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Structural Characterizations Of Phosphorylatable Residues In Transmembrane Proteins From Arabidopsis Thaliana, Bin Xue, Vladimir N. Uversky
Structural Characterizations Of Phosphorylatable Residues In Transmembrane Proteins From Arabidopsis Thaliana, Bin Xue, Vladimir N. Uversky
Molecular Medicine Faculty Publications
Phosphorylation is a common post-translational modification that plays important roles in a wide range of biochemical and cellular processes. Many enzymes and receptors can be switched “on” or “off” by conformational changes induced by phosphorylation. The phosphorylation process is mediated by a family of enzymes called kinase. Currently, more than 1,000 different kinases have been identified in Arabidopsis thaliana proteome. Kinases interact with each other and with many regulatory proteins forming phosphorylation networks. These phosphorylation networks modulate the signaling processes and control the functions of cells. Normally, kinases phosphorylate serines, threonines, and tyrosines. However, in many proteins, not all of …