Linked Life Data

18795236

Source:http://linkedlifedata.com/resource/pubmed/id/18795236

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-3
pubmed:dateCreated
2008-12-22
pubmed:abstractText
Integrins are cell surface heterodimers that bind adhesion molecules expressed on other cells or in the extracellular matrix. Integrin-mediated interactions are critical for T cell development in the thymus, migration of T cells in the periphery, and induction of T cell effector functions. In resting T cells, integrins are maintained in a low affinity state. Engagement of the T cell receptor or chemokine receptors increases integrin affinity, enabling integrins to bind their ligands and initiate a signaling cascade resulting in altered cell morphology and motility. Our laboratory is interested how adapter proteins, mediators of intracellular signal transduction, regulate both signals from the T cell receptor to integrins (inside-out signaling) and (outside-in) signals from integrins into the cell.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0257-277X
pubmed:author
pubmed:issnType
Print
pubmed:volume
42
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
132-44
pubmed:meshHeading
pubmed:year
2008
pubmed:articleTitle
Regulation of T cell integrin function by adapter proteins.
pubmed:affiliation
Leonard and Madlyn Abramson Family Cancer Research Institute, University of Pennsylvania School of Medicine, Philadelphia, PA, 19104, USA.
pubmed:publicationType
Journal Article, Review