The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Median based absolute quantification of proteins using Fully Unlabelled Generic Internal Standard (FUGIS)
Open accessPreprint — published as 10.1021/acs.jproteome.1c00596 · Paper page
Abstract
By reporting molar abundances of proteins, absolute quantification determines their stoichiometry in complexes, pathways or networks. Typically, absolute quantification relies either on protein-specific isotopically labelled peptide standards or on a semi-empirical calibration against the average abundance of peptides chosen from arbitrary selected proteins. In contrast, a generic protein standard FUGIS (for F ully U nlabelled G eneric I nternal S tandard) requires no isotopic labelling, chemical synthesis or external calibration and is applicable to quantifying proteins of any organismal origin. The median intensity of peptide peaks produced by the digestion of FUGIS is used as a single point calibrant to determine the molar abundance of any co-digested protein. Powered by FUGIS, median based absolute quantification (MBAQ) outperformed other available methods of untargeted proteome-wide absolute quantification.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Global quantification of mammalian gene expression control
Schwanhäusser, B., Busse, D., Li, N., Dittmar, G., Schuchhardt, J., Wolf, J., Chen, W., & Selbach, M. (2011) · Nature · doi:10.1038/nature10098 · Cited by 6,566
Flagged first, then by citations
Research works printed but not linked: 37
- 10.1021/pr060447s · DOI
- 2015, Studying Macromolecular Complex Stoichiometries by Peptide-Based Mass Spectrometry, Proteomics, 15, 862, 10.1002/pmic.201400466 · DOI
- 2014, Multi-Enzyme Digestion FASP and the ‘Total Protein Approach’-Based Absolute Quantification of the Escherichia Coli Proteome, J. Proteomics, 109, 322, 10.1016/j.jprot.2014.07.012 · DOI
- 2020, A Metabolic Switch Regulates the Transition between Growth and Diapause in C. Elegans, BMC Biol, 18, 31, 10.1186/s12915-020-0760-3 · DOI
- 2011, Metabolic Engineering, Synthetic Biology and Systems Biology, FEMS Yeast Res, 12, 2628
- 10.1074/mcp.M500230-MCP200 · DOI · Paper page
- 10.2174/138920208784533647 · DOI
- 2018, Absolute Quantification of Major Photosynthetic Protein Complexes in Chlamydomonas Reinhardtii Using Quantification Concatamers (QconCATs), Front. Plant Sci, 9, 1265, 10.3389/fpls.2018.01265 · DOI
- 2020, Absolute Quantification of Proteins in the Eye of Drosophila Melanogaster, Proteomics, 20, 1900049, 10.1002/pmic.201900049 · DOI
- 2018, Stoichiometry, Absolute Abundance, and Localization of Proteins in the Bacillus Cereus Spore Coat Insoluble Fraction Determined Using a QconCAT Approach, J. Proteome Res, 17, 903, 10.1021/acs.jproteome.7b00732 · DOI
- 10.1586/14789450.1.4.503 · DOI
- 2018, Standardization Approaches in Absolute Quantitative Proteomics with Mass Spectrometry, Mass Spectrom. Rev, 37, 715, 10.1002/mas.21542 · DOI
- 10.1146/annurev-anchem-061516-045357 · DOI
- 10.1002/pmic.201300135 · DOI · Paper page
- 10.1073/pnas.0832254100 · DOI · Paper page
- 10.1038/nmeth774 · DOI
- 10.1038/nmeth.1649 · DOI
- 10.1074/mcp.O111.009613 · DOI · Paper page
- 2016, A Strategy for Absolute Proteome Quantification with Mass Spectrometry by Hierarchical Use of Peptide-Concatenated Standards, Proteomics, 16, 1457, 10.1002/pmic.201500414 · DOI
- 10.1074/mcp.RA117.000284 · DOI
- 2017, DOSCATs: Double Standards for Protein Quantification, Sci. Rep, 7, 45570, 10.1038/srep45570 · DOI
- 10.1074/mcp.O117.067082 · DOI
- 2010, Minimally Permutated Peptide Analogs as Internal Standards for Relative and Absolute Quantification of Peptides and Proteins, Proteomics, 10, 1510, 10.1002/pmic.200900695 · DOI
- 2012, Evaluation of Protein Quantification Using Standard Peptides Containing Single Conservative Amino Acid Replacements, J. Mass Spectrom, 47, 188, 10.1002/jms.2053 · DOI
- 2017, Scrambled Internal Standard Method for High-Throughput Protein Quantification by Matrix-Assisted Laser Desorption Ionization Tandem Mass Spectrometry, J. Proteome Res, 16, 1556, 10.1021/acs.jproteome.6b00941 · DOI
- 2019, An LC-MS/MS Assay with a Label-Free Internal Standard for Quantitation of Serum Cystatin C, Anal. Biochem, 587, 113451, 10.1016/j.ab.2019.113451 · DOI
- 10.1074/mcp.M500061-MCP200 · DOI · Paper page
- 10.1038/nbt1270 · DOI · Paper page
- 10.1093/bioinformatics/btu200 · DOI
- 10.1074/mcp.M112.025445 · DOI
- 10.1074/mcp.M113.037309 · DOI · Paper page
- 2021, From Coarse to Fine: The Absolute Escherichia Coli Proteome under Diverse Growth Conditions, Mol. Syst. Biol, 17, e9536, 10.15252/msb.20209536 · DOI
- 10.1021/ac701628m · DOI
- 10.1074/mcp.M111.007633 · DOI
- 10.1186/s12915-020-00857-6 · DOI
- 2016, Design and Expression of a QconCAT Protein to Validate Hi3 Protein Quantification of Influenza Vaccine Antigens, J. Proteomics, 146, 133, 10.1016/j.jprot.2016.06.024 · DOI
- 10.1021/acs.jproteome.6b00645 · DOI
Metadata
- Authors
- Raghuraman, B. K., Bogdanova, A., Moon, H., Rzagalinski, I., Geertsma, E. R., Hersemann, L., & Shevchenko, A.
- Affiliations
- Max Planck Institute of Molecular Cell Biology and Genetics (DE)
- Corresponding author
- Shevchenko, Andrej
- Venue
- Journal of Proteome Research
- Publisher
- openRxiv
- Published
- 2021-06-29
- Volume
- 21
- Issue
- 1
- Pages
- 132-141
- ISSN
- 1535-3893 (ISSN-L)
- PMC
- PMC8749952
- OpenAlex
- W3217139745
- Cited by
- 9
- References
- 1
- Citations by year
- 2026: 1 · 2025: 4 · 2024: 2 · 2022: 1 · 2021: 1
- FWCI
- 0.37
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- cc-by
- Locations
- Journal of Proteome Research (publishedVersion, cc-by)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- Max-Planck-Gesellschaft
- Topics
- Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Advanced Biosensing Techniques and Applications
- Physical Sciences › Chemistry › Spectroscopy › Mass Spectrometry Techniques and Applications
- Keywords
- absolute protein quantification, trypsin digestion
- MeSH terms
- Calibration, Isotope Labeling, Peptides, Reference Standards, Proteome
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
