Phosphorylation

Phosphorylation is the addition of a phosphate (PO43-) group to a protein or other organic molecule. Phosphorylation turns many protein enzymes on and off, thereby altering their function and activity.

Protein phosphorylation in particular plays a significant role in a wide range of cellular processes. Its prominent role in biochemistry is the subject of a very large body of research (as of March 2012, the Medline database returns nearly 200,000 articles on the subject, largely on protein phosphorylation).

Read more about Phosphorylation:  Other Kinds

Other articles related to "phosphorylation":

Phosphorylation Cascade
... A phosphorylation cascade is a sequence of events where one enzyme phosphorylates another, causing a chain reaction leading to the phosphorylation of thousands of proteins ...
CDCP1 - Function
... The tyrosine phosphorylation of Trask is tightly regulated and reciprocally linked with the state of cell adhesion ... The tyrosine phosphorylation of CDCP1 in cultured cells occurs when cells are induced to detach by trypsin or EDTA, or seen spontaneously during mitotic detachment ... CDCP1 is widely expressed in human epithelial tissues, but its phosphorylation is only seen in mitotically detached or shedding cells, consistent with its role in the negative regulation of cell adhesion ...
Phosphorylation - Other Kinds
... to ADP in a process referred to as oxidative phosphorylation ... ATP is also synthesized by substrate-level phosphorylation during glycolysis ... Phosphorylation of sugars is often the first stage of their catabolism ...
Chloride Potassium Symporter 5 - Regulation - Post-translational Regulation: Phosphorylation
... It is conventionally thought that phosphorylation inactivates or downregulates KCC2, however there is recent evidence to suggest that phosphorylation at different sites ... TrkB) phosphorylation downregulates KCC2 activity ... PKC phosphorylation of the C-terminus Ser940 residue of the KCC2 protein upregulates KCC2 activity by increasing surface stability ...