Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
1998-8-5
pubmed:abstractText
NK cells are regulated by opposing signals from receptors that activate and inhibit effector function. While positive stimulation may be initiated by an array of costimulatory receptors, specificity is provided by inhibitory signals transduced by receptors for MHC class I. Three distinct receptor families, Ly49, CD94/NKG2, and KIR, are involved in NK cell recognition of polymorphic MHC class I molecules. A common pathway of inhibitory signaling is provided by ITIM sequences in the cytoplasmic domains of these otherwise structurally diverse receptors. Upon ligand binding and activation, the inhibitory NK cell receptors become tyrosine phosphorylated and recruit tyrosine phosphatases, SHP-1 and possibly SHP-2, resulting in inhibition of NK cell-mediated cytotoxicity and cytokine expression. Recent studies suggest these inhibitory NK cell receptors are members of a larger superfamily containing ITIM sequences, the inhibitory receptor superfamily (IRS).
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD, http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Ly, http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Surface, http://linkedlifedata.com/resource/pubmed/chemical/GEM protein, human, http://linkedlifedata.com/resource/pubmed/chemical/GTP-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Immediate-Early Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Intracellular Signaling Peptides..., http://linkedlifedata.com/resource/pubmed/chemical/KLRD1 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Lectins, C-Type, http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins, http://linkedlifedata.com/resource/pubmed/chemical/Monomeric GTP-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/NK Cell Lectin-Like Receptor..., http://linkedlifedata.com/resource/pubmed/chemical/PTPN11 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/PTPN6 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Protein Tyrosine Phosphatase..., http://linkedlifedata.com/resource/pubmed/chemical/Protein Tyrosine Phosphatase..., http://linkedlifedata.com/resource/pubmed/chemical/Protein Tyrosine Phosphatases, http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Immunologic, http://linkedlifedata.com/resource/pubmed/chemical/Receptors, NK Cell Lectin-Like, http://linkedlifedata.com/resource/pubmed/chemical/beta 2-Microglobulin
pubmed:status
MEDLINE
pubmed:issn
0732-0582
pubmed:author
pubmed:issnType
Print
pubmed:volume
16
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
359-93
pubmed:dateRevised
2009-3-24
pubmed:meshHeading
pubmed-meshheading:9597134-Animals, pubmed-meshheading:9597134-Antigens, CD, pubmed-meshheading:9597134-Antigens, Ly, pubmed-meshheading:9597134-Antigens, Surface, pubmed-meshheading:9597134-Cytotoxicity, Immunologic, pubmed-meshheading:9597134-GTP-Binding Proteins, pubmed-meshheading:9597134-Humans, pubmed-meshheading:9597134-Immediate-Early Proteins, pubmed-meshheading:9597134-Intracellular Signaling Peptides and Proteins, pubmed-meshheading:9597134-Killer Cells, Natural, pubmed-meshheading:9597134-Lectins, C-Type, pubmed-meshheading:9597134-Membrane Glycoproteins, pubmed-meshheading:9597134-Monomeric GTP-Binding Proteins, pubmed-meshheading:9597134-NK Cell Lectin-Like Receptor Subfamily D, pubmed-meshheading:9597134-Protein Tyrosine Phosphatase, Non-Receptor Type 11, pubmed-meshheading:9597134-Protein Tyrosine Phosphatase, Non-Receptor Type 6, pubmed-meshheading:9597134-Protein Tyrosine Phosphatases, pubmed-meshheading:9597134-Receptors, Immunologic, pubmed-meshheading:9597134-Receptors, NK Cell Lectin-Like, pubmed-meshheading:9597134-Signal Transduction, pubmed-meshheading:9597134-beta 2-Microglobulin
pubmed:year
1998
pubmed:articleTitle
NK cell receptors.
pubmed:affiliation
DNAX Research Institute of Molecular and Cellular Biology, Palo Alto, California 94304, USA. lanier@dnax.org
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't