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Lecture 11
Lecture 11

... 3. The allosteric regulators bind to sites that are not active sites and elicit their effects by causing a Change in Shape of the Catalytic Subunit ...
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... Protein kinases mediate most intracellular signal transduction via the reversible phosphorylation on serine, threonine, or tyrosine residue of specific protein/peptide substrates. Such phosphorylation is employed by all eukaryotes in regulation of enzyme activity, protein-protein interaction, subcel ...
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... The review paper by Dr Delia and Buscemi’s groups systematically reviewed the research progresses of CHK2 kinase, particularly focusing on its responses to DNA damage. CHK2 is well known as a nuclear serine/threonine protein kinase involved in the spreading of DNA damage signal through a phosphoryla ...
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... FD, a bZIP transcription factor, preferentially expressed in the shoot apical meristem is required for FT protein to promote flowering. FD and FT proteins interact and act as a complex at the shoot apical meristem (SAM) to promote flowering. FD contains a possible phosphorylation sequence in its C-t ...
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Phosphorylation



Phosphorylation is the addition of a phosphate (PO43−) group to a protein or other organic molecule. Phosphorylation and its counterpart, dephosphorylation, turn many protein enzymes on and off, thereby altering their function and activity. Protein phosphorylation is one type of post-translational modification.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 2015, the Medline database returns over 240,000 articles on the subject, largely on protein phosphorylation).
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