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In pituitary cells C/EBP beta was
phosphorylated in response to increased intracellular
calcium concentrations as a consequence of the activation of
a calcium-calmodulin-dependent protein kinase.
Phosphorylation of serine at position 276 within the leucine
zipper of C/EBP beta appeared to confer calcium-regulated
transcriptional stimulation of a promoter that contained
binding sites for C/EBP beta.
In pituitary cells C/EBP beta was
phosphorylated in response to increased intracellular
calcium concentrations as a consequence of the activation of
a calcium-calmodulin-dependent protein kinase.
Phosphorylation of serine at position 276 within the leucine
zipper of C/EBP beta appeared to confer calcium-regulated
transcriptional stimulation of a promoter that contained
binding sites for C/EBP beta.