Linked Life Data

19381598

Source:http://linkedlifedata.com/resource/pubmed/id/19381598

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
2009-4-21
pubmed:abstractText
Recent studies indicate that protein glutathionylation is an important regulatory mechanism. The develop-ment of redox proteomics techniques to identify proteins undergoing glutathionylation has a key role in defining the importance of this post-translational modification, although the available methods are not yet comparable to those for the study of other modifications like phosphorylation. We describe here methods that have been successfully employed to identify in vitro glutathionylated proteins.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1064-3745
pubmed:author
pubmed:issnType
Print
pubmed:volume
519
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
397-415
pubmed:meshHeading
pubmed:year
2009
pubmed:articleTitle
Detection of protein glutathionylation.
pubmed:affiliation
Dipartimento di Scienze Farmacologiche, Universitá degli, studi di Milano, Milan, Italy.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't