Hinoprotein glukoza dehidrogenaza (Serbian Wikipedia)

Analysis of information sources in references of the Wikipedia article "Hinoprotein glukoza dehidrogenaza" in Serbian language version.

refsWebsite
Global rank Serbian rank
4th place
8th place

nih.gov

ncbi.nlm.nih.gov

  • Yamada, M., Sumi, K., Matsushita, K., Adachi, O. and Yamada, Y. (1993). „Topological analysis of quinoprotein glucose-dehydrogenase in Escherichia coli and its ubiquinone-binding site”. J. Biol. Chem. 268: 12812—12817. PMID 8509415. 
  • Dewanti, A.R. & Duine, J.A. (1998). „Reconstitution of membrane-integrated quinoprotein glucose dehydrogenase apoenzyme with PQQ and the holoenzyme's mechanism of action”. Biochemistry. 37: 6810—6818. PMID 9578566. 
  • Duine, J.A., Frank, J. and Van Zeeland, J.K. (1979). „Glucose dehydrogenase from Acinetobacter calcoaceticus: a 'quinoprotein'”. FEBS Lett. 108: 443—446. PMID 520586. 
  • Ameyama, M., Matsushita, K., Ohno, Y., Shinagawa, E. and Adachi, O. (1981). „Existence of a novel prosthetic group, PQQ, in membrane-bound, electron transport chain-linked, primary dehydrogenases of oxidative bacteria”. FEBS Lett. 130: 179—183. PMID 6793395. 
  • Cozier, G.E. & Anthony, C. (1995). „Structure of the quinoprotein glucose dehydrogenase of Escherichia coli modelled on that of methanol dehydrogenase from Methylobacterium extorquens”. Biochem. J. 312: 679—685. PMID 8554505. 
  • Cozier, G.E., Salleh, R.A. and Anthony, C. (1999). „Characterization of the membrane quinoprotein glucose dehydrogenase from Escherichia coli and characterization of a site-directed mutant in which histidine-262 has been changed to tyrosine”. Biochem. J. 340: 639—647. PMID 10359647. 
  • Elias, M.D., Tanaka, M., Sakai, M., Toyama, H., Matsushita, K., Adachi, O. and Yamada, M. (2001). „C-terminal periplasmic domain of Escherichia coli quinoprotein glucose dehydrogenase transfers electrons to ubiquinone”. J. Biol. Chem. 276: 48356—48361. PMID 11604400. 
  • James, P.L. & Anthony, C. (2003). „The metal ion in the active site of the membrane glucose dehydrogenase of Escherichia coli”. Biochim. Biophys. Acta. 1647: 200—205. PMID 12686133. 
  • Elias, M.D., Nakamura, S., Migita, C.T., Miyoshi, H., Toyama, H., Matsushita, K., Adachi, O. and Yamada, M. (2004). „Occurrence of a bound ubiquinone and its function in Escherichia coli membrane-bound quinoprotein glucose dehydrogenase”. J. Biol. Chem. 279: 3078—3083. PMID 14612441. 
  • Mustafa, G., Ishikawa, Y., Kobayashi, K., Migita, C.T., Elias, M.D., Nakamura, S., Tagawa, S. and Yamada, M. (2008). „Amino acid residues interacting with both the bound quinone and coenzyme, pyrroloquinoline quinone, in Escherichia coli membrane-bound glucose dehydrogenase”. J. Biol. Chem. 283: 22215—22221. PMID 18550551.