Cytopathies involving mitochondrial complex II

HIFα Targeted for VHL-Mediated Destruction by Proline Hydroxylation: Implications for O ₂ Sensing

Ivan, M., Kondo, K., Yang, H., Kim, W., Valiando, J., Ohh, M., Salic, A., Asara, J. M., Lane, W. S., & Kaelin Jr., W. G. (2001) · Science · doi:10.1126/science.1059817 · Cited by 4,735 · see citing works

Friedreich's Ataxia: Autosomal Recessive Disease Caused by an Intronic GAA Triplet Repeat Expansion

Campuzano, V., Montermini, L., Moltò, M. D., Pianese, L., Cossée, M., Cavalcanti, F., Monros, E., Rodius, F., Duclos, F., Monticelli, A., et al. (1996) · Science · doi:10.1126/science.271.5254.1423 · Cited by 2,786 · see citing works

Reactive oxygen species generated at mitochondrial complex III stabilize hypoxia-inducible factor-1α during hypoxia

Chandel, N. S., McClintock, D. S., Feliciano, C. E., Wood, T. M., Melendez, J. A., Rodriguez, A. M., & Schumacker, P. T. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m001914200 · Cited by 2,000 · see citing works

Mitochondrial reactive oxygen species trigger hypoxia-induced transcription

Chandel, N. S., Maltepe, E., Goldwasser, E., Mathieu, C. E., Simon, M. C., & Schumacker, P. T. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.20.11715 · Cited by 1,926 · see citing works

Mutations in <i>SDHD</i> , 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 · see citing works

Chemistry and Biochemistry of Flavoenzymes

Müller, F. (2018) · CRC Press eBooks · doi:10.1201/9781351070577 · Cited by 1,219 · see citing works

Gene Mutations in the Succinate Dehydrogenase Subunit SDHB Cause Susceptibility to Familial Pheochromocytoma and to Familial Paraganglioma

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 · see citing works

Neurochemical and histologic characterization of striatal excitotoxic lesions produced by the mitochondrial toxin 3-nitropropionic acid

Beal, M. F., Brouillet, E., Jenkins, B. G., Ferrante, R. J., Kowall, N. W., Miller, J., Storey, E., Srivastava, R., Rosen, B. R., & Hyman, B. T. (1993) · Journal of Neuroscience · doi:10.1523/jneurosci.13-10-04181.1993 · Cited by 1,026 · see citing works

Regulation of Mitochondrial Iron Accumulation by Yfh1p, a Putative Homolog of Frataxin

Babcock, M., de Silva, D., Oaks, R., Davis-Kaplan, S., Jiralerspong, S., Montermini, L., Pandolfo, M., & Kaplan, J. (1997) · Science · doi:10.1126/science.276.5319.1709 · Cited by 921 · see citing works

Oxidative damage and metabolic dysfunction in Huntington's disease: Selective vulnerability of the basal ganglia

Browne, S. E., Bowling, A. C., Macgarvey, U., Baik, M. J., Berger, S. C., Muquit, M. M. K., Bird, E. D., & Beal, M. F. (1997) · Annals of Neurology · doi:10.1002/ana.410410514 · Cited by 885 · see citing works

Mitochondrial defect in Huntington's disease caudate nucleus

Gu, M., Gash, M. T., Mann, V. M., Javoy‐Agid, F., Cooper, J. M., & Schapira, A. H. V. (1996) · Annals of Neurology · doi:10.1002/ana.410390317 · Cited by 758 · see citing works

Mouse models for Friedreich ataxia exhibit cardiomyopathy, sensory nerve defect and Fe-S enzyme deficiency followed by intramitochondrial iron deposits

Puccio, H., Simon, D., Cossée, M., Criqui-Filipe, P., Tiziano, F., Melki, J., Hindelang, C., Matyas, R., Rustin, P., & Koenig, M. (2001) · Nature Genetics · doi:10.1038/84818 · Cited by 738 · see citing works

