Predicate |
Object |
assignee |
http://rdf.ncbi.nlm.nih.gov/pubchem/patentassignee/MD5_abc36084eea610bbe304a980b8498a24 http://rdf.ncbi.nlm.nih.gov/pubchem/patentassignee/MD5_a7357fbc6e0d3759b0c0ae26907069bd http://rdf.ncbi.nlm.nih.gov/pubchem/patentassignee/MD5_389022a42b5ebb85b301574f3ca81d0d http://rdf.ncbi.nlm.nih.gov/pubchem/patentassignee/MD5_c26be1b02a4ef8fd8a6c9437cede8a27 http://rdf.ncbi.nlm.nih.gov/pubchem/patentassignee/MD5_b3127c0ebee3f865b211b019fac84286 http://rdf.ncbi.nlm.nih.gov/pubchem/patentassignee/MD5_dc62792656aa2e858252e97e5ffaca79 |
classificationCPCInventive |
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/A61P35-00 http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/A61K31-337 http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/G01N33-57423 http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/A61K31-47 http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/A61K31-4375 |
classificationIPCInventive |
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/A61P35-00 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/A61K31-337 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/A61K38-18 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/A61K31-47 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/A61K31-4375 |
filingDate |
2010-09-15-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
inventor |
http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_a2a3a66f27a54fa478d0c97380bf47ec http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_dd67b6de666968a07708141034b3bb58 http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_e51304adf1817306e5cf5de8743ab1c2 http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_a4b1d2aa71f5dcc21a9e1cb3cbdea47e |
publicationDate |
2011-03-24-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
publicationNumber |
WO-2011034919-A2 |
titleOfInvention |
Sh2 domain profiling to characterize tyrosine phosphorylation signaling in cancer |
abstract |
A phosphoproteomic method termed SH2 profiling to characterize phosphotyrosine (pTyr) signaling in lung cancer. This method provides quantitative values for the phosphorylated binding sites for Src Homology 2 (SH2) domains, which the cell uses to relay signals from tyrosine kinases. Lung cancer cell lines with known mutational status of the epidermal growth factor receptor (EGFR) and Ras were profiled. Changes in SH2 domain binding were characterized in response to the EGFR inhibitor erlotinib, and the SRC/multi-kinase inhibitor dasatinib. Cell lines grouped based on SH2 binding patterns. Clusters correlated with EGFR mutation status or MET activation. Binding of specific SH2 domains correlated with EGFR mutation and erlotinib sensitivity. SH2 domain profiling identifies subsets of lung cancer cells with distinct patterns of pTyr signaling and provides a powerful molecular diagnostic tool for classification and biomarker identification. This analysis has therapeutic importance for personalized use of tyrosine kinase inhibitors in cancer. |
isCitedBy |
http://rdf.ncbi.nlm.nih.gov/pubchem/patent/WO-2019241308-A1 http://rdf.ncbi.nlm.nih.gov/pubchem/patent/CN-111699001-A |
priorityDate |
2009-09-15-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
type |
http://data.epo.org/linked-data/def/patent/Publication |