Linked Life Data

15724974

Source:http://linkedlifedata.com/resource/pubmed/id/15724974

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
8
pubmed:dateCreated
2005-2-23
pubmed:abstractText
The cysteine-hydrolase dimethylargininase-1 (DDAH-1) is an important regulator of NO production in mammalian tissue for which the availability of an inhibitor for clinics and research would be most appreciated. While studying the effect of the endogenously occurring S-nitroso-l-homocysteine on DDAH-1, an unusual N-thiosulfoximide modification was identified in the active site of the enzyme. Thus, S-nitroso-l-homocysteine in combination with the mechanism proposed herein offers a basis for the rational design of DDAH inhibitors.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0002-7863
pubmed:author
pubmed:issnType
Print
pubmed:day
2
pubmed:volume
127
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2372-3
pubmed:dateRevised
2008-1-17
pubmed:meshHeading
pubmed:year
2005
pubmed:articleTitle
Searching for DDAH inhibitors: S-nitroso-L-homocysteine is a chemical lead.
pubmed:affiliation
Institute of Biochemistry, University of Zürich, Winterthurerstrasse 190, CH-8057 Zürich, Switzerland. knippy@bioc.unizh.ch
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't