good
- L. V. Dekker
- P. J. Parker
- R. Gigg
- R. H. Palmer
- R. Woscholski
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| - Activation of PRK1 by phosphatidylinositol 4,5-bisphosphate and phosphatidylinositol 3,4,5-trisphosphate. A comparison with protein kinase C isotypes (en)
- Activation of PRK1 by phosphatidylinositol 4,5-bisphosphate and phosphatidylinositol 3,4,5-trisphosphate. A comparison with protein kinase C isotypes (nl)
- Activation of PRK1 by phosphatidylinositol 4,5-bisphosphate and phosphatidylinositol 3,4,5-trisphosphate. A comparison with protein kinase C isotypes (ast)
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| - Activation of PRK1 by phosphatidylinositol 4,5-bisphosphate and phosphatidylinositol 3,4,5-trisphosphate. A comparison with protein kinase C isotypes (en)
- Activation of PRK1 by phosphatidylinositol 4,5-bisphosphate and phosphatidylinositol 3,4,5-trisphosphate. A comparison with protein kinase C isotypes (nl)
- Activation of PRK1 by phosphatidylinositol 4,5-bisphosphate and phosphatidylinositol 3,4,5-trisphosphate. A comparison with protein kinase C isotypes (ast)
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| - Activation of PRK1 by phosphatidylinositol 4,5-bisphosphate and phosphatidylinositol 3,4,5-trisphosphate. A comparison with protein kinase C isotypes (en)
- Activation of PRK1 by phosphatidylinositol 4,5-bisphosphate and phosphatidylinositol 3,4,5-trisphosphate. A comparison with protein kinase C isotypes (nl)
- Activation of PRK1 by phosphatidylinositol 4,5-bisphosphate and phosphatidylinositol 3,4,5-trisphosphate. A comparison with protein kinase C isotypes (ast)
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| title
| - Activation of PRK1 by phosphatidylinositol 4,5-bisphosphate and phosphatidylinositol 3,4,5-trisphosphate. A comparison with protein kinase C isotypes (en)
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of | - Insulin stimulates PKCzeta -mediated phosphorylation of insulin receptor substrate-1 (IRS-1). A self-attenuated mechanism to negatively regulate the function of IRS proteins
- An aPKC-exocyst complex controls paxillin phosphorylation and migration through localised JNK1 activation
- Protein kinase C isozymes and substrates
- A role for nuclear phosphatidylinositol-specific phospholipase C in the G2/M phase transition
- JAK/STAT, Raf/MEK/ERK, PI3K/Akt and BCR-ABL in cell cycle progression and leukemogenesis
- Protein kinase C-zeta as a downstream effector of phosphatidylinositol 3-kinase during insulin stimulation in rat adipocytes. Potential role in glucose transport
- Specific binding of the Akt-1 protein kinase to phosphatidylinositol 3,4,5-trisphosphate without subsequent activation
- Phosphoinositide 3-kinases: a conserved family of signal transducers
- A 3-phosphoinositide-dependent protein kinase-1 (PDK1) docking site is required for the phosphorylation of protein kinase Czeta (PKCzeta ) and PKC-related kinase 2 by PDK1
- p110δ, a novel phosphoinositide 3-kinase in leukocytes
- The Drosophila phosphoinositide 3-kinase Dp110 promotes cell growth.
- Aggregation-dependent, integrin-mediated increases in cytoskeletally associated PtdInsP2 (4,5) levels in human platelets are controlled by translocation of PtdIns 4-P 5-kinase C to the cytoskeleton
- Signalling through the lipid products of phosphoinositide-3-OH kinase
- Synaptojanin is the major constitutively active phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase in rodent brain.
- Multiple interactions of PRK1 with RhoA. Functional assignment of the Hr1 repeat motif
- Rho GTPases and their effector proteins
- Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B
- The product of par-4, a gene induced during apoptosis, interacts selectively with the atypical isoforms of protein kinase C
- The extended protein kinase C superfamily
- The PRK2 kinase is a potential effector target of both Rho and Rac GTPases and regulates actin cytoskeletal organization
- Isolation and characterization of a structural homologue of human PRK2 from rat liver. Distinguishing substrate and lipid activator specificities
- Rho GTPase control of protein kinase C-related protein kinase activation by 3-phosphoinositide-dependent protein kinase
- Phosphoinositide 3-kinase: the key switch mechanism in insulin signalling
- Downstream signalling events regulated by phosphatidylinositol 3-kinase activity.
- The versatility of inositol phosphates as cellular signals
- Platelet-derived growth factor stimulates protein kinase D through the activation of phospholipase Cgamma and protein kinase C.
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