Reversal of tumoral immune resistance by inhibition of tryptophan 2,3-dioxygenase. Proceedings of the National Academy of Sciences of the United States of America, February 2012, s. 2497–2502. DOI: 10.1073/pnas.1113873109. PMID 22308364.
Über den Mechanismus der Kynureninbildung aus Tryptophan. Z. Physiol. Chem., 1936, s. 237–244. DOI: 10.1515/bchm2.1936.243.6.237.
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Expression of rat liver tryptophan 2,3-dioxygenase in Escherichia coli: structural and functional characterization of the purified enzyme. Archives of Biochemistry and Biophysics, September 1996, s. 96–102. DOI: 10.1006/abbi.1996.0368. PMID 8806758.
Human tryptophan dioxygenase: a comparison to indoleamine 2,3-dioxygenase. Journal of the American Chemical Society, December 2007, s. 15690–15701. DOI: 10.1021/ja076186k. PMID 18027945.
A kinetic, spectroscopic, and redox study of human tryptophan 2,3-dioxygenase. Biochemistry, April 2008, s. 4752–4760. DOI: 10.1021/bi702393b. PMID 18370401.
Structure and reaction mechanism in the heme dioxygenases. Biochemistry, April 2011, s. 2717–2724. DOI: 10.1021/bi101732n. PMID 21361337.
Molecular insights into substrate recognition and catalysis by tryptophan 2,3-dioxygenase. Proceedings of the National Academy of Sciences of the United States of America, January 2007, s. 473–478. DOI: 10.1073/pnas.0610007104. PMID 17197414.
The second enzyme in pyrrolnitrin biosynthetic pathway is related to the heme-dependent dioxygenase superfamily. Biochemistry, October 2007, s. 12393–12404. DOI: 10.1021/bi7012189. PMID 17924666.
Crystal structure and mechanism of tryptophan 2,3-dioxygenase, a heme enzyme involved in tryptophan catabolism and in quinolinate biosynthesis. Biochemistry, January 2007, s. 145–155. DOI: 10.1021/bi0620095. PMID 17198384.
Exploring the mechanism of tryptophan 2,3-dioxygenase. Biochemical Society Transactions, December 2008, s. 1120–1123. DOI: 10.1042/bst0361120. PMID 19021508.
Molecular basis for catalysis and substrate-mediated cellular stabilization of human tryptophan 2,3-dioxygenase. Scientific Reports, October 2016, s. 35169. DOI: 10.1038/srep35169. PMID 27762317.
Evidence for a ferryl intermediate in a heme-based dioxygenase. Proceedings of the National Academy of Sciences of the United States of America, October 2009, s. 17371–17376. DOI: 10.1073/pnas.0906655106. PMID 19805032.
Identification of the Fe-O2 and the Fe=O heme species for indoleamine 2,3-dioxygenase during catalytic turnover. Chem Lett, 2010, s. 36–37. Dostupné online. DOI: 10.1246/cl.2010.36.
The mechanism of formation of N-formylkynurenine by heme dioxygenases. Journal of the American Chemical Society, October 2011, s. 16251–16257. DOI: 10.1021/ja207066z. PMID 21892828.
Tryptophan 2,3-dioxygenase is a key modulator of physiological neurogenesis and anxiety-related behavior in mice. Molecular Brain, March 2009, s. 8. DOI: 10.1186/1756-6606-2-8. PMID 19323847.
nih.gov
ncbi.nlm.nih.gov
Reversal of tumoral immune resistance by inhibition of tryptophan 2,3-dioxygenase. Proceedings of the National Academy of Sciences of the United States of America, February 2012, s. 2497–2502. DOI: 10.1073/pnas.1113873109. PMID 22308364.
Expression of rat liver tryptophan 2,3-dioxygenase in Escherichia coli: structural and functional characterization of the purified enzyme. Archives of Biochemistry and Biophysics, September 1996, s. 96–102. DOI: 10.1006/abbi.1996.0368. PMID 8806758.
Human tryptophan dioxygenase: a comparison to indoleamine 2,3-dioxygenase. Journal of the American Chemical Society, December 2007, s. 15690–15701. DOI: 10.1021/ja076186k. PMID 18027945.
A kinetic, spectroscopic, and redox study of human tryptophan 2,3-dioxygenase. Biochemistry, April 2008, s. 4752–4760. DOI: 10.1021/bi702393b. PMID 18370401.
Structure and reaction mechanism in the heme dioxygenases. Biochemistry, April 2011, s. 2717–2724. DOI: 10.1021/bi101732n. PMID 21361337.
Molecular insights into substrate recognition and catalysis by tryptophan 2,3-dioxygenase. Proceedings of the National Academy of Sciences of the United States of America, January 2007, s. 473–478. DOI: 10.1073/pnas.0610007104. PMID 17197414.
The second enzyme in pyrrolnitrin biosynthetic pathway is related to the heme-dependent dioxygenase superfamily. Biochemistry, October 2007, s. 12393–12404. DOI: 10.1021/bi7012189. PMID 17924666.
Crystal structure and mechanism of tryptophan 2,3-dioxygenase, a heme enzyme involved in tryptophan catabolism and in quinolinate biosynthesis. Biochemistry, January 2007, s. 145–155. DOI: 10.1021/bi0620095. PMID 17198384.
Exploring the mechanism of tryptophan 2,3-dioxygenase. Biochemical Society Transactions, December 2008, s. 1120–1123. DOI: 10.1042/bst0361120. PMID 19021508.
Molecular basis for catalysis and substrate-mediated cellular stabilization of human tryptophan 2,3-dioxygenase. Scientific Reports, October 2016, s. 35169. DOI: 10.1038/srep35169. PMID 27762317.
Evidence for a ferryl intermediate in a heme-based dioxygenase. Proceedings of the National Academy of Sciences of the United States of America, October 2009, s. 17371–17376. DOI: 10.1073/pnas.0906655106. PMID 19805032.
The mechanism of formation of N-formylkynurenine by heme dioxygenases. Journal of the American Chemical Society, October 2011, s. 16251–16257. DOI: 10.1021/ja207066z. PMID 21892828.
Tryptophan 2,3-dioxygenase is a key modulator of physiological neurogenesis and anxiety-related behavior in mice. Molecular Brain, March 2009, s. 8. DOI: 10.1186/1756-6606-2-8. PMID 19323847.
researchgate.net
Identification of the Fe-O2 and the Fe=O heme species for indoleamine 2,3-dioxygenase during catalytic turnover. Chem Lett, 2010, s. 36–37. Dostupné online. DOI: 10.1246/cl.2010.36.
