| Predicate |
Object |
| assignee |
http://rdf.ncbi.nlm.nih.gov/pubchem/patentassignee/MD5_f21c1009c60308a64b8e7dc0bb989632 |
| classificationCPCAdditional |
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/A61K48-00
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C07K2319-31
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/A61K38-00
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12Y304-21022
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12Y304-21021
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C07K2319-50 |
| classificationCPCInventive |
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C07K14-745
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C07K14-755
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C07K14-76
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C07K14-765
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12N9-6437
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12N9-6424
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12N9-6443
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/A61P7-00
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/A61P7-04
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12N9-6472 |
| classificationIPCInventive |
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N9-64
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C07K14-765 |
| filingDate |
2017-11-09-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| inventor |
http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_41b2a917644e7647d953222d7c8c6b57
http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_d5f3186aabda571cc88e21228823e8d1
http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_e53bd74d8d74d721c11a8ba5a27949c9 |
| publicationDate |
2018-05-03-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| publicationNumber |
US-2018119128-A1 |
| titleOfInvention |
Proteolytically cleavable fusion proteins with high molar specific activity |
| abstract |
The invention relates to therapeutic fusion proteins in which a coagulation factor is fused to a half-life enhancing polypeptide, and in which both are connected by a linker peptide that is proteolytically cleavable. The cleavage of such linkers liberates the coagulation factor from activity-compromising steric hindrance caused by the half-life enhancing polypeptide and thereby allows the generation of fusion proteins may show relatively high molar specific activity when tested in coagulation-related assays. Furthermore, the fact that the linker is cleavable can enhance the rates of inactivation and/or elimination after proteolytic cleavage of the peptide linker compared to the rates measured for corresponding therapeutic fusion proteins linked by the non-cleavable linker having the amino acid sequence GGGGGGV. |
| isCitedBy |
http://rdf.ncbi.nlm.nih.gov/pubchem/patent/WO-2020232305-A1
http://rdf.ncbi.nlm.nih.gov/pubchem/patent/US-11739132-B2
http://rdf.ncbi.nlm.nih.gov/pubchem/patent/US-11535658-B2
http://rdf.ncbi.nlm.nih.gov/pubchem/patent/US-11352403-B2 |
| priorityDate |
2006-06-14-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| type |
http://data.epo.org/linked-data/def/patent/Publication |