The DOI matches its Crossref record; 118 of the 118 references it cites were found in a registry or an index.
Proteomic Identification of Carbonylated Proteins and Their Oxidation Sites
Open accessAbstract
Excessive oxidative stress leaves a protein carbonylation fingerprint in biological systems. Carbonylation is an irreversible post-translational modification (PTM) that often leads to the loss of protein function and can be a component of multiple diseases. Protein carbonyl groups can be generated directly (by amino acids oxidation and the alpha-amidation pathway) or indirectly by forming adducts with lipid peroxidation products or glycation and advanced glycation end-products. Studies of oxidative stress are complicated by the low concentration of oxidation products and a wide array of routes by which proteins are carbonylated. The development of new selection and enrichment techniques coupled with advances in mass spectrometry are allowing the identification of hundreds of new carbonylated protein products from a broad range of proteins located at many sites in biological systems. The focus of this review is on the use of proteomics tools and methods to identify oxidized proteins along with specific sites of oxidative damage and the consequences of protein oxidation.
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1 retracted
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Reisz, J. A., Bansal, N., Qian, J., Zhao, W., & Furdui, C. M. (2014) · Antioxidants & Redox Signaling · doi:10.1089/ars.2013.5489 · Cited by 833
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Exploring the Biology of Lipid Peroxidation-Derived Protein Carbonylation
Fritz, K. S., & Petersen, D. R. (2011) · Chemical Research in Toxicology · doi:10.1021/tx200169n · Cited by 129
Age-Related Oxidative Stress Compromises Endosomal Proteostasis
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Chemoproteomic profiling and discovery of protein electrophiles in human cells
Matthews, M. L., He, L., Horning, B. D., Olson, E. J., Correia, B. E., Yates, J. R., Dawson, P. E., & Cravatt, B. F. (2017) · Nature Chemistry · doi:10.1038/nchem.2645 · Cited by 90
Analysis of protein carbonylation — pitfalls and promise in commonly used methods
Rogowska-Wrzesinska, A., Wojdyla, K., Nedić, O., Baron, C. P., & Griffiths, H. R. (2014) · Free Radical Research · doi:10.3109/10715762.2014.944868 · Cited by 65
Kwiatkowski, M., Wurlitzer, M., Krutilin, A., Kiani, P., Nimer, R., Omidi, M., Mannaa, A., Bussmann, T., Bartkowiak, K., Kruber, S., et al. (2016) · Journal of Proteomics · doi:10.1016/j.jprot.2015.12.029 · Cited by 43
Wang, X., Peng, M.-J., Wang, Z.-H., Yang, Q.-L., & Peng, S. (2020) · Archives of Biological Sciences · doi:10.2298/abs191216015w · Cited by 34
Metadata
- Authors
- Madian, A. G., & Regnier, F. E.
- Venue
- Journal of Proteome Research
- Publisher
- American Chemical Society (ACS)
- Published
- 2010-06-22
- Volume
- 9
- Issue
- 8
- Pages
- 3766-3780
- ISSN
- 1535-3893 (ISSN-L)
- 1535-3907
- OpenAlex
- W1994351798
- Cited by
- 272
- References
- 118
- FWCI
- 8.74
- Type
- journal article
- Language
- en
- Open access
- green
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