Thomas H. Scheuermann, Ph.D.

2004 Yale University, New Haven, CT 
General Biophysics, Biochemistry
"Thomas Scheuermann"
Mean distance: 13271


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Elias Lolis grad student 2004 Yale
 (Structural studies of thiopurine methyltransferase from Pseudomonas syringae, a bacterial orthologue of a polymorphic, drug -metabolizing enzyme.)
Kevin H. Gardner post-doc 2004-2010 UT Southwestern
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Yin J, Babaoglu K, Brautigam CA, et al. (2016) Structure and ligand-binding mechanism of the human OX1 and OX2 orexin receptors. Nature Structural & Molecular Biology
Scheuermann TH, Padrick SB, Gardner KH, et al. (2015) On the acquisition and analysis of microscale thermophoresis data. Analytical Biochemistry
Scheuermann TH, Stroud D, Sleet CE, et al. (2015) Isoform-Selective and Stereoselective Inhibition of Hypoxia Inducible Factor-2. Journal of Medicinal Chemistry
Guo Y, Scheuermann TH, Partch CL, et al. (2015) Coiled-coil coactivators play a structural role mediating interactions in hypoxia-inducible factor heterodimerization. The Journal of Biological Chemistry. 290: 7707-21
Scheuermann TH, Li Q, Ma HW, et al. (2013) Allosteric inhibition of hypoxia inducible factor-2 with small molecules. Nature Chemical Biology. 9: 271-6
Rogers JL, Bayeh L, Scheuermann TH, et al. (2013) Development of inhibitors of the PAS-B domain of the HIF-2α transcription factor. Journal of Medicinal Chemistry. 56: 1739-47
Key J, Scheuermann TH, Anderson PC, et al. (2009) Principles of ligand binding within a completely buried cavity in HIF2α PAS-B Journal of the American Chemical Society. 131: 17647-17654
Scheuermann TH, Tomchick DR, Machius M, et al. (2009) Artificial ligand binding within the HIF2α PAS-B domain of the HIF2 transcription factor Proceedings of the National Academy of Sciences of the United States of America. 106: 450-455
Scheuermann TH, Yang J, Zhang L, et al. (2007) Hypoxia-Inducible Factors Per/ARNT/Sim Domains: Structure and Function Methods in Enzymology. 435: 1,3-24
Scheuermann TH, Lolis E, Hodsdon ME. (2003) Tertiary structure of thiopurine methyltransferase from Pseudomonas syringae, a bacterial orthologue of a polymorphic, drug-metabolizing enzyme. Journal of Molecular Biology. 333: 573-85
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