ReviewBiochemistry2013
Targeted quantitation of proteins by mass spectrometry.
Review in Biochemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 144 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
144 citing papers in PubMed.
- Mass Spectrometry-Based Chromatographic and Computational Workflows for Biomarker and Therapeutic Target Discovery: A Comprehensive Review.Biomedical chromatography : BMC · 2026Review
- Pipettes and Pipelines: The Weapons of Omics Sciences for a New Age of Clinical Studies.Current issues in molecular biology · 2026Review
- Repurposing the liquid-based Pap test for the detection of ovarian cancer protein biomarkers.Clinical proteomics · 2026Article
- Review
- Peptide ratios for post-mortem interval estimation using targeted liquid chromatography triple quadrupole mass spectrometry.International journal of legal medicine · 2026Article
- tRNA modifications in cancer: from molecular mechanisms to clinical translation.Biomarker research · 2026Review
- Advances in Multiple Reaction Monitoring (MRM) for Targeted Proteomics in Biomedical Research.Advances in experimental medicine and biology · 2026Review
- LCMSpector: A simple open-source viewer for targeted hyphenated mass spectrometry analysis.PLoS computational biology · 2025Article
- Enrichment of mutant calmodulin protein in a murine model of a human calmodulinopathy.JCI insight · 2025Article
- Potential Markers for Thyroid Neoplasms in the Upstream Analysis of the Plasma Proteome.Bulletin of experimental biology and medicine · 2025Article
- Noncanonical altPIDD1 protein: unveiling the true major translational output of theLife science alliance · 2025Article
- Challenges and Insights in Absolute Quantification of Recombinant Therapeutic Antibodies by Mass Spectrometry: An Introductory Review.Antibodies (Basel, Switzerland) · 2025Review
- Proteomics: An Essential Tool to Study Plant-Specialized Metabolism.Biomolecules · 2024Review
- Aerobic adaptation and metabolic dynamics ofmSystems · 2024Article
- Quantitative Analysis of Complement Membrane Attack Complex Proteins Associated with Extracellular Vesicles.Proteomes · 2024Article
- GLUT2 regulation of p38 MAPK isoform protein expression and p38 phosphorylation in male versus female rat hypothalamic primary astrocyte Cultures.IBRO neuroscience reports · 2024Article
- Elevated Temperature Effects on Protein Turnover Dynamics inInternational journal of molecular sciences · 2024Article
- Immunoassays and Mass Spectrometry for Determination of Protein Concentrations in Genetically Modified Crops.Journal of agricultural and food chemistry · 2024Review
- A Top-Down Proteomic Assay to Evaluate KRAS4B-Compound Engagement.Analytical chemistry · 2024Article
- Review
84 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors.
Funding
Abstract
Quantitative measurement of proteins is one of the most fundamental analytical tasks in a biochemistry laboratory, but widely used immunochemical methods often have limited specificity and high measurement variation. In this review, we discuss applications of multiple-reaction monitoring (MRM) mass spectrometry, which allows sensitive, precise quantitative analyses of peptides and the proteins from which they are derived. Systematic development of MRM assays is permitted by databases of peptide mass spectra and sequences, software tools for analysis design and data analysis, and rapid evolution of tandem mass spectrometer technology. Key advantages of MRM assays are the ability to target specific peptide sequences, including variants and modified forms, and the capacity for multiplexing that allows analysis of dozens to hundreds of peptides. Different quantitative standardization methods provide options that balance precision, sensitivity, and assay cost. Targeted protein quantitation by MRM and related mass spectrometry methods can advance biochemistry by transforming approaches to protein measurement.
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What OpenQuestion holds
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.