The DOI matches its Crossref record; 12 of the 12 references it cites were found in a registry or an index.
Nitric oxide and mitochondria
Open accessAbstract
Nitric oxide (NO) and its derivatives (reactive nitrogen species) have multiple effects on mitochondria that impact on cell physiology and cell death. Mitochondria may produce and consume NO and NO stimulates mitochondrial biogenesis, apparently via cGMP upregulation of transcriptional factors. NO inhibits mitochondrial respiration via: (A) an acute and reversible inhibition of cytochrome oxidase by NO in competition with O2, and (B) irreversible inhibition of multiple sites by reactive nitrogen species. NO is a potent vasodilator (via cGMP), increasing O2 and respiratory substrate supply to mitochondria. NO stimulates reactive oxygen and nitrogen species production from mitochondria via respiratory inhibition, reaction with ubiquinol and reaction with O2 in the membrane. NO can induce apoptosis, mainly via oxidative stress. NO induces necrosis, mainly via energy depletion. Reactive nitrogen species activation of the mitochondrial permeability transition pore may cause apoptosis or necrosis. NO may protect against mitochondria-mediated cell death by multiple mechanisms.
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Cites
Mediation of Poly(ADP-Ribose) Polymerase-1-Dependent Cell Death by Apoptosis-Inducing Factor
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Calorie restriction promotes mitochondrial biogenesis by inducing the expression of eNOS
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Nitrite reductase activity is a novel function of mammalian mitochondria
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Brookes, P. S., Salinas, E. P., Darley-Usmar, K., Eiserich, J. P., Freeman, B. A., Darley-Usmar, V. M., & Anderson, P. G. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m001077200 · Cited by 321
Protein Kinase G Transmits the Cardioprotective Signal From Cytosol to Mitochondria
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On the mechanism by which vascular endothelial cells regulate their oxygen consumption
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Direct evidence for S-nitrosation of mitochondrial complex I
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The adenine nucleotide translocator: a target of nitric oxide, peroxynitrite, and 4-hydroxynonenal
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“NO/RNS may also directly oxidise the protein thiols that regulate opening of the MPT pore (52).”
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Cited by
Cooper, C. E., & Brown, G. C. (2008) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-008-9166-6 · Cited by 718
Self-citationTerman, A., Kurz, T., Navratil, M., Arriaga, E. A., & Brunk, U. T. (2010) · Antioxidants & Redox Signaling · doi:10.1089/ars.2009.2598 · Cited by 490
Resveratrol: Its Biologic Targets and Functional Activity
Pervaiz, S., & Holme, A. L. (2009) · Antioxidants & Redox Signaling · doi:10.1089/ars.2008.2412 · Cited by 405
Mitochondrial biogenesis and healthy aging
López-Lluch, G., Irusta, P. M., Navas, P., & de Cabo, R. (2008) · Experimental Gerontology · doi:10.1016/j.exger.2008.06.014 · Cited by 364
Mitochondria as a Therapeutic Target in Heart Failure
Bayeva, M., Gheorghiade, M., & Ardehali, H. (2013) · Journal of the American College of Cardiology · doi:10.1016/j.jacc.2012.08.1021 · Cited by 332
Metadata
- Authors
- Brown, G.
- Venue
- Frontiers in Bioscience
- Publisher
- IMR Press
- Published
- 2007
- Volume
- 12
- Issue
- 1
- Pages
- 1024
- ISSN
- 1093-4715 (ISSN-L)
- 1093-9946
- DOI
- 10.2741/2122
- OpenAlex
- W167171351
- Cited by
- 172
- References
- 12
- FWCI
- 3.07
- Type
- journal article
- Language
- en
- Open access
- bronze
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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