Ohio University

Jennifer V. Hines

Jennifer Hines Profile Picture
Biochemistry Research Facility

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Ph.D., University of Michigan


The focus of our research group is RNA drug discovery. We employ an interdisciplinary approach to developing RNA-targeted medicinal agents that could potentially treat diseases such as AIDS, multidrug resistant bacterial infections, and cancer. RNA plays a critical role in viral replication, bacterial regulation and cancer biogenesis. By targeting key RNA-mediated regulatory processes for these diseases we hope to ultimately develop novel medicinal agents. Through a combination of chemical, molecular, and structural biology studies we are determining the structure-function relationships of medicinally relevant RNA targets and the structure-activity relationships of small molecule ligands that bind the RNA. We utilize a variety of approaches ranging from biophysical (fluorescence, UV, NMR) to bioinformatics, computational and molecular biology techniques. Our goal is to gain an in-depth understanding of the factors that govern molecular recognition of RNA by small molecules and to use this knowledge in the development of novel medicinal agents.

Selected Publications

Liu, J.; Zeng, C.; Hogan, V.; Zhou, S.; Monwar, M. M.; Hines, J. V. Identification of spermidine binding site in T-box riboswitch antiterminator RNA. Chem. Biol. Drug Design 2016, 87, 182-189.

Zhou, S.; Anupam, R.; Hines, J. V. Fluorescence anisotropy: Analysis of tRNA binding to the T box riboswitch. Methods in Mol. Biol. 2015, 1240, 143-152.

Zeng, C.; Zhou, S.; Bergmeier, S. C.; Hines, J. V. Factors that influence T box riboswitch efficacy and tRNA affinity. Bioorg. Med. Chem. 2015, 23, 5702-5708.

Liu, J.; Zeng, C.; Zhou, S.; Means, J. A.; Hines, J. V. Fluorescence assays for monitoring RNA-ligand interactions and riboswitch-targeted drug discovery screening. Methods Enzymol. 2015, 550, 363-383.

Anupam, R.; Zhou, S.; Hines, J. V. Electrophoretic mobility shift assay of RNA-RNA complexes. Methods in Mol. Biol. 2015, 1240, 153-164.

Zhou, S.; Acquaah-Harrison, G.; Bergmeier, S. C.; Hines, J. V. Anisotropy studies of tRNA - T box antiterminator RNA complex in the presence of 1,4-disubstituted 1,2,3-triazoles. Bioorg. Med. Chem. Lett. 2011, 21, 7059-7063.

Zhou, S.; Acquaah-Harrison, G.; Jack, K. D.; Bergmeier, S. C.; Hines, J. V. Ligand-induced changes in T box antiterminator RNA stability. Chem. Biol. Drug Design 2011, 79, 202-208.

Zhou, S.; Means, J. A.; Acquaah-Harrison, G.; Bergmeier, S. C.; Hines, J. V. Characterization of a 1,4-disubstituted 1,2,3-triazole binding to T box antiterminator RNA Bioorg. Med. Chem. 2011, 20, 1298-1302.

Orac, C. M.; Zhou, S.; Means, J. A.; Boehme, D.; Bergmeier, S. C.; Hines, J. V. Synthesis and stereospecificity of 4,5-disubstituted oxazolidinone ligands binding to T-box riboswitch RNA. J. Med. Chem. 2011, 54, 6786-6795.

Maciagiewicz, I.; Zhou, S.; Bergmeier, S. C.; Hines, J. V. Structure activity studies of RNA-binding oxazolidinone derivatives. Bioorg. Med. Chem. Letters 2011, 21, 4524-4527.

Jentzsh, F.; Hines, J. V. Interfacing medicinal chemistry with structural bioinformatics: Implications for T box riboswitch RNA drug discovery BMC Bioinformatics (GLBIO 2011 Special Issue) 2011, 13, S5-S10.

Acquaah-Harrison, G.; Zhou, S.; Hines, J. V.; Bergmeier, S. C. Library of 1,4-disubstituted 1,2,3-triazole analogs of oxazolidinone RNA-binding agents. J. Comb. Chem. 2010, 12, 491-496.

Means, J. A.; Simson, C. M.; Zhou, S.; Rachford, A. A.; Rack, J.; Hines, J. V. Fluorescence probing of T box antiterminator RNA: Insights into riboswitch discernment of the tRNA discriminator base. Biochem. Biophys. Res. Commun. 2009, 389, 616-621.

Fauzi, H.; Agyeman, A.; Hines, J. V. T box transcription antitermination riboswitch: Influence of nucleotide sequence and orientation on tRNA binding by the antiterminator element. BBA-Gene Reg. Mech. 2009, 1789, 185-191.

Jack, K. D.; Means, J. A.; Hines, J. V. Characterizing riboswitch function: Identification of Mg2+ binding site in T box antiterminator RNA. Biochem. Biophys. Res. Commun. 2008, 370, 306-310.

Anupam, R.; Bergmeier, S. C.; Green, N. J.; Grundy, F. J.; Henkin, T. M.; Means, J. A.; Nayek, A.; Hines, J. V. 4,5-Disubstituted Oxazolidinones: High affinity molecular effectors of RNA function. Bioorg. Med. Chem. Lett. 2008, 18, 3541-3544.

Anupam, R.; Denapoli, L.; Muchenditsi, A. M.; Hines, J. V. Identification of neomycin B binding site in T box antiterminator model RNA. Bioorg. Med. Chem. 2008, 16, 4466-4470.

Means, J. A.; Wolf, S.; Agyeman, A.; Burton, J. S.; Simson, C. M.; Hines, J. V. T box riboswitch antiterminator affinity modulated by tRNA structural elements Chem. Biol. Drug Design 2007, 69, 139-145.

Means, J. A.; Katz, S. J.; Nayek, A.; Anupam, R.; Hines, J. V.; Bergmeier, S. C. Structure activity studies of oxazolidinone analogs as RNA-binding agents. Bioorg. Med. Chem. Lett. 2006, 16, 3600-3604.

Means, J. A.; Hines, J. V. Fluorescence resonance energy transfer studies of aminoglycoside binding to a T box antiterminator RNA. Bioorg. Med. Chem. Lett. 2005, 15, 2169-2172.

Fauzi, H.; Jack, K. D.; Hines, J. V. In vitro selection to identify determinants in tRNA for Bacillus subtilis tyrS T box antiterminator mRNA binding. Nucleic Acids Res. 2005, 8, 2595-2602.

Gerdeman, M. S.; Henkin, T. M.; Hines, J. V. Solution structure of the B. subtilis T box antiterminator RNA: Seven-nucleotide bulge characterized by stacking and flexibility. J. Mol. Biol. 2003, 326, 189-201.

Gerdeman, M. S.; Henkin, T. M.; Hines, J. V. In vitro structure-function studies of the Bacillus subtilis tyrS mRNA antiterminator: Evidence for factor independent tRNA acceptor stem binding specificity. Nucleic Acids Res. 2002, 30, 1065-1072.