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Keyword
- DIA3
- DDA2
- ETD2
- EThcD2
- FDR2
- HCD2
- multiple reaction monitoring2
- parallel reaction monitoring2
- SILAC2
- AGP1
- CCS1
- Chinese Hamster Ovary1
- CHO1
- CID1
- Collisional-Induced Dissociation1
- Data-Dependent Acquisition1
- Data-Independent Acquisition1
- Electron Transfer Dissociation1
- Electron Transfer/Collisional-Induced Dissociation1
- Electron Transfer/Higher-Energy Dissociation1
- Electrospray Ionization1
- ESI1
- ETciD1
Reviews & Perspectives
3 Results
- ReviewOpen Access
An Introduction to Advanced Targeted Acquisition Methods
Molecular & Cellular ProteomicsVol. 20100165Published online: October 18, 2021- Mirjam van Bentum
- Matthias Selbach
Cited in Scopus: 0In Brief The analytical power of targeted proteomics depends on how efficiently the mass spectrometer detects target peptides. A number of “smart” acquisition approaches have been developed that enable more targets per run and improve analytical performance such as sensitivity, specificity, and quantitative accuracy. This review provides an introduction to these methods and highlights their inherent strengths and weaknesses. - 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.