ArticleJournal of proteome research2012
Label-free quantitation of protein modifications by pseudo selected reaction monitoring with internal reference peptides.
Article in Journal of proteome research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
37 citing papers in PubMed, 70 citations in OpenAlex.
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- Prospective observational study on biomarkers of response in pancreatic ductal adenocarcinoma.Nature medicine · 2024Observational
- Selenium Nanoparticles (SeNPs) Immunomodulation Is More Than Redox Improvement: Serum Proteomics and Transcriptomic Analyses.Antioxidants (Basel, Switzerland) · 2022Article
- Article
- Proteomic Approaches to Study Cysteine Oxidation: Applications in Neurodegenerative Diseases.Frontiers in molecular neuroscience · 2021Review
- The Skyline ecosystem: Informatics for quantitative mass spectrometry proteomics.Mass spectrometry reviews · 2020Review
- ANPELA: analysis and performance assessment of the label-free quantification workflow for metaproteomic studies.Briefings in bioinformatics · 2020Article
- Identification of endogenous small peptides involved in rice immunity through transcriptomics- and proteomics-based screening.Plant biotechnology journal · 2020Article
- The impact of thioredoxin reduction of allosteric disulfide bonds on the therapeutic potential of monoclonal antibodies.The Journal of biological chemistry · 2019Article
- Application of targeted mass spectrometry in bottom-up proteomics for systems biology research.Journal of proteomics · 2018Review
- Multiple modes of PRC2 inhibition elicit global chromatin alterations in H3K27M pediatric glioma.Science advances · 2018Article
- Panorama Public: A Public Repository for Quantitative Data Sets Processed in Skyline.Molecular & cellular proteomics : MCP · 2018Article
- Green-fruited Solanum habrochaites lacks fruit-specific carotenogenesis due to metabolic and structural blocks.Journal of experimental botany · 2017Article
- Quantitative proteomic characterization of redox-dependent post-translational modifications on protein cysteines.Molecular bioSystems · 2017Review
- A Perspective on Extracellular Vesicles Proteomics.Frontiers in chemistry · 2017Review
- Specificity of Protein Covalent Modification by the Electrophilic Proteasome Inhibitor Carfilzomib in Human Cells.Molecular & cellular proteomics : MCP · 2016Article
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
Abstract
Liquid chromatography tandem mass spectrometry (LC-MS/MS) based methods provide powerful tools for the quantitative analysis of modified proteins. We have developed a label-free approach using internal reference peptides (IRP) from the target protein for signal normalization without the need for isotope labeling. Ion-trap mass spectrometry and pseudo-selected reaction monitoring (pSRM) were used to acquire full MS/MS and MS(3) spectra from target peptides. Skyline, a widely used software for SRM experiments, was used for chromatographic ion extraction. Phosphopeptides spiked into a BSA background yielded concentration response curves with high correlation coefficients (typically >0.9) and low coefficients of variation (≤15%) over a 200-fold concentration range. Stable isotope dilution (SID) and IRP methods were compared for quantitation of six site-specific phosphorylations in the epidermal growth factor receptor (EGFR) in epidermal growth factor-stimulated A431 cells with or without the addition of EGFR inhibitors cetuximab and gefitinib. Equivalent responses were observed with both IRP and SID methods, although analyses using the IRP method typically had higher median CVs (22-31%) than SID (10-20%). Analyses using both methods were consistent with immunoblot using site-selective antibodies. The ease of implementation and the suitability for targeted quantitative comparisons make this method suitable for broad application in protein biochemistry.
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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.