HIGHLIGHTS
SUMMARY
The authors combine theoretical kinetic modeling with experimental pulsed stable isotope labeling of amino_acids in cell culture (pSILAC) for the study of protein phosphorylation. In cell culture experiments, arginine and lysine labeled with stable carbon and nitrogen isotopes are typically used in a method called pulsed (or dynamic) stable isotope labeling of amino_acids in cell culture (pSILAC)1,2. Instead of readily giving information on protein stability per se, differences in clearance rates suggest hypotheses on the temporal ordering of modification events along the synthesis-maturation-degradation axis (i.e., age or lifetime) of . . .
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