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Phosphate Selective Uranyl Photo‐Affinity Cleavage of Proteins. Determination of Phosphorylation Sites
Author(s) -
Kristensen Line Hyltoft,
Nielsen Peter Eigil,
Jørgensen Christian Isak,
Kragelund Birthe B.,
Møllegaard Niels Erik
Publication year - 2008
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.200800387
Subject(s) - phosphorylation , uranyl , chemistry , cleavage (geology) , protein phosphorylation , phosphate , biochemistry , biology , protein kinase a , organic chemistry , ion , paleontology , fracture (geology)
Phototcleavage of phosphorylated proteins . Phosphorylation of proteins is one of the most important mechanisms in cellular signaling and is involved in cellular processes such as metabolism, apoptosis, and differentiation. Uranyl photocleavage at high specificity as well as efficiency of proteins with phosphorylated residues was systematically analyzed. The results open the way for the detection of phosphorylation sites in proteins by uranyl photocleavage.