The DOI matches its Crossref record; 25 of the 25 references it cites were found in a registry or an index.
Mitochondrial composition and function under the control of hypoxia
Open accessAbstract
Hypoxia triggers several mechanisms to adapt cells to a low oxygen environment. Mitochondria are major consumers of oxygen and a potential source of reactive oxygen species (ROS). In response to hypoxia they exchange or modify distinct subunits of the respiratory chain and adjust their metabolism, especially lowering the citric acid cycle. Intermediates of the citric acid cycle participate in regulating hypoxia inducible factors (HIF), the key mediators of adaptation to hypoxia. Here we summarize how hypoxia conditions mitochondria with consequences for ROS-production and the HIF-pathway.
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Cites
1 retracted
Mitochondrial Autophagy Is an HIF-1-dependent Adaptive Metabolic Response to Hypoxia
Zhang, H., Bosch-Marce, M., Shimoda, L. A., Tan, Y. S., Baek, J. H., Wesley, J. B., Gonzalez, F. J., & Semenza, G. L. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m800102200 · Cited by 1,601
RetractedActivation of apoptosis signalling pathways by reactive oxygen species
Redza-Dutordoir, M., & Averill-Bates, D. A. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2016.09.012 · Cited by 3,731
Ischaemic 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
Reductive glutamine metabolism by IDH1 mediates lipogenesis under hypoxia
Metallo, C. M., Gameiro, P. A., Bell, E. L., Mattaini, K. R., Yang, J., Hiller, K., Jewell, C. M., Johnson, Z. R., Irvine, D. J., Guarente, L., et al. (2012) · Nature · doi:10.1038/nature10602 · Cited by 1,791
Bellot, G., Garcia-Medina, R., Gounon, P., Chiche, J., Roux, D., Pouysségur, J., & Mazure, N. M. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.00166-09 · Cited by 1,501
Reductive carboxylation supports growth in tumour cells with defective mitochondria
Mullen, A. R., Wheaton, W. W., Jin, E. S., Chen, P.-H., Sullivan, L. B., Cheng, T., Yang, Y., Linehan, W. M., Chandel, N. S., & DeBerardinis, R. J. (2012) · Nature · doi:10.1038/nature10642 · Cited by 1,328
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Wise, D. R., Ward, P. S., Shay, J. E. S., Cross, J. R., Gruber, J. J., Sachdeva, U. M., Platt, J. M., DeMatteo, R. G., Simon, M. C., & Thompson, C. B. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1117773108 · Cited by 975
Oxygen sensing requires mitochondrial ROS but not oxidative phosphorylation
Brunelle, J. K., Bell, E. L., Quesada, N. M., Vercauteren, K., Tiranti, V., Zeviani, M., Scarpulla, R. C., & Chandel, N. S. (2005) · Cell Metabolism · doi:10.1016/j.cmet.2005.05.002 · Cited by 763
High-resolution genome-wide mapping of HIF-binding sites by ChIP-seq
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Cited by
Cellular Adaptation to Hypoxia through Hypoxia Inducible Factors and beyond
Lee, P., Chandel, N. S., & Simon, M. C. (2020) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-0227-y · Cited by 1,272
Cano Sanchez, M., Lancel, S., Boulanger, E., & Neviere, R. (2018) · Antioxidants · doi:10.3390/antiox7080098 · Cited by 574
Zhou, H., Wang, S., Zhu, P., Hu, S., Chen, Y., & Ren, J. (2018) · Redox Biology · doi:10.1016/j.redox.2017.12.019 · Cited by 550
“The mitochondrial content is modest in endothelial cells compared to other cell types with a higher energy requirement, indicating a primary role for mitochondria as essential signaling organelles in vascular endothelium [10,11].”
BackgroundActivation of AMPK under Hypoxia: Many Roads Leading to Rome
Dengler, F. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21072428 · Cited by 133
Maintenance of redox homeostasis by hypoxia-inducible factors
Samanta, D., & Semenza, G. L. (2017) · Redox Biology · doi:10.1016/j.redox.2017.05.022 · Cited by 127
“Major sites of ROS production in mammalian mitochondria are the ubiquinone reduction site of complex I and the outer quinone-binding site of the Q cycle in complex III [26].”
Background
Metadata
- Authors
- Fuhrmann, D. C., & Brüne, B.
- Venue
- Redox Biology
- Publisher
- Elsevier BV
- Published
- 2017-08
- Volume
- 12
- Pages
- 208-215
- ISSN
- 2213-2317 (ISSN-L)
- OpenAlex
- W2591395115
- Cited by
- 643
- References
- 25
- FWCI
- 12.44
- Type
- journal article
- Language
- en
- Open access
- gold
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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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