Comparative Studies of the Indoleamine Dioxygenase-like Myoglobin from the Abalone Sulculus diversicolor
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Physiology,Biochemistry
Reference26 articles.
1. The ear-shell (Sulculus diversicolor aquatilis) myoglobin is composed of an unusual 39 kDa polypeptide chain;Suzuki;Experientia,1989
2. Convergent evolution. The gene structure of Sulculus 41 kDa myoglobin is homologous with that of human indoleamine dioxygenase;Suzuki;Biochim. Biophys. Acta,1996
3. A myoglobin evolved from indoleamine 2,3-dioxygenase;Suzuki;J. Mol. Biol.,1992
4. Gene structure of human indoleamine 2,3-dioxygenase;Kadoya;Biochem. Biophys. Res. Commun.,1992
5. Abalone myoglobins evolved from indoleamine dioxygenase. The cDNA-derived amino acid sequence of myoglobin from Nordotis madaka;Suzuki;J. Protein Chem.,1994
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1. Physiology: Energetics, metabolism, and gas exchange;Abalone: Biology, Ecology, Aquaculture and Fisheries;2023
2. Inhibition of indoleamine 2,3 dioxygenase activity by H2O2;Archives of Biochemistry and Biophysics;2006-06
3. Indoleamine 2,3-dioxygenase in cancer: targeting pathological immune tolerance with small-molecule inhibitors;Expert Opinion on Therapeutic Targets;2005-08
4. Do molluscs possess indoleamine 2,3-dioxygenase?;Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology;2005-03
5. Comparison of the sequences of Turboand Sulculus indoleamine dioxygenase-like myoglobin genes;Gene;2003-04
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