@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 {4550,
	title = {A comparison of NMR distance determinations in the solid state by cross polarization, REDOR, and TEDOR techniques},
	journal = {Canadian Journal of Chemistry-Revue Canadienne De Chimie},
	volume = {77},
	number = {11},
	year = {1999},
	note = {ISI Document Delivery No.: 253FETimes Cited: 14Cited Reference Count: 64},
	month = {Nov},
	pages = {1984-1993},
	type = {Article},
	abstract = {Solid-state NMR distance determinations using Hartmann-Hahn cross polarization between spin-1/2 nuclei (F-19/Si-29) are reported. F-19 {\textendash}> Si-29 polarization transfer for the T-1 silicon site in the clathrasil octadecasil shows an oscillatory behaviour as a function of the contact time. These oscillations were observed for non-spinning powder samples and also for different spinning speeds at the various MAS sideband matching conditions. Three analytical functions that allow efficient nonlinear least-square regression analyses of the experimental data to determine the internuclear distances for non-spinning powder samples as well as at the +/-1 and +/-2 MAS sideband matching conditions are reported. Using these functions, a F-19-Si-29 distance of 2.53 +/- 0.04 Angstrom was determined for the T-1 silicon in octadecasil from fitting of the oscillatory behaviour. This distance is in good agreement with that known from the X-ray structure and the previous F-19/Si-29 REDOR and TEDOR distance measurements. The advantages and limits of the different dipolar-based NMR techniques for heteronuclear distance determinations are examined and discussed.},
	keywords = {ANGLE-SPINNING NMR, cross polarization (CP), DISTANCE, distances F-19-Si-29, HELICAL PEPTIDE, HETERONUCLEAR DIPOLAR, interactions, INTERATOMIC, LOCK, NMR distance measurements, NUCLEAR-MAGNETIC-RESONANCE, octadecasil, PROTON-ENHANCED NMR, REDOR, ROTATIONAL-ECHO, SEQUENCES, SPIN-1/2 NUCLEI, TEDOR, TRANSIENT OSCILLATIONS},
	isbn = {0008-4042},
	url = {<Go to ISI>://000083545300032},
	author = {Fyfe, C. A. and Lewis, A. R. and Chezeau, J. M.}
}
