ArticleAnalytical chemistry2020
Selective Maleylation-Directed Isobaric Peptide Termini Labeling for Accurate Proteome Quantification.
Article in Analytical chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 13 citations in OpenAlex.
- Development of novel isobaric tags enables accurate and sensitive multiplexed proteomics using complementary ions.Analytical and bioanalytical chemistry · 2023Article
- Chemical isotope labeling for quantitative proteomics.Mass spectrometry reviews · 2023Review
- Review
- Comparison of LFQ and IPTL for Protein Identification and Relative Quantification.Molecules (Basel, Switzerland) · 2021Article
- A Versatile Isobaric Tag Enables Proteome Quantification in Data-Dependent and Data-Independent Acquisition Modes.Analytical chemistry · 2020Article
- A Collision-Induced Dissociation Cleavable Isobaric Tag for Peptide Fragment Ion-Based Quantification in Proteomics.Journal of proteome research · 2020Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Isobaric peptide termini labeling (IPTL) is an attractive protein quantification method because it provides more accurate and reliable quantification information than traditional isobaric labeling methods (e.g., TMT and iTRAQ) by making use of the entire fragment-ion series instead of only a single reporter ion. The multiplexing capacity of published IPTL implementations is, however, limited to three. Here, we present a selective maleylation-directed isobaric peptide termini labeling (SMD-IPTL) approach for quantitative proteomics of LysC protein digestion. SMD-IPTL extends the multiplexing capacity to 4-plex with the potential for higher levels of multiplexing using commercially available
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