@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.}
}
@article {1029,
	title = {Pachymoside A - A novel glycolipid isolated from the marine sponge Pachymatisma johnstonia},
	journal = {Canadian Journal of Chemistry-Revue Canadienne De Chimie},
	volume = {82},
	number = {2},
	year = {2004},
	note = {ISI Document Delivery No.: 802BHTimes Cited: 5Cited Reference Count: 21},
	month = {Feb},
	pages = {102-112},
	type = {Article},
	abstract = {Crude extracts of the North Sea marine sponge Pachymatisma johnstonia showed promising activity in a new assay for inhibitors of bacterial type III secretion. Bioassay-guided fractionation resulted in the isolation of the pachymosides, a new family of sponge glycolipids. A major part of the structural diversity in this family of glycolipids involves increasing degrees of acetylation and differing positions of acetylation on a common pachymoside glycolipid template. All of the metabolites with these variations in acetylation pattern were converted into the same peracetylpachymoside methyl ester (2) for purification and spectroscopic analysis. Pachymoside A (1) is the component of the mixture that has natural acetylation at the eight galactose hydroxyls and at the C-6 hydroxyls of glucose-B and glucose-D. Chemical degradation and transformation in conjunction with extensive analysis of 800 MHz NMR data was used to elucidate the structure of pachymoside A (1).},
	keywords = {BACTERIAL VIRULENCE, ENTEROPATHOGENIC ESCHERICHIA-COLI, glycolipid, GLYCOSPHINGOLIPIDS, HOST-CELLS, III SECRETION, inhibitors, marine sponge, NATURAL-PRODUCTS, Pachymatisma johnstonia, pachymoside, PLAKORTIS-SIMPLEX, PLAKOSIDE, PRENYLATED, RECEPTOR},
	isbn = {0008-4042},
	url = {<Go to ISI>://000220138500006},
	author = {Warabi, K. and Zimmerman, W. T. and Shen, J. K. and Gauthier, A. and Robertson, M. and Finlay, B. B. and Van Soest, R. and Andersen, R. J.}
}
