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

File
Publisher
Florida Atlantic University
Date Issued
2013
Description
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.
Note

Includes bibliography.

Language
Type
Extent
187 p.
Identifier
FA00004256
Rights

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.

Additional Information
Includes bibliography.
Dissertation (Ph.D.)--Florida Atlantic University, 2013.
Date Backup
2013
Date Text
2013
Date Issued (EDTF)
2013
Extension


FAU
FAU

IID
FA00004256
Person Preferred Name

Sempertegui Plaza, Tito S.

author

Graduate College
Physical Description

application/pdf
187 p.
Title Plain
Physiological and non-physiological regulation of indoleamine-2,3-dioxygenase
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.
http://rightsstatements.org/vocab/InC/1.0/
Origin Information

2013
Florida Atlantic University
Physical Location
Florida Atlantic University Digital Library
Sub Location
Boca Raton, Fla.
Title
Physiological and non-physiological regulation of indoleamine-2,3-dioxygenase
Other Title Info

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