Stephanie A. Leavitt, Ph.D.

Affiliations: 
2006 Johns Hopkins University, Baltimore, MD 
Area:
General Biophysics
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"Stephanie Leavitt"
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Ernesto Freire grad student 2006 Johns Hopkins
 (Characterization of the allosteric mechanism of HIV-1 proteins gp120 and NEF.)
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Publications

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Link JO, Rhee MS, Tse WC, et al. (2020) Clinical targeting of HIV capsid protein with a long-acting small molecule. Nature
Velazquez-Campoy A, Leavitt SA, Freire E. (2015) Characterization of protein-protein interactions by isothermal titration calorimetry. Methods in Molecular Biology (Clifton, N.J.). 1278: 183-204
Hung M, Niedziela-Majka A, Jin D, et al. (2013) Large-Scale Functional Purification of Recombinant HIV-1 Capsid Plos One. 8
Callebaut C, Stray K, Tsai L, et al. (2011) In vitro characterization of GS-8374, a novel phosphonate-containing inhibitor of HIV-1 protease with a favorable resistance profile. Antimicrobial Agents and Chemotherapy. 55: 1366-76
Lansdon EB, Liu Q, Leavitt SA, et al. (2011) Structure and binding analysis of active site inhibitors targeting HIV-1 RNase H Acta Crystallographica Section a Foundations of Crystallography. 67: C303-C303
Fischer CJ, Khaki AR, Field C, et al. (2010) Nucleic Acid Translocation By Hepatitis C Virus Helicase NS3h Is Dependent on Sugar and Base Moieties Biophysical Journal. 98: 12a
Kirschberg TA, Balakrishnan M, Squires NH, et al. (2009) RNase H active site inhibitors of human immunodeficiency virus type 1 reverse transcriptase: design, biochemical activity, and structural information. Journal of Medicinal Chemistry. 52: 5781-4
Cihlar T, He GX, Liu X, et al. (2006) Suppression of HIV-1 protease inhibitor resistance by phosphonate-mediated solvent anchoring. Journal of Molecular Biology. 363: 635-47
Bacha U, Barrila J, Velazquez-Campoy A, et al. (2004) Identification of novel inhibitors of the SARS coronavirus main protease 3CLpro. Biochemistry. 43: 4906-12
Velazquez-Campoy A, Leavitt SA, Freire E. (2004) Characterization of protein-protein interactions by isothermal titration calorimetry. Methods in Molecular Biology (Clifton, N.J.). 261: 35-54
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