You are here

Physiological and non-physiological regulation of indoleamine-2,3-dioxygenase

Download pdf | Full Screen View

Date Issued:
2013
Summary:
The heme enzyme indoleamine 2,3-dioxygenase (IDO) catalyses L-tryptophan (LTrp) oxidation along the kynurenine pathway and is a key regulator of the mammalian immune system. It’s unknown if the enzyme is under redox control and the use of new potent inhibitors of IDO represents a novel therapeutic approach.
Title: Physiological and non-physiological regulation of indoleamine-2,3-dioxygenase.
138 views
56 downloads
Name(s): Sempertegui Plaza, Tito S., author
Terentis, Andrew C., Thesis advisor
Charles E. Schmidt College of Science
Department of Chemistry and Biochemistry
Florida Atlantic University, Degree Grantor
Type of Resource: text
Genre: Electronic Thesis Or Dissertation
Date Issued: 2013
Publisher: Florida Atlantic University
Physical Form: application/pdf
Extent: 187 p.
Language(s): English
Summary: The heme enzyme indoleamine 2,3-dioxygenase (IDO) catalyses L-tryptophan (LTrp) oxidation along the kynurenine pathway and is a key regulator of the mammalian immune system. It’s unknown if the enzyme is under redox control and the use of new potent inhibitors of IDO represents a novel therapeutic approach.
Identifier: FA00004256 (IID)
Note(s): Includes bibliography.
Dissertation (Ph.D.)--Florida Atlantic University, 2013.
Held by: Florida Atlantic University Digital Library
Sublocation: Boca Raton, Fla.
Persistent Link to This Record: http://purl.flvc.org/fau/fd/FA00004256
Use and Reproduction: Copyright © is held by the author, with permission granted to Florida Atlantic University to digitize, archive and distribute this item for non-profit research and educational purposes. Any reuse of this item in excess of fair use or other copyright exemptions requires permission of the copyright holder.
Use and Reproduction: http://rightsstatements.org/vocab/InC/1.0/
Host Institution: FAU