@article{de leoz_duewer_fung_liu_yau_potter_staples_furuki_frenkel_hu_et al._2019, title={NIST Interlaboratory Study on Glycosylation Analysis of Monoclonal Antibodies: Comparison of Results from Diverse Analytical Methods}, volume={19}, ISSN={1535-9476 1535-9484}, url={http://dx.doi.org/10.1074/mcp.RA119.001677}, DOI={10.1074/mcp.RA119.001677}, abstractNote={Glycosylation is a topic of intense current interest in the development of biopharmaceuticals because it is related to drug safety and efficacy. This work describes results of an interlaboratory study on the glycosylation of the Primary Sample (PS) of NISTmAb, a monoclonal antibody reference material. Seventy-six laboratories from industry, university, research, government, and hospital sectors in Europe, North America, Asia, and Australia submitted a total of 103 reports on glycan distributions. The principal objective of this study was to report and compare results for the full range of analytical methods presently used in the glycosylation analysis of mAbs. Therefore, participation was unrestricted, with laboratories choosing their own measurement techniques. Protein glycosylation was determined in various ways, including at the level of intact mAb, protein fragments, glycopeptides, or released glycans, using a wide variety of methods for derivatization, separation, identification, and quantification. Consequently, the diversity of results was enormous, with the number of glycan compositions identified by each laboratory ranging from 4 to 48. In total, one hundred sixteen glycan compositions were reported, of which 57 compositions could be assigned consensus abundance values. These consensus medians provide community-derived values for NISTmAb PS. Agreement with the consensus medians did not depend on the specific method or laboratory type. The study provides a view of the current state-of-the-art for biologic glycosylation measurement and suggests a clear need for harmonization of glycosylation analysis methods.}, number={1}, journal={Molecular & Cellular Proteomics}, publisher={American Society for Biochemistry & Molecular Biology (ASBMB)}, author={De Leoz, Maria Lorna A. and Duewer, David L. and Fung, Adam and Liu, Lily and Yau, Hoi Kei and Potter, Oscar and Staples, Gregory O. and Furuki, Kenichiro and Frenkel, Ruth and Hu, Yunli and et al.}, year={2019}, month={Oct}, pages={11–30} }
 @article{kottke_lee_jonke_seneviratne_hecht_muddiman_torres_fedorov_2017, title={DRILL: An electrospray ionization-mass spectrometry interface for improved sensitivity via inertial droplet sorting and electrohydrodynamic focusing in a swirling flow}, volume={89}, DOI={10.1021/acs.analchem.7b01555}, number={17}, journal={Analytical Chemistry}, author={Kottke, P. A. and Lee, J. Y. and Jonke, A. P. and Seneviratne, C. A. and Hecht, E. S. and Muddiman, D. C. and Torres, M. P. and Fedorov, A. G.}, year={2017}, pages={8981–8987} }
 @article{loziuk_hecht_muddiman_2017, title={N-linked glycosite profiling and use of Skyline as a platform for characterization and relative quantification of glycans in differentiating xylem of Populus trichocarpa}, volume={409}, DOI={10.1007/s00216-016-9776-5}, number={2}, journal={Analytical and Bioanalytical Chemistry}, author={Loziuk, P. L. and Hecht, E. S. and Muddiman, D. C.}, year={2017}, pages={487–497} }
 @article{hecht_loziuk_muddiman_2017, title={Xylose migration during tandem mass spectrometry of N-linked glycans}, volume={28}, DOI={10.1007/s13361-016-1588-5}, number={4}, journal={Journal of the American Society for Mass Spectrometry}, author={Hecht, E. S. and Loziuk, P. L. and Muddiman, D. C.}, year={2017}, pages={729–732} }
 @article{hecht_mccord_muddiman_2016, title={A quantitative glycomics and proteomics combined purification strategy}, number={109}, journal={Jove-Journal of Visualized Experiments}, author={Hecht, E. S. and McCord, J. P. and Muddiman, D. C.}, year={2016} }
 @misc{hecht_oberg_muddiman_2016, title={Optimizing mass spectrometry analyses: a tailored review on the utility of design of experiments}, volume={27}, DOI={10.1007/s13361-016-1344-x}, number={5}, journal={Journal of the American Society for Mass Spectrometry}, author={Hecht, E. S. and Oberg, A. L. and Muddiman, D. C.}, year={2016}, pages={767–785} }
 @article{hecht_mccord_muddiman_2015, title={Definitive screening design optimization of mass spectrometry parameters for sensitive comparison of filter and solid phase extraction purified, INLIGHT plasma N-glycans}, volume={87}, DOI={10.1021/acs.analchem.5b01609}, number={14}, journal={Analytical Chemistry}, author={Hecht, E. S. and McCord, J. P. and Muddiman, D. C.}, year={2015}, pages={7305–7312} }
 @article{hecht_scholl_walker_taylor_cliby_motsinger-reif_muddiman_2015, title={Relative quantification and higher-order modeling of the plasma glycan cancer burden ratio in ovarian cancer case-control samples}, volume={14}, DOI={10.1021/acs.jproteome.5b00703}, number={10}, journal={Journal of Proteome Research}, author={Hecht, E. S. and Scholl, E. H. and Walker, S. H. and Taylor, A. D. and Cliby, W. A. and Motsinger-Reif, A. A. and Muddiman, D. C.}, year={2015}, pages={4394–4401} }