ArticleMethods in molecular biology (Clifton, N.J.)2021
Targeted Protein Quantification Using Parallel Reaction Monitoring (PRM).
Article in Methods in molecular biology (Clifton, N.J.), 2021. 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.
- Article
- The GF-NEO discovery platform unveils a [KQE][DG] sequence motif within fusion neoantigens in pediatric cancer.iScience · 2026Article
- Article
- Multi-Omic Analysis Identifies Key Genes Driving Testicular Fusion inInternational journal of molecular sciences · 2025Article
- Proteomic profiling of cerebrospinal fluid uncovers distinctive pathophysiological changes and potential biomarkers in pediatric tubercular meningitis.Frontiers in cellular and infection microbiology · 2025Article
- Specification of neural circuit architecture shaped by context-dependent patterned LAR-RPTP microexons.Nature communications · 2024Article
- Exoproteome analysis of Pseudomonas aeruginosa response to high alkane stress.Archives of microbiology · 2024Article
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Targeted proteomics represents an efficient method to quantify proteins of interest with high sensitivity and accuracy. Targeted approaches were first established for triple quadrupole instruments, but the emergence of hybrid instruments allowing for high-resolution and accurate-mass measurements of MS/MS fragment ions enabled the development of parallel reaction monitoring (PRM). In PRM analysis, specific peptides are measured as representatives of proteins in complex samples, with the full product ion spectra being acquired, allowing for identification and quantification of the peptides. Ideally, corresponding stable isotope-labeled peptides are spiked into the analyzed samples to account for technical variation and enhance the precision. Here, we describe the development of a PRM assay including the selection of appropriate peptides that fulfill the criteria to serve as unique surrogates of the targeted proteins. We depict the sequential steps of method development and the generation of calibration curves. Furthermore, we present the open-access tool CalibraCurve for the determination of the linear concentration ranges and limits of quantification (LOQ).
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Registered trials
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