Mutation of a nuclear succinate dehydrogenase gene results in mitochondrial respiratory chain deficiency

Bourgeron, T., Rustin, P., Chretien, D., Birch-Machin, M., Bourgeois, M., Viegas-Péquignot, E., Munnich, A., & Rötig, A. (1995) · Nature Genetics · doi:10.1038/ng1095-144 · Cited by 730 · see citing works

The mitochondrial proteins Atm1p and Nfs1p are essential for biogenesis of cytosolic Fe/S proteins

Kispál, G., Csere, P., Prohl, C., & Lill, R. (1999) · The EMBO Journal · doi:10.1093/emboj/18.14.3981 · Cited by 699 · see citing works

Cysteine desulfurase activity indicates a role for NIFS in metallocluster biosynthesis.

Zheng, L., White, R. H., Cash, V. L., Jack, R. F., & Dean, D. R. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.7.2754 · Cited by 597 · see citing works

Ataxia with isolated vitamin E deficiency is caused by mutations in the α–tocopherol transfer protein

Ouahchi, K., Arita, M., Kayden, H. J., Hentati, F., Hamida, M. B., Sokol, R. J., Arai, H., Inoue, K., Mandel, J., & Koenig, M. (1995) · Nature Genetics · doi:10.1038/ng0295-141 · Cited by 574 · see citing works

Evidence for irnnairment of energy metabofism in vivo in Huntington's disease using localized 1H NMR spectroscopy

Jenkins, B. G., Koroshetz, W. J., Beal, M. F., & Rosen, B. R. (1993) · Neurology · doi:10.1212/wnl.43.12.2689 · Cited by 479 · see citing works

Succinate: quinone oxidoreductases

Hägerhäll, C. (1997) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(97)00019-4 · Cited by 439 · see citing works

Structure of the Escherichia coli Fumarate Reductase Respiratory Complex

Iverson, T. M., Luna-Chavez, C., Cecchini, G., & Rees, D. C. (1999) · Science · doi:10.1126/science.284.5422.1961 · Cited by 416 · see citing works

Inactivation of the Friedreich ataxia mouse gene leads to early embryonic lethality without iron accumulation

Cossee, M. (2000) · Human Molecular Genetics · doi:10.1093/hmg/9.8.1219 · Cited by 377 · see citing works

The R22X mutation of the SDHD gene in hereditary paraganglioma abolishes the enzymatic activity of complex II in the mitochondrial respiratory chain and activates the hypoxia pathway

Gimenez-Roqueplo, A.-P., Favier, J., Rustin, P., Mourad, J.-J., Plouin, P.-F., Corvol, P., Rötig, A., & Jeunemaitre, X. (2001) · The American Journal of Human Genetics · doi:10.1086/324413 · Cited by 364 · see citing works

Structure of fumarate reductase from Wolinella succinogenes at 2.2 Å resolution

Lancaster, C. R. D., Kröger, A., Auer, M., & Michel, H. (1999) · Nature · doi:10.1038/46483 · Cited by 339 · see citing works

Clinical, biochemical and molecular genetic correlations in Friedreich's ataxia

Bradley, J. L. (2000) · Human Molecular Genetics · doi:10.1093/hmg/9.2.275 · Cited by 339 · see citing works

NifS-directed assembly of a transient [2Fe-2S] cluster within the NifU protein

Yuvaniyama, P., Agar, J. N., Cash, V. L., Johnson, M. K., & Dean, D. R. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.2.599 · Cited by 330 · see citing works

Evidence for a conserved system for iron metabolism in the mitochondria of Saccharomyces cerevisiae

Schilke, B. A., Voisine, C., Beinert, H., & Craig, E. A. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.18.10206 · Cited by 284 · see citing works

Transfer of Sulfur from IscS to IscU during Fe/S Cluster Assembly

Urbina, H. D., Silberg, J. J., Hoff, K. G., & Vickery, L. E. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m106907200 · Cited by 278 · see citing works

The Yeast Frataxin Homologue Mediates Mitochondrial Iron Efflux

Radisky, D. C., Babcock, M. C., & Kaplan, J. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.8.4497 · Cited by 277 · see citing works

Somatic and occult germ-line mutations in SDHD, a mitochondrial complex II gene, in nonfamilial pheochromocytoma.

