Linked Life Data

18228476

Source:http://linkedlifedata.com/resource/pubmed/id/18228476

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
2008-1-29
pubmed:abstractText
Integrins are a family of heterodimeric alpha/beta transmembrane cell adhesion receptors that play important roles in the regulation of cell migration, proliferation, and survival. Integrins do not possess intrinsic catalytic activity, and signaling events are mediated by their lateral association with other cell surface receptors or clustering of their cytoplasmic domains with signaling proteins. Rapid activation of protein-tyrosine kinases is one of the first signaling events associated with integrin binding to the extracellular matrix protein fibronectin. The intracellular focal adhesion kinase (FAK) is recruited to sites of integrin clustering, and this unit describes the methods with which to analyze FAK phosphorylation, activity, and localization within fibroblasts. Additional methods on how to grow primary FAK+/+ and FAK-/- fibroblasts and measure integrin-stimulated cell motility are described as well as methods for evaluating the activity of the FAK-related kinase, Pyk2, which is expressed in FAK-/- cells.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
1934-2616
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
Chapter 14
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
Unit 14.7
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed:year
2006
pubmed:articleTitle
Analyzing FAK and Pyk2 in early integrin signaling events.
pubmed:affiliation
The Scripps Research Institute, La Jolla, California, USA.
pubmed:publicationType
Journal Article