| Predicate |
Object |
| assignee |
http://rdf.ncbi.nlm.nih.gov/pubchem/patentassignee/MD5_18d92c46f60af8af24e262b67381d7eb |
| classificationCPCAdditional |
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/G01N2500-02 |
| classificationCPCInventive |
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/G01N33-573
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C07K16-40 |
| classificationIPCInventive |
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/G01N33-567
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/A61K39-395 |
| filingDate |
2006-04-28-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| inventor |
http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_f8afa5be1b7b87c8d1cbe0edab6dbbf8
http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_fa20dd894b8d683766ef6bd82f8285a0 |
| publicationDate |
2006-11-02-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| publicationNumber |
US-2006246076-A1 |
| titleOfInvention |
Inducible nitric oxide synthase binds, S-nitrosylates, and activates cyclooxygenase-2 |
| abstract |
Cyclooxygenase (COX2) and inducible nitric oxide synthase (iNOS) are two major inflammatory mediators. Inducible NOS specifically binds to COX2 and S-nitrosylates it, enhancing COX2 catalytic activity. Selectively disrupting iNOS—COX2 binding prevents NO-mediated activation of COX2. The synergistic molecular interaction between two inflammatory systems permits assays for developing anti-inflammatory drugs. |
| isCitedBy |
http://rdf.ncbi.nlm.nih.gov/pubchem/patent/US-2007269442-A1 |
| priorityDate |
2005-04-28-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| type |
http://data.epo.org/linked-data/def/patent/Publication |