@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 = {<Go to ISI>://000259911600005},
	author = {Hoffman, M. D. and Sniatynski, M. J. and Kast, J.}
}
@article {1414,
	title = {Multiple neutral loss monitoring (MNM): A multiplexed method for post-translational modification screening},
	journal = {Journal of the American Society for Mass Spectrometry},
	volume = {17},
	number = {3},
	year = {2006},
	note = {ISI Document Delivery No.: 021SETimes Cited: 11Cited Reference Count: 20},
	month = {Mar},
	pages = {307-317},
	type = {Article},
	abstract = {Post-translational modifications of proteins are involved in determining the activity of proteins and are essential for proper protein function. Current mass spectrometric strategies require one to specify a particular type of modification, in some cases also a particular charge state of a protein or peptide that is to be studied before the actual analysis. Due to these requirements, most of the modifications on proteins are not considered in such an experiment and, thus, a series of similar analyses need to be performed to ensure a more extensive characterization. A novel scan strategy has been developed, multiple neutral loss monitoring (MNM), allowing for the comprehensive screening of post-translational modifications (PTM) on proteins that fragment as neutral losses in a mass spectrometer. MNM method parameters were determined by performing product ion scans on a number of modified peptides over a range of collision energies, providing neutral loss energy profiles and optimal collision energies (OCE) for each modification, supplying valuable information pertaining to the fragmentation of these modifications and the necessary parameters that would be required to obtain the best analysis. As the optimal collision energy was highly dependent on the type of modification and the charge state of the peptide, the MNM scan was operated with a collision energy gradient. Autocorrelation analyses identified the type of modification, and convolution mapping analyses identified the associated peptide. The MNM scan with the new collision energy parameters was successfully applied to a mixture of four modified peptides in a BSA digest. The implementation of this technique will allow for comprehensive screening of all modifications that fragment as neutral losses.},
	keywords = {COLLISION-INDUCED DISSOCIATION, PEPTIDES, PROTEIN-PHOSPHORYLATION, PROTEOMIC ANALYSIS, SCAN, TANDEM MASS-SPECTROMETRY},
	isbn = {1044-0305},
	url = {<Go to ISI>://000236004700004},
	author = {Hoffman, M. D. and Sniatynski, M. J. and Rogalski, J. C. and Le Blanc, J. C. Y. and Kast, J.}
}
