@article {2575,
	title = {An electropneumatic-heated nebulizer for enhancing spray ionization in PhotoSpray atmospheric pressure photoionization sources for liquid chromatography/mass spectrometry},
	journal = {Rapid Communications in Mass Spectrometry},
	volume = {23},
	number = {21},
	year = {2009},
	note = {ISI Document Delivery No.: 514YATimes Cited: 1Cited Reference Count: 30Robb, Damon B. Blades, Michael W.},
	month = {Nov},
	pages = {3394-3400},
	type = {Article},
	abstract = {We introduce a novel electropneumatic-heated nebulizer (EPn-HN), incorporating an electrified internal pneumatic nebulizer, to enhance the yield of sprayed ions from PhotoSpray (TM) atmospheric pressure photoionization (APPI) sources for liquid chromatography/mass spectrometry (LC/MS). Spray ionization from the pneumatic-heated nebulizers used in APPI sources provides a supplemental, complementary ionization method to be used for involatile and thermally labile compounds, otherwise intractable to APPI. Details of the construction and operation of the EPn-HN device are provided. The performance of the EPn-HN is demonstrated using two model compounds: substance P, a peptide used as a standard in studies of ion fragmentation mechanisms, and aztreonam, a thermally labile antibiotic. At the optimum voltage for spray ionization, improvements in sensitivity of two orders of magnitude are obtained relative to when the sprayer is grounded, the conventional case. Since both substance P and aztreonam cannot be detected using the APPI method alone, the results demonstrate how spray ionization from the EPn-HN may be used to extend the range of compounds amenable to PhotoSpray sources. Copyright (C) 2009 John Wiley \& Sons, Ltd.},
	keywords = {CHEMICAL-IONIZATION, ELECTROSPRAY, PEPTIDES, RESIDUES, TANDEM MASS-SPECTROMETRY},
	isbn = {0951-4198},
	url = {<Go to ISI>://000271431500006},
	author = {Robb, D. B. and Blades, M. W.}
}
@article {2648,
	title = {Implementation of a data repository-driven approach for targeted proteomics experiments by multiple reaction monitoring},
	journal = {Journal of Proteomics},
	volume = {72},
	number = {5},
	year = {2009},
	note = {ISI Document Delivery No.: 478RATimes Cited: 5Cited Reference Count: 30Walsh, Geraldine M. Lin, Shujun Evans, Daniel M. Khosrovi-Eghbal, Arash Beavis, Ronald C. Kast, Juergen},
	month = {Jul},
	pages = {838-852},
	type = {Article},
	abstract = {Multiple reaction monitoring (MRM), commonly employed for the mass spectrometric detection of small molecules, is rapidly gaining ground in proteomics. Its high sensitivity and specificity makes this targeted approach particularly useful when sample throughput or proteome coverage limits global studies. Existing tools to design MRM assays rely exclusively on theoretical predictions, or combine them with previous observations on the same type of sample. The additional mass spectrometric experimentation this requires can pose significant demands on time and material. To overcome these challenges, a new MRM worksheet was introduced into The Global Proteome Machine database (GPMDB) that provided all of the information needed to design MRM transitions based solely on archived observations made by other researchers in previous experiments. This required replacing the precursor ion intensity by the number of peptide observations, which proved to be an adequate substitute if peptides did not occur in multiple forms. While the absence of collision energy information proved largely inconsequential, successful prediction of unique transitions depended on the type of fragment ion involved. The design of MRM assays for iTRAQ-labeled tryptic peptides obtained from human platelet proteins demonstrated the usefulness of the MRM worksheet also for quantitative applications. This workflow, which relies exclusively on experimental observations stored in data repositories, therefore represents an attractive alternative for the prediction of MRM transitions prior to experimental validation and optimization. (C) 2008 Elsevier B.V. All rights reserved.},
