Cited by 784Redox biology and oxidative stressAntioxidant Activity and Oxidative StressNitric Oxide and Endothelin Effects

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Redox-based regulation of signal transduction: Principles, pitfalls, and promises

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Janssen-Heininger, Yvonne M.W., Mossman, Brooke T., Heintz, Nicholas H., Forman, Henry J., Kalyanaraman, Balaraman, Finkel, Toren, Stamler, Jonathan S., Rhee, Sue Goo, van der Vliet, Albert·2008·Free Radical Biology and Medicine

DOI 10.1016/j.freeradbiomed.2008.03.011PMC PMC2453533

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Abstract

Oxidants are produced as a by-product of aerobic metabolism, and organisms ranging from prokaryotes to mammals have evolved with an elaborate and redundant complement of antioxidant defenses to confer protection against oxidative insults. Compelling data now exist demonstrating that oxidants are used in physiological settings as signaling molecules with important regulatory functions controlling cell division, migration, contraction, and mediator production. These physiological functions are carried out in an exquisitely regulated and compartmentalized manner by mild oxidants, through subtle oxidative events that involve targeted amino acids in proteins. The precise understanding of the physiological relevance of redox signal transduction has been hampered by the lack of specificity of reagents and the need for chemical derivatization to visualize reversible oxidations. In addition, it is difficult to measure these subtle oxidation events in vivo. This article reviews some of the recent findings that illuminate the significance of redox signaling and exciting future perspectives. We also attempt to highlight some of the current pitfalls and the approaches needed to advance this important area of biochemical and biomedical research.

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NOX enzymes and the biology of reactive oxygen
Lambeth, J. D. (2004) · Nature Reviews Immunology · doi:10.1038/nri1312 · Cited by 3,125
Requirement for Generation of H 2 O 2 for Platelet-Derived Growth Factor Signal Transduction
Sundaresan, M., Yu, Z.-X., Ferrans, V. J., Irani, K., & Finkel, T. (1995) · Science · doi:10.1126/science.270.5234.296 · Cited by 2,520
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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
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Kobayashi, A., Kang, M.-I., Okawa, H., Ohtsuji, M., Zenke, Y., Chiba, T., Igarashi, K., & Yamamoto, M. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.16.7130-7139.2004 · Cited by 2,224
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Rhee, S. G. (2006) · Science · doi:10.1126/science.1130481 · Cited by 2,160
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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
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Dinkova-Kostova, A. T., Holtzclaw, W. D., Cole, R. N., Itoh, K., Wakabayashi, N., Katoh, Y., Yamamoto, M., & Talalay, P. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.172398899 · Cited by 1,947
Reactive Oxygen Species Promote TNFα-Induced Death and Sustained JNK Activation by Inhibiting MAP Kinase Phosphatases
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Authors: Janssen-Heininger, Y. M. W., Mossman, B. T., Heintz, N. H., Forman, H. J., Kalyanaraman, B., Finkel, T., Stamler, J. S., Rhee, S. G., & van der Vliet, A.
Affiliations: University of Vermont (US)
University of California, Merced (US)
Medical College of Wisconsin (US)
National Institutes of Health (US)
Duke University (US)
Ewha Womans University (KR)
Corresponding author: Janssen-Heininger, Yvonne M.W.
ORCID: Janssen-Heininger, Yvonne M.W.
Mossman, Brooke T.
Forman, Henry J.
Kalyanaraman, Balaraman
Finkel, Toren
Stamler, Jonathan S.
Rhee, Sue Goo
Venue: Free Radical Biology and Medicine
Publisher: Elsevier BV
Published: 2008-07
Volume: 45
Issue: 1
Pages: 1-17
ISSN: 0891-5849 (ISSN-L)
DOI: 10.1016/j.freeradbiomed.2008.03.011
PMC: PMC2453533
OpenAlex: W1980385765
Cited by: 784
References: 246
Citations by year: 2026: 12 · 2025: 25 · 2024: 18 · 2023: 26 · 2022: 32 · 2021: 45 · 2020: 47 · 2019: 43 · 2018: 37 · 2017: 39 · 2016: 47 · 2015: 48 · 2014: 50 · 2013: 69 · 2012: 60
FWCI: 4.76
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
Locations: Free Radical Biology and Medicine (publishedVersion)
PubMed (publishedVersion)
Europe PMC (PubMed Central) (acceptedVersion)
PubMed Central (acceptedVersion)
Funders: National Heart, Lung, and Blood Institute (P01HL067004, R01 HL60014, P01 HL67004, R01HL074295, R01HL079331, R01HL085646, R01HL068865, R01HL060014)
National Institute of Environmental Health Sciences (R01ES05511, R01ES005511)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
Health Sciences › Medicine › Biochemistry (medical) › Antioxidant Activity and Oxidative Stress
Health Sciences › Medicine › Physiology (medical) › Nitric Oxide and Endothelin Effects
Keywords: redox signaling, protein oxidation, antioxidant defense, oxidative stress, cell division, cell migration, cell contraction
MeSH terms: Amino Acids, Animals, Gene Expression Regulation, Humans, Hydrogen Peroxide, Oxidation-Reduction, Signal Transduction, Oxidants

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