http://rdf.ncbi.nlm.nih.gov/pubchem/patent/CA-2528427-A1

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classificationCPCInventive http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/A61P43-00
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12N9-16
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classificationIPCInventive http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N15-55
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/A61K38-46
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http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N9-16
filingDate 2004-06-10-04:00^^<http://www.w3.org/2001/XMLSchema#date>
inventor http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_f94eb24fce1c7a7cdb947a3d34e7e5fd
http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_96a15810f5d670c26f65f9758688ce26
http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_646aa9dc2d0e37ca5c1ef2de343a7c07
publicationDate 2004-12-23-04:00^^<http://www.w3.org/2001/XMLSchema#date>
publicationNumber CA-2528427-A1
titleOfInvention Modified human acid sphingomyelinase having increased activity, and methods for making the same
abstract Deficiencies in the enzymatic activity of acid sphingomyelinase (ASM) result in Niemann-Pick disease. A variety of modifications which eliminate the activity of the free thiol on the C-terminal cysteine residue of ASM all result in substantially increased specific activity of the enzyme. Methods used to alter the activity of this residue include site-directed mutagenesis to delete or alter the residue, enzymatic degradation of the ASM to remove the residue, copper-promoted dimerization of ASM (via the terminal cysteine residues) and chemical modification of the free thiol group on this residue.
priorityDate 2003-06-12-04:00^^<http://www.w3.org/2001/XMLSchema#date>
type http://data.epo.org/linked-data/def/patent/Publication

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Total number of triples: 493.