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.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
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
Skulachev, V. P. (1996) · Quarterly Reviews of Biophysics · doi:10.1017/s0033583500005795 · Cited by 703
Self-citationComplex patterns formed by motile cells of Escherichia coli
Budrene, E. O., & Berg, H. C. (1991) · Nature · doi:10.1038/349630a0 · Cited by 584
Superoxide Dismutase Activity Is Essential for Stationary Phase Survival in Saccharomyces cerevisiae
Longo, V. D., Gralla, E. B., & Valentine, J. S. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.21.12275 · Cited by 531
Costantini, P., Chernyak, B. V., Petronilli, V., & Bernardi, P. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.12.6746 · Cited by 516
Superoxide sensitivity of the Escherichia coli aconitase.
Gardner, P. R., & Fridovich, I. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)55001-8 · Cited by 514
Superoxide Radical and Iron Modulate Aconitase Activity in Mammalian Cells
Gardner, P. R., Raineri, I., Epstein, L. B., & White, C. W. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.22.13399 · Cited by 469
Skulachev, V. P. (1996) · FEBS Letters · doi:10.1016/0014-5793(96)00989-1 · Cited by 378
Self-citationDypbukt, J. M., Ankarcrona, M., Burkitt, M. J., Sjöholm, Å., Ström, K., Orrenius, S., & Nicotera, P. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)43849-5 · Cited by 361
Cytochrome oxidase : a synthesis
Wikström, M. K. F., Krab, K., & Saraste, M. (1981) · Andalas University Repository (Andalas University) · Cited by 329
The Role of Reactive Oxygen Species in Mitochondrial Permeability Transition
Vercesi, A. E., Kowaltowski, A. J., Grijalba, M. T., Meinicke, A. R., & Castilho, R. F. (1997) · Bioscience Reports · doi:10.1023/a:1027335217774 · Cited by 325
Does the alternative pathway ameliorate chilling injury in sensitive plant tissues?
Purvis, A. C., & Shewfelt, R. L. (1993) · Physiologia Plantarum · doi:10.1111/j.1399-3054.1993.tb01393.x · Cited by 320
Papa, S. (1996) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(96)00077-1 · Cited by 266
Effect of Oxygen on Growth of Azotobacter chroococcum in Batch and Continuous Cultures
Dalton, H., & Postgate, J. R. (1968) · Journal of General Microbiology · doi:10.1099/00221287-54-3-463 · Cited by 260
Vanlerberghe, G. C., & Mclntosh, L. (1996) · PLANT PHYSIOLOGY · doi:10.1104/pp.111.2.589 · Cited by 259
The Physiological Significance of Mitochondrial Proton Leak in Animal Cells and Tissues
Rolfe, D. F. S., & Brand, M. D. (1997) · Bioscience Reports · doi:10.1023/a:1027327015957 · Cited by 233
Loss of Function of Cytochrome c in Jurkat Cells Undergoing Fas-mediated Apoptosis
Krippner, A., Matsuno‐Yagi, A., Gottlieb, R. A., & BABIOR, B. M. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.35.21629 · Cited by 221
Cyanide-Resistant Respiration in Higher Plants
Solomos, T. (1977) · Annual Review of Plant Physiology · doi:10.1146/annurev.pp.28.060177.001431 · Cited by 221
HENDERSON, L. M., & Chappell, J. (1996) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(95)00140-9 · Cited by 205
Role of the Mitochondrial Permeability Transition Pore in Apoptosis
Hirsch, T., Marzo, I., & Kroemer, G. (1997) · Bioscience Reports · doi:10.1023/a:1027339418683 · Cited by 203
Wagner, A. M. (1995) · FEBS Letters · doi:10.1016/0014-5793(95)00688-6 · Cited by 194
Superoxide-Driven Aconitase FE-S Center Cycling
Gardner, P. R. (1997) · Bioscience Reports · doi:10.1023/a:1027383100936 · Cited by 190
Growth and Physiology of Azotobacter chroococcum in Continuous Culture
Dalton, H., & Postgate, J. R. (1969) · Journal of General Microbiology · doi:10.1099/00221287-56-3-307 · Cited by 187
Harper, M., & Brand, M. D. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)82411-5 · Cited by 171
Vanlerberghe, G. C., & McIntosh, L. (1994) · PLANT PHYSIOLOGY · doi:10.1104/pp.105.3.867 · Cited by 167
Macho, A., Castedo, M., Marchetti, P., Aguilar, J., Decaudin, D., Zamzami, N., Girard, P., Uriel, J., & Kroemer, G. (1995) · Blood · doi:10.1182/blood.v86.7.2481.2481 · Cited by 145
Thyroid hormone action on mitochondrial energy transfer
Soboll, S. (1993) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(93)90024-a · Cited by 135
Oxygen taxis and proton motive force in Azospirillum brasilense
Zhulin, I. B., Bespalov, V. A., Johnson, M. S., & Taylor, B. L. (1996) · Journal of Bacteriology · doi:10.1128/jb.178.17.5199-5204.1996 · Cited by 134
Mechanisms of protein import across the mitochondrial outer membrane
Lill, R., & Neupert, W. (1996) · Trends in Cell Biology · doi:10.1016/0962-8924(96)81015-4 · Cited by 123
Minagawa, N., Koga, S., Nakano, M., Sakajo, S., & Yoshimoto, A. (1992) · FEBS Letters · doi:10.1016/0014-5793(92)80444-l · Cited by 122
Evidence for superoxide radical-dependent coronary vasospasm after angioplasty in intact dogs.
