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Quantitative analysis of complex protein mixtures using isotope-coded affinity tags
Abstract
We describe an approach for the accurate quantification and concurrent sequence identification of the individual proteins within complex mixtures. The method is based on a class of new chemical reagents termed isotope-coded affinity tags (ICATs) and tandem mass spectrometry. Using this strategy, we compared protein expression in the yeast Saccharomyces cerevisiae, using either ethanol or galactose as a carbon source. The measured differences in protein expression correlated with known yeast metabolic function under glucose-repressed conditions. The method is redundant if multiple cysteinyl residues are present, and the relative quantification is highly accurate because it is based on stable isotope dilution techniques. The ICAT approach should provide a widely applicable means to compare quantitatively global protein expression in cells and tissues.
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“Chemical labeling (39–41) is in principle universally applicable, but because the labels are introduced later in the sample processing, some of the advantages in robustness are lost.”
From Accurate proteome-wide label-free quantification by delayed normalization and maximal peptide ratio extraction, termed MaxLFQ (2014) · cites this paper as [39]
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Research works printed but not linked: 1
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Cytoscape: A software Environment for integrated models of biomolecular interaction networks
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Metadata
- Authors
- Gygi, S. P., Rist, B., Gerber, S. A., Turecek, F., Gelb, M. H., & Aebersold, R.
- Affiliations
- University of Washington (US)
- Corresponding author
- Aebersold, Ruedi
- Venue
- Nature Biotechnology
- Published
- 1999-10
- Volume
- 17
- Issue
- 10
- Pages
- 994-999
- ISSN
- 0733-222X (ISSN-L)
- 1087-0156
- 1546-1696
- OpenAlex
- W2111208057
- Semantic Scholar
- 8929f01bc9a788127bcff7a09432f4f7979c8e6b
- Cited by
- 4,683
- References
- 24
- Citations by year
- 2026: 19 · 2025: 27 · 2024: 31 · 2023: 54 · 2022: 50 · 2021: 63 · 2020: 51 · 2019: 70 · 2018: 77 · 2017: 104 · 2016: 123 · 2015: 171 · 2014: 188 · 2013: 235 · 2012: 296
- FWCI
- 75.18
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Biotechnology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Human Genome Research Institute (T32 HG-00035, T32HG000035)
- National Center for Research Resources (RR-11823, P41RR011823)
- Eunice Kennedy Shriver National Institute of Child Health and Human Development (HD 02274, P30HD002274)
- Topics
- Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
- Physical Sciences › Chemistry › Spectroscopy › Mass Spectrometry Techniques and Applications
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Keywords
- ICAT, protein quantification, tandem mass spectrometry, protein expression profiling, Saccharomyces cerevisiae, glucose repression, ethanol carbon source, stable isotope dilution, cysteine labeling
- MeSH terms
- Affinity Labels, Amino Acid Sequence, Chromatography, Liquid, Isotope Labeling, Proteins, Mass Spectrometry
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