Regulation by phosphorylation of reversible association of a myristoylated protein kinase C substrate with the plasma membrane.

In Vitro Neutrophil Migration Requires Protein Kinase C-Delta (δ-PKC)-Mediated Myristoylated Alanine-Rich C-Kinase Substrate (MARCKS) Phosphorylation.

A novel predictor of cancer malignancy: up-regulation of myristoylated alanine-rich C kinase substrate phosphorylation in lung cancer.

Phosphorylation of PACSIN2 by protein kinase C triggers the removal of caveolae from the plasma membrane.

Phosphorylation of the plasma-membrane H(+)-ATPase of oat roots by a calcium-stimulated protein kinase.

Requirement of protein association with membranes for phosphorylation by protein kinase C.

Regulation of Smoothened Phosphorylation and High-Level Hedgehog Signaling Activity by a Plasma Membrane Associated Kinase.

Evidence for a non-myristoylated pool of the 80 kDa protein kinase C substrate of rat brain.

Phosphorylation of MARCKS (80-kDa) protein, a major substrate for protein kinase C in oligodendroglial progenitors.

Relationship between the major protein kinase C substrates acidic 80-kDa protein-kinase-C substrate (80K) and myristoylated alanine-rich C-kinase substrate (MARCKS). Members of a gene family or equivalent genes in different species.

Targeting myristoylated alanine-rich C kinase substrate phosphorylation site domain in lung cancer. Mechanisms and therapeutic implications.

Phosphorylation of Alzheimer amyloid precursor protein by protein kinase C.

Alterations of the myristoylated, alanine-rich C kinase substrate (MARCKS) in prefrontal cortex in schizophrenia.

Increased phosphorylation of a 17-kDa protein kinase C substrate (P17) in long-term potentiation.

Phosphorylation of membrane-bound acetylcholine receptor by protein kinase C: characterization and subunit specificity.

A 64-kDa protein is a substrate for phosphorylation by a distinct thylakoid protein kinase.

Regulation of arachidonate-mobilizing phospholipase A2 by phosphorylation via protein kinase C in macrophages.

Substrate-dependent inhibition of protein kinase C by specific inhibitors.

Multisite phosphorylation of P-Rex1 by protein kinase C.

Protein kinase-A inhibits phospholipase-C activity and alters protein phosphorylation in rat myometrial plasma membranes.

C 3T3 mouse fibroblasts.

Transformation-specific decrease of phosphorylation of 80K protein, a substrate of protein kinase C, in NIH3T3 cells.

The role of myristoylated protein kinase C substrates in intracellular signaling pathways in macrophages.

Membrane-bound Dictyostelium myosin heavy chain kinase: a developmentally regulated substrate-specific member of the protein kinase C family.

Ca(2+)-dependent protein kinase (protein kinase C).

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In Vitro Neutrophil Migration Requires Protein Kinase C-Delta (δ-PKC)-Mediated Myristoylated Alanine-Rich C-Kinase Substrate (MARCKS) Phosphorylation.

A novel predictor of cancer malignancy: up-regulation of myristoylated alanine-rich C kinase substrate phosphorylation in lung cancer.

Phosphorylation of PACSIN2 by protein kinase C triggers the removal of caveolae from the plasma membrane.

Phosphorylation of the plasma-membrane H(+)-ATPase of oat roots by a calcium-stimulated protein kinase.

Requirement of protein association with membranes for phosphorylation by protein kinase C.

Regulation of Smoothened Phosphorylation and High-Level Hedgehog Signaling Activity by a Plasma Membrane Associated Kinase.

Evidence for a non-myristoylated pool of the 80 kDa protein kinase C substrate of rat brain.

Phosphorylation of MARCKS (80-kDa) protein, a major substrate for protein kinase C in oligodendroglial progenitors.

Relationship between the major protein kinase C substrates acidic 80-kDa protein-kinase-C substrate (80K) and myristoylated alanine-rich C-kinase substrate (MARCKS). Members of a gene family or equivalent genes in different species.

Targeting myristoylated alanine-rich C kinase substrate phosphorylation site domain in lung cancer. Mechanisms and therapeutic implications.

Phosphorylation of Alzheimer amyloid precursor protein by protein kinase C.

Alterations of the myristoylated, alanine-rich C kinase substrate (MARCKS) in prefrontal cortex in schizophrenia.

Increased phosphorylation of a 17-kDa protein kinase C substrate (P17) in long-term potentiation.

Phosphorylation of membrane-bound acetylcholine receptor by protein kinase C: characterization and subunit specificity.

A 64-kDa protein is a substrate for phosphorylation by a distinct thylakoid protein kinase.

Regulation of arachidonate-mobilizing phospholipase A2 by phosphorylation via protein kinase C in macrophages.

Substrate-dependent inhibition of protein kinase C by specific inhibitors.

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Protein kinase-A inhibits phospholipase-C activity and alters protein phosphorylation in rat myometrial plasma membranes.

C 3T3 mouse fibroblasts.

Transformation-specific decrease of phosphorylation of 80K protein, a substrate of protein kinase C, in NIH3T3 cells.

The role of myristoylated protein kinase C substrates in intracellular signaling pathways in macrophages.

Membrane-bound Dictyostelium myosin heavy chain kinase: a developmentally regulated substrate-specific member of the protein kinase C family.

Ca(2+)-dependent protein kinase (protein kinase C).

Regulation by phosphorylation of reversible association of a myristoylated protein kinase C substrate with the plasma membrane.

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