Benjamin G. Bobay

Milton, M. E., Draughn, G. L., Bobay, B. G., Stowe, S. D., Olson, A. L., Feldmann, E. A., … Cavanagh, J. (2020). The Solution Structures and Interaction of SinR and Sinl: Elucidating the Mechanism of Action of the Master Regulator Switch for Biofilm Formation in Bacillus subtilis. JOURNAL OF MOLECULAR BIOLOGY, 432(2), 343–357. https://doi.org/10.1016/j.jmb.2019.08.019

Bordelon, T., Bobay, B., Murphy, A., Reese, H., Shanahan, C., Odeh, F., … Menegatti, S. (2019). Translating antibody-binding peptides into peptoid ligands with improved affinity and stability. JOURNAL OF CHROMATOGRAPHY A, 1602, 284–299. https://doi.org/10.1016/j.chroma.2019.05.047

Kish, W. S., Sachi, H., Naik, A. D., Roach, M. K., Bobay, B. G., Blackburn, R. K., … Carbonell, R. G. (2017). Design, selection, and development of cyclic peptide ligands for human erythropoietin. Journal of Chromatography. A, 1500, 105–120. https://doi.org/10.1016/j.chroma.2017.04.019

Milton, M. E., Allen, C. L., Feldmann, E. A., Bobay, B. G., Jung, D. K., Stephens, M. D., … Cavanagh, J. (2017). Structure of the Francisella response regulator QseB receiver domain, and characterization of QseB inhibition by antibiofilm 2-aminoimidazole-based compounds. Molecular Microbiology, 106(2), 223–235. https://doi.org/10.1111/mmi.13759

Moore, M. D., Bobay, B. G., Mertens, B., & Jaykus, L. A. (2016). Human norovirus aptamer exhibits high degree of target conformation-dependent binding similar to that of receptors and discriminates particle functionality. Msphere, 1(6). https://doi.org/10.1128/msphere.00298-16

Harris, K. A., Bobay, B. G., Sarachan, K. L., Sims, A. F., Bilbille, Y., Deutsch, C., … Agris, P. F. (2015). NMR-based structural analysis of threonylcarbamoyl-AMP synthase and Its substrate interactions. Journal of Biological Chemistry, 290(33), 20032–20043.

Tucker, A. T., Bobay, B. G., Banse, A. V., Olson, A. L., Soderblom, E. J., Moseley, M. A., … Cavanagh, J. (2014). A DNA Mimic: The Structure and Mechanism of Action for the Anti-Repressor Protein AbbA. Journal of Molecular Biology, 426(9), 1911–1924. https://doi.org/10.1016/j.jmb.2014.02.010

Bobay, B. G., Thompson, R. J., Milton, D. L., & Cavanagh, J. (2014). Chemical shift assignments and secondary structure prediction of the phosphorelay protein VanU from Vibrio anguillarum. Biomolecular NMR Assignments, 8(1), 177–179. https://doi.org/10.1007/s12104-013-9478-2

Olson, A. L., Tucker, A. T., Bobay, B. G., Soderblom, E. J., Moseley, M. A., Thompson, R. J., & Cavanagh, J. (2014). Structure and DNA-binding traits of the transition state regulator AbrB. Structure (Cambridge, Mass. : 2001), 22(11), 1650–1656. https://doi.org/10.1016/j.str.2014.08.018

Olson, A. L., Bobay, B. G., Melander, C., & Cavanagh, J. (2012). H-1, C-13, and N-15 resonance assignments and secondary structure prediction of the full-length transition state regulator AbrB from Bacillus anthracis. Biomolecular NMR Assignments, 6(1), 95–98. https://doi.org/10.1007/s12104-011-9333-2

Thompson, R. J., Bobay, B. G., Stowe, S. D., Olson, A. L., Peng, L. L., Su, Z. M., … Cavanagh, J. (2012). Identification of BfmR, a response regulator involved in biofilm development, as a target for a 2-aminoimidazole-based antibiofilm agent. Biochemistry, 51(49), 9776–9778. https://doi.org/10.1021/bi3015289

Bobay, B. G., Stewart, A. L., Tucker, A. T., Thompson, R. J., Varney, K. M., & Cavanagh, J. (2012). Structural insights into the calcium-dependent interaction between calbindin-D28K and caspase-3. FEBS Letters, 586(20), 3582–3589. https://doi.org/10.1016/j.febslet.2012.08.032

Yang, H. O., Gurgel, P. V., Williams, D. K., Bobay, B. G., Cavanagh, J., Muddiman, D. C., & Carbonell, R. G. (2010). Binding site on human immunoglobulin G for the affinity ligand HWRGWV. Journal of Molecular Recognition, 23(3), 271–282.

