@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 {1413,
	title = {Mass spectrometric characterization of lipid-modified peptides for the analysis of acylated proteins},
	journal = {Journal of Mass Spectrometry},
	volume = {41},
	number = {2},
	year = {2006},
	note = {ISI Document Delivery No.: 016BVTimes Cited: 13Cited Reference Count: 45},
	month = {Feb},
	pages = {229-241},
	type = {Article},
	abstract = {The analysis of acylated proteins by mass spectrometry (MS) has largely been overshadowed in proteomics by the analysis of glycosylated and phosphorylated proteins; however, lipid modifications on proteins are proving to be of increasing importance in biomedical research. In order to identify the marker ions and/or neutral loss fragments that are produced upon collision-induced dissociation, providing a means to identify the common lipid modifications on proteins, peptides containing an N-terminally myristoylated glycine, a palmitoylated cysteine and a farnesylated cysteine were chemically synthesized. Matrix-assisted laser desorption/ionization time-of-flight time-of-flight (MALDI-TOF-TOF), electrospray ionization quadrupole time-of-flight (ESI Q-TOF), and electrospray ionization hybrid triple-quadrupole/linear ion trap (ESI QqQ(LIT)) mass spectrometers were used for the analysis. The peptide containing the N-terminally myristoylated glycine, upon CID, produced the characteristic fragments a(1) (240.4 Th) and b(1) (268.4 Th) ions as well as a low-intensity neutral loss of 210 Da (C14H26O). The peptides containing a farnesylated cysteine residue fragmented to produce a marker ion at a m/z of 205 Th (C15H25) as well as other intense farnesyl fragment ions, and a neutral loss of 204 Da (C15H24). The peptides containing a palmitoylated cysteine moiety generated neutral losses of 238 Da (C16H30O) and 272 Da (C16H32OS); however, no marker ions were produced. The neutral losses were more prominent in the MALDI-TOF-TOF spectra, whereas the marker ions were more abundant in the ESI QqQ(LIT) and Q-TOF mass spectra. Copyright (c) 2006 John Wiley \& Sons, Ltd.},
	keywords = {ACID, ELECTROSPRAY-IONIZATION, farnesylation, IMMUNODEFICIENCY-VIRUS TYPE-1, marker ion, MATRIX PROTEIN, MEMBRANE ASSOCIATION, myristoylation, N-MYRISTOYLATION, neutral loss, palmitoylation, PHOSPHORYLATION, POSTTRANSLATIONAL MODIFICATIONS, PRENYLATED, PROTEINS},
	isbn = {1076-5174},
	url = {<Go to ISI>://000235596500011},
	author = {Hoffman, M. D. and Kast, J.}
}
