Examples of phosphorylation

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Serine phosphorylation can affect the distribution between main state and the substate occupancies of certain connexins.
The kinase domain is in equilibrium between an 'open, accessible ' state, subject to phosphorylation, and a 'closed, competent' state, able to perform catalysis.
This process, termed protein phosphorylation, is essential for the normal regulation of protein function in cells.
The phosphorylation of three classes of proteins is depicted, although many other types of proteins are regulated by phosphorylation.
No significant differences in serine phosphorylation were detected at 14 days after inflammation for all four sites.
This block corresponds to a period when behavioral signs of hyperalgesia also disappear, which indicates that the phosphorylation depends on primary afferent input.
Calcium-dependent protein phosphorylation may mediate the gibberellic acid response in barley aleurone.
There is precedent in the retina for the opening of gap junctions by phosphorylation.
These findings suggest that protein phosphorylation, not protein synthesis, controls the formation of pronuclei following fertilisation.
It is a dynamic structure which changes its shape, structure, protein composition and phosphorylation state during the cell cycle.
They are rapidly phosphorylated in response to light, but the functional relevance of this phosphorylation is not yet fully understood.
This variation in protein phosphorylation represents one of the earliest reported biochemical differences in imbibed dormant and germinable seed embryos.
This suggests that the loss of non-phosphorylated neurofilament observed after monocular deprived was not due to epitope masking by phosphorylation.
The high phosphorylation of the four polypeptides was maintained throughout grain maturation.
These differences in phosphorylation might be due to different maturation conditions, especially the different culture medium additives.
Stage-specific changes in protein phosphorylation accompanying meiotic maturation of mouse oocytes and fertilization of mouse eggs.

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