@article {2103, title = {Current approaches for global post-translational modification discovery and mass spectrometric analysis}, journal = {Analytica Chimica Acta}, volume = {627}, number = {1}, year = {2008}, note = {ISI Document Delivery No.: 358IYTimes Cited: 13Cited Reference Count: 77Hoffman, Michael D. Sniatynski, Matthew J. Kast, JuergenSp. Iss. SI}, month = {Oct}, pages = {50-61}, type = {Review}, abstract = {More and more attention is being focused on the analysis of post-translational modifications (PTMs) on proteins as researchers are continually learning how essential they are for proper cellular function. As there are hundreds of different types of known PTMs, traditional methods of modification analysis are incapable of comprehensively monitoring for post-translational modifications, a task which is a necessity for truly understanding a cell{\textquoteright}s biology. This review highlights recent developments in novel multiplexed methods of PTM analysis including: fluorescent stain and immuno-based methods, hardware-based mass spectrometric methods and computational-based mass spectrometric methods. Many of these techniques show great promise and will likely be a valuable resource for the biological community. (C) 2008 Elsevier B.V. All rights reserved.}, keywords = {computational, glycosylation, IDENTIFICATION, IONIZATION, marker ion, MASS SPECTROMETRY, MODIFIED PEPTIDES, neutral loss, post-translational modifications, protein array, PROTEIN-PHOSPHORYLATION, PROTEOMIC ANALYSIS, S-NITROSYLATION, SEQUENCES, SIGNALING NETWORKS, SPECTRA}, isbn = {0003-2670}, url = {://000259911600005}, author = {Hoffman, M. D. and Sniatynski, M. J. and Kast, J.} }