The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
MeSH Review

Rhus

 
 
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.
 

Disease relevance of Rhus

 

High impact information on Rhus

  • The magnetic susceptibility of Rhus vernicifera laccase has been remeasured over the temperature range 5-260 K [3].
  • Interaction of Rhus laccase with dioxygen and its reduction intermediates [4].
  • With Rhus laccase, the new signal is shown to originate from one of the copper ions that are nondetectable in the resting enzyme, and evidence is presented for the signals in Polyporus laccase and cytochrome c oxidase also stemming from the metal pairs that are antiferromagnetically coupled in the oxidized enzymes [5].
  • The type 1 site of a plant laccase (Rhus vernicifera) is reduced moderately slowly by both Fe(II) and a bulky organic substrate, 1,4-hydroquinone (with 6 equiv of substrate, k(obs) = 0.029 and 0.013 s(-)(1), respectively) [6].
  • The effect of pH on Cu(I) and Cu(II) forms of the isolated soluble domain of the stellacyanin from Rhus vernicifera (SCu), the Japanese lacquer tree, has been studied by electronic and NMR spectroscopy and using direct electrochemical measurements [7].
 

Biological context of Rhus

 

Anatomical context of Rhus

  • The present study was carried out to investigate the antioxidative and antiapoptotic activities of 36 kDa RVS glycoprotein isolated from Rhus verniciflua Stokes fruits (RVS) in NIH/3T3 cells in vitro [11].
 

Associations of Rhus with chemical compounds

  • Spectroscopic and kinetic studies on the oxygen-centered radical formed during the four-electron reduction process of dioxygen by Rhus vernicifera laccase [13].
  • Fluoride effects on the activity of Rhus laccase and the catalytic mechanism under steady-state conditions [14].
  • Stability of Japanese-lacquer-tree (Rhus vernicifera) laccase to thermal and chemical denaturation: comparison with ascorbate oxidase [15].
  • Anaerobic reactions of Rhus vernicifera laccase and its type-2 copper-depleted derivatives with hexacyanoferrate(II) [16].
  • Stellacyanin from Rhus vernificera is a blue copper protein in which the metal is coordinated to a Cys, two His, and a Gln residue [17].
 

Gene context of Rhus

 

