The DOI matches its Crossref record; 44 of the 44 references it cites were found in a registry or an index.
The role of cysteine residues as redox-sensitive regulatory switches
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Cites
Structure, mechanism and regulation of peroxiredoxins
Wood, Z. A., Schröder, E., Robin Harris, J., & Poole, L. B. (2003) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(02)00003-8 · Cited by 2,544
Protein Tyrosine Phosphatases in the Human Genome
Alonso, A., Sasin, J., Bottini, N., Friedberg, I., Friedberg, I., Osterman, A., Godzik, A., Hunter, T., Dixon, J., & Mustelin, T. (2004) · Cell · doi:10.1016/j.cell.2004.05.018 · Cited by 1,886
Oxidant signals and oxidative stress
Finkel, T. (2003) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(03)00002-4 · Cited by 1,393
Peroxiredoxin Evolution and the Regulation of Hydrogen Peroxide Signaling
Wood, Z. A., Poole, L. B., & Karplus, P. A. (2003) · Science · doi:10.1126/science.1080405 · Cited by 1,367
Epidermal Growth Factor (EGF)-induced Generation of Hydrogen Peroxide
Bae, Y. S., Kang, S. W., Seo, M. S., Baines, I. C., Tekle, E., Chock, P. B., & Rhee, S. G. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.1.217 · Cited by 1,208
Activation of the OxyR Transcription Factor by Reversible Disulfide Bond Formation
Zheng, M., Åslund, F., & Storz, G. (1998) · Science · doi:10.1126/science.279.5357.1718 · Cited by 1,196
Reversible oxidation and inactivation of protein tyrosine phosphatases in vivo
Meng, T.-C., Fukada, T., & Tonks, N. K. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00445-8 · Cited by 1,040
ATP-dependent reduction of cysteine–sulphinic acid by S. cerevisiae sulphiredoxin
Biteau, B., Labarre, J., & Toledano, M. B. (2003) · Nature · doi:10.1038/nature02075 · Cited by 970
Redox regulation of protein tyrosine phosphatase 1B involves a sulphenyl-amide intermediate
Salmeen, A., Andersen, J. N., Myers, M. P., Meng, T.-C., Hinks, J. A., Tonks, N. K., & Barford, D. (2003) · Nature · doi:10.1038/nature01680 · Cited by 951
Self-citationDenu, J. M., & Tanner, K. G. (1998) · Biochemistry · doi:10.1021/bi973035t · Cited by 938
Cited by
The NOX Family of ROS-Generating NADPH Oxidases: Physiology and Pathophysiology
Bedard, K., & Krause, K.-H. (2007) · Physiological Reviews · doi:10.1152/physrev.00044.2005 · Cited by 6,989
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
NADPH Oxidases (NOX): An Overview from Discovery, Molecular Mechanisms to Physiology and Pathology
Vermot, A., Petit-Härtlein, I., Smith, S. M. E., & Fieschi, F. (2021) · Antioxidants · doi:10.3390/antiox10060890 · Cited by 766
Nitric oxide and redox mechanisms in the immune response
Wink, D. A., Hines, H. B., Cheng, R. Y. S., Switzer, C. H., Flores-Santana, W., Vitek, M. P., Ridnour, L. A., & Colton, C. A. (2011) · Journal of Leukocyte Biology · doi:10.1189/jlb.1010550 · Cited by 765
Functions of ROS in Macrophages and Antimicrobial Immunity
Herb, M., & Schramm, M. (2021) · Antioxidants · doi:10.3390/antiox10020313 · Cited by 633
Metadata
- Authors
- Barford, D.
- Venue
- Current Opinion in Structural Biology
- Publisher
- Elsevier BV
- Published
- 2004-12
- Volume
- 14
- Issue
- 6
- Pages
- 679-686
- ISSN
- 0959-440X (ISSN-L)
- OpenAlex
- W2020285880
- Cited by
- 329
- References
- 44
- FWCI
- 5.90
- Type
- journal article
- Language
- en
- Open access
- closed
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- Barford, D. (2004). The role of cysteine residues as redox-sensitive regulatory switches. Current Opinion in Structural Biology. https://doi.org/10.1016/j.sbi.2004.09.012
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.
