Methods for Quantification of in vivo Changes in Protein Ubiquitination following Proteasome and Deubiquitinase Inhibition
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Data from MassIVE, [[http://proteomics.ucsd.edu/ProteoSAFe/status.jsp?task=TRANCHE-MSV000077546 MSV000077546]]. Experiment: exp2_rep1_Proteome, file: K20110724_NU_Jurkat_rep1B_Proteome_SILAC_L-no_M-17uMPR619_H-5uMMG13217uM_SCXFxn24.mzml. Published as part of Mol Cell Proteomics. 2012 May;11(5):148-59 . From the Abstract: {{i}} ... The introduction of antibodies that specifically recognize peptides with lysine residues that harbor a di-glycine remnant (K-eplison-GG) following tryptic digestion has dramatically improved the ability to enrich and identify ubiquitination sites from cellular lysates. We used this enrichment technique to study the effects of proteasome inhibition by MG-132 and deubiquitinase inhibition by PR-619 on ubiquitination sites in human Jurkat cells by quantitative high performance mass spectrometry. ... {{/i}}



