x
Filter:
Filters applied
- Reviews
- HCDRemove HCD filter
- collision-induced dissociationRemove collision-induced dissociation filter
- ETDRemove ETD filter
Publication Date
Please choose a date range between 2020 and 2021.
Reviews & Perspectives
3 Results
- Review Special Issue: GlycoproteomicsOpen Access
Recent Advances in Software Tools for More Generic and Precise Intact Glycopeptide Analysis
Molecular & Cellular ProteomicsVol. 20100060Published online: February 5, 2021- Weiqian Cao
- Mingqi Liu
- Siyuan Kong
- Mengxi Wu
- Yang Zhang
- Pengyuan Yang
Cited in Scopus: 0In Brief This article provides a systematic review of the most recent MS-based strategies and corresponding software tools for the analysis of intact glycopeptides, particularly intact N-glycopeptides, reported in the last decade, including the process of identifying N-glycopeptides from MS data, the existing methods of MS data acquisition and interpretation, the quality control methods, the display of results, and the software applications. - Review Special Issue: GlycoproteomicsOpen Access
Developments in Mass Spectrometry for Glycosaminoglycan Analysis: A Review
Molecular & Cellular ProteomicsVol. 20100025Published online: January 5, 2021- Lauren E. Pepi
- Patience Sanderson
- Morgan Stickney
- I. Jonathan Amster
Cited in Scopus: 0In Brief Glycosaminoglycans (GAGs) participate in a variety of biological functions and have a multitude of medicinal properties. Due to their non template driven biosynthesis, GAGs are produced as nonuniform complex mixtures. Mass spectrometry paired with on-line separation techniques has been utilized to determine the composition of these complex mixtures. Advances in tandem mass spectrometry have also made determining sequence information such as sulfation location and C-5 epimerization possible. This review covers recent developments in the analysis of GAGs using mass spectrometry. - Review Special Issue: GlycoproteomicsOpen Access
Meta-heterogeneity: Evaluating and Describing the Diversity in Glycosylation Between Sites on the Same Glycoprotein
Molecular & Cellular ProteomicsVol. 20100010Published online: December 7, 2020- Tomislav Čaval
- Albert J.R. Heck
- Karli R. Reiding
Cited in Scopus: 0In Brief Diversity in protein glycosylation can be described in terms of micro-heterogeneity and macro-heterogeneity, respectively, referring to the variation and occupancy of glycans at a given glycosylation site. However, these terms are not sufficient to describe a higher level of regulation when proteins are multiply glycosylated. For this, we propose the term meta-heterogeneity: variation in glycosylation across multiple sites of a given glycoprotein. In this review, we describe several remarkable examples of glycoprotein meta-heterogeneity and underline the need for its investigation.