The DOI matches its Crossref record; 25 of the 25 references it cites were found in a registry or an index.
Thiol Chemistry in Peroxidase Catalysis and Redox Signaling
Open accessAbstract
The oxidation chemistry of thiols and disulfides of biologic relevance is described. The review focuses on the interaction and kinetics of hydrogen peroxide with low-molecular-weight thiols and protein thiols and, in particular, on sulfenic acid groups, which are recognized as key intermediates in several thiol oxidation processes. In particular, sulfenic and selenenic acids are formed during the catalytic cycle of peroxiredoxins and glutathione peroxidases, respectively. In turn, these enzymes are in close redox communication with the thioredoxin and glutathione systems, which are the major controllers of the thiol redox state. Oxidants formed in the cell originate from several different sources, but the major producers are NADPH oxidases and mitochondria. However, a different role of the oxygen species produced by these sources is apparent as oxidants derived from NADPH oxidase are involved mainly in signaling processes, whereas those produced by mitochondria induce cell death in pathways including also the thioredoxin system, presently considered an important target for cancer chemotherapy.
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Cites
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
Mitochondrial membrane permeabilization in cell death
Kroemer, G., Galluzzi, L., & Brenner, C. (2007) · Physiological Reviews · doi:10.1152/physrev.00013.2006 · Cited by 3,598
NOX enzymes and the biology of reactive oxygen
Lambeth, J. D. (2004) · Nature Reviews Immunology · doi:10.1038/nri1312 · Cited by 3,125
Calcium, ATP, and ROS: a mitochondrial love-hate triangle
Brookes, P. S., Yoon, Y., Robotham, J. L., Anders, M. W., & Sheu, S.-S. (2004) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00139.2004 · Cited by 2,575
Mammalian thioredoxin is a direct inhibitor of apoptosis signal‐regulating kinase (ASK) 1
Saitoh, M., Nishitoh, H., Fujii, M., Takeda, K., Tobiume, K., Sawada, Y., Kawabata, M., Miyazono, K., & Ichijo, H. (1998) · The EMBO Journal · doi:10.1093/emboj/17.9.2596 · Cited by 2,377
H 2 O 2 , a Necessary Evil for Cell Signaling
Rhee, S. G. (2006) · Science · doi:10.1126/science.1130481 · Cited by 2,160
Protein S-nitrosylation: Purview and parameters
Hess, D. T., Matsumoto, A., Kim, S.-O., Marshall, H. E., & Stamler, J. S. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1569 · Cited by 2,153
Zhang, D. D., & Hannink, M. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.22.8137-8151.2003 · Cited by 1,480 · cited 1×
“In cytoplasm, the transcription factor Nrf2 is associated with a specific repressor protein, Keap1, that inhibits its translocation to the nucleus (165) but also acts as a participant in causing the rapid turnover of Nrf2 by ubiquitination and degradation (180).”
Tissue-specific functions of individual glutathione peroxidases
Brigelius-Flohé, R. (1999) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(99)00173-2 · Cited by 1,114
Mitochondria, oxygen free radicals, disease and ageing
Raha, S., & Robinson, B. H. (2000) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(00)01674-1 · Cited by 1,066 · cited 1×
“…display different roles in metabolism as, in addition to their well-known bioenergetic functions, they are also able to control the fluxes of cellular calcium (17, 59), to induce apoptosis by releasing proapoptotic factors (79), and to produce reactive oxygen species (20, 45, 95, 96, 126).”
Cited by
Oxidative stress and autophagy: The clash between damage and metabolic needs
Filomeni, G., De Zio, D., & Cecconi, F. (2015) · Cell Death & Differentiation · doi:10.1038/cdd.2014.150 · Cited by 2,195
Thiyl Radicals in Organic Synthesis
Dénès, F., Pichowicz, M., Povie, G., & Renaud, P. (2014) · Chemical Reviews · doi:10.1021/cr400441m · Cited by 985
Pattison, D. I., Rahmanto, A. S., & Davies, M. J. (2012) · Photochemical & Photobiological Sciences · doi:10.1039/c1pp05164d · Cited by 573
Mitochondrial ROS regulation of proliferating cells
Diebold, L., & Chandel, N. S. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.04.198 · Cited by 391
Neuronal Calcium Homeostasis and Dysregulation
Gleichmann, M., & Mattson, M. P. (2011) · Antioxidants & Redox Signaling · doi:10.1089/ars.2010.3386 · Cited by 360
Metadata
- Authors
- Bindoli, A., Fukuto, J. M., & Forman, H. J.
- Venue
- Antioxidants & Redox Signaling
- Publisher
- SAGE Publications
- Published
- 2008-09
- Volume
- 10
- Issue
- 9
- Pages
- 1549-1564
- ISSN
- 1523-0864 (ISSN-L)
- 1557-7716
- OpenAlex
- W2051740739
- Cited by
- 244
- References
- 25
- FWCI
- 7.57
- Type
- journal article
- Language
- en
- Open access
- green
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