Quantitative analysis of global protein stability rates in tissues
Open accessPublished version of a preprint
Abstract
Protein degradation is an essential mechanism for maintaining proteostasis in response to internal and external perturbations. Disruption of this process is implicated in many human diseases. We present a new technique, QUAD (Quantification of Azidohomoalanine Degradation), to analyze the global degradation rates in tissues using a non-canonical amino acid and mass spectrometry. QUAD analysis reveals that protein stability varied within tissues, but discernible trends in the data suggest that cellular environment is a major factor dictating stability. Within a tissue, different organelles and protein functions were enriched with different stability patterns. QUAD analysis demonstrated that protein stability is enhanced with age in the brain but not in the liver. Overall, QUAD allows the first global quantitation of protein stability rates in tissues, which will allow new insights and hypotheses in basic and translational research.
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
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.
No citation lists for this paper
No citation lists for this paper yet — checked again daily.
References 81 · Cited by 19
- Authors
- McClatchy, D. B., Martínez-Bartolomé, S., Gao, Y., Lavallée-Adam, M., & Yates, J. R.
- Affiliations
- Scripps Research Institute (US)
- University of Illinois Chicago (US)
- Corresponding author
- Yates, John R.
- Venue
- Scientific Reports
- Published
- 2020-09-29
- Volume
- 10
- Issue
- 1
- Pages
- 15983-15983
- ISSN
- 2045-2322 (ISSN-L)
- OpenAlex
- W3091497311
- Cited by
- 19
- References
- 81
- Citations by year
- 2025: 5 · 2024: 2 · 2023: 6 · 2022: 3 · 2021: 3
- FWCI
- 0.97
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- Scientific Reports (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (P41 GM103533)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Aging › Genetics, Aging, and Longevity in Model Organisms
- Keywords
- protein stability, protein degradation, proteostasis, Quad, azidohomoalanine, brain aging, liver aging
- MeSH terms
- Proteostasis, Age Factors, Alanine, Animals, Brain, Liver, Male, Organ Specificity, Mass Spectrometry, Proteome, Mice, Protein Stability, Click Chemistry, Proteolysis
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