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   https://doi.org/10.1039/d1mo00025j  

   Xu, Senhan ; Sun, Fangxu ; Tong, Ming ; Wu, Ronghu ( April 2021 , Molecular Omics)

   null (Ed.)

   Protein O -GlcNAcylation refers to the covalent binding of a single N -acetylglucosamine (GlcNAc) to the serine or threonine residue. This modification primarily occurs on proteins in the nucleus and the cytosol, and plays critical roles in many cellular events, including regulation of gene expression and signal transduction. Aberrant protein O -GlcNAcylation is directly related to human diseases such as cancers, diabetes and neurodegenerative diseases. In the past decades, considerable progress has been made for global and site-specific analysis of O -GlcNAcylation in complex biological samples using mass spectrometry (MS)-based proteomics. In this review, we summarized previous efforts on comprehensive investigation of protein O -GlcNAcylation by MS. Specifically, the review is focused on methods for enriching and site-specifically mapping O -GlcNAcylated peptides, and applications for quantifying protein O -GlcNAcylation in different biological systems. As O -GlcNAcylation is an important protein modification for cell survival, effective methods are essential for advancing our understanding of glycoprotein functions and cellular events. 

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2. LC/MS at the whole protein level: Studies of biomolecular structure and interactions using native LC/MS and cross-path reactive chromatography (XP-RC) MS

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3. Crosslinked zwitterionic polymeric ionic liquid-functionalized nitinol wires for fiber-in-tube solid-phase microextraction and UHPLC-MS/MS as an amyloid beta peptide binding protein assay in biological fluids

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4. A static headspace GC-MS/MS method for the determination of ethanol, iso-butanol, and n -butanol at nanomolar concentrations in aqueous environmental samples: Headspace GC-MS/MS

   https://doi.org/10.1002/lom3.10220  

   Mead, Ralph N. ; Cala, John M. ; Felix, J. David ; Shimizu, Megumi S. ; Casas, Matthew S. ; Lathrope, Thomas ; Avery, G. Brooks ; Kieber, Robert J. ; Willey, Joan D. ( December 2017 , Limnology and Oceanography: Methods)
5. Separation, identification, and confirmation of cyclic and tadpole macromolecules via UPLC-MS/MS

   https://doi.org/10.1039/d2an00208f  

   O'Neill, Jason M. ; Mao, Jialin ; Haque, Farihah M. ; Barroso-Bujans, Fabienne ; Grayson, Scott M. ; Wesdemiotis, Chrys ( May 2022 , The Analyst)

   Macrocyclic poly(glycidyl phenyl ether) (pGPE) synthesized via zwitterionic ring opening polymerization is typically contaminated by chains with linear and tadpole architecture. Although mass spectrometry (MS) analysis can readily confirm the presence of the linear byproduct, due to its unique mass, it is unable to differentiate between the cyclic and tadpole structures, which are constitutional isomers produced by backbiting reactions in monomeric or dimeric chains, respectively. To overcome this problem, ultraperformance reversed-phase liquid chromatography interfaced with electrospray ionization tandem mass spectrometry (UPLC-ESI-MS/MS) was employed. The separation achieved by UPLC revealed that the tadpole isomer elutes before the cyclic structure because of the increased polarity afforded by its distinctive substituents. The ratio of tadpole to cyclic species increased with the degree of polymerization, in agreement with the synthetic method used, as the potential for forming tadpole structures by backbiting is entropically favored in longer polymer chains. Once separated, the two isomers could be independently characterized by tandem mass spectrometry. The macrocyclic and tadpole species exhibit unique fragmentation patterns, including structurally diagnostic fragments for each structure. 

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