Patent application number | Description | Published |
20090118193 | PEGYLATED MUTATED CLOSTRIDIUM BOTULINUM TOXIN - The invention relates to a modified botulinum toxin comprising a natural heavy chain and a modified light chain, characterized in that the modification of the light chain resides in that it comprises (i) an extension of the chain on its N-terminus which has the structure ā(C) | 05-07-2009 |
20110189158 | CLOSTRIDIAL NEUROTOXINS WITH ALTERED PERSISTENCY - The invention relates to a polypeptide comprising:
| 08-04-2011 |
20120107362 | NEUROTOXINS EXHIBITING SHORTENED BIOLOGICAL ACTIVITY - The present invention relates to the pharmaceutical field. Specifically, it contemplates a polynucleotide encoding a neurotoxin polypeptide exhibiting a reduced duration of the biological effect in a subject, wherein the polypeptide comprises at least one degradation signal in the light chain of the neurotoxin polypeptide as well as vectors and host cells comprising the polynucleotide, polypeptides encoded thereby and antibodies specifically binding to the polypeptides. Moreover, the invention relates to medicaments comprising the polynucleotides and polypeptides, as well as specific therapeutic applications thereof. Furthermore, the present invention contemplates methods for the manufacture of the polypeptides and medicaments. | 05-03-2012 |
20130156747 | PEGylated Mutated Clostridium botulinum Toxin - The invention relates to a modified botulinum toxin comprising a natural heavy chain and a modified light chain, characterized in that the modification of the light chain resides in that it comprises (i) an extension of the chain on its N-terminus which has the structure ā(C) | 06-20-2013 |
20140045760 | NEUROTOXINS EXHIBITING SHORTENED BIOLOGICAL ACTIVITY - The present invention relates to the pharmaceutical field. Specifically, it contemplates a polynucleotide encoding a Neurotoxin polypeptide exhibiting a reduced duration of biological effect in a subject, wherein the polypeptide comprises at least one degradation signal in the light chain as well as vectors and host cells comprising the polynucleotide, polypeptides encoded thereby and antibodies specifically binding to the polypeptides. Moreover, the invention relates to medicaments comprising the polynucleotides and polypeptides as well as specific therapeutic applications thereof. Furthermore, the present invention contemplates methods for the manufacture of the polypeptides and medicaments. | 02-13-2014 |
20140170133 | ALTERATION OF PROTEOLYTIC CLEAVAGE OF BOTULINUM NEUROTOXINS - The present invention pertains to a polynucleotide encoding a modified neurotoxin polypeptide comprising a modified neurotoxin light chain and a heavy chain, said modified light chain having at least one modification conferring altered cleavage by calpain proteases. Further encompassed by the present invention are vectors and host cells comprising the polynucleotide of the invention as well as polypeptides encoded by the said polynucleotide. In addition, the invention relates to compositions comprising the polynucleotide, vector, host cell or polypeptide of the invention as a medicament. | 06-19-2014 |
20140187755 | CLOSTRIDIAL NEUROTOXINS WITH ALTERED PERSISTENCY - The invention relates to a polypeptide comprising:
| 07-03-2014 |
20150232828 | METHOD FOR THE MANUFACTURING OF RECOMBINANT PROTEINS HARBOURING AN N-TERMINAL LYSINE - This invention relates to a novel method for manufacturing and obtaining recombinant proteins, such as clostridial neurotoxins, harbouring an N-terminal lysine from precursor proteins. The method comprises the step of expressing a nucleic acid sequence encoding a precursor protein comprising an N-terminal motif, which can be recognised by an endoprotease specific for a lysine in Pā²1 position, and the step of cleaving the precursor protein with the endoprotease. The invention further relates to novel precursor proteins used in such methods, nucleic acid sequences encoding such precursor proteins and novel recombinant proteins, such as clostridial neurotoxins, harbouring an N-terminal lysine. | 08-20-2015 |