@article {2277,
	title = {Phosphorylation of U24 from Human Herpes Virus type 6 (HHV-6) and its potential role in mimicking myelin basic protein (MBP) in multiple sclerosis},
	journal = {Febs Letters},
	volume = {582},
	number = {18},
	year = {2008},
	note = {ISI Document Delivery No.: 332UKTimes Cited: 2Cited Reference Count: 31Tait, Andrew R. Straus, Suzana K.},
	month = {Aug},
	pages = {2685-2688},
	type = {Article},
	abstract = {Myelin basic protein (MBP) from multiple sclerosis ( MS) patients contains lower levels of phosphorylation at Thr97 than normal individuals. The significance of phosphorylation at this site is not fully understood, but it is proposed to play a role in the normal functioning of MBP. Human Herpesvirus Type 6 encodes the protein U24, which has tentatively been implicated in the pathology of MS. U24 shares a 7 amino acid stretch encompassing the Thr97 phosphorylation site of MBP: PRTPPPS. We demonstrate using a combination of mass spectrometry, thin layer chromatography and autoradiography, that U24 can be phosphorylated at the equivalent threonine. Phospho-U24 may confound signalling or other pathways in which phosphorylated MBP may participate, precipitating a pathological process.},
	keywords = {BINDING, EXPRESSION, HUMAN-HERPESVIRUS-6, IDENTIFICATION, KINASE, MEMBRANE MICRODOMAINS, mimicry, myelin, PHOSPHORYLATION, POSTTRANSLATIONAL MODIFICATIONS, SITE, T-ANTIGEN, U24},
	isbn = {0014-5793},
	url = {<Go to ISI>://000258108400002},
	author = {Tait, A. R. and Straus, S. K.}
}
@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.}
}
