Crystal structure of mitochondrial respiratory membrane protein complex II.

By F. Sun, X. Huo, Y. Zhai, Aojin Wang, Jianxing Xu, D. Su, M. Bartlam, Z. Rao. Cell, 2005

843 citations recorded by the source corpus.

Subfields: Cancer Research, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/ae0238d12c2dedbd48324da09c438159f3471c1d

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In Cancer Research

1. A. Gimenez-Roqueplo

In Molecular Biology

1. H. Avenot
2. T. Michailides
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4. Shuai Jiang
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Citations in the corpus

• Mitochondrial electron transport chain, ROS generation and uncoupling (Review) (2019, background): “Complex II (CII). cII, namely, succinate dehydrogenase, is a component of the Krebs cycle as well as the ETc, serving as a link between metabolism and OXPHOS (19,20).”
• Characterization of mutations in the membrane-anchored subunits AaSDHC and AaSDHD of succinate dehydrogenase from Alternaria alternata isolates conferring field resistance to the fungicide boscalid (2009, background): “The UQ-binding site is highly conserved between bacteria and eukaryotes and is formed by residues from subunits B, C and D (Yankovskaya et al., 2003; Sun et al., 2005; Horsefield et al., 2006).”
• Mitochondrial Complex II Can Generate Reactive Oxygen Species at High Rates in Both the Forward and Reverse Reactions* (2012, background): “1 Å edge-to-edge distance between the [3Fe-4S] center and Q facilitates electron tunneling (16).”
• Progress in understanding molecular mechanisms and evolution of resistance to succinate dehydrogenase inhibiting (SDHI) fungicides in phytopathogenic fungi (2010, background): “As previously described (Baysal et al., 2001; Cecchini, 2003), the deduced amino acid sequences exhibited low similarities with SDHC and SDHD peptides frommodel organisms, namely E. coli and Saccharomyces cereviviae, but residues essential to form the ubiquinone-binding site or important in SQR asse”
• SDHA is a tumor suppressor gene causing paraganglioma. (2010, background): “Arg589 is located at the apex of SDHA (18,19), about 20 Å removed from the flavin moiety and distal to the interface with SDHB (.”