The DOI matches its Crossref record; 83 of the 83 references it cites were found in a registry or an index.
Succinate dehydrogenase – Assembly, regulation and role in human disease
Open accessAbstract
Succinate dehydrogenase (or Electron Transport Chain Complex II) has been the subject of a focused but significant renaissance. This complex, which has been the least studied of the mitochondrial respiratory complexes has seen renewed interest due to the discovery of its role in human disease. Under this heightened scrutiny, the succinate dehydrogenase complex has proven to be a fascinating machine, whose regulation and assembly requires additional factors that are beginning to be discovered. Mutations in these factors and in the structural subunits of the complex itself cause a variety of human diseases. The mechanisms underlying the pathogenesis of SDH mutations is beginning to be understood.
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Cites
Sequence and organization of the human mitochondrial genome
Anderson, S., Bankier, A. T., Barrell, B. G., de Bruijn, M. H. L., Coulson, A. R., Drouin, J., Eperon, I. C., Nierlich, D. P., Roe, B. A., Sanger, F., et al. (1981) · Nature · doi:10.1038/290457a0 · Cited by 9,636
The Hsp70 and Hsp60 Chaperone Machines
Bukau, B., & Horwich, A. L. (1998) · Cell · doi:10.1016/s0092-8674(00)80928-9 · Cited by 2,815
Mitochondria: Dynamic Organelles in Disease, Aging, and Development
Chan, D. C. (2006) · Cell · doi:10.1016/j.cell.2006.06.010 · Cited by 1,987
Mutations in SDHD , a Mitochondrial Complex II Gene, in Hereditary Paraganglioma
Baysal, B. E., Ferrell, R. E., Willett-Brozick, J. E., Lawrence, E. C., Myssiorek, D., Bosch, A., Mey, A. V. D., Taschner, P. E. M., Rubinstein, W. S., Myers, E. N., et al. (2000) · Science · doi:10.1126/science.287.5454.848 · Cited by 1,638
Biochemical, physiological and medical aspects of ubiquinone function
Ernster, L., & Dallner, G. (1995) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/0925-4439(95)00028-3 · Cited by 1,227
Astuti, D., Latif, F., Dallol, A., Dahia, P. L. M., Douglas, F., George, E., Sköldberg, F., Husebye, E. S., Eng, C., & Maher, E. R. (2001) · The American Journal of Human Genetics · doi:10.1086/321282 · Cited by 1,087
Architecture of succinate dehydrogenase and reactive oxygen species generation
Yankovskaya, V., Horsefield, R., Törnroth, S., Luna-Chavez, C., Miyoshi, H., Léger, C., Byrne, B., Cecchini, G., & Iwata, S. (2003) · Science · doi:10.1126/science.1079605 · Cited by 927
Neumann, H. P. H. (2004) · JAMA · doi:10.1001/jama.292.8.943 · Cited by 893
Crystal Structure of Mitochondrial Respiratory Membrane Protein Complex II
Sun, F., Huo, X., Zhai, Y., Wang, A., Xu, J., Su, D., Bartlam, M., & Rao, Z. (2005) · Cell · doi:10.1016/j.cell.2005.05.025 · Cited by 881
Mutations in SDHC cause autosomal dominant paraganglioma, type 3
Niemann, S., & Müller, U. (2000) · Nature Genetics · doi:10.1038/81551 · Cited by 875
Cited by
SDH mutations establish a hypermethylator phenotype in paraganglioma
Letouzé, E., Martinelli, C., Loriot, C., Burnichon, N., Abermil, N., Ottolenghi, C., Janin, M., Menara, M., Nguyen, A. T., Benit, P., et al. (2013) · Cancer Cell · doi:10.1016/j.ccr.2013.04.018 · Cited by 776
The role of mitochondria in energy production for human sperm motility
Piomboni, P., Focarelli, R., Stendardi, A., Ferramosca, A., & Zara, V. (2012) · International Journal of Andrology · doi:10.1111/j.1365-2605.2011.01218.x · Cited by 458
Metabolic adaptation in hypoxia and cancer
Paredes, F., Williams, H. C., & San Martin, A. (2021) · Cancer Letters · doi:10.1016/j.canlet.2020.12.020 · Cited by 259
Pyruvate and metabolic flexibility: illuminating a path toward selective cancer therapies
Olson, K. A., Schell, J. C., & Rutter, J. (2016) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2016.01.002 · Cited by 154
Self-citationMetabolic Remodeling during Liver Regeneration
Caldez, M. J., Van Hul, N., Koh, H. W. L., Teo, X. Q., Fan, J. J., Tan, P. Y., Dewhurst, M. R., Too, P. G., Talib, S. Z. A., Chiang, B. E., et al. (2018) · Developmental Cell · doi:10.1016/j.devcel.2018.09.020 · Cited by 133
Metadata
- Authors
- Rutter, J., Winge, D. R., & Schiffman, J. D.
- Venue
- Mitochondrion
- Publisher
- Elsevier BV
- Published
- 2010-06
- Volume
- 10
- Issue
- 4
- Pages
- 393-401
- ISSN
- 1567-7249 (ISSN-L)
- OpenAlex
- W1964025113
- Cited by
- 462
- References
- 83
- FWCI
- 8.74
- Type
- journal article
- Language
- en
- Open access
- green
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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.
