http://rdf.ncbi.nlm.nih.gov/pubchem/patent/AU-2010248206-A1

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classificationCPCAdditional http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C07C2603-18
classificationCPCInventive http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C07C391-00
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classificationIPCInventive http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/A61K31-198
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filingDate 2010-05-12-04:00^^<http://www.w3.org/2001/XMLSchema#date>
inventor http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_cdb844f8ca0540b692c94a5895df0627
http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_ee35bfeb8a9d1c8e7445e9f1be83bea9
publicationDate 2011-12-01-04:00^^<http://www.w3.org/2001/XMLSchema#date>
publicationNumber AU-2010248206-A1
titleOfInvention Lysine compounds and their use in site- and chemoselective modification of peptides and proteins
abstract The present invention concerns new thiolysine and selenolysine compounds that can be used as building blocks for peptides and proteins, providing ligation handles for site-and chemoselective modification of said peptides and proteins. In particular, the invention provides. In particular, the invention provides (the use of) the compounds 5-thiolysine (also referred to as δ-thiolysine); 4-thiolysine (also referred to as γ-thiolysine); 5-selenolysine (also referred to as δ-selenolysine) and 4- selenolysine (also referred to as γ-selenolysine). The positioning of the thiol or selenol group at the respective carbon atom allows for a very efficient intramolecular transfer reaction to take place after conjugation with a selected ligand, and the thiol or selenol group may subsequently be removed using reported procedures, thereby restoring the native lysine structure, or be used as an additional conjugation handle. The methodology is fast and gives well-defined material.
priorityDate 2009-05-15-04:00^^<http://www.w3.org/2001/XMLSchema#date>
type http://data.epo.org/linked-data/def/patent/Publication

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http://rdf.ncbi.nlm.nih.gov/pubchem/protein/ACCC0HJR0
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http://rdf.ncbi.nlm.nih.gov/pubchem/protein/ACCC0HKB7
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Total number of triples: 622.