The DOI matches its Crossref record; 187 of the 187 references it cites were found in a registry or an index.
The physiological role of reversible methionine oxidation
Abstract
Sulfur-containing amino acids such as cysteine and methionine are particularly vulnerable to oxidation. Oxidation of cysteine and methionine in their free amino acid form renders them unavailable for metabolic processes while their oxidation in the protein-bound state is a common post-translational modification in all organisms and usually alters the function of the protein. In the majority of cases, oxidation causes inactivation of proteins. Yet, an increasing number of examples have been described where reversible cysteine oxidation is part of a sophisticated mechanism to control protein function based on the redox state of the protein. While for methionine the dogma is still that its oxidation inhibits protein function, reversible methionine oxidation is now being recognized as a powerful means of triggering protein activity. This mode of regulation involves oxidation of methionine to methionine sulfoxide leading to activated protein function, and inactivation is accomplished by reduction of methionine sulfoxide back to methionine catalyzed by methionine sulfoxide reductases. Given the similarity to thiol-based redox-regulation of protein function, methionine oxidation is now established as a novel mode of redox-regulation of protein function. This article is part of a Special Issue entitled: Thiol-Based Redox Processes.
Overview
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
Verification
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.
Citations
Cites
1 retracted
Oxidation of Helix-3 Methionines Precedes the Formation of PK Resistant PrPSc
Canello, T., Frid, K., Gabizon, R., Lisa, S., Friedler, A., Moskovitz, J., Gasset, M., & Gabizon, R. (2010) · PLoS Pathogens · doi:10.1371/journal.ppat.1000977 · Cited by 54
RetractedBuxton, G. V., Greenstock, C. L., Helman, W. P., & Ross, A. B. (1988) · Journal of Physical and Chemical Reference Data · doi:10.1063/1.555805 · Cited by 12,332
Ong, S.-E., Blagoev, B., Kratchmarova, I., Kristensen, D. B., Steen, H., Pandey, A., & Mann, M. (2002) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m200025-mcp200 · Cited by 5,574
THE OXIDATIVE BURST IN PLANT DISEASE RESISTANCE
Lamb, C. J., & Dixon, R. A. (1997) · Annual Review of Plant Physiology and Plant Molecular Biology · doi:10.1146/annurev.arplant.48.1.251 · Cited by 3,219
H2O2 from the oxidative burst orchestrates the plant hypersensitive disease resistance response
Levine, A., Tenhaken, R., Dixon, R. A., & Lamb, C. J. (1994) · Cell · doi:10.1016/0092-8674(94)90544-4 · Cited by 2,773
Toxic DNA damage by hydrogen peroxide through the Fenton reaction in vivo and in vitro
Imlay, J. A., Chin, S. M., & Linn, S. (1988) · Science · doi:10.1126/science.2834821 · Cited by 1,555 · cited 1×
“Free intracellular iron is a major source of cytotoxic HO that is formed by Fenton chemistry [107].”
BackgroundThe oxidative environment and protein damage
Davies, M. J. (2005) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2004.08.007 · Cited by 1,392
A Dynamic Pathway for Calcium-Independent Activation of CaMKII by Methionine Oxidation
Erickson, J. R., Joiner, M.-L. A., Guan, X., Kutschke, W., Yang, J., Oddis, C. V., Bartlett, R. K., Lowe, J. S., O'Donnell, S. E., Aykin-Burns, N., et al. (2008) · Cell · doi:10.1016/j.cell.2008.02.048 · Cited by 1,122
Rapid proteolysis of IκB-α is necessary for activation of transcription factor NF-κB
Henkel, T., Machleidt, T., Alkalay, I., Krönke, M., Ben‐Neriah, Y., & Baeuerle, P. A. (1993) · Nature · doi:10.1038/365182a0 · Cited by 1,085
The Arabidopsis CDPK-SnRK Superfamily of Protein Kinases
Hrabak, E. M., Chan, C. W. M., Gribskov, M., Harper, J. F., Choi, J. H., Halford, N. G., Kudla, J., Luan, S., Nimmo, H. G., Sussman, M. R., et al. (2003) · PLANT PHYSIOLOGY · doi:10.1104/pp.102.011999 · Cited by 1,080
Flagged first, then by citations
Cited by
Sorted by citations
Sies, H., Berndt, C., & Jones, D. P. (2017) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-061516-045037 · Cited by 3,520
Superoxide dismutases: Dual roles in controlling ROS damage and regulating ROS signaling
Wang, Y., Branicky, R. S., Noë, A., & Hekimi, S. (2018) · The Journal of Cell Biology · doi:10.1083/jcb.201708007 · Cited by 2,284
“Like cysteines, methionines also contain reactive sulfur atoms that are susceptible to reversible redox modifications and thus may also mediate redox signaling (Drazic and Winter, 2014).”
Cellular mechanisms and physiological consequences of redox-dependent signalling
Holmström, K. M., & Finkel, T. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3801 · Cited by 2,093
The world of protein acetylation
Drazic, A., Myklebust, L. M., Ree, R., & Arnesen, T. (2016) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2016.06.007 · Cited by 847
“Methionine sulfoxide reductase A (MSRA) plays a crucial role in protecting proteins from oxidation and repairs damages caused by reactive oxygen species (ROS), which also crucially affects tunorigenesis [2].”
BackgroundSelf-citationHorsman, G. P., & Zechel, D. L. (2016) · Chemical Reviews · doi:10.1021/acs.chemrev.6b00536 · Cited by 604
Metadata
- Authors
- Drazic, A., & Winter, J.
- Affiliations
- Center for Integrated Protein Science Munich (DE)
- Corresponding author
- Winter, Jeannette
- ORCID
- Drazic, Adrian
- Venue
- Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
- Publisher
- Elsevier BV
- Published
- 2014-08
- Volume
- 1844
- Issue
- 8
- Pages
- 1367-1382
- ISSN
- 1570-9639 (ISSN-L)
- OpenAlex
- W2039213528
- Cited by
- 198
- References
- 187
- Citations by year
- 2026: 8 · 2025: 13 · 2024: 19 · 2023: 11 · 2022: 22 · 2021: 14 · 2020: 15 · 2019: 17 · 2018: 12 · 2017: 18 · 2016: 15 · 2015: 20 · 2014: 13
- FWCI
- 2.08
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Sulfur Compounds in Biology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Keywords
- methionine sulfoxide, methionine sulfoxide reductase, post-translational modification, protein inactivation, cysteine oxidation, sulfur-containing amino acids
- MeSH terms
- Animals, Cell Physiological Phenomena, Humans, Methionine, Oxidation-Reduction, Signal Transduction
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
