Linked Life Data

17430106

Source:http://linkedlifedata.com/resource/pubmed/id/17430106

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2007-4-13
pubmed:abstractText
Tryptophan oxidation occurs via both extra-hepatic and hepatic pathways. Although these pathways share many enzymes, the first and rate-limiting step in each pathway is carried out by two different enzymes: Indoleamine-Pyrrole 2,3 Dioxygenase (INDO) and Tryptophan 2,3-Dioxygenase (TDO2). Over the course of the last forty years extensive and detailed research by many groups have led to an understanding of some of the important biologic functions of these pathways and their metabolic products. One of the tasks that now lie ahead is linking variations in these genes with variable human responses in different disease states. This short review will focus on known aspects of the INDO and TDO2 gene structure and variability. In addition to INDO and TDO2 a third related gene, the Indoleamine-Pyrrole 2,3 Dioxygenase-like 1 (INDOL1) gene will be discussed. INDOL1 is a gene of unknown function that lies adjacent to INDO on chromosome 8.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
1389-2002
pubmed:author
pubmed:issnType
Print
pubmed:volume
8
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
197-200
pubmed:meshHeading
pubmed:year
2007
pubmed:articleTitle
The human indoleamine 2,3-dioxygenase gene and related human genes.
pubmed:affiliation
Clinical Chief, Genetics Division, Brigham and Women's Hospital, Harvard Medical School, Boston, MA 02115, USA. mmurray@partners.org
pubmed:publicationType
Journal Article, Review