@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 {1464,
	title = {PseG of pseudaminic acid biosynthesis - A UDP-sugar hydrolase as a masked glycosyltransferase},
	journal = {Journal of Biological Chemistry},
	volume = {281},
	number = {30},
	year = {2006},
	note = {ISI Document Delivery No.: 065VFTimes Cited: 12Cited Reference Count: 40Liu, Feng Tanner, Martin E.},
	month = {Jul},
	pages = {20902-20909},
	type = {Article},
	abstract = {The flagellin proteins in pathogenic bacteria such as Campylobacter jejuni and Helicobacter pylori are heavily glycosylated with the nine-carbon alpha-keto acid, pseudaminic acid. The presence of this posttranslational modification is absolutely required for assembly of functional flagella. Since motility is required for colonization, pseudaminic acid biosynthesis represents a virulence factor in these bacteria. Pseudaminic acid is generated from UDP-N-acetylglucosamine in five biosynthetic steps. The final step has been shown to involve the condensation of 2,4-diacetamido- 2,4,6-trideoxy-L-altrose ( 6-deoxy-AltdiNAc) with phosphoenolpyruvate as catalyzed by the enzyme pseudaminic acid synthase, NeuB3. The 6-deoxy-AltdiNAc used in this process is generated from its nucleotide-linked form, UDP-6-deoxy-AltdiNAc, by the action of a hydrolase that cleaves the glycosidic bond and releases UDP. This manuscript describes the first characterization of a UDP-6-deoxy-AltdiNAc hydrolase, namely PseG ( Cj1312) from C. jejuni. The activity of this enzyme is independent of the presence of divalent metal ions, and the values of the catalytic constants were found to be k(cat) = 27 s(-1) and K-m = 174 mu M. The enzyme was shown to hydrolyze the substrate with an overall inversion of stereochemistry at C-1 and to utilize a C-O bond cleavage mechanism during catalysis. These results, coupled with homology comparisons, suggest that the closest ancestors to the hydrolase are members of the metal-independent GT-B family of glycosyltransferases that include the enzyme MurG.},
	keywords = {CAMPYLOBACTER-JEJUNI, FLAGELLIN, FUNCTIONAL-CHARACTERIZATION, GLYCOPROTEINS, glycosylation, HELICOBACTER-PYLORI, IDENTIFICATION, MECHANISM, N-ACETYLGLUCOSAMINE 2-EPIMERASE, NUDIX HYDROLASES, SYNTHASE},
	isbn = {0021-9258},
	url = {<Go to ISI>://000239187300027},
	author = {Liu, F. and Tanner, M. E.}
}
