MARCKS is an actin filament crosslinking protein regulated by protein kinase C and calcium-calmodulin.

Hepatocanalicular organic-anion transport is regulated by protein kinase C.

The glutamate receptor of the Qp-type activates protein kinase C and is regulated by protein kinase C.

The MARCKS brothers: a family of protein kinase C substrates.

Comparison of an endogenous protein kinase C substrate in rat aorta with rat brain MARCKS.

Endocytosis is regulated by protein kinase A, but not protein kinase C in a secretory epithelial cell line.

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

Three different actin filament assemblies occur in every hair cell: each contains a specific actin crosslinking protein.

Phosducin is a protein kinase A-regulated G-protein regulator.

Protein kinase A- and protein kinase C-regulated interaction of plectin with lamin B and vimentin.

AR-v7 protein expression is regulated by protein kinase and phosphatase.

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

Localization of the MARCKS (87 kDa) protein, a major specific substrate for protein kinase C, in rat brain.

The Toxoplasma gondii rhoptry protein ROP18 is an Irga6-specific kinase and regulated by the dense granule protein GRA7.

FKBP-12 is not an inhibitor of protein kinase C.

Inhibition of actin filament depolymerization by the Dictyostelium 30,000-D actin-bundling protein.

MacMARCKS, a novel member of the MARCKS family of protein kinase C substrates.

Surface immunoglobulin crosslinking activates a tyrosine kinase pathway in B cells that is independent of protein kinase C.

Phosphorylation-regulated crosslinking of gold nanoparticles: a new strategy for colorimetric detection of protein kinase activity.

Endocytosis of GABA(C) receptors depends on subunit composition and is regulated by protein kinase C-ζ and protein phosphatase 1.

A mouse brain cDNA encodes a novel protein with the protein kinase C phosphorylation site domain common to MARCKS.

Cysteine-rich protein 2 accelerates actin filament cluster formation.

Actin polymerization is stimulated by actin cross-linking protein palladin.

Phosphoinositide hydrolysis is not negatively regulated by protein kinase C in the peripheral tissues of rat and chick.

The role of protein kinase C and its neuronal substrates dephosphin, B-50, and MARCKS in neurotransmitter release.

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Hepatocanalicular organic-anion transport is regulated by protein kinase C.

The glutamate receptor of the Qp-type activates protein kinase C and is regulated by protein kinase C.

The MARCKS brothers: a family of protein kinase C substrates.

Comparison of an endogenous protein kinase C substrate in rat aorta with rat brain MARCKS.

Endocytosis is regulated by protein kinase A, but not protein kinase C in a secretory epithelial cell line.

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

Three different actin filament assemblies occur in every hair cell: each contains a specific actin crosslinking protein.

Phosducin is a protein kinase A-regulated G-protein regulator.

Protein kinase A- and protein kinase C-regulated interaction of plectin with lamin B and vimentin.

AR-v7 protein expression is regulated by protein kinase and phosphatase.

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

Localization of the MARCKS (87 kDa) protein, a major specific substrate for protein kinase C, in rat brain.

The Toxoplasma gondii rhoptry protein ROP18 is an Irga6-specific kinase and regulated by the dense granule protein GRA7.

FKBP-12 is not an inhibitor of protein kinase C.

Inhibition of actin filament depolymerization by the Dictyostelium 30,000-D actin-bundling protein.

MacMARCKS, a novel member of the MARCKS family of protein kinase C substrates.

Surface immunoglobulin crosslinking activates a tyrosine kinase pathway in B cells that is independent of protein kinase C.

Phosphorylation-regulated crosslinking of gold nanoparticles: a new strategy for colorimetric detection of protein kinase activity.

Endocytosis of GABA(C) receptors depends on subunit composition and is regulated by protein kinase C-ζ and protein phosphatase 1.

A mouse brain cDNA encodes a novel protein with the protein kinase C phosphorylation site domain common to MARCKS.

Cysteine-rich protein 2 accelerates actin filament cluster formation.

Actin polymerization is stimulated by actin cross-linking protein palladin.

Phosphoinositide hydrolysis is not negatively regulated by protein kinase C in the peripheral tissues of rat and chick.

The role of protein kinase C and its neuronal substrates dephosphin, B-50, and MARCKS in neurotransmitter release.

MARCKS is an actin filament crosslinking protein regulated by protein kinase C and calcium-calmodulin.

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