The DOI matches its Crossref record; 58 of the 59 references it cites were found in a registry or an index.
Membrane-Linked Systems Preventing Superoxide Formation
Abstract
New facts and ideas concerning the membrane-linked mechanisms preventing superoxide formation are summarised here. It is assumed that aerobic cells possess several lines of anti-ROS defence, including optimisation of the intracellular oxygen concentration, decrease in the concentration and life-time of one-electron O2 reductants such as CoQH; and mitochondrial and cell selections, i.e. elimination of mitochondria and cells producing ROS at high rate. It is postulated that ROS-dependent pore opening and ROS-dependent apoptosis are involved in mitochondrial and cell selections.
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In the citing paper
“Δψm is an important factor for maintaining cellular energy homeostasis, and small reductions in Δψm induced by mild uncoupling were shown to decrease H2O2 emissions (51,52) and produce a natural antioxidant effect (53).”
From TFAM Enhances Fat Oxidation and Attenuates High-Fat Diet–Induced Insulin Resistance in Skeletal Muscle (2019) · cites this paper as [53]
In the citing paper
“Protein oxidation can lead to unfolding and result in loss of catalytic function and degradation (289) [e.g., ROS can damage the Na/K ATPase complex (287)].”
From Mitochondrial reactive oxygen species production in excitable cells: Modulators of mitochondrial and cell function (2009) · cites this paper as [287]
Citations
Cites
Induction of Apoptotic Program in Cell-Free Extracts: Requirement for dATP and Cytochrome c
Liu, X., Kim, C. N., Yang, J., Jemmerson, R., & Wang, X. (1996) · Cell · doi:10.1016/s0092-8674(00)80085-9 · Cited by 5,167
The ferritins: molecular properties, iron storage function and cellular regulation
Harrison, P. M., & Arosio, P. (1996) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(96)00022-9 · Cited by 2,667
Boveris, A., & Chance, B. (1973) · Biochemical Journal · doi:10.1042/bj1340707 · Cited by 2,626
The mitochondrial permeability transition
Zoratti, M., & Szabó, I. (1995) · Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes · doi:10.1016/0304-4157(95)00003-a · Cited by 2,410
Photosynthesis: from Light to Biosphere
GIORDANO, M., & G., B. (1995) · Springer eBooks · doi:10.1007/978-94-009-0173-5 · Cited by 1,670
Mitochondrial control of nuclear apoptosis.
Zamzami, N., Susín, S. A., Marchetti, P., Hirsch, T., Gomez-Monterrey, I. M., Castedo, M., & Kroemer, G. (1996) · The Journal of Experimental Medicine · doi:10.1084/jem.183.4.1533 · Cited by 1,360
Exercise physiology: Human bioenergetics and its applications
Brooks, G. A. (1984) · Medical Entomology and Zoology · Cited by 1,188
Active Oxygen Species in the Induction of Plant Systemic Acquired Resistance by Salicylic Acid
Chen, Z., Silva, H., & Klessig, D. F. (1993) · Science · doi:10.1126/science.8266079 · Cited by 1,184
Bcl-2 inhibits the mitochondrial release of an apoptogenic protease.
Susín, S. A., Zamzami, N., Castedo, M., Hirsch, T., Marchetti, P., Macho, A., Daugas, É., Geuskens, M., & Kroemer, G. (1996) · The Journal of Experimental Medicine · doi:10.1084/jem.184.4.1331 · Cited by 1,133
Superoxide production by the mitochondrial respiratory chain
Turrens, J. F. (1997) · Bioscience Reports · doi:10.1023/a:1027374931887 · Cited by 903
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1 of the 59 references couldn’t be matched to a known paper.
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Antioxidants, Oxidative Damage and Oxygen Deprivation Stress: a Review
Blokhina, O. B. (2002) · Annals of Botany · doi:10.1093/aob/mcf118 · Cited by 4,018
Uncoupling: new approaches to an old problem of bioenergetics
Skulachev, V. P. (1998) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(97)00091-1 · Cited by 893
Self-citationMitochondrial permeability transition and oxidative stress
Kowaltowski, A. J., Castilho, R. F., & Vercesi, A. E. (2001) · FEBS Letters · doi:10.1016/s0014-5793(01)02316-x · Cited by 832
Tarpey, M. M., Wink, D. A., & Grisham, M. B. (2004) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00361.2003 · Cited by 673
Energy metabolism in uncoupling protein 3 gene knockout mice
Vidal-Puig, A. J., Grujic, D., Zhang, C.-Y., Hagen, T., Boss, O., Ido, Y., Szczepanik, A., Wade, J., Mootha, V., Cortright, R., et al. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m910179199 · Cited by 677
Metadata
- Authors
- Skulachev, V. P.
- Affiliations
- Lomonosov Moscow State University (RU)
- Corresponding author
- Skulachev, Vladimir P.
- Venue
- Bioscience Reports
- Publisher
- Portland Press Ltd.
- Published
- 1997-06-01
- Volume
- 17
- Issue
- 3
- Pages
- 347-366
- ISSN
- 0144-8463 (ISSN-L)
- 1573-4935
- OpenAlex
- W1876476959
- Cited by
- 162
- References
- 59
- Citations by year
- 2025: 1 · 2024: 1 · 2023: 1 · 2022: 2 · 2021: 3 · 2019: 3 · 2018: 2 · 2016: 3 · 2015: 1 · 2014: 6 · 2013: 3 · 2012: 8
- FWCI
- 3.42
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Bioscience Reports (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
- Keywords
- superoxide, reactive oxygen species, intracellular oxygen concentration, coenzyme Q10, cell selection
- MeSH terms
- Aconitate Hydratase, Animals, Azotobacter, Bacteria, Cell Membrane, Cell Membrane Permeability, DNA, Mitochondrial, Humans, Mitochondria, Oxidation-Reduction, Permeability, Plants, Superoxides, Uncoupling Agents, Apoptosis, Reactive Oxygen Species
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