Indolamin 2,3-dioksigenaza (Serbo-Croatian Wikipedia)

Analysis of information sources in references of the Wikipedia article "Indolamin 2,3-dioksigenaza" in Serbo-Croatian language version.

refsWebsite
Global rank Serbo-Croatian rank
4th place
3rd place

nih.gov

ncbi.nlm.nih.gov

  • Yamamoto, S. and Hayaishi, O. (1967). „Tryptophan pyrrolase of rabbit intestine. D- and L-tryptophan-cleaving enzyme or enzymes”. J. Biol. Chem. 242: 5260-5266. PMID 6065097. 
  • Yasui, H., Takai, K., Yoshida, R. and Hayaishi, O. (1986). „Interferon enhances tryptophan metabolism by inducing pulmonary indoleamine 2,3-dioxygenase: its possible occurrence in cancer patients”. Proc. Natl. Acad. Sci. USA 83: 6622-6626. PMID 2428037. 
  • Takikawa, O., Yoshida, R., Kido, R. and Hayaishi, O. (1986). „Tryptophan degradation in mice initiated by indoleamine 2,3-dioxygenase”. J. Biol. Chem. 261: 3648-3653. PMID 2419335. 
  • Hirata, F., Ohnishi, T. and Hayaishi, O. (1977). „Indoleamine 2,3-dioxygenase. Characterization and properties of enzyme. O2- complex”. J. Biol. Chem. 252: 4637-4642. PMID 194886. 
  • Dang, Y., Dale, W.E. and Brown, O.R. (2000). „Comparative effects of oxygen on indoleamine 2,3-dioxygenase and tryptophan 2,3-dioxygenase of the kynurenine pathway”. Free Radic. Biol. Med. 28: 615-624. PMID 10719243. 
  • Littlejohn, T.K., Takikawa, O., Truscott, R.J. and Walker, M.J. (2003). „Asp274 and His346 are essential for heme binding and catalytic function of human indoleamine 2,3-dioxygenase”. J. Biol. Chem. 278: 29525-29531. PMID 12766158. 
  • Thomas, S.R. and Stocker, R. (1999). „Redox reactions related to indoleamine 2,3-dioxygenase and tryptophan metabolism along the kynurenine pathway”. Redox Rep. 4: 199-220. PMID 10731095. 
  • Sono, M. (1990). „Spectroscopic and equilibrium studies of ligand and organic substrate binding to indolamine 2,3-dioxygenase”. Biochemistry 29: 1451-1460. PMID 2334706.