Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Keith S, Dillman"'
Autor:
Sébastien L, Degorce, Rana, Anjum, Andrew, Bloecher, Rodrigo J, Carbajo, Keith S, Dillman, Lisa, Drew, Christopher T, Halsall, Eva M, Lenz, Nicola A, Lindsay, Michele F, Mayo, Jennifer H, Pink, Graeme R, Robb, Alan, Rosen, James S, Scott, Yafeng, Xue
Publikováno v:
Journal of medicinal chemistry. 62(21)
In this article, we report the discovery of a series of 5-azaquinazolines as selective IRAK4 inhibitors. From modestly potent quinazoline
Autor:
James S, Scott, Sébastien L, Degorce, Rana, Anjum, Janet, Culshaw, Robert D M, Davies, Nichola L, Davies, Keith S, Dillman, James E, Dowling, Lisa, Drew, Andrew D, Ferguson, Sam D, Groombridge, Christopher T, Halsall, Julian A, Hudson, Scott, Lamont, Nicola A, Lindsay, Stacey K, Marden, Michele F, Mayo, J Elizabeth, Pease, David R, Perkins, Jennifer H, Pink, Graeme R, Robb, Alan, Rosen, Minhui, Shen, Claire, McWhirter, Dedong, Wu
Publikováno v:
Journal of medicinal chemistry. 60(24)
Herein we report the optimization of a series of pyrrolopyrimidine inhibitors of interleukin-1 receptor associated kinase 4 (IRAK4) using X-ray crystal structures and structure based design to identify and optimize our scaffold. Compound 28 demonstra
Autor:
Samuel P. Simons, Mahmoud N. Mansour, Peter K. LeMotte, Frank S. Menniti, Paul A. Aeed, Shenping Liu, Dennis E. Danley, Jose R. Perez, Keith S. Dillman
Publikováno v:
Proceedings of the National Academy of Sciences. 105:13309-13314
The phosphodiesterases (PDEs) are metal ion-dependent enzymes that regulate cellular signaling by metabolic inactivation of the ubiquitous second messengers cAMP and cGMP. In this role, the PDEs are involved in many biological and metabolic processes
Publikováno v:
The Journal of Neuroscience. 21:5079-5088
Chronic activity blockade increases synaptic levels of NMDA receptor immunoreactivity in hippocampal neurons. We show here that blockade-induced synaptic NMDA receptors are functional and mediate enhanced excitotoxicity in response to synaptically re
Autor:
Michael D. Forman, Keith S. Dillman, Frank S. Menniti, Kimberly F. Fennell, Jayvardhan Pandit
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 106(43)
We report the X-ray crystal structure of a phosphodiesterase (PDE) that includes both catalytic and regulatory domains. PDE2A (215–900) crystallized as a dimer in which each subunit had an extended organization of regulatory GAF-A and GAF-B and cat