The DOI matches its Crossref record; 171 of the 171 references it cites were found in a registry or an index.
Protein carbonylation as a major hallmark of oxidative damage: Update of analytical strategies
Abstract
Protein carbonylation, one of the most harmful irreversible oxidative protein modifications, is considered as a major hallmark of oxidative stress‐related disorders. Protein carbonyl measurements are often performed to assess the extent of oxidative stress in the context of cellular damage, aging and several age‐related disorders. A wide variety of analytical techniques are available to detect and quantify protein‐bound carbonyls generated by metal‐catalyzed oxidation, lipid peroxidation or glycation/glycoxidation. Here we review current analytical approaches for protein carbonyl detection with a special focus on mass spectrometry‐based techniques. The utility of several carbonyl‐derivatization reagents, enrichment protocols and especially advanced mass spectrometry techniques are compared and discussed in detail. Furthermore, the mechanisms and biology of protein carbonylation are summarized based on recent high‐throughput proteomics data. © 2013 Wiley Periodicals, Inc. Mass Spec Rev 33: 79–97, 2014.
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Measurement and Clinical Significance of Biomarkers of Oxidative Stress in Humans
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Miller, M. W., & Sadeh, N. (2014) · Molecular Psychiatry · doi:10.1038/mp.2014.111 · Cited by 288
de Oliveira Alves, N., Martins Pereira, G., Di Domenico, M., Costanzo, G., Benevenuto, S., de Oliveira Fonoff, A. M., de Souza Xavier Costa, N., Ribeiro Júnior, G., Satoru Kajitani, G., Cestari Moreno, N., et al. (2020) · Environment International · doi:10.1016/j.envint.2020.106150 · Cited by 94
Seed quality and carbon primary metabolism.
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Metadata
- Authors
- Fedorova, M., Bollineni, R. C., & Hoffmann, R.
- Venue
- Mass Spectrometry Reviews
- Publisher
- Wiley
- Published
- 2013-07-07
- Volume
- 33
- Issue
- 2
- Pages
- 79-97
- ISSN
- 0277-7037 (ISSN-L)
- 1098-2787
- OpenAlex
- W1514296965
- Cited by
- 516
- References
- 171
- FWCI
- 8.34
- Type
- journal article
- Language
- en
- Open access
- closed
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