	keywords = {ABSOLUTE, Data repository, HIGH-SENSITIVITY, LIBRARIES, Multiple reaction monitoring, PEPTIDES, PHOSPHORYLATION, PLASMA-PROTEINS, PLATELETS, PREDICTION, PROTEIN IDENTIFICATION, PROTEOMICS, QUANTIFICATION, SHOTGUN PROTEOMICS, Tandem mass spectrometry, TANDEM MASS-SPECTROMETRY, Targeted},
	isbn = {1874-3919},
	url = {<Go to ISI>://000268604400013},
	author = {Walsh, G. M. and Lin, S. and Evans, D. M. and Khosrovi-Eghbal, A. and Beavis, R. C. and Kast, J.}
}
@article {1414,
	title = {Multiple neutral loss monitoring (MNM): A multiplexed method for post-translational modification screening},
	journal = {Journal of the American Society for Mass Spectrometry},
	volume = {17},
	number = {3},
	year = {2006},
	note = {ISI Document Delivery No.: 021SETimes Cited: 11Cited Reference Count: 20},
	month = {Mar},
	pages = {307-317},
	type = {Article},
	abstract = {Post-translational modifications of proteins are involved in determining the activity of proteins and are essential for proper protein function. Current mass spectrometric strategies require one to specify a particular type of modification, in some cases also a particular charge state of a protein or peptide that is to be studied before the actual analysis. Due to these requirements, most of the modifications on proteins are not considered in such an experiment and, thus, a series of similar analyses need to be performed to ensure a more extensive characterization. A novel scan strategy has been developed, multiple neutral loss monitoring (MNM), allowing for the comprehensive screening of post-translational modifications (PTM) on proteins that fragment as neutral losses in a mass spectrometer. MNM method parameters were determined by performing product ion scans on a number of modified peptides over a range of collision energies, providing neutral loss energy profiles and optimal collision energies (OCE) for each modification, supplying valuable information pertaining to the fragmentation of these modifications and the necessary parameters that would be required to obtain the best analysis. As the optimal collision energy was highly dependent on the type of modification and the charge state of the peptide, the MNM scan was operated with a collision energy gradient. Autocorrelation analyses identified the type of modification, and convolution mapping analyses identified the associated peptide. The MNM scan with the new collision energy parameters was successfully applied to a mixture of four modified peptides in a BSA digest. The implementation of this technique will allow for comprehensive screening of all modifications that fragment as neutral losses.},
	keywords = {COLLISION-INDUCED DISSOCIATION, PEPTIDES, PROTEIN-PHOSPHORYLATION, PROTEOMIC ANALYSIS, SCAN, TANDEM MASS-SPECTROMETRY},
	isbn = {1044-0305},
	url = {<Go to ISI>://000236004700004},
	author = {Hoffman, M. D. and Sniatynski, M. J. and Rogalski, J. C. and Le Blanc, J. C. Y. and Kast, J.}
}
@article {4306,
	title = {Indirect enzyme-linked immunosorbent assay for the quantitative estimation of lysergic acid diethylamide in urine},
	journal = {Clinical Chemistry},
	volume = {44},
	number = {5},
	year = {1998},
	note = {ISI Document Delivery No.: ZL795Times Cited: 5Cited Reference Count: 27},
	month = {May},
	pages = {985-990},
	type = {Article},
	abstract = {A new antibody to lysergic acid diethylamide (LSD) was used to develop a novel indirect ELISA for the quantification of drug in urine. Evaluation of the new assay with the commercially available LSD ELISA (STC Diagnostics) shows improved performance. The test requires 50 mu L of urine, which is used to measure concentrations of drug in the mu g/L to ng/L range. The Limit of detection was 8 ng/L compared with 85 ng/L in the commercial assay, and analytical recoveries were 98-106\%. Our test detected 0.1 mu g/L of LSD in urine with an intraassay CV of 2.4\% (n = 8) compared with 6.0\% for a 0.5 mu g/L sample in the commercial assay (n = 20). The upper and lower limits of quantification were estimated to be 7 mu g/L and 50 ng/L, respectively. Specificity was evaluated by measuring the extent of cross-reactivity with 24 related substances. Drug determination using the new assay offers both improved sensitivity and precision compared with existing methods, thus facilitating the preliminary quantitative estimation of LSD in urine at lower concentrations with a greater degree of certainty.},
