pf-3644022 and Shock--Septic

pf-3644022 has been researched along with Shock--Septic* in 1 studies

Other Studies

1 other study(ies) available for pf-3644022 and Shock--Septic

Article	Year
Mitogen-activated protein kinase-activated protein kinase 2 (MAPKAP-K2) as an antiinflammatory target: discovery and in vivo activity of selective pyrazolo[1,5-a]pyrimidine inhibitors using a focused library and structure-based optimization approach. Journal of medicinal chemistry, 2012, Aug-09, Volume: 55, Issue:15 A novel class of mitogen-activated protein kinase-activated protein kinase 2 (MAPKAP-K2) inhibitors was discovered through screening a kinase-focused library. A homology model of MAPKAP-K2 was generated and used to guide the initial SAR studies and to rationalize the observed selectivity over CDK2. An X-ray crystal structure of a compound from the active series bound to crystalline MAPKAP-K2 confirmed the predicted binding mode. This has enabled the discovery of a series of pyrazolo[1,5-a]pyrimidine derivatives showing good in vitro cellular potency as anti-TNF-α agents and in vivo efficacy in a mouse model of endotoxin shock. Topics: Animals; Anti-Inflammatory Agents, Non-Steroidal; Cell Line; Crystallography, X-Ray; HSP27 Heat-Shock Proteins; Humans; Intracellular Signaling Peptides and Proteins; Lipopolysaccharides; Male; Mice; Mice, Inbred C57BL; Models, Molecular; Phosphorylation; Protein Conformation; Protein Serine-Threonine Kinases; Pyrazoles; Pyrimidines; Shock, Septic; Small Molecule Libraries; Stereoisomerism; Structure-Activity Relationship; Tumor Necrosis Factor-alpha	2012

Article

Year

Mitogen-activated protein kinase-activated protein kinase 2 (MAPKAP-K2) as an antiinflammatory target: discovery and in vivo activity of selective pyrazolo[1,5-a]pyrimidine inhibitors using a focused library and structure-based optimization approach.

Journal of medicinal chemistry, 2012, Aug-09, Volume: 55, Issue:15

A novel class of mitogen-activated protein kinase-activated protein kinase 2 (MAPKAP-K2) inhibitors was discovered through screening a kinase-focused library. A homology model of MAPKAP-K2 was generated and used to guide the initial SAR studies and to rationalize the observed selectivity over CDK2. An X-ray crystal structure of a compound from the active series bound to crystalline MAPKAP-K2 confirmed the predicted binding mode. This has enabled the discovery of a series of pyrazolo[1,5-a]pyrimidine derivatives showing good in vitro cellular potency as anti-TNF-α agents and in vivo efficacy in a mouse model of endotoxin shock.

Topics: Animals; Anti-Inflammatory Agents, Non-Steroidal; Cell Line; Crystallography, X-Ray; HSP27 Heat-Shock Proteins; Humans; Intracellular Signaling Peptides and Proteins; Lipopolysaccharides; Male; Mice; Mice, Inbred C57BL; Models, Molecular; Phosphorylation; Protein Conformation; Protein Serine-Threonine Kinases; Pyrazoles; Pyrimidines; Shock, Septic; Small Molecule Libraries; Stereoisomerism; Structure-Activity Relationship; Tumor Necrosis Factor-alpha

2012