ArticleAnalytical chemistry2013
Resin-assisted enrichment of N-terminal peptides for characterizing proteolytic processing.
Article in Analytical chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Exploiting Selective Position Labeling to Unveil the Hidden Complexity of Terminomics.Molecules (Basel, Switzerland) · 2026Review
- Resin and Magnetic Nanoparticle-Based Free Radical Probes for Glycan Capture, Isolation, and Structural Characterization.Analytical chemistry · 2019Article
- Identification of N-terminal protein processing sites by chemical labeling mass spectrometry.Rapid communications in mass spectrometry : RCM · 2019Article
- Pharmacological Modulation of the N-End Rule Pathway and Its Therapeutic Implications.Trends in pharmacological sciences · 2015Review
- Mining proteomic data to expose protein modifications in Methanosarcina mazei strain Gö1.Frontiers in microbiology · 2015Article
- N-Terminal-oriented proteogenomics of the marine bacterium roseobacter denitrificans Och114 using N-Succinimidyloxycarbonylmethyl)tris(2,4,6-trimethoxyphenyl)phosphonium bromide (TMPP) labeling and diagonal chromatography.Molecular & cellular proteomics : MCP · 2014Article
- Solid-phase N-terminal peptide enrichment study by optimizing trypsin proteolysis on homoarginine-modified proteins by mass spectrometry.Rapid communications in mass spectrometry : RCM · 2014Article
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Authors and funding
8 authors.
Funding
Abstract
A resin-assisted enrichment method has been developed for specific isolation of protein N-terminal peptides to facilitate LC-MS/MS characterization of proteolytic processing, a major form of posttranslational modifications. In this method, protein thiols are blocked by reduction and alkylation, and protein lysine residues are converted to homoarginines. Protein N-termini are selectively converted to reactive thiol groups, and the thiol-containing N-terminal peptides are then captured by a thiol-affinity resin with high specificity (>97%). The efficiencies of these sequential reactions were demonstrated to be nearly quantitative. The resin-assisted N-terminal peptide enrichment approach was initially applied to a cell lysate of the filamentous fungus Aspergillus niger. Subsequent C-MS/MS analyses resulted in the identification of 1672 unique protein N-termini or proteolytic cleavage sites from 690 unique proteins.
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