Linked Life Data

18429318

Source:http://linkedlifedata.com/resource/pubmed/id/18429318

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
2008-4-22
pubmed:abstractText
Identification of protease substrates is essential to identify and understand the functional consequences of normal and dysregulated proteolysis in disease on the proteome. Isobaric tags for relative and absolute quantification (iTRAQ) can be used to identify novel protease substrates in the cellular context. An amine-targeted iTRAQ tag labels tryptic peptides generated from the proteins and protease cleavage products of secreted proteins, as well as protein domains shed from the cell membrane or pericellular matrix of protease-transfected cells that have accumulated in conditioned medium; a second iTRAQ tag is used for control cells. MS/MS fragmentation enables sequencing of the pooled pairs of differently labeled but identical peptides and generates a low mass signature ion peak unique for each label. This signature ion peak identifies the peptides originating from the protease-transfected or control cells; comparison of the peak areas enables relative quantitation of the peptide between the samples.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
1934-3663
pubmed:author
pubmed:copyrightInfo
(c) 2007 by John Wiley & Sons, Inc.
pubmed:issnType
Electronic
pubmed:volume
Chapter 21
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
Unit 21.18
pubmed:meshHeading
pubmed:year
2007
pubmed:articleTitle
Proteomic identification of cellular protease substrates using isobaric tags for relative and absolute quantification (iTRAQ).
pubmed:affiliation
University of British Columbia, Vancouver, British Columbia, Canada.
pubmed:publicationType
Journal Article