	keywords = {AFFINITY, BODY-FLUIDS, ELISA, GAS-CHROMATOGRAPHY, METABOLITES, MONOCLONAL-ANTIBODIES, N-DEMETHYL-LSD, RADIOIMMUNOASSAY, SERUM, TANDEM MASS-SPECTROMETRY},
	isbn = {0009-9147},
	url = {<Go to ISI>://000073472300014},
	author = {Kerrigan, S. and Brooks, D. E.}
}
@article {4069,
	title = {Design and synthesis of 2{\textquoteright}-deoxy-2{\textquoteright}-fluorodisaccharides as mechanism-based glycosidase inhibitors that exploit aglycon specificity},
	journal = {Journal of the American Chemical Society},
	volume = {119},
	number = {25},
	year = {1997},
	note = {ISI Document Delivery No.: XG882Times Cited: 37Cited Reference Count: 23},
	month = {Jun},
	pages = {5792-5797},
	type = {Article},
	abstract = {Stable, aglycon-specific inactivators of glycosidases have considerable potential as fools in the study of mechanisms of oligosaccharide processing, and possibly as avenues toward new therapeutics. Glycosidases for which the rate-determining step with the natural substrate is the hydrolysis of the glycosyl-enzyme intermediate are shown to be inactivated by the 2{\textquoteright}-deoxy-2{\textquoteright}-fluoro derivative of this substrate. Thus Agrobacterium faecalis beta-glucosidase is inactivated by 2{\textquoteright}-deoxy-2{\textquoteright}-fluorocellobiose according to inactivation parameters of k(i) = 0.018 min(-1) and K-i = 20 mM. Inactivation is shown to occur via the accumulation of the same 2-deoxy-2-fluoroglycosyl-enzyme intermediate as that formed using activated 2-deoxy-2-fluoroglycosides by identification of the labeled peptide in proteolytic digests. Thus, interactions between the enzyme and the sugar aglycon provide sufficient transition state stabilization to allow formation and trapping of the glycosyl-enzyme. beta-Glucocerebrosidase, a beta-glucosidase specific for hydrolysis of glucocerebrosides, is not inactivated by 2{\textquoteright}-deoxy-2{\textquoteright}-fluorocellobiose, thereby demonstrating the aglycon specificity of this class of inactivator.},
	keywords = {ACTIVE-SITE NUCLEOPHILE, beta-glucosidase, GALACTOSIDASE, IDENTIFICATION, residue, TANDEM MASS-SPECTROMETRY},
	isbn = {0002-7863},
	url = {<Go to ISI>://A1997XG88200003},
	author = {McCarter, J. D. and Yeung, W. and Chow, J. and Dolphin, D. and Withers, S. G.}
}
@article {3716,
	title = {NMR, MS and X-ray crystal structure determination of the bixin family of apocarotenoids},
	journal = {Journal of Chemical Research-S},
	number = {10},
	year = {1996},
	note = {ISI Document Delivery No.: VT903Times Cited: 4Cited Reference Count: 70},
	month = {Oct},
	pages = {446-\&},
	type = {Article},
	abstract = {The assignment of the H-1 and C-13 NMR spectra of alpha-bixin, methyl alpha-bixin, beta-bixin and methyl beta-bixin have been carried out using a combination of one- and two-dimensional techniques; the FAB(+) mass spectra of all these bixins had the molecular ion and methyl tropylium as high abundance peaks; also, the structures of alpha-bixin and methyl alpha-bixin have been confirmed by X-ray crystal structure determinations.},
	keywords = {ALL-TRANS, ANNATTO, ASSIGNMENTS, BETA-CAROTENE, COMPLETE H-1, FAST-ATOM-BOMBARDMENT, ORELLANA, SPECTRA, TANDEM MASS-SPECTROMETRY, THERMAL-DEGRADATION},
	isbn = {0308-2342},
	url = {<Go to ISI>://A1996VT90300006},
	author = {Kelly, D. R. and Edwards, A. A. and Parkinson, J. A. and Olovsson, G. and Trotter, J. and Jones, S. and Malik, K. M. A. and Hursthouse, M. B. and Hibbs, D. E.}
}
