http://rdf.ncbi.nlm.nih.gov/pubchem/patent/US-6124502-A

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assignee http://rdf.ncbi.nlm.nih.gov/pubchem/patentassignee/MD5_14effe3850d2129f863b969dac4f1db8
classificationCPCInventive http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C07D307-33
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C07C319-20
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C07C323-60
classificationIPCInventive http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C07C323-60
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C07C319-20
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C07D307-33
filingDate 1998-10-09-04:00^^<http://www.w3.org/2001/XMLSchema#date>
grantDate 2000-09-26-04:00^^<http://www.w3.org/2001/XMLSchema#date>
inventor http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_0692619d49ad8dc4f37dae1a3aca0aa8
publicationDate 2000-09-26-04:00^^<http://www.w3.org/2001/XMLSchema#date>
publicationNumber US-6124502-A
titleOfInvention Mercaptoketones and mercaptoalcohols and a process for their preparation
abstract This invention relates to matrix metalloproteinase (MMP) inhibiting compounds of the formula: where R1 is C1-C12 alkyl, straight or branched and optionally substituted by halogen, hydroxy, C1-C6 alkoxy, amino, carboxyl, C1-C6 alkoxycarbonyl, carboxamido, nitrile, mono- or di-(C1-C6)alkylamino, thio, C1-C6 alkylthio, aryl, -Oaryl or -OCH2aryl where aryl is optionally substituted with C1-C6 alkyl, C1-C6 alkoxy, carboxy, halogen, cyano, nitro, carboxamido, or hydroxy; and C1-C6 alkanesulfonyloxy. R2 is alpha -OH or beta -OH and R6 is H or R2 and R6 together are carbonyl; the chemical intermediates; and processes for the preparation of these compounds and the intermediates thereto. Matrix metalloproteinases (MMP) are a family of zinc-containing calcium dependent proteinases, including stromelysins, collagenases, and gelatinases. These MMP enzymes are capable of degrading the proteinaceous components of connective tissue and appear to be involved in tissue remodeling, i.e., wound healing and connective tissue turnover. Unexpectedly, the mercaptoalcohols with the S-configuration at the hydroxyl-bearing carbon have been found to be at least 4 times more potent than the analogous (R)-alcohols both in vitro and in vivo in inhibiting the MMP enzyme.
isCitedBy http://rdf.ncbi.nlm.nih.gov/pubchem/patent/EP-2181704-A2
priorityDate 1996-07-10-04:00^^<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: 518.