human pro-mmp13 (Millipore)
Structured Review
Human Pro Mmp13, supplied by Millipore, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/pro-mmp13/mmp+9+antibody/us08536313-152-24-30
Average 90 stars, based on 1 article reviews
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Recombinant:Article Title: α-Biphenylsulfonylamino 2-methylpropyl phosphonates: Enantioselective synthesis and selective inhibition of MMPs Article Snippet: (R)-a-Biphenylsulfonylamino 2-methylpropyl phosphonates attain nM potency against several MMPs and are the most effective inhibitors based on phosphonate as zinc binding group.. Since their preparation by direct N-acylation of expensive, enantiopure, a-aminophosphonic acids proceeds in low yields, we devised and evaluated a stereoselective and straightforward method of synthesis that avoids the unfavourable step of N-acylation.. The key intermediate (R)-4-bromophenylsulfonylamino 2-methylpropyl phosphonate 9 was obtained by highly stereoselective addition of dibenzylphosphite to the enantiopure (S)-N-isobutylidene-pbromobenzenesulfinamide 3, followed by oxidation with m-CPBA. Article Title: Novel 1-hydroxypiperazine-2,6-diones as new leads in the inhibition of metalloproteinases. Article Snippet: New compounds containing a novel zinc-binding group (1-hydroxypiperazine-2,6-dione, HPD) have been identified as effective inhibitors of matrix metalloproteinases (MMPs), with activities in the nanomolar concentration range.. That moiety seemed to bind the catalytic zinc ion of MMPs, revealing itself as a new potential substitute for the hydroxamate group in the next generation of metalloproteinase inhibitors.. The X-ray crystal structure of 1b elucidated its 3D conformation and supramolecular packing in solid state. Article Title: Design, synthesis, biological evaluation, and NMR studies of a new series of arylsulfones as selective and potent matrix metalloproteinase-12 inhibitors. Article Snippet: Elisa Nuti, Laura Panelli, Francesca Casalini, Stanislava I. Avramova, Elisabetta Orlandini, Salvatore Santamaria, SusannaNencetti, TizianoTuccinardi, AdrianoMartinelli, Giovanni Cercignani,NicolaD’Amelio, AlessandroMaiocchi, ) Fulvio Uggeri, ) and Armando Rossello* Dipartimento di Scienze Farmaceutiche, Universit a di Pisa, via Bonanno 6, 56126 Pisa, Italy, Dipartimento di Biologia, Unit a di Biochimica, Universit a di Pisa, Via San Zeno 51, 56127 Pisa, Italy, Bracco Imaging;CRB Trieste Area Science Park, edificio Q S.S. 14 Km 163.5, 34012 Basovizza Trieste, Italy, and Centro Ricerche Bracco, Bracco Imaging SpA, Via Ribes 5, 10010 Colleretto Giacosa (TO), Italy Transfection:Article Title: α-Biphenylsulfonylamino 2-methylpropyl phosphonates: Enantioselective synthesis and selective inhibition of MMPs Article Snippet: (R)-a-Biphenylsulfonylamino 2-methylpropyl phosphonates attain nM potency against several MMPs and are the most effective inhibitors based on phosphonate as zinc binding group.. Since their preparation by direct N-acylation of expensive, enantiopure, a-aminophosphonic acids proceeds in low yields, we devised and evaluated a stereoselective and straightforward method of synthesis that avoids the unfavourable step of N-acylation.. The key intermediate (R)-4-bromophenylsulfonylamino 2-methylpropyl phosphonate 9 was obtained by highly stereoselective addition of dibenzylphosphite to the enantiopure (S)-N-isobutylidene-pbromobenzenesulfinamide 3, followed by oxidation with m-CPBA. Article Title: Novel 1-hydroxypiperazine-2,6-diones as new leads in the inhibition of metalloproteinases. Article Snippet: New compounds containing a novel zinc-binding group (1-hydroxypiperazine-2,6-dione, HPD) have been identified as effective inhibitors of matrix metalloproteinases (MMPs), with activities in the nanomolar concentration range.. That moiety seemed to bind the catalytic zinc ion of MMPs, revealing itself as a new potential substitute for the hydroxamate group in the next generation of metalloproteinase inhibitors.. The X-ray crystal structure of 1b elucidated its 3D conformation and supramolecular packing in solid state. Article Title: Design, synthesis, biological evaluation, and NMR studies of a new series of arylsulfones as selective and potent matrix metalloproteinase-12 inhibitors. Article Snippet: Elisa Nuti, Laura Panelli, Francesca Casalini, Stanislava I. Avramova, Elisabetta Orlandini, Salvatore Santamaria, SusannaNencetti, TizianoTuccinardi, AdrianoMartinelli, Giovanni Cercignani,NicolaD’Amelio, AlessandroMaiocchi, ) Fulvio Uggeri, ) and Armando Rossello* Dipartimento di Scienze Farmaceutiche, Universit a di Pisa, via Bonanno 6, 56126 Pisa, Italy, Dipartimento di Biologia, Unit a di Biochimica, Universit a di Pisa, Via San Zeno 51, 56127 Pisa, Italy, Bracco Imaging;CRB Trieste Area Science Park, edificio Q S.S. 14 Km 163.5, 34012 Basovizza Trieste, Italy, and Centro Ricerche Bracco, Bracco Imaging SpA, Via Ribes 5, 10010 Colleretto Giacosa (TO), Italy |

