Agency
National Institute of Health (NIH)
Institute
National Institute of Environmental Health Sciences (NIEHS)
Type
Research Project (R01)
Project #
7R01ES003654-08
Application #
3251199
Study Section
Physical Biochemistry Study Section (PB)
Project Start
1991-04-01
Project End
1995-08-31
Budget Start
1991-04-01
Budget End
1991-08-31
Support Year
8
Fiscal Year
1990
Total Cost
Indirect Cost
Name
Institute for Cancer Research
Department
Type
DUNS #
872612445
City
Philadelphia
State
PA
Country
United States
Zip Code
19111
Jaffe, Eileen K (2016) The Remarkable Character of Porphobilinogen Synthase. Acc Chem Res 49:2509-2517
Ramirez, Ursula D; Nikonova, Anna S; Liu, Hanqing et al. (2015) Compounds identified by virtual docking to a tetrameric EGFR extracellular domain can modulate Grb2 internalization. BMC Cancer 15:436
Lentz, Christian S; Halls, Victoria S; Hannam, Jeffrey S et al. (2014) wALADin benzimidazoles differentially modulate the function of porphobilinogen synthase orthologs. J Med Chem 57:2498-510
Lawrence, Sarah H; Selwood, Trevor; Jaffe, Eileen K (2013) Environmental contaminants perturb fragile protein assemblies and inhibit normal protein function. Curr Chem Biol 7:196-206
Jaffe, Eileen K (2013) Impact of quaternary structure dynamics on allosteric drug discovery. Curr Top Med Chem 13:55-63
Jaffe, Eileen K; Lawrence, Sarah H (2012) Allostery and the dynamic oligomerization of porphobilinogen synthase. Arch Biochem Biophys 519:144-53
Selwood, Trevor; Jaffe, Eileen K (2012) Dynamic dissociating homo-oligomers and the control of protein function. Arch Biochem Biophys 519:131-43
Jaffe, Eileen K; Lawrence, Sarah H (2012) The morpheein model of allostery: evaluating proteins as potential morpheeins. Methods Mol Biol 796:217-31
Jaffe, Eileen K; Shanmugam, Dhanasekaran; Gardberg, Anna et al. (2011) Crystal structure of Toxoplasma gondii porphobilinogen synthase: insights on octameric structure and porphobilinogen formation. J Biol Chem 286:15298-307
Lawrence, Sarah H; Selwood, Trevor; Jaffe, Eileen K (2011) Diverse clinical compounds alter the quaternary structure and inhibit the activity of an essential enzyme. ChemMedChem 6:1067-73

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