COR1/YBL045C Literature Guide Help

Other names published for COR1: QCR1, ubiquinol--cytochrome-c reductase subunit COR1, YBL045C

COR1 - Function/Process (31)

ReferenceOther Genes Addressed
Braun RJ, et al.  (2011) Neurotoxic 43-kDa TAR DNA-binding protein (TDP-43) triggers mitochondrion-dependent programmed cell death in yeast. J Biol Chem 286(22):19958-72
Rottenberg H, et al.  (2009) Membrane Potential Greatly Enhances Superoxide Generation by the Cytochrome bc1 Complex Reconstituted into Phospholipid Vesicles. J Biol Chem 284(29):19203-10
Wenz T, et al.  (2009) Role of phospholipids in respiratory cytochrome bc(1) complex catalysis and supercomplex formation. Biochim Biophys Acta 1787(6):609-16
Ulanovskaya OA, et al.  (2008) Synthesis enables identification of the cellular target of leucascandrolide A and neopeltolide. Nat Chem Biol 4(7):418-24
Wenz T, et al.  (2007) Mutational analysis of cytochrome b at the ubiquinol oxidation site of yeast complex III. J Biol Chem 282(6):3977-88
Covian R and Trumpower BL  (2006) Regulatory interactions between ubiquinol oxidation and ubiquinone reduction sites in the dimeric cytochrome bc1 complex. J Biol Chem 281(41):30925-32
Ding MG, et al.  (2006) Investigating the Qn site of the cytochrome bc1 complex in Saccharomyces cerevisiae with mutants resistant to ilicicolin H, a novel Qn site inhibitor. J Biol Chem 281(47):36036-43
Hagerman RA, et al.  (2006) Ubiquinone accumulates in the mitochondria of yeast mutated in the ubiquinone binding protein, Qcr8p. Biochem Biophys Res Commun 344(1):241-5
Solans A, et al.  (2006) Cytotoxicity of a mutant huntingtin fragment in yeast involves early alterations in mitochondrial OXPHOS complexes II and III. Hum Mol Genet 15(20):3063-81
Brasseur G, et al.  (2004) QO site deficiency can be compensated by extragenic mutations in the hinge region of the iron-sulfur protein in the bc1 complex of Saccharomyces cerevisiae. J Biol Chem 279(23):24203-11
Gutierrez-Cirlos EB, et al.  (2004) Inhibition of the yeast cytochrome bc1 complex by ilicicolin H, a novel inhibitor that acts at the Qn site of the bc1 complex. J Biol Chem 279(10):8708-14
Kessl JJ, et al.  (2003) Molecular basis for atovaquone binding to the cytochrome bc1 complex. J Biol Chem 278(33):31312-8
Muller FL, et al.  (2003) Architecture of the Qo site of the cytochrome bc1 complex probed by superoxide production. Biochemistry 42(21):6493-9
Palsdottir H, et al.  (2003) Structure of the yeast cytochrome bc1 complex with a hydroxyquinone anion Qo site inhibitor bound. J Biol Chem 278(33):31303-11
Dimmer KS, et al.  (2002) Genetic basis of mitochondrial function and morphology in Saccharomyces cerevisiae. Mol Biol Cell 13(3):847-53
Gutierrez-Cirlos EB and Trumpower BL  (2002) Inhibitory analogs of ubiquinol act anti-cooperatively on the Yeast cytochrome bc1 complex. Evidence for an alternating, half-of-the-sites mechanism of ubiquinol oxidation. J Biol Chem 277(2):1195-202
Gutierrez-Cirlos EB, et al.  (2002) Failure to insert the iron-sulfur cluster into the Rieske iron-sulfur protein impairs both center N and center P of the cytochrome bc1 complex. J Biol Chem 277(52):50703-9
Ghosh M, et al.  (2001) Substituting leucine for alanine-86 in the tether region of the iron-sulfur protein of the cytochrome bc1 complex affects the mobility of the [2Fe2S] domain. Biochemistry 40(2):327-35
Hsu AY, et al.  (2000) Genetic evidence for a multi-subunit complex in the O-methyltransferase steps of coenzyme Q biosynthesis. Biochim Biophys Acta 1484(2-3):287-97
Nett JH, et al.  (2000) Changes to the length of the flexible linker region of the Rieske protein impair the interaction of ubiquinol with the cytochrome bc1 complex. Eur J Biochem 267(18):5777-82
Obungu VH, et al.  (2000) Mutations in the tether region of the iron-sulfur protein affect the activity and assembly of the cytochrome bc(1) complex of yeast mitochondria. Biochim Biophys Acta 1457(1-2):36-44
Boumans H, et al.  (1998) The respiratory chain in yeast behaves as a single functional unit. J Biol Chem 273(9):4872-7
Santos-Ocana C, et al.  (1998) Coenzyme Q6 and iron reduction are responsible for the extracellular ascorbate stabilization at the plasma membrane of Saccharomyces cerevisiae. J Biol Chem 273(14):8099-105
Gencic S, et al.  (1991) Core I protein of bovine ubiquinol-cytochrome-c reductase; an additional member of the mitochondrial-protein-processing family. Cloning of bovine core I and core II cDNAs and primary structure of the proteins. Eur J Biochem 199(1):123-31
Crivellone MD, et al.  (1988) Assembly of the mitochondrial membrane system. Analysis of structural mutants of the yeast coenzyme QH2-cytochrome c reductase complex. J Biol Chem 263(28):14323-33
Zhu QS and Beattie DS  (1988) Direct interaction between yeast NADH-ubiquinone oxidoreductase, succinate-ubiquinone oxidoreductase, and ubiquinol-cytochrome c oxidoreductase in the reduction of exogenous quinones. J Biol Chem 263(1):193-9
di Rago JP and Colson AM  (1988) Molecular basis for resistance to antimycin and diuron, Q-cycle inhibitors acting at the Qi site in the mitochondrial ubiquinol-cytochrome c reductase in Saccharomyces cerevisiae. J Biol Chem 263(25):12564-70
Tzagoloff A, et al.  (1986) Assembly of the mitochondrial membrane system. Characterization of COR1, the structural gene for the 44-kilodalton core protein of yeast coenzyme QH2-cytochrome c reductase. J Biol Chem 261(36):17163-9
Beattie DS, et al.  (1984) The preferential binding of dicyclohexylcarbodiimide to cytochrome b and phospholipids in soluble complex III from yeast mitochondria. J Biol Chem 259(16):10526-32
Clejan L and Beattie DS  (1983) Dicyclohexylcarbodiimide blocks proton ejection and affects antimycin binding but not electron transport in complex III from yeast mitochondria. J Biol Chem 258(23):14271-5