Laurindo, F. R. M., da Luz, P. L., Uint, L., Rocha, T. F., Jaeger, R. G., & Lopes, E. A. (1991) · Circulation · doi:10.1161/01.cir.83.5.1705 · Cited by 117
Dassa, J., Fsihi, H., Marck, C., Dion, M., Kieffer-Bontemps, M., & Boquet, P. L. (1991) · Molecular and General Genetics MGG · doi:10.1007/bf00267454 · Cited by 109
Coordinate Regulation of Cytochrome and Alternative Pathway Respiration in Tobacco
Vanlerberghe, G. C., & McIntosh, L. (1992) · PLANT PHYSIOLOGY · doi:10.1104/pp.100.4.1846 · Cited by 109
Nohl, H., Gille, L., Schönheit, K., & Liu, Y. (1996) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(95)02038-1 · Cited by 101
Reactive Oxygen and Nitrogen Species Regulate Mitochondrial Ca2+ Homeostasis and Respiration
Richter, C. (1997) · Bioscience Reports · doi:10.1023/a:1027387301845 · Cited by 97
Voltage activation of heart inner mitochondrial membrane channels
Zorov, D. B., Kinnally, K. W., & Tedeschi, H. (1992) · Journal of Bioenergetics and Biomembranes · doi:10.1007/bf00769538 · Cited by 83
Salicylic Acid Induces Cyanide-Resistant Respiration in Tobacco Cell-Suspension Cultures
Kapulnik, Y., Yalpani, N., & Raskin, I. (1992) · PLANT PHYSIOLOGY · doi:10.1104/pp.100.4.1921 · Cited by 74
Cytochrome and Alternative Pathway Respiration in Tobacco (Effects of Salicylic Acid)
Rhoads, D. M., & McIntosh, L. (1993) · PLANT PHYSIOLOGY · doi:10.1104/pp.103.3.877 · Cited by 73
Localization of HIV RNA in mitochondria of infected cells: potential role in cytopathogenicity.
Somasundaran, M., Zapp, M. L., Beattie, L. K., Pang, L., Byron, K. S., Bassell, G. J., Sullivan, J. L., & Singer, R. H. (1994) · The Journal of Cell Biology · doi:10.1083/jcb.126.6.1353 · Cited by 71
Melo, A. M. P., Roberts, T. H., & Møller, I. M. (1996) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(96)00068-0 · Cited by 66
Effects of thyroid hormones on oxidative phosphorylation
Harper, M., Ballantyne, J. S., Leach, M. F., & Brand, M. D. (1993) · Biochemical Society Transactions · doi:10.1042/bst0210785 · Cited by 63
Reception of the energy level in bacterial taxis
Glagolev, A. N. (1980) · Journal of Theoretical Biology · doi:10.1016/0022-5193(80)90097-1 · Cited by 57
A Possible Role of Slips in Cytochrome C Oxidase in the Antioxygen Defense System of the Cell
Papa, S., GUERRIERI, F., & Capitanio, N. (1997) · Bioscience Reports · doi:10.1023/a:1027331116866 · Cited by 49
Sensing of ΔμH+ in phototaxis of Halobacterium halobium
Baryshev, V. A., Glagolev, A. N., & Skulachev, V. P. (1981) · Nature · doi:10.1038/292338a0 · Cited by 38
Self-citationCôt́e, C. H., Boulet, D., & Poirier, J. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)39146-x · Cited by 28
Mechanisms of Oxygen Taxis in Bacteria
Grishanin, R. N., & Bibikov, S. I. (1997) · Bioscience Reports · doi:10.1023/a:1027391402753 · Cited by 18
Hyperthyroidism and Mitochondrial Uncoupling
Luvisetto, S. (1997) · Bioscience Reports · doi:10.1023/a:1027379000027 · Cited by 11
Belikova, Y. O., Kotlyar, A. B., & Vinogradov, A. D. (1989) · FEBS Letters · doi:10.1016/0014-5793(89)80244-3 · Cited by 8
A study of dependence of protein synthesis in mitochondria on the transmembrane potential
Rabinovitz, Y. M., Pinus, H. A., & Kotelnikova, A. V. (1977) · Molecular and Cellular Biochemistry · doi:10.1007/bf01734173 · Cited by 8
Flagged first, then by citations
1 of the 59 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
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
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review