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Reviews & Perspectives
3 Results
- ReviewOpen Access
Proteomics-Based Insights Into the SARS-CoV-2–Mediated COVID-19 Pandemic: A Review of the First Year of Research
Molecular & Cellular ProteomicsVol. 20100103Published online: June 2, 2021- Jeremy L. Praissman
- Lance Wells
Cited in Scopus: 0In Brief SARS-CoV-2, the betacoronavirus that caused the COVID-19 pandemic, became a major source of human disease and death in 2020. The fundamental constituents of a virus being its genome and proteome, characterizing the proteome is essential to understanding its biology. In this review article, we survey the proteomics literature from the first year of the COVID-19 pandemic, including protein–protein interaction studies, post-translational modification studies, and work using proteomics technologies to probe host response, which collectively inform efforts to ameliorate the pandemic. - Review Special Issue: GlycoproteomicsOpen Access
Recent Advances in Analytical Approaches for Glycan and Glycopeptide Quantitation
Molecular & Cellular ProteomicsVol. 20100054Published online: February 19, 2021- Daniel G. Delafield
- Lingjun Li
Cited in Scopus: 0In Brief Recent years have seen an explosion in novel strategies for quantitative glycomics and glycoproteomics. Whether through metabolic incorporation of stable isotopes, deposition of custom isotopic labels, or high-throughput isobaric chemical tags, these numerous novel strategies provide ease of access to glycomic and glycoproteomic investigation. This review highlights the recent innovations in labeling methods, label-free strategies, acquisition modes, and bioinformatic tools for glycan and glycopeptide quantitation, while providing critical evaluations and technical considerations to enable effective analysis. - Review Special Issue: GlycoproteomicsOpen Access
Calculating Glycoprotein Similarities From Mass Spectrometric Data
Molecular & Cellular ProteomicsVol. 20100028Published online: January 5, 2021- William E. Hackett
- Joseph Zaia
Cited in Scopus: 0In Brief To understand the roles of glycoproteins in biological processes, it is necessary to quantify the changes that occur to glycosylation at individual sites and to the whole molecule. That glycoprotein glycosylation is inherently heterogeneous means that the distribution of glycoforms at each glycosite must be quantified in order to inform calculation of molecular similarities. We review analytical and statistical methods for determining glycoprotein molecular similarities from glycoproteomics data.