Gimm, O., Armanios, M. Y., Dziema, H., Neumann, H. P. H., & Eng, C. (2000) · PubMed · Cited by 274 · see citing works

A mitochondrial ferredoxin is essential for biogenesis of cellular iron-sulfur proteins

Lange, H., Kaut, A., Kispál, G., & Lill, R. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.3.1050 · Cited by 272 · see citing works

A defect in the cytochrome b large subunit in complex II causes both superoxide anion overproduction and abnormal energy metabolism in Caenorhabditis elegans

Senoo-Matsuda, N., Yasuda, K., Tsuda, M., Ohkubo, T., Yoshimura, S., Nakazawa, H., Hartman, P. S., & Ishii, N. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m104718200 · Cited by 271 · see citing works

IscA, an Alternate Scaffold for Fe−S Cluster Biosynthesis

Krebs, C., Agar, J. N., Smith, A. D., Jeverson Frazzon, B., Dean, D. R., Huynh, B. H., & Johnson, M. K. (2001) · Biochemistry · doi:10.1021/bi015656z · Cited by 252 · see citing works

Germline SDHD mutation in familial phaeochromocytoma

Astuti, D., Douglas, F., Lennard, T. W., Aligianis, I. A., Woodward, E. R., Evans, D. G. R., Eng, C., Latif, F., & Maher, E. R. (2001) · The Lancet · doi:10.1016/s0140-6736(00)04378-6 · Cited by 246 · see citing works

Antioxidant treatment improves in vivo cardiac and skeletal muscle bioenergetics in patients with Friedreich's ataxia

Lodi, R., Hart, P. E., Rajagopalan, B., Taylor, D. J., Crilley, J. G., Bradley, J. L., Blamire, A. M., Manners, D. N., Styles, P., Schapira, A. H. V., et al. (2001) · Annals of Neurology · doi:10.1002/ana.1001 · Cited by 235 · see citing works

Dominant isolated renal magnesium loss is caused by misrouting of the Na+,K+-ATPase γ-subunit

Meij, I. C., Koenderink, J. B., van Bokhoven, H., Assink, K., Groenestege, W. M. T., de Pont, J. J. H. H. M., Bindels, R. J. M., Monnens, L. A. H., van den Heuvel, L. P. W. J., & Knoers, N. V. A. M. (2000) · Nature Genetics · doi:10.1038/81543 · Cited by 232 · see citing works

Dominant Isolated Renal Magnesium Loss Is Caused by Misrouting of the Na+,K+‐ATPase γ‐Subunit

Meij, I. C., Koenderink, J. B., de Jong, J. C., Pont, J. J. H. H. M. D., Monnens, L. A. H., van den Heuvel, L. P. W. J., & Knoers, N. V. A. M. (2003) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2003.tb07226.x · Cited by 224 · see citing works

Iron-Sulfur Cluster Assembly

de Choudens, S. O., Mattioli, T. A., Takahashi, Y., & Fontecave, M. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m102902200 · Cited by 211 · see citing works

Compound heterozygous mutations in the flavoprotein gene of the respiratory chain complex II in a patient with Leigh syndrome

Parfait, B., Chrétien, D., Rötig, A., Marsac, C., Münnich, A., & Rustin, P. (2000) · Human Genetics · doi:10.1007/s004399900218 · Cited by 211 · see citing works

Partial Inhibition of Brain Succinate Dehydrogenase by 3‐Nitropropionic Acid Is Sufficient to Initiate Striatal Degeneration in Rat

Brouillet, E., Guyot, M., Mittoux, V., Altairac, S., Condé, F., Palfi, S., & Hantraye, P. (1998) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1998.70020794.x · Cited by 210 · see citing works