Bobay, B. G., Thompson, R. J., Hoch, J. A., & Cavanagh, J. (2010). Long range dynamic effects of point-mutations trap a response regulator in an active conformation. FEBS Letters, 584(19), 4203–4207. https://doi.org/10.1016/j.febslet.2010.08.051

Hobbs, C. A., Bobay, B. G., Thompson, R. J., Perego, M., & Cavanagh, J. (2010). NMR solution structure and DNA-binding model of the DNA-binding domain of competence protein A. Journal of Molecular Biology, 398(2), 248–263. https://doi.org/10.1016/j.jmb.2010.03.003

Hobbs, C. A., Deterding, L. J., Perera, L., Bobay, B. G., Thompson, R. J., Darden, T. A., … Tomer, K. B. (2009). Structural characterization of the conformational change in calbindin-d-28k upon calcium binding using differential surface modification analyzed by mass spectrometry. Biochemistry, 48(36), 8603–8614. https://doi.org/10.1021/bi900350q

Szurmant, H., Bobay, B. G., White, R. A., Sullivan, D. M., Thompson, R. J., Hwa, T., … Cavanagh, J. (2008). Co-evolving motions at protein-protein interfaces of two-component signaling systems identified by covariance analysis. Biochemistry, 47(30), 7782–7784. https://doi.org/10.1021/bi8009604

Sullivan, D. M., Bobay, B. G., Kojetin, D. J., Thompson, R. J., Rance, M., Strauch, M. A., & Cavanagh, J. (2008). Insights into the nature of DNA binding of AbrB-like transcription factors. Structure (Cambridge, Mass. : 2001), 16(11), 1702–1713. https://doi.org/10.1016/j.str.2008.08.014

Burns, V. A., Bobay, B. G., Basso, A., Cavanagh, J., & Melander, C. (2008). Targeting RNA with cysteine-constrained peptides. Bioorganic & Medicinal Chemistry Letters, 18(2), 565–567. https://doi.org/10.1016/j.bmcl.2007.11.096

Strauch, M. A., Bobay, B. G., Cavanagh, J., Yao, F., Wilson, A., & Le Breton, Y. (2007). Abh and AbrB control of Bacillus subtilis antimicrobial gene expression. Journal of Bacteriology, 189(21), 7720–7732. https://doi.org/10.1128/JB.01081-07

Kordys, D. R., Bobay, B. G., Thompson, R. J., Venters, R. A., & Cavanagh, J. (2007). Peptide binding proclivities of calcium loaded calbindin-D28k. FEBS Letters, 581(24), 4778–4782. https://doi.org/10.1016/j.febslet.2007.09.004

McLaughlin, P. D., Bobay, B. G., Regel, E. J., Thompson, R. J., Hoch, J. A., & Cavanagh, J. (2007). Predominantly buried residues in the response regulator Spo0F influence specific sensor kinase recognition. FEBS Letters, 581(7), 1425–1429. https://doi.org/10.1016/j.febslet.2007.02.061

Soderblom, E. J., Bobay, B. G., Cavanagh, J., & Goshe, M. B. (2007). Tandem mass spectrometry acquisition approaches to enhance identification of protein-protein interactions using low-energy collision-induced dissociative chemical crosslinking reagents. Rapid Communications in Mass Spectrometry, 21(21), 3395–3408. https://doi.org/10.1002/rcm.3213

Bobay, B. G., Mueller, G. A., Thompson, R. J., Murzin, A. G., Venters, R. A., Strauch, M. A., & Cavanagh, J. (2006). NMR structure of AbhN and comparison with AbrBN - First insights into the DNA binding promiscuity and specificity of AbrB-like transition state regulator proteins. Journal of Biological Chemistry, 281(30), 21399–21409. https://doi.org/10.1074/jbc.M601963200

Bobay, B. G., Andreeva, A., Mueller, G. A., Cavanagh, J., & Murzin, A. G. (2005). Revised structure of the AbrB N-terminal domain unifies a diverse superfamily of putative DNA-binding proteins. FEBS Letters, 579(25), 5669–5674. https://doi.org/10.1016/j.febslet.2005.09.045

Bobay, B. G., Benson, L., Naylor, S., Feeney, B., Clark, A. C., Goshe, M. B., … Cavanagh, J. (2004). Evaluation of the DNA binding tendencies of the transition state regulator AbrB. Biochemistry, 43(51), 16106–16118. https://doi.org/10.1021/bi048399h

Benson, L. M., Vaughn, J. L., Strauch, M. A., Bobay, B. G., Thompson, R., Naylor, S., & Cavanagh, J. (2002). Macromolecular assembly of the transition state regulator AbrB in its unbound and complexed states probed by microelectrospray ionization mass spectrometry. Analytical Biochemistry, 306(2), 222–227. https://doi.org/10.1006/abio.2002.5704

Cavanagh, J., Thompson, R., Bobay, B., Benson, L. M., & Naylor, S. (2002). Stoichiometries of protein - Protein/DNA binding and conformational changes for the transition-state regulator AbrB measured by pseudo cell-size exclusion chromatography-mass spectrometry. Biochemistry, 41(25), 7859–7865. https://doi.org/10.1021/bi0202225