123039-88-3Relevant articles and documents
A formyl peptide substituted with a conformationally constrained phenylalanine residue evokes a selective immune response in human neutrophils
Hayashi, Ryo,Miyazaki, Masaya,Osada, Satoshi,Kawasaki, Hiroshi,Fujita, Ichiro,Hamasaki, Yuhei,Kodama, Hiroaki
supporting information, p. 668 - 675 (2013/02/25)
Formyl-Met-Leu-Phe-OH (fMLP) binds to formyl peptide receptors, FPR1 and FPR2, and evokes migration and superoxide anion production in human neutrophils. To obtain a more effective and selective ligand, fMLP analogs in which the Phe residue was substitute
CATHEPSIN CYSTEINE PROTEASE INHIBITORS FOR THE TREATMENT OF VARIOUS DISEASES
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Page/Page column 32-33, (2011/01/12)
The present invention relates to compounds capable of inhibiting and/or decreasing the activity of one or more cathepsins, thereby treating and/or preventing various disease states associated with one or more cysteine proteases including, but not limited
Design and synthesis of dipeptidyl nitriles as potent, selective, and reversible inhibitors of cathepsin C
Guay, Daniel,Beaulieu, Christian,Jagadeeswar Reddy,Zamboni, Robert,Methot, Nathalie,Rubin, Joel,Ethier, Diane,David Percival
scheme or table, p. 5392 - 5396 (2010/05/02)
A series of dipeptide nitriles with a thienyl alanine in P2 were identified as potent and selective cathepsin C inhibitors. Incorporation of a substituted cyclopropyl moiety in P1 effectively protects these derivatives against hydrolase activity in whole blood.
