The method has been used to study protein kinase C, ubiquitin, and many other proteins.

The term "protein kinase C" usually refers to the entire family of isoforms.

Some forms of protein kinase C require Ca 2 + for activation.

It is an effective protein kinase C inhibitor.

The site, or sites, at which protein kinase C exerts these inhibitory effects is unresolved.

Phosphorylation by protein kinase C lowers its binding ability.

It is a potent, selective, and cell-permeable protein kinase C inhibitor.

The calcium function in vertebrates also involves activation of protein kinase C and its effects.

As an activator of protein kinase C, it is a weak tumor promoter compared to 12-O-tetradecanoylphorbol-13-acetate.

Safingol is a lyso-sphingolipid protein kinase C inhibitor.

Protein kinase C controls the cell cycle, so chemicals that interact with it can have pro-proliferative or anti-proliferative effects.

The cause is e.g. oxidative stress, by activating protein kinase C and lead to apoptosis of some cells.

They inhibit viral replication of the Protein kinase C and virus-induced cellular fusion.

Protein kinase C inhibitors, such as ruboxistaurin, may potentially be beneficial in peripheral diabetic retinopathy.

Protein kinase C, which is activated by phorbol esters, can fulfill the same function as Ras.

Pleckstrin, the protein where this domain was first detected, is the major substrate of protein kinase C in platelets.

Thrombin binding to its receptor activates protein kinase C and increases the level of inositol triphosphate.

Protein kinase C phosphorylates Gi and prevents its inhibitory action on the catalytic subunit.

Bryostatin 1 is a potent modulator of protein kinase C (PKC).

Several classes of protein kinases, including protein kinase C, are not cAMP-dependent.

The most understood mechanisms include phosphorylation by the second messenger protein kinase C (PKC).

Mania is associated with irregular increases in protein kinase C (PKC) activity within the brain.

It is proposed that diacylglycerol enters the cell directly, stimulating protein kinase C, which is involved in intracellular signal transduction.

Mezerein and other phorbol esters interact with protein kinase C (PKC).

Phorbol esters can directly stimulate protein kinase C, PKC.