Article ID Journal Published Year Pages File Type
10802668 Biochimica et Biophysica Acta (BBA) - Molecular Cell Research 2013 9 Pages PDF
Abstract
► The kinase that phosphorylates Ser258 within TF is identified as p38α ► The reaction rate increases by 10 fold on previous phosphorylation of Ser253 in TF ► This arises as a result of exposure of Ser258 following phosphorylation of Ser253 ► The activation of p38 may occur by the retention of TF within activated cells ► A mechanism for the regulation of the release of TF into microparticles is proposed
Related Topics
Life Sciences Biochemistry, Genetics and Molecular Biology Biochemistry
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