ArticlePloS one2011
Simultaneous analysis of proteome, phospho- and glycoproteome of rat kidney tissue with electrostatic repulsion hydrophilic interaction chromatography.
Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 54 citations in OpenAlex.
- Recent advancements in sample pretreatment methods for glycoproteomics.Biophysics reports · 2026Article
- Decoding Kidney Pathophysiology: Omics-Driven Approaches in Precision Medicine.Journal of personalized medicine · 2024Review
- Review
- Integrated proteomic, phosphoproteomic, and N-glycoproteomic analyses of theCurrent research in food science · 2022Article
- Finding the Sweet Spot in ERLIC Mobile Phase for Simultaneous Enrichment of N-Glyco and Phosphopeptides.Journal of the American Society for Mass Spectrometry · 2019Article
- Sweet and SourFrontiers in microbiology · 2019Article
- Glycoprotein Enrichment Analytical Techniques: Advantages and Disadvantages.Methods in enzymology · 2017Article
- HILIC and ERLIC Enrichment of Glycopeptides Derived from Breast and Brain Cancer Cells.Journal of proteome research · 2016Article
- O-glycosylation sites identified from mucin core-1 type glycopeptides from human serum.Glycoconjugate journal · 2016Article
- Sensing Small Changes in Protein Abundance: Stimulation of Caco-2 Cells by Human Whey Proteins.Journal of proteome research · 2016Article
- Current strategies and findings in clinically relevant post-translational modification-specific proteomics.Expert review of proteomics · 2015Review
- Anion-exchange chromatography of phosphopeptides: weak anion exchange versus strong anion exchange and anion-exchange chromatography versus electrostatic repulsion-hydrophilic interaction chromatography.Analytical chemistry · 2015Article
- Solid-phase extraction strategies to surmount body fluid sample complexity in high-throughput mass spectrometry-based proteomics.Journal of analytical methods in chemistry · 2015Review
- Hypoxia-induced changes to integrin α 3 glycosylation facilitate invasion in epidermoid carcinoma cell line A431.Molecular & cellular proteomics : MCP · 2014Article
- Urinary proteomic and non-prefractionation quantitative phosphoproteomic analysis during pregnancy and non-pregnancy.BMC genomics · 2013Article
- Protein analysis by shotgun/bottom-up proteomics.Chemical reviews · 2013Review
- Online nanoscale ERLIC-MS outperforms RPLC-MS for shotgun proteomics in complex mixtures.Journal of proteome research · 2012Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein post-translational modifications (PTMs) are regulated separately from protein expression levels. Thus, simultaneous characterization of the proteome and its PTMs is pivotal to an understanding of protein regulation, function and activity. However, concurrent analysis of the proteome and its PTMs by mass spectrometry is a challenging task because the peptides bearing PTMs are present in sub-stoichiometric amounts and their ionization is often suppressed by unmodified peptides of high abundance. We describe here a method for concurrent analysis of phosphopeptides, glycopeptides and unmodified peptides in a tryptic digest of rat kidney tissue with a sequence of ERLIC and RP-LC-MS/MS in a single experimental run, thereby avoiding inter-experimental variation. Optimization of loading solvents and elution gradients permitted ERLIC to be performed with totally volatile solvents. Two SCX and four ERLIC gradients were compared in details, and one ERLIC gradient was found to perform the best, which identified 2929 proteins, 583 phosphorylation sites in 338 phosphoproteins and 722 N-glycosylation sites in 387 glycoproteins from rat kidney tissue. Two hundred low-abundance proteins with important functions were identified only from the glyco- or phospho-subproteomes, reflecting the importance of the enrichment and separation of modified peptides by ERLIC. In addition, this strategy enables identification of unmodified and corresponding modified peptides (partial phosphorylation and N-glycosylation) from the same protein. Interestingly, partially modified proteins tend to occur on proteins involved in transport. Moreover, some membrane or extracellular proteins, such as versican core protein and fibronectin, were found to have both phosphorylation and N-glycosylation, which may permit an assessment of the potential for cross talk between these two vital PTMs and their roles in regulation.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.