PubMed:10209036
Annnotations
PMID_GLOBAL
{"project":"PMID_GLOBAL","denotations":[{"id":"T1","span":{"begin":0,"end":120},"obj":"Sentence"},{"id":"T2","span":{"begin":121,"end":334},"obj":"Sentence"},{"id":"T3","span":{"begin":335,"end":443},"obj":"Sentence"},{"id":"T4","span":{"begin":444,"end":528},"obj":"Sentence"},{"id":"T5","span":{"begin":529,"end":728},"obj":"Sentence"},{"id":"T6","span":{"begin":729,"end":1000},"obj":"Sentence"},{"id":"T7","span":{"begin":1001,"end":1217},"obj":"Sentence"}],"text":"SHP2-interacting transmembrane adaptor protein (SIT), a novel disulfide-linked dimer regulating human T cell activation.\nT lymphocytes express several low molecular weight transmembrane adaptor proteins that recruit src homology (SH)2 domain-containing intracellular molecules to the cell membrane via tyrosine-based signaling motifs. We describe here a novel molecule of this group termed SIT (SHP2 interacting transmembrane adaptor protein). SIT is a disulfide-linked homodimeric glycoprotein that is expressed in lymphocytes. After tyrosine phosphorylation by src and possibly syk protein tyrosine kinases SIT recruits the SH2 domain-containing tyrosine phosphatase SHP2 via an immunoreceptor tyrosine-based inhibition motif. Overexpression of SIT in Jurkat cells downmodulates T cell receptor- and phytohemagglutinin-mediated activation of the nuclear factor of activated T cells (NF-AT) by interfering with signaling processes that are probably located upstream of activation of phospholipase C. However, binding of SHP2 to SIT is not required for inhibition of NF-AT induction, suggesting that SIT not only regulates NF-AT activity but also controls NF-AT unrelated pathways of T cell activation involving SHP2."}
jnlpba-st-training
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pubmed-sentences-benchmark
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genia-medco-coref
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GENIAcorpus
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bionlp-st-gro-2013-training
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transmembrane adaptor protein (SIT), a novel disulfide-linked dimer regulating human T cell activation.\nT lymphocytes express several low molecular weight transmembrane adaptor proteins that recruit src homology (SH)2 domain-containing intracellular molecules to the cell membrane via tyrosine-based signaling motifs. We describe here a novel molecule of this group termed SIT (SHP2 interacting transmembrane adaptor protein). SIT is a disulfide-linked homodimeric glycoprotein that is expressed in lymphocytes. After tyrosine phosphorylation by src and possibly syk protein tyrosine kinases SIT recruits the SH2 domain-containing tyrosine phosphatase SHP2 via an immunoreceptor tyrosine-based inhibition motif. Overexpression of SIT in Jurkat cells downmodulates T cell receptor- and phytohemagglutinin-mediated activation of the nuclear factor of activated T cells (NF-AT) by interfering with signaling processes that are probably located upstream of activation of phospholipase C. However, binding of SHP2 to SIT is not required for inhibition of NF-AT induction, suggesting that SIT not only regulates NF-AT activity but also controls NF-AT unrelated pathways of T cell activation involving SHP2."}