Inhibition of Succinate Dehydrogenase by Malonic Acid Produces an “Excitotoxic” Lesion in Rat Striatum

Greene, J. G., Porter, R. H. P., Eller, R. V., & Greenamyre, J. T. (1993) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1993.tb03634.x · Cited by 208 · see citing works

Biogenesis of iron–sulfur proteins in eukaryotes: a novel task of mitochondria that is inherited from bacteria

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Yeast Mitochondrial Protein, Nfs1p, Coordinately Regulates Iron-Sulfur Cluster Proteins, Cellular Iron Uptake, and Iron Distribution

Li, J., Kogan, M., Knight, S. A. B., Pain, D., & Dancis, A. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.46.33025 · Cited by 201 · see citing works

Disabled early recruitment of antioxidant defenses in Friedreich's ataxia

Chantrel-Groussard, K. (2001) · Human Molecular Genetics · doi:10.1093/hmg/10.19.2061 · Cited by 189 · see citing works

Synthetic approaches to the active sites of iron-sulfur proteins

Holm, R. H. (1977) · Accounts of Chemical Research · doi:10.1021/ar50120a001 · Cited by 175 · see citing works

Nearly all hereditary paragangliomas in The Netherlands are caused by two founder mutations in the SDHD gene

Taschner, P. E. M., Jansen, J. C., Baysal, B. E., Bosch, A. M., Rosenberg, E. H., Bröcker‐Vriends, A. H. J. T., van der Mey, A. G. L., van Ommen, G. B., Cornelisse, C. J., & Devilee, P. (2001) · Genes Chromosomes and Cancer · doi:10.1002/gcc.1144 · Cited by 165 · see citing works

Inhibition of Mitochondrial Complex II Induces a Long-Term Potentiation of NMDA-Mediated Synaptic Excitation in the Striatum Requiring Endogenous Dopamine

Calabresi, P., Gubellini, P., Picconi, B., Centonze, D., Pisani, A., Bonsi, P., Greengard, P., Hipskind, R. A., Borrelli, E., & Bernardi, G. (2001) · Journal of Neuroscience · doi:10.1523/jneurosci.21-14-05110.2001 · Cited by 163 · see citing works

Combinatorial mRNA Regulation: Iron Regulatory Proteins and Iso-iron-responsive Elements (Iso-IREs)

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Structural and mechanistic mapping of a unique fumarate reductase.

Walkinshaw, M. D., Taylor, P., Pealing, S. L., Reid, G. A., & Chapman, S. K. (1999) · Nature Structural Biology · doi:10.1038/70045 · Cited by 159 · see citing works

Genetics and molecular biology of Huntington's disease

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The phylogenetic distribution of frataxin indicates a role in iron-sulfur cluster protein assembly

Huynen, M. A. (2001) · Human Molecular Genetics · doi:10.1093/hmg/10.21.2463 · Cited by 157 · see citing works

Low iron concentration and aconitase deficiency in a yeast frataxin homologue deficient strain

Foury, F. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)00961-8 · Cited by 145 · see citing works

Progress in understanding structure-function relationships in respiratory chain complex II.

Ackrell, B. A. C. (2000) · FEBS Letters · doi:10.1016/s0014-5793(99)01749-4 · Cited by 144 · see citing works

A structural moDAl for the membrane‐integral domain of succinate:quinone oxidoreductases

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Jac1, a mitochondrial J-type chaperone, is involved in the biogenesis of Fe/S clusters in Saccharomyces cerevisiae

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Rapid suppression of free radical formation by nerve growth factor involves the mitogen-activated protein kinase pathway

Dugan, L. L., Creedon, D. J., Johnson, E. M., & Holtzman, D. M. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.8.4086 · Cited by 128 · see citing works

Properties of bovine heart mitochondrial cytochrome b560.

