Architecture of Succinate Dehydrogenase and Reactive Oxygen Species Generation

By V. Yankovskaya, R. Horsefield, S. Törnroth, C. Luna-Chavez, H. Miyoshi, C. Léger, B. Byrne, G. Cecchini, S. Iwata. Science, 2003

897 citations recorded by the source corpus.

Subfields: Cancer Research, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/35becc3d72eabc907d0db7314d7f644fe030c44e

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In Cancer Research

Eyal Gottlieb

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Citations in the corpus

Progress in understanding molecular mechanisms and evolution of resistance to succinate dehydrogenase inhibiting (SDHI) fungicides in phytopathogenic fungi (2010, background): “In fact, insights about the location of the ubiquinone-binding sites have been revealed in several crystallographic and computational studies with the use of UQ-binding sites inhibitors (Table 1) (Horsefield et al., 2006; Huang et al., 2006; Sun et al., 2005; Yankovskaya et al., 2003).”
Succinate dehydrogenase and fumarate hydratase: linking mitochondrial dysfunction and cancer (2006, background): “Structural and functional analysis of SDH (complex II) from Escherichia coli did indicate the potential of ROS production on the SDHA site (Yankovskaya et al., 2003).”
Insights into the respiratory electron transfer pathway from the structure of nitrate reductase A (2003, background): “NarI exhibits a unique fold within the thus far solved structures of membrane-integral cytochromes b”
Iron‐sulphur clusters and the problem with oxygen (2006, background): “H 2 O2 stress is sensed by the OxyR or PerR systems, which direct activation of about two dozen genes (Zheng et al., 2001; Helmann et al., 2003).”
The Role of Oxidative Stress in Neurodegenerative Diseases (2015, background): “Complex II is involved in the reduction of CoQ and is known to be involved in producing low levels of O2 - [16, 17].”
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).”