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Concepcion Remoroza, Meghan Burke Harris, Tytus Mak, Sergey Sheetlin, Yuri Mirokhin, Zachary Goecker, Brian T. Cooper, Mark Lowenthal, Xiaoyu (Sara) Yang, Guanghui Wang, Dmitrii V. Tchekhovskoi, Stephen E. Stein
We report the comparison of mass-spectral-based abundances of tryptic glycopeptides to fluorescence abundances of released labeled glycans and the effects of mass and charge state and in-source fragmentation on glycopeptide abundances. The primary
Cassandra Pegg, Benjamin Schulz, Ben Neely, Gregory Albery, Colin Carlson
The sugars that coat the outsides of viruses and host cells are key to successful disease transmission, but they remain understudied compared to other molecular features. Understanding the comparative zoology of glycosylation - and harnessing it for
Concepcion Remoroza, Meghan Burke Harris, Xiaoyu (Sara) Yang, Sergey Sheetlin, Yuri Mirokhin, Sanford Markey, Dmitrii V. Tchekhovskoi, Stephen E. Stein
We present a mass-spectral library-based method for analyzing site-specific N-linked protein glycosylation. Its operation and utility are illustrated by applying it to both newly measured and available proteomics data of human milk glycoproteins. It
Mark Lowenthal, Blaza Toman, Brian Lang, Karen W. Phinney
Standard Reference Material (SRM) 3655 is intended primarily for use as a calibration standard for the measurement of enzymatically released N-linked glycans. Applications of SRM 3655 include the benchmarking and comparability of analytical techniques, as
Background The ability to measure and describe the microbiome has led to a surge in information about the gut microbiome and its role in health and disease. The relationship between nutrition and the gut microbiome is central, as the diet is a source of
Concepcion Remoroza, Meghan Burke Harris, Yi Liu, Yuri Mirokhin, Dmitrii V. Tchekhovskoi, Xiaoyu (Sara) Yang, Stephen E. Stein
A method for representing and comparing distributions of N-linked glycans located at specific sites in proteins is presented. The representation takes the form of a simple mass spectrum for a given peptide sequence, with each peak corresponding to a
Concepcion A. Remoroza, Tytus D. Mak, Yuri A. Mirokhin, Sergey L. Sheetlin, Xiaoyu Yang, Stephen E. Stein, Power L. Michael, San Andres V. Joice, Yuxue Liang
This study significantly expands both the scope and method of identification for construction of a previously reported tandem mass spectral library of 74 human milk oligosaccharides (HMOs) derived from results of LC-MS/MS experiments. In the present work
M. L. De Leoz, David L. Duewer, Scientists Multiple, Stephen E. Stein
Glycosylation is a topic of intense current interest in the development of biologic drugs since it is related to drug safety and efficacy. This work describes results of an interlaboratory study on the glycosylation of NISTmAb, a monoclonal antibody
M. L. De Leoz, Yamil Simon, Robert J. Woods, Stephen E. Stein
Reference spectral library searching, while widely used to identify compounds in other areas of mass spectrometry, is not commonly used in glycomics. Building on a study by Cotter and coworkers on analysis of sialylated oligosaccharides using atmospheric
Mark S. Lowenthal, Christina M. Jones, Joan Adamo, Robert Bienvenu, Owen Fields, Soma Ghosh, Michael Liebman, Robert Schuck, Scott Steele
Building on the recent advances in next-generation sequencing, the integration of genomics, proteomics, metabolomics, and other approaches hold tremendous promise for precision medicine. The approval and adoption of these rapidly advancing technologies and
Concepcion A. Remoroza, Tytus D. Mak, M. L. De Leoz, Yuri A. Mirokhin, Stephen E. Stein
We report the development and availability of a mass spectral reference library for oligosaccharides in human milk. This represents a new variety of spectral library that includes consensus spectra of compounds annotated through various data analysis
Maria Lorna A. De Leoz, David L. Duewer, Stephen E. Stein
The National Institute of Standards and Technology coordinated an interlaboratory study for laboratories that measure glycosylation in monoclonal antibodies. This report describes the design of and results for the NIST Interlaboratory Study on the
Mark S. Lowenthal, Kiersta S. Davis, Lisa E. Kilpatrick, Catherine A. Mouchahoir, Karen W. Phinney
N-glycosylation is well known to occur at asparagine residues in the canonical consensus sequence N-X-S/T, but has also been identified at a small number of N-X-C motifs including the Asn491 residue of human serotransferrin. Here we report additional novel