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Fumarate Reductase Mutants of Escherichia coli That Lack Covalently Bound Flavin

Blaut, M., Whittaker, K. M., Valdovinos, A., Ackrell, B. A. C., Gunsalus, R. P., & Cecchini, G. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)80039-4 · Cited by 107 · see citing works

Effect of iron deficiency on succinate- and NADH-ubiquinone oxidoreductases in skeletal muscle mitochondria.

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Structure ofL-aspartate oxidase: implications for the succinate dehydrogenase/fumarate reductase oxidoreductase family

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Mitochondrial myopathy with succinate dehydrogenase and aconitase deficiency. Abnormalities of several iron-sulfur proteins.

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Thermodynamic and electron paramagnetic resonance characterization of flavin in succinate dehydrogenase.

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Identification of regulatory sequences in the gene for 5-aminolevulinate synthase from rat.

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Frataxin expression rescues mitochondrial dysfunctions in FRDA cells

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Frataxin deficiency enhances apoptosis in cells differentiating into neuroectoderm

Santos, M. M. (2001) · Human Molecular Genetics · doi:10.1093/hmg/10.18.1935 · Cited by 79 · see citing works

Kearns‐Sayre syndrome and complex II deficiency

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CCC1 Suppresses Mitochondrial Damage in the Yeast Model of Friedreich's Ataxia by Limiting Mitochondrial Iron Accumulation

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Phenotypic dichotomy in mitochondrial complex II genetic disorders

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Novel mutations in the SDHD gene in pedigrees with familial carotid body paraganglioma and sensorineural hearing loss

Badenhop, R. F., Cherian, S. M., Lord, R. S. A., Baysal, B. E., Taschner, P. E. M., & Schofield, P. R. (2001) · Genes Chromosomes and Cancer · doi:10.1002/gcc.1142 · Cited by 74 · see citing works

Selective pathological changes of the periaqueductal gray matter in Alzheimer's disease

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Effects of dietary iron deficiency on iron-sulfur proteins and bioenergetic functions of skeletal muscle mitochondria

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Biosynthesis and membrane binding of succinate dehydrogenase in Bacillus subtilis

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Cytochrome b in human complex II (succinate-ubiquinone oxidoreductase): cDNA cloning of the components in liver mitochondria and chromosome assignment of the genes for the large (SDHC) and small (SDHD) subunits to 1q21 and 11q23

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Promoter analysis of the human succinate dehydrogenase iron‐protein gene

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Brain-derived neurotrophic factor inhibits apoptosis and dopamine-induced free radical production in striatal neurons but does not prevent cell death

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Regulation of the 75-kDa Subunit of Mitochondrial Complex I by Iron

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The Quinone-binding Sites of the Saccharomyces cerevisiae Succinate-ubiquinone Oxidoreductase

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Transmembrane topology and axial ligands to hemes in the cytochrome b subunit of Bacillus subtilis succinate:menaquinone reductase

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Retention of Heme in Axial Ligand Mutants of Succinate-Ubiquinone Oxidoreductase (Complex II) from Escherichia coli

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Identification of Novel Saccharomyces cerevisiaeProteins with Nuclear Export Activity: Cell Cycle-Regulated Transcription Factor Ace2p Shows Cell Cycle-Independent Nucleocytoplasmic Shuttling

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An Escherichia coli Mutant Quinol:Fumarate Reductase Contains an EPR-detectable Semiquinone Stabilized at the Proximal Quinone-binding Site

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The investigation of respiratory chain disorders in heart using endomyocardial biopsies

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Multiple defects of the respiratory chain including complex II in a family with myopathy and encephalopathy

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Single Muscle Fibre Analyses in 2 Brothers with Succinate Dehydrogenase Deficiency

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Identification of Quinone-binding and Heme-ligating Residues of the Smallest Membrane-anchoring Subunit (QPs3) of Bovine Heart Mitochondrial Succinate:Ubiquinone Reductase

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Peroxynitrite and Mitochondrial Cytochromes

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An Investigation Into the Molecular Mechanisms and Genes Involved in Hypoxic Signalling Pathways in Neural Crest Derived Tumours

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