The DOI matches its Crossref record; 7 of the 7 references it cites were found in a registry or an index.
Metal and Redox Modulation of Cysteine Protein Function
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Citations
Cites
Oxidized Redox State of Glutathione in the Endoplasmic Reticulum
Hwang, C., Sinskey, A. J., & Lodish, H. F. (1992) · Science · doi:10.1126/science.1523409 · Cited by 1,968
The ZIP family of metal transporters
Guerinot, M. L. (2000) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/s0005-2736(00)00138-3 · Cited by 1,200
S-nitrosylation of matrix metalloproteinases: signaling pathway to neuronal cell death
Gu, Z., Kaul, M., Yan, B., Kridel, S. J., Cui, J., Strongin, A., Smith, J. W., Liddington, R. C., & Lipton, S. A. (2002) · Science · doi:10.1126/science.1073634 · Cited by 950
Bush, A. (2000) · Current Opinion in Chemical Biology · doi:10.1016/s1367-5931(99)00073-3 · Cited by 731
Mechanism of inhibition of the human matrix metalloproteinase stromelysin-1 by TIMP-1.
Gomis-R¨th, F.-X., Maskos, K., Betz, M., Bergner, A., Huber, R., Suzuki, K., Yoshida, N., Nagase, H., Brew, K., Bourenkov, G. P., et al. (1997) · Nature · doi:10.1038/37995 · Cited by 619
Hypochlorous Acid Oxygenates the Cysteine Switch Domain of Pro-matrilysin (MMP-7)
Fu, X., Kassim, S. Y., Parks, W. C., & Heinecke, J. W. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m106958200 · Cited by 482
Great Metalloclusters in Enzymology
Rees, D. C. (2002) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.71.110601.135406 · Cited by 220
Cited by
Reactive oxygen species are essential for autophagy and specifically regulate the activity of Atg4
Scherz‐Shouval, R., Shvets, E., Fass, E., Shorer, H., Gil, L., & Elazar, Z. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601623 · Cited by 2,101
Critical Role of Zinc as Either an Antioxidant or a Prooxidant in Cellular Systems
Lee, S. R. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/9156285 · Cited by 458
An Activity-Guided Map of Electrophile-Cysteine Interactions in Primary Human T Cells
Vinogradova, E. V., Zhang, X., Remillard, D., Lazar, D. C., Suciu, R. M., Wang, Y., Bianco, G., Yamashita, Y., Crowley, V. M., Schafroth, M. A., et al. (2020) · Cell · doi:10.1016/j.cell.2020.07.001 · Cited by 351
Jacob, C. (2006) · Natural Product Reports · doi:10.1039/b609523m · Cited by 373
Self-citationOne- and two-electron oxidation of thiols: mechanisms, kinetics and biological fates
Trujillo, M., Alvarez, B., & Radi, R. (2016) · Free Radical Research · doi:10.3109/10715762.2015.1089988 · Cited by 142
Metadata
- Authors
- Giles, N. M., Watts, A. B., Giles, G. I., Fry, F. H., Littlechild, J. A., & Jacob, C.
- Venue
- Chemistry & Biology
- Publisher
- Elsevier BV
- Published
- 2003-08
- Volume
- 10
- Issue
- 8
- Pages
- 677-693
- ISSN
- 1074-5521 (ISSN-L)
- OpenAlex
- W1998408986
- Cited by
- 486
- References
- 7
- FWCI
- 3.86
- Type
- journal article
- Language
- en
- Open access
- bronze
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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.
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Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
