The DOI matches its Crossref record; 46 of the 46 references it cites were found in a registry or an index.
Site-Specific Proteomic Mapping Identifies Selectively Modified Regulatory Cysteine Residues in Functionally Distinct Protein Networks
Open accessAbstract
S-Acylation, S-glutathionylation, S-nitrosylation, and S-sulfenylation are prominent, chemically distinct modifications that regulate protein function, redox sensing, and trafficking. Although the biological significance of these modifications is increasingly appreciated, their integration in the proteome remains unknown. Novel mass spectrometry-based technologies identified 2,596 predominately unique sites in 1,319 mouse liver proteins under physiological conditions. Structural analysis localized the modifications in unique, evolutionary conserved protein segments, outside commonly annotated functional regions. Contrary to expectations, propensity for modification did not correlate with biophysical properties that regulate cysteine reactivity. However, the in vivo chemical reactivity is fine-tuned for specificity, demonstrated by the nominal complementation between the four modifications and quantitative proteomics which showed that a reduction in S-nitrosylation is not correlated with increased S-glutathionylation. A comprehensive survey uncovered clustering of modifications within biologically related protein networks. The data provide the first evidence for the occurrence of distinct, endogenous protein networks that undergo redox signaling through specific cysteine modifications.
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“Recent studies of the proteome of eNOS−/− mice compared with wild type mice identify a more limited set of S-nitrosated proteins (125, 378).”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [378]
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Quantitative reactivity profiling predicts functional cysteines in proteomes
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Hydrogen Sulfide-Linked Sulfhydration of NF-κB Mediates Its Antiapoptotic Actions
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Integrated proteomic analysis of post-translational modifications by serial enrichment
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Cardioprotection by S-nitrosation of a cysteine switch on mitochondrial complex I
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BackgroundS-glutathionylation in protein redox regulation
Dalle‐Donne, I., Rossi, R., Giustarini, D., Colombo, R., & Milzani, A. (2007) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.06.014 · Cited by 506
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Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation
Tejero, J., Shiva, S., & Gladwin, M. T. (2019) · Physiological Reviews · doi:10.1152/physrev.00036.2017 · Cited by 541
Sulfhydryl groups as targets of mercury toxicity
Ajsuvakova, O. P., Tinkov, A. A., Aschner, M., da Rocha, J. B. T., Michalke, B., Геннадиевна, С. М., Skalny, A. V., Butnariu, M., Dadar, M., Sărac, I., et al. (2020) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2020.213343 · Cited by 384
Stomberski, C. T., Hess, D. T., & Stamler, J. S. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7403 · Cited by 297
Chemical proteomics reveals new targets of cysteine sulfinic acid reductase
Akter, S., Fu, L., Jung, Y., Conte, M. L., Lawson, J. R., Lowther, W. T., Sun, R., Liu, K., Yang, J. H., & Carroll, K. S. (2018) · Nature Chemical Biology · doi:10.1038/s41589-018-0116-2 · Cited by 235
Self-citationCysteine Sulfenylation Directs IRE-1 to Activate the SKN-1/Nrf2 Antioxidant Response
Hourihan, J. M., Mazzeo, L. E. M., Fernández-Cárdenas, L. P., & Blackwell, T. K. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.07.019 · Cited by 209
Metadata
- Authors
- Gould, N. S., Evans, P., Martínez-Acedo, P., Marino, S. M., Gladyshev, V. N., Carroll, K. S., & Ischiropoulos, H.
- Affiliations
- Children's Hospital of Philadelphia (US)
- Scripps Research Institute (US)
- Akdeniz University (TR)
- Brigham and Women's Hospital (US)
- Corresponding author
- Ischiropoulos, Harry
- Venue
- Chemistry & Biology
- Publisher
- Elsevier BV
- Published
- 2015-07
- Volume
- 22
- Issue
- 7
- Pages
- 965-975
- ISSN
- 1074-5521 (ISSN-L)
- PMC
- PMC4515171
- OpenAlex
- W1867506901
- Cited by
- 128
- References
- 46
- Citations by year
- 2026: 2 · 2025: 11 · 2024: 11 · 2023: 11 · 2022: 10 · 2021: 12 · 2020: 12 · 2019: 9 · 2018: 17 · 2017: 14 · 2016: 14 · 2015: 5
- FWCI
- 7.23
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Chemistry & Biology (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institutes of Health
- National Heart, Lung, and Blood Institute (HL54926, R01HL054926)
- National Cancer Institute (R01CA174864, CA174986)
- National Institute of General Medical Sciences (GM 065204, R37GM065204, GM102187, R01GM065204, R01GM102187)
- National Institute of Environmental Health Sciences (P30ES013508)
- Eunice Kennedy Shriver National Institute of Child Health and Human Development (U54HD086984)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Keywords
- cysteine modification, S-acylation, S-glutathionylation, S-nitrosylation, redox signaling, protein networks, post-translational modification
- MeSH terms
- Amino Acid Sequence, Animals, Cysteine, Humans, Models, Molecular, Molecular Sequence Data, Peptide Mapping, Protein Processing, Post-Translational, Mass Spectrometry, Proteome, Proteomics, Mice, Protein Interaction Maps
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