Fenilalaninska amonijak-lijaza (Serbo-Croatian Wikipedia)

Analysis of information sources in references of the Wikipedia article "Fenilalaninska amonijak-lijaza" in Serbo-Croatian language version.

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  • Koukol, J. and Conn, E.E. (1961). „The metabolism of aromatic compounds in higher plants. IV. Purification and properties of the phenylalanine deaminase of Hordeum vulgare. J. Biol. Chem. 236: 2692-2698. PMID 14458851. 
  • Louie, G.V., Bowman, M.E., Moffitt, M.C., Baiga, T.J., Moore, B.S. and Noel, J.P. (2006). „Structural determinants and modulation of substrate specificity in phenylalanine-tyrosine ammonia-lyases”. Chem. Biol. 13: 1327-1338. PMID 17185228. 
  • Calabrese, J.C., Jordan, D.B., Boodhoo, A., Sariaslani, S. and Vannelli, T. (2004). „Crystal structure of phenylalanine ammonia lyase: multiple helix dipoles implicated in catalysis”. Biochemistry 43: 11403-11416. PMID 15350127. 
  • Ritter, H. and Schulz, G.E. (2004). „Structural basis for the entrance into the phenylpropanoid metabolism catalyzed by phenylalanine ammonia-lyase”. Plant Cell 16: 3426-3436. PMID 15548745. 
  • Watts, K.T., Mijts, B.N., Lee, P.C., Manning, A.J. and Schmidt-Dannert, C. (2006). „Discovery of a substrate selectivity switch in tyrosine ammonia-lyase, a member of the aromatic amino acid lyase family”. Chem. Biol. 13: 1317-1326. PMID 17185227. 
  • Appert, C., Logemann, E., Hahlbrock, K., Schmid, J. and Amrhein, N. (1994). „Structural and catalytic properties of the four phenylalanine ammonia-lyase isoenzymes from parsley (Petroselinum crispum Nym.)”. Eur. J. Biochem. 225: 491-499. PMID 7925471. 
  • Cochrane, F.C., Davin, L.B. and Lewis, N.G. (2004). „The Arabidopsis phenylalanine ammonia lyase gene family: kinetic characterization of the four PAL isoforms”. Phytochemistry 65: 1557-1564. PMID 15276452. 
  • Schwede, T.F., Rétey, J. and Schulz, G.E. (1999). „Crystal structure of histidine ammonia-lyase revealing a novel polypeptide modification as the catalytic electrophile”. Biochemistry 38: 5355-5361. PMID 10220322.