1452574-00-3Relevant articles and documents
CDP PROTEIN SECRETION INHIBITORS
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Paragraph 0077-0078, (2019/10/19)
rovided herein are compounds that inhibit protein secretion, e.g., via inhibition of Sec61. Also provided are compositions of the inhibitor compounds, and methods of using these inhibitors. The compounds disclosed herein can be used, e.g., for the treatme
Matrix metalloproteinase inhibitors: A structure-activity study
Levy, Daniel E.,Lapierre, France,Liang, Weisheng,Ye, Wenqing,Lange, Christopher W.,Li, Xiaoyuan,Grobelny, Damian,Casabonne, Marie,Tyrrell, David,Holme, Kevin,Nadzan, Alex,Galardy, Richard E.
, p. 199 - 223 (2007/10/03)
Modifications around the dipeptide-mimetic core of a hydroxamic acid based matrix metalloproteinase inhibitor were studied. These variations incorporated a variety of natural, unnatural, and synthetic amino acids inaddition to modifications of the P1' and P3' substituents. The results of this study indicate the following structural requirements: (2) Potent inhibitorsmust possess string zinc-binding functionalities. (3) The potential importance of the hydrophobic group at position R3 as illustratedby itsability to impart greater relative potency against stromelysin when larger hydrophobic groups are used. (4) Requirements surrounding the nature of the amino acid appear to be more restrictive for stromelysin than for neutrophil collagenase, 72 kDa gelatinase, and 92 kDa gelatinase. These requirements may involve planar fused-ring aryl systems and possibly hydrogen-bonding capabilities.
Tetrapeptide CCK-A agonists: Effect of backbone N-methylations on in vitro and in vivo CCK activity
Holladay,Kopecka,Miller,Bednarz,Nikkel,Bianchi,Witte,Shiosaki,Chun Wel Lin,Asin,Nadzan
, p. 630 - 635 (2007/10/02)
N-Methylation of backbone amide bonds was conducted on a tetrapeptide that had been identified previously (Shiosaki, K.; et al. J. Med. Chem. 1991, 34, 2387-2842) as a potent and selective CCK-A agonist. N(α)-Methylation at the position corresponding to A
