The DOI matches its Crossref record; 6 of the 6 references it cites were found in a registry or an index.
Redox outside the Box: Linking Extracellular Redox Remodeling with Intracellular Redox Metabolism
Open accessAbstract
Aerobic organisms generate reactive oxygen species as metabolic side products and must achieve a delicate balance between using them for signaling cellular functions and protecting against collateral damage. Small molecule (e.g. glutathione and cysteine)- and protein (e.g. thioredoxin)-based buffers regulate the ambient redox potentials in the various intracellular compartments, influence the status of redox-sensitive macromolecules, and protect against oxidative stress. Less well appreciated is the fact that the redox potential of the extracellular compartment is also carefully regulated and is dynamic. Changes in intracellular metabolism alter the redox poise in the extracellular compartment, and these are correlated with cellular processes such as proliferation, differentiation, and death. In this minireview, the mechanism of extracellular redox remodeling due to intracellular sulfur metabolism is discussed in the context of various cell-cell communication paradigms.
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Cites
Reactivity of biologically important thiol compounds with superoxide and hydrogen peroxide
Winterbourn, C. C., & Metodiewa, D. (1999) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(99)00051-9 · Cited by 799
Thioredoxin and Related Molecules–From Biology to Health and Disease
Lillig, C. H., & Holmgren, A. (2007) · Antioxidants & Redox Signaling · doi:10.1089/ars.2007.9.25 · Cited by 724
Jones, D. P., Mody, V. C., Carlson, J. L., Lynn, M. J., & Sternberg, P. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)01040-7 · Cited by 392
Chang, T.-S., Jeong, W., Woo, H. A., Lee, S. M., Park, S., & Rhee, S. G. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m409482200 · Cited by 388
Redox-Sensing Release of Human Thioredoxin from T Lymphocytes with Negative Feedback Loops
Kondo, N., Ishii, Y., Kwon, Y.-W., Tanito, M., Horita, H., Nishinaka, Y., Nakamura, H., & Yodoi, J. (2004) · The Journal of Immunology · doi:10.4049/jimmunol.172.1.442 · Cited by 116
Redox remodeling as an immunoregulatory strategy
Yan, Z., & Banerjee, R. (2010) · Biochemistry · doi:10.1021/bi902022n · Cited by 82
Self-citation
Cited by
Extracellular Cysteine in Connexins: Role as Redox Sensors
Retamal, M. A., García, I. E., Pinto, B. I., Pupo, A., Báez, D., Stehberg, J., Del Rio, R., & González, C. (2016) · Frontiers in Physiology · doi:10.3389/fphys.2016.00001 · Cited by 482
Regulation of protein function and signaling by reversible cysteine S-nitrosylation
Gould, N., Doulias, P.-T., Tenopoulou, M., Raju, K., & Ischiropoulos, H. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.r113.460261 · Cited by 274
Go, Y.-M., & Jones, D. P. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.r113.464131 · Cited by 260
Hecklau, C., Pering, S., Seibel, R., Schnellbaecher, A., Wehsling, M., Eichhorn, T., Hagen, J. V., & Zimmer, A. (2016) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2015.11.022 · Cited by 42
A Redox-Switchable Colorimetric Probe for “Naked-Eye” Detection of Hypochlorous Acid and Glutathione
Han, Q., Zhou, F., Wang, Y., Feng, H., Meng, Q., Zhang, Z., & Zhang, R. (2019) · Molecules · doi:10.3390/molecules24132455 · Cited by 23
Metadata
- Authors
- Banerjee, R.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2012-02
- Volume
- 287
- Issue
- 7
- Pages
- 4397-4402
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2077580537
- Cited by
- 204
- References
- 6
- FWCI
- 4.70
- Type
- journal article
- Language
- en
- Open access
- hybrid
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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.
