@article{williams_saggese_toups_frahm_an_li_lebrilla_muddiman_2008, title={Investigations with O-linked protein glycosylations by matrix-assisted laser desorption/ionization Fourier transform ion cyclotron resonance mass spectrometry}, volume={43}, ISSN={["1076-5174"]}, url={http://europepmc.org/abstract/med/18324610}, DOI={10.1002/jms.1398}, abstractNote={Abstract}, number={9}, journal={JOURNAL OF MASS SPECTROMETRY}, author={Williams, Taufika Islam and Saggese, Diana A. and Toups, Kristina L. and Frahm, Jennifer L. and An, Hyun Joo and Li, Bensheng and Lebrilla, Carlito B. and Muddiman, David C.}, year={2008}, month={Sep}, pages={1215–1223} }
 @article{frahm_bori_comins_hawkridge_muddiman_2007, title={Achieving augmented limits of detection for peptides with hydrophobic alkyl tags}, volume={79}, ISSN={["0003-2700"]}, DOI={10.1021/ac070558q}, abstractNote={The wide range of protein concentrations found in biological matrixes presents a formidable analytical challenge in proteomics experiments. It is predicted that low-abundance proteins are the likely clinically relevant targets in disease-based proteomics analyses. To effectively analyze low-abundance proteins by electrospray ionization mass spectrometry, limits of detection must be improved upon. Previous studies have demonstrated hydrophobicity is a main determinant of the electrospray ionization response. One would expect to improve the electrospray ionization response of a hydrophilic peptide by making it more hydrophobic, thus increasing the molecule's affinity for the surface of the electrospray droplet, thereby allowing the molecule to more effectively compete for charge. In this report, we demonstrate a strategy to increase the electrospray ionization response of cysteine-containing peptides with the addition of an octylcarboxyamidomethyl modification via alkylation chemistry, which we name the ALiPHAT strategy (augmented limits of detection for peptides with hydrophobic alkyl tags). We demonstrate the relative increase in electrospray ionization response of peptides with an octylcarboxyamidomethyl modification compared to carboxyamidomethyl-modified peptides upon LC-MS analysis. Furthermore, we show the octylcarboxyamidomethyl group does not fragment or undergo neutral loss during collision-induced dissociation. Collectively, our results demonstrate the feasibility of the octylcarboxyamidomethyl modification to improve limits of detection for cysteine-containing peptides.}, number={11}, journal={ANALYTICAL CHEMISTRY}, author={Frahm, Jennifer L. and Bori, Ibrahim D. and Comins, Daniel L. and Hawkridge, Adam M. and Muddiman, David C.}, year={2007}, month={Jun}, pages={3989–3995} }
 @article{frahm_capo velez_muddiman_2007, title={Understanding the influence of post-excite radius and axial confinement on quantitative proteomic measurements using Fourier transform ion cyclotron resonance mass spectrometry}, volume={21}, ISSN={["1097-0231"]}, DOI={10.1002/rcm.2957}, abstractNote={Abstract}, number={7}, journal={RAPID COMMUNICATIONS IN MASS SPECTROMETRY}, author={Frahm, Jennifer L. and Capo Velez, Coral M. and Muddiman, David C.}, year={2007}, pages={1196–1204} }
 @article{frahm_howard_heber_muddiman_2006, title={Accessible proteomics space and its implications for peak capacity for zero-, one- and two-dimensional separations coupled with FT-ICR and TOF mass spectrometry}, volume={41}, ISSN={["1096-9888"]}, DOI={10.1002/jms.1024}, abstractNote={Abstract}, number={3}, journal={JOURNAL OF MASS SPECTROMETRY}, author={Frahm, JL and Howard, BE and Heber, S and Muddiman, DC}, year={2006}, month={Mar}, pages={281–288} }