Analytical, diagnostic and therapeutic context of Rhus

References

  1. Putative skin-protective formulations in preventing and/or inhibiting experimentally-produced irritant and allergic contact dermatitis. Zhai, H., Willard, P., Maibach, H.I. Contact Derm. (1999) [Pubmed]
  2. Robustaflavone, a potential non-nucleoside anti-hepatitis B agent. Zembower, D.E., Lin, Y.M., Flavin, M.T., Chen, F.C., Korba, B.E. Antiviral Res. (1998) [Pubmed]
  3. Magnetic susceptibility studies of laccase and oxyhemocyanin. Dooley, D.M., Scott, R.A., Ellinghaus, J., Solomon, E.I., Gray, H.B. Proc. Natl. Acad. Sci. U.S.A. (1978) [Pubmed]
  4. Interaction of Rhus laccase with dioxygen and its reduction intermediates. Goldberg, M., Farver, O., Pecht, I. J. Biol. Chem. (1980) [Pubmed]
  5. A new copper(II) electron paramagnetic resonance signal in two laccases and in cytochrome c oxidase. Reinhammar, B., Malkin, R., Jensen, P., Karlsson, B., Andréasson, L.E., Aasa, R., Vänngård, T., Malmström, B.G. J. Biol. Chem. (1980) [Pubmed]
  6. Spectroscopy and reactivity of the type 1 copper site in Fet3p from Saccharomyces cerevisiae: correlation of structure with reactivity in the multicopper oxidases. Machonkin, T.E., Quintanar, L., Palmer, A.E., Hassett, R., Severance, S., Kosman, D.J., Solomon, E.I. J. Am. Chem. Soc. (2001) [Pubmed]
  7. Alkaline transition of phytocyanins: a comparison of stellacyanin and umecyanin. Dennison, C., Harrison, M.D., Lawler, A.T. Biochem. J. (2003) [Pubmed]
  8. Kinetics of the reduction of Rhus vernicifera laccase by ferrocyanide ion. Holwerda, R.A., Gray, H.B. J. Am. Chem. Soc. (1975) [Pubmed]
  9. Gallotannin biosynthesis: two new galloyltransferases from Rhus typhina leaves preferentially acylating hexa- and heptagalloylglucoses. Fröhlich, B., Niemetz, R., Gross, G.G. Planta (2002) [Pubmed]
  10. Selective antiproliferative and apoptotic effects of flavonoids purified from Rhus verniciflua Stokes on normal versus transformed hepatic cell lines. Son, Y.O., Lee, K.Y., Lee, J.C., Jang, H.S., Kim, J.G., Jeon, Y.M., Jang, Y.S. Toxicol. Lett. (2005) [Pubmed]
  11. 36 kDa glycoprotein isolated from Rhus verniciflua Stokes fruit has a protective activity to glucose/glucose oxidase-induced apoptosis in NIH/3T3 cells. Ko, J.H., Lee, S.J., Lim, K.T. Toxicology in vitro : an international journal published in association with BIBRA. (2005) [Pubmed]
  12. 36 kDa glycoprotein isolated from Rhus verniciflua stokes inhibits G/GO-induced mitochondrial apoptotic signal pathways in BNL CL.2 cells. Lee, S.J., Oh, P.S., Lim, K., Lim, K.T. Basic & clinical pharmacology & toxicology. (2005) [Pubmed]
  13. Spectroscopic and kinetic studies on the oxygen-centered radical formed during the four-electron reduction process of dioxygen by Rhus vernicifera laccase. Huang, H., Zoppellaro, G., Sakurai, T. J. Biol. Chem. (1999) [Pubmed]
  14. Fluoride effects on the activity of Rhus laccase and the catalytic mechanism under steady-state conditions. Koudelka, G.B., Ettinger, M.J. J. Biol. Chem. (1988) [Pubmed]
  15. Stability of Japanese-lacquer-tree (Rhus vernicifera) laccase to thermal and chemical denaturation: comparison with ascorbate oxidase. Agostinelli, E., Cervoni, L., Giartosio, A., Morpurgo, L. Biochem. J. (1995) [Pubmed]
  16. Anaerobic reactions of Rhus vernicifera laccase and its type-2 copper-depleted derivatives with hexacyanoferrate(II). Sakurai, T. Biochem. J. (1992) [Pubmed]
  17. Alkaline transition of Rhus vernicifera stellacyanin, an unusual blue copper protein. Fernández, C.O., Sannazzaro, A.I., Vila, A.J. Biochemistry (1997) [Pubmed]
  18. Pulsed electron paramagnetic resonance studies of types I and II coper of Rhus vernicifera laccase and porcine ceruloplasmin. Mondoví, B., Graziani, M.T., Mims, W.B., Oltzik, R., Peisach, J. Biochemistry (1977) [Pubmed]
  19. Stereochemistry of anion complexes of type 2 Cu(II) in Rhus vernicifera laccase. Analogy with superoxide dismutase and Cu(II) carbonic anhydrase. Desideri, A., Morpurgo, L., Rotilio, G., Mondovì, B. FEBS Lett. (1979) [Pubmed]
  20. Room temperature ESR spectra of Rhus vernicifera laccase and derivatives. Sakurai, T., Takahashi, J. Biochem. Biophys. Res. Commun. (1995) [Pubmed]
  21. Nitrite reactivity of the binuclear copper site in T2D Rhus laccase: preparation of half met-NO2- T2D laccase and its correlation to half met-NO2- hemocyanin and tyrosinase. Spira, D.J., Solomon, E.I. Biochem. Biophys. Res. Commun. (1983) [Pubmed]
  22. Titrations with ferrocyanide of japanese-lacquer-tree (Rhus vernicifera) laccase and of the type 2 copper-depleted enzyme. Interrelation of the copper sites. Morpurgo, L., Graziani, M.T., Desideri, A., Rotilio, G. Biochem. J. (1980) [Pubmed]
  23. A circular dichroism study of the reactions of Rhus laccase with dioxygen. Farver, O., Goldberg, M., Pecht, I. Eur. J. Biochem. (1980) [Pubmed]
  24. Development of a gas-phase oxygen biosensor using a blue copper-containing oxidase. Gardiol, A.E., Hernandez, R.J., Reinhammar, B., Harte, B.R. Enzyme Microb. Technol. (1996) [Pubmed]
  25. Effects of glycoprotein isolated from Rhus verniciflua stokes on TPA-induced apoptosis and production of cytokines in cultured mouse primary splenocytes. Lim, K.T., Lee, S.J., Heo, K.S., Lim, K. Toxicol. Lett. (2003) [Pubmed]
 
WikiGenes - Universities