1027951-62-7Relevant academic research and scientific papers
A multidisciplinary approach to probing enthalpy-entropy compensation and the interfacial mobility model
Wilfong, Erin M.,Kogiso, Yuri,Muthukrishnan, Sivaramakrishnan,Kowatz, Thomas,Du, Yu,Bowie, Amber,Naismith, James H.,Hadad, Christopher M.,Toone, Eric J.,Gustafson, Terry L.
, p. 11515 - 11523 (2011)
In recent years, interfacial mobility has gained popularity as a model with which to rationalize both affinity in ligand binding and the often observed phenomenon of enthalpy-entropy compensation. While protein contraction and reduced mobility, as demonst
Discovery of CGS 27023A, a non, peptidic, potent, and orally active stromelysin inhibitor that blocks cartilage degradation in rabbits
MacPherson, Lawrence J.,Bayburt, Erol K.,Capparelli, Michael P.,Carroll, Brian J.,Goldstein, Robert,Justice, Michael R.,Zhu, Lijuan,Hu, Shou-Ih,Melton, Richard A.,Fryer, Lynn,Goldberg, Ron L.,Doughty, John R.,Spirito, Salvatore,Blancuzzi, Vincent,Wilson, Doug,O'Byrne, Elizabeth M.,Ganu, Vishwas,Parker, David T.
, p. 2525 - 2532 (2007/10/03)
Structure-activity relationships of a lead hydroxamic acid inhibitor of recombinant human stromelysin were systematically defined by taking advantage of a concise synthesis that allowed diverse functionality to be explored at each position in a template. An ex vivo rat model and an in vivo rabbit model of stromelysin-induced cartilage degradation were used to further optimize these analogs for oral activity and duration of action. The culmination of these modifications resulted in CGS 27023A, a potent, orally active stromelysin inhibitor that blocks the erosion of cartilage matrix.
