The DOI matches its Crossref record; 12 of the 12 references it cites were found in a registry or an index.
On the sidedness of the ubiquinone redox cycle. Kinetic studies in mitochondrial membranes
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The mitochondrion likely releases small amounts of H2O2 as a natural chemical messenger in the modulation of mitochondrial and cellular function.
“Although the mitochondrion is largely a sink for O2•− and H2O2 due to its ROS scavenger systems, it likely releases small amounts of H2O2 as a natural chemical messenger in the modulation of mitochondrial and cellular function (27, 113, 126, 183, 203, 206).”
From Mitochondrial reactive oxygen species production in excitable cells: Modulators of mitochondrial and cell function (2009) · cites this paper as [206]
Citations
Cites
DETERMINATION OF SERUM PROTEINS BY MEANS OF THE BIURET REACTION
Gornall, A. G., Bardawill, C. J., & David, M. M. (1949) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)57021-6 · Cited by 16,164
Halliwell, B. B. (1978) · FEBS Letters · doi:10.1016/0014-5793(78)80279-8 · Cited by 313
Rieske, J. S. (1967) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(67)10047-5 · Cited by 285
The restoration of DPNH oxidase activity by coenzyme Q (ubiquinone)
Szarkowska, L. (1966) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(66)90228-1 · Cited by 161
Hatefi, Y., & Stempel, K. E. (1969) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)78232-5 · Cited by 157
Organic structural specificity and sites of coenzyme Q in succinoxidase and DPNH-oxidase systems
Lenaz, G., Daves, G. D., & Folkers, K. (1968) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(68)90175-6 · Cited by 80
Self-citationPacker, L., Mehard, C. W., Meissner, G., et al. (1974) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/0005-2736(74)90056-x · Cited by 78
Electron Transfer Chains and Oxidative Phosphorylation
Linnett, P. E. (1976) · Biochemical Society Transactions · doi:10.1042/bst0041181 · Cited by 63
Hauska, G. A. (1977) · FEBS Letters · doi:10.1016/0014-5793(77)80817-x · Cited by 53
The inhibition of NADH oxidase by the lower homologs of coenzyme Q
Lenaz, G., Pasquali, P., Bertoli, E., Parenti-Castelli, G., & Folkers, K. (1975) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(75)90335-5 · Cited by 45
Self-citationChance, B., Erecińska, M., & Radda, G. K. (1975) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1975.tb04165.x · Cited by 44
Effect of hydroxy analogs of coenzyme Q on DPNH- and succin-oxidase activities of yeast mitochondria
Castelli, A., Bertoli, E., Littarru, G. P., et al. (1971) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(71)90501-8 · Cited by 12
Flagged first, then by citations
Research works printed but not linked: 2
- Lee, 1966, vol. 7, 218
- Spisni, 1978, Arch. Biochem. Biophys
Cited by
Sorted by citations
Stowe, D. F., & Camara, A. K. S. (2009) · Antioxidants & Redox Signaling · doi:10.1089/ars.2008.2331 · Cited by 471
Metadata
- Authors
- Lenaz, G., Landi, L., Cabrini, L., Pasquali, P., Sechi, A. M., & Ozawa, T.
- Affiliations
- University of Bologna (IT)
- Venue
- Biochemical and Biophysical Research Communications
- Publisher
- Elsevier BV
- Published
- 1978-12
- Volume
- 85
- Issue
- 3
- Pages
- 1047-1053
- ISSN
- 0006-291X (ISSN-L)
- OpenAlex
- W2089649125
- Cited by
- 20
- References
- 12
- Citations by year
- 2020: 1
- FWCI
- 1.45
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Biochemical and Biophysical Research Communications (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Coenzyme Q10 studies and effects
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Pharmacology, Toxicology and Pharmaceutics › Toxicology › Bioactive Compounds and Antitumor Agents
- Keywords
- NADH dehydrogenase, ubiquinol oxidase, succinate oxidation, NADH oxidation, mitochondrial membrane, submitochondrial particles, lipid bilayers
- MeSH terms
- Animals, Cattle, Intracellular Membranes, Kinetics, Mitochondria, Heart, NADH, NADPH Oxidoreductases, Oxidation-Reduction, Submitochondrial Particles, Temperature, Ubiquinone
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