Christopher E. Heise, Ph.D.

Affiliations: 
2002 University of Virginia, Charlottesville, VA 
Area:
receptor pharmacology
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"Christopher Heise"
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Parents

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Kevin R. Lynch grad student 2002 UVA
 (Analysis of LPA receptors by informed medicinal chemistry.)
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Publications

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Lee W, Crawford JJ, Aliagas I, et al. (2016) Synthesis and evaluation of a series of 4-azaindole-containing p21-activated kinase-1 inhibitors. Bioorganic & Medicinal Chemistry Letters
Rudolph J, Murray LJ, Ndubaku CO, et al. (2016) Chemically diverse Group I p21-activated kinase (PAK) inhibitors impart acute cardiovascular toxicity with a narrow therapeutic window. Journal of Medicinal Chemistry
Ndubaku CO, Crawford JJ, Drobnick J, et al. (2015) Design of Selective PAK1 Inhibitor G-5555: Improving Properties by Employing an Unorthodox Low-pK a Polar Moiety. Acs Medicinal Chemistry Letters. 6: 1241-6
Burdick DJ, Wang S, Heise C, et al. (2015) Fragment-based discovery of potent ERK2 pyrrolopyrazine inhibitors. Bioorganic & Medicinal Chemistry Letters
Rudolph J, Aliagas I, Crawford JJ, et al. (2015) Leveraging the Pre-DFG Residue Thr-406 To Obtain High Kinase Selectivity in an Aminopyrazole-Type PAK1 Inhibitor Series. Acs Medicinal Chemistry Letters. 6: 711-5
Crawford JJ, Lee W, Aliagas I, et al. (2015) Structure-Guided Design of Group I Selective p21-Activated Kinase Inhibitors. Journal of Medicinal Chemistry. 58: 5121-36
Staben ST, Feng JA, Lyle K, et al. (2014) Back pocket flexibility provides group II p21-activated kinase (PAK) selectivity for type I 1/2 kinase inhibitors. Journal of Medicinal Chemistry. 57: 1033-45
Lauffer BE, Mintzer R, Fong R, et al. (2013) Histone deacetylase (HDAC) inhibitor kinetic rate constants correlate with cellular histone acetylation but not transcription and cell viability. The Journal of Biological Chemistry. 288: 26926-43
Heise CE, Murray J, Augustyn KE, et al. (2012) Mechanistic and structural understanding of uncompetitive inhibitors of caspase-6. Plos One. 7: e50864
Ramaswamy S, Yen I, Sideris S, et al. (2010) A plate-based assay to measure cellular ERK substrate phosphorylation: utility for drug discovery of the MAPK-signaling cascade. Assay and Drug Development Technologies. 8: 497-503
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