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Gene Review

CYTB  -  cytochrome b

Oryctolagus cuniculus

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High impact information on CYTB

  • Affinity-purified rabbit anti-neutrophil cytochrome b light or heavy chain antibodies were used to immunocytochemically and biochemically localize cytochrome b in neutrophils and eosinophils [1].
  • However, the system showed high O2(-)-generating activity of 31.8 mol/s/mol of cytochrome b558 (52.5% of the original O2(-)-generating activity of the solubilized membranes) in the presence of a nitro blue tetrazolium (NBT) reductase fraction that was separated from the cytochrome b fraction by heparin-Sepharose chromatography [2].
  • Furthermore, mRNA transcripts from these nuclear genes encoding mitochondrial proteins did not increase to the same extent as mRNA transcripts of mitochondrial genes such as cytochrome b, which increased 5.9-fold after 21 days of stimulation [3].
  • When cardiac muscle and Type I (red, oxidative) skeletal muscle were compared to Type II (white, glycolytic) skeletal muscle, mitochondrial DNA, mitochondrial ribosomal RNA, and cytochrome b mRNA, each increased in direct proportion to increases in oxidative capacity [4].
  • We demonstrated an upregulation of the U6 snRNA binding protein Lsm5, cytochrome b, an expressed sequence tag, and the actin-depolymerizing factor cofilin2 mRNA in collateral arteries 24h after femoral ligation [5].

Biological context of CYTB


Anatomical context of CYTB

  • Furthermore, when the phenotypic characteristics of Type II skeletal muscle were altered by electrical stimulation in vivo, mitochondrial DNA, mitochondrial rRNA, and cytochrome b mRNA also increased proportionately with increases in oxidative capacity [4].
  • Differential responses of mitochondrial respiration and cytochrome b redox states in the presence and absence of magnesium indicate that with magnesium present, heart mitochondria retain the ability to phosphorylate ADP after calcium uptake [9].

Associations of CYTB with chemical compounds


  1. Ultrastructural localization of cytochrome b in the membranes of resting and phagocytosing human granulocytes. Jesaitis, A.J., Buescher, E.S., Harrison, D., Quinn, M.T., Parkos, C.A., Livesey, S., Linner, J. J. Clin. Invest. (1990) [Pubmed]
  2. Reconstitution of superoxide-forming NADPH oxidase activity with cytochrome b558 purified from porcine neutrophils. Requirement of a membrane-bound flavin enzyme for reconstitution of activity. Miki, T., Yoshida, L.S., Kakinuma, K. J. Biol. Chem. (1992) [Pubmed]
  3. Adaptation of skeletal muscle to increased contractile activity. Expression nuclear genes encoding mitochondrial proteins. Williams, R.S., Garcia-Moll, M., Mellor, J., Salmons, S., Harlan, W. J. Biol. Chem. (1987) [Pubmed]
  4. Mitochondrial gene expression in mammalian striated muscle. Evidence that variation in gene dosage is the major regulatory event. Williams, R.S. J. Biol. Chem. (1986) [Pubmed]
  5. Identification of differentially expressed genes like cofilin2 in growing collateral arteries. Boengler, K., Pipp, F., Broich, K., Fernandez, B., Schaper, W., Deindl, E. Biochem. Biophys. Res. Commun. (2003) [Pubmed]
  6. Phylogeography of the European rabbit (Oryctolagus cuniculus) in the Iberian Peninsula inferred from RFLP analysis of the cytochrome b gene. Branco, M., Ferrand, N., Monnerot, M. Heredity (2000) [Pubmed]
  7. Cytochrome b phylogeny of North American hares and jackrabbits (Lepus, lagomorpha) and the effects of saturation in outgroup taxa. Halanych, K.M., Demboski, J.R., van Vuuren, B.J., Klein, D.R., Cook, J.A. Mol. Phylogenet. Evol. (1999) [Pubmed]
  8. Mitochondrial biogenesis in rabbit articular chondrocytes transferred to culture. Mignotte, F., Champagne, A.M., Froger-Gaillard, B., Benel, L., Gueride, M., Adolphe, M., Mounolou, J.C. Biol. Cell (1991) [Pubmed]
  9. Pathological accumulation of calcium by mitochondria: modulation by magnesium. Sordahl, L.A., Silver, B.B. Recent advances in studies on cardiac structure and metabolism. (1975) [Pubmed]
  10. Superoxide production by wound neutrophils. Evidence for increased activity of the NADPH oxidase. Paty, P.B., Graeff, R.W., Mathes, S.J., Hunt, T.K. Archives of surgery (Chicago, Ill. : 1960) (1990) [Pubmed]
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