The DOI matches its Crossref record; 17 of the 17 references it cites were found in a registry or an index.
Control of mitochondrial superoxide production by reverse electron transport at complex I
Open accessAbstract
production by RET is highly responsive to small changes in Δp and the CoQ redox state, indicating that complex I RET represents a major mode of mitochondrial redox signaling.
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Citations
Cites
How mitochondria produce reactive oxygen species
Murphy, M. P. (2009) · Biochemical Journal · doi:10.1042/bj20081386 · Cited by 8,207
Self-citationIschaemic accumulation of succinate controls reperfusion injury through mitochondrial ROS
Chouchani, E. T., Pell, V. R., Gaude, E., Aksentijević, D., Sundier, S. Y., Robb, E. L., Logan, A., Nadtochiy, S. M., Ord, E. N. J., Smith, A. C., et al. (2014) · Nature · doi:10.1038/nature13909 · Cited by 2,907 · cited 1×
“For example, during ischemia, high levels of succinate accumulate, and it is oxidized upon reperfusion to drive a burst of ROS via RET (14, 48).”
BackgroundSelf-citationSignal transduction by reactive oxygen species
Finkel, T. (2011) · Journal of Cell Biology · doi:10.1083/jcb.201102095 · Cited by 2,322
OWEN, M. R., DORAN, E., & HALESTRAP, A. P. (2000) · Biochemical Journal · doi:10.1042/bj3480607 · Cited by 2,157
Topology of superoxide production from different sites in the mitochondrial electron transport chain
St-Pierre, J., Buckingham, J. A., Roebuck, S. J., & Brand, M. D. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m207217200 · Cited by 1,545
Metformin as a tool to target aging
Barzilai, N., Crandall, J. P., Kritchevsky, S. B., & Espeland, M. A. (2016) · Cell Metabolism · doi:10.1016/j.cmet.2016.05.011 · Cited by 1,096 · cited 1×
“production by RET, in addition to stimulating AMP-activated protein kinase by inhibiting complex I (46, 47).”
BackgroundSelective Targeting of a Redox-active Ubiquinone to Mitochondria within Cells
Kelso, G. F., Porteous, C. M., Coulter, C. V., Hughes, G., Porteous, W. K., Ledgerwood, E. C., Smith, R. A. J., & Murphy, M. P. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m009093200 · Cited by 1,091
Self-citationSupercomplex assembly determines electron flux in the mitochondrial electron transport chain
Lapuente-Brun, E., Moreno-Loshuertos, R., Acín-Pérez, R., Latorre-Pellicer, A., Colás, C., Balsa, E., Perales-Clemente, E., Quirós, P. M., Calvo, E., Rodríguez-Hernández, M. A., et al. (2013) · Science · doi:10.1126/science.1230381 · Cited by 830
Redox-based regulation of signal transduction: principles, pitfalls, and promises
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. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.03.011 · Cited by 784
A Unifying Mechanism for Mitochondrial Superoxide Production during Ischemia-Reperfusion Injury
Chouchani, E. T., Pell, V. R., James, A. M., Work, L. M., Saeb-Parsy, K., Frezza, C., Krieg, T., & Murphy, M. P. (2016) · Cell Metabolism · doi:10.1016/j.cmet.2015.12.009 · Cited by 752
Self-citation
Cited by
Nolfi-Donegan, D., Braganza, A., & Shiva, S. (2020) · Redox Biology · doi:10.1016/j.redox.2020.101674 · Cited by 1,488
The Role of Oxidative Stress in Skeletal Muscle Myogenesis and Muscle Disease
Lian, D., Chen, M.-M., Wu, H., Deng, S., & Hu, X. (2022) · Antioxidants · doi:10.3390/antiox11040755 · Cited by 232
“Complex II is succinate, a substrate for the TCA cycle enzyme succinate dehydrogenase(SDH) [19].”
BackgroundFumarate is a terminal electron acceptor in the mammalian electron transport chain
Spinelli, J. B., Rosen, P. C., Sprenger, H.-G., Puszynska, A. M., Mann, J. L., Roessler, J. M., Cangelosi, A. L., Henne, A., Condon, K. J., Zhang, T., et al. (2021) · Science · doi:10.1126/science.abi7495 · Cited by 221
Glossmann, H. H., & Lutz, O. M. D. (2019) · Gerontology · doi:10.1159/000502257 · Cited by 149
A break in mitochondrial endosymbiosis as a basis for inflammatory diseases
Murphy, M. P., & O’Neill, L. A. J. (2024) · Nature · doi:10.1038/s41586-023-06866-z · Cited by 138
Self-citationLarge neutral amino acid levels tune perinatal neuronal excitability and survival
Knaus, L. S., Basilico, B., Malzl, D., Gerykova Bujalkova, M., Smogavec, M., Schwarz, L. A., Gorkiewicz, S., Amberg, N., Pauler, F. M., Knittl-Frank, C., et al. (2023) · Cell · doi:10.1016/j.cell.2023.02.037 · Cited by 70
Metadata
- Authors
- Robb, E. L., Hall, A. R., Prime, T. A., Eaton, S., Szibor, M., Viscomi, C., James, A. M., & Murphy, M. P.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2018-06
- Volume
- 293
- Issue
- 25
- Pages
- 9869-9879
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2799333965
- Cited by
- 331
- References
- 17
- FWCI
- 8.87
- Type
- journal article
- Language
- en
- Open access
- hybrid
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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.
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
