Linked Life Data

18423224

Source:http://linkedlifedata.com/resource/pubmed/id/18423224

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
2008-4-21
pubmed:abstractText
The S-nitrosation of protein thiols is a redox-based posttranslational modification that modulates protein function and cell phenotype. Although the detection of S-nitrosated proteins is problematical because of the lability of S-nitrosothiols, an increasing range of proteins has been shown to undergo S-nitrosation with the improvement of molecular tools. This chapter describes the methodology used to identify potential targets of S-nitrosation in cultured primary human hepatocytes using proteomic approaches. This methodology is based on the biotin switch method, which labels S-nitrosated proteins with an affinity tag, allowing their selective detection and proteomic identification.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0076-6879
pubmed:author
pubmed:issnType
Print
pubmed:volume
440
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
273-81
pubmed:meshHeading
pubmed:year
2008
pubmed:articleTitle
Detection and proteomic identification of S-nitrosated proteins in human hepatocytes.
pubmed:affiliation
Liver Research Unit, Hospital Universitario Reina Sofía, Córdoba, Spain.
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't