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Kim, I.M. and Szurmant, H. A Bacterial Goldilocks Mechanism. Elife. 24: e54244, 2020.

Rosales-Hurtado, M., Meffre, P., Szurmant, H., Benfodda, Z. Synthesis of Histidine Kinase Inhibitors and Their Biological Properties. Med. Res. Rev. 40: 1440-1495, 2020.

Croce, G., Gueudré, T., Ruiz Cuevas, M.V., Keidel, V., Figliuzzi, M., Szurmant, H. and Weigt, M. A Multi-Scale Coevolutionary Approach to Predict Interactions between Protein Domains. PLoS Comput. Biol. 15: e1006891, 2019.

Szurmant, H. Evolutionary Couplings of Amino Acid Residues Reveal Structure and Function of Bacterial Signaling Proteins. Mol. Microbiol. 112: 432-437, 2019.

Szurmant, H. and Weigt, M. Inter-Residue, Inter-Protein and Inter-Family Coevolution: Bridging the Scales. Curr. Opin. Struct. Biol. 2018:26-32, 2018.

Uguzzoni, G., John Lovis, S., Oteri, F., Schug, A.*, Szurmant, H.* and Weigt, M.* Large-Scale Identification of Coevolution Signals across Homo-Oligomeric Protein Interfaces by Direct Coupling Analysis. Proc. Natl. Acad. Sci. USA. 114: E2662-E2671, 2017. *Co-corresponding authors.

Boibessot, T., Zschiedrich, C.P., Lebeau, A., Bénimèlis, D., Dunyach-Rémy, C., Lavigne, J.P., Szurmant, H.*, Benfodda, Z.* and Meffre, P.*. The Rational Design, Synthesis, and Antimicrobial Properties of Thiophene Derivatives That Inhibit Bacterial Histidine Kinases. J. Med. Chem. 59: 8830-8847, 2016. *Co-corresponding authors

Zschiedrich, C. P., Keidel, V. and Szurmant, H. Molecular Mechanisms of Two-component Signal Transduction. J. Mol. Biol. 428: 3752-75, 2016.

Feinauer, C., Szurmant, H., Weigt, M. and Pagnani, A. Inter-Protein Sequence Co-Evolution Predicts Known Physical Interactions in Bacterial Ribosomes and the Trp Operon PLoS ONE. 11: e0149166, 2016.

Pokkuluri P.R., Dwulit-Smith, J., Duke, N.E., Wilton, R., Mack, J.C., Bearden, J., Rakowski, E., Babnigg, G., Szurmant, H., Joachimiak, A., and Schiffer, M. Analysis of Periplasmic Sensor Domains from Anaeromyxobacter dehalogenans 2CP-C: Structure of One Sensor Domain from a Histidine Kinase and Another from a Chemotaxis Protein. Microbiology Open. 2: 766-77, 2013.

Wu, R., Gu, M., Wilton, R., Babnigg, G., Kim, Y., Pokkuluri, P.R., Szurmant, H., Joachimiak, A., Schiffer, M. Insight into the Sporulation Phosphorelay: Crystal Structure of the Sensor Domain of Bacillus subtilis Histidine Kinase KinD. Protein Sci. 22: 564-76, 2013.

Szurmant, H. and Hoch, J.A. Statistical Analyses of Protein Databases Identify Structures and Mechanisms in Signal Activation of Sensor Histidine Kinases. Mol. Microbiol. 87: 707-12, 2013.

Dago, A.E., Schug, A., Procaccini, A., Hoch, J.A., Weigt, M., and Szurmant, H. The Structural Basis of Histidine Kinase Autophosphorylation: Integrating Genomics, Molecular Dynamics and Mutagenesis. Proc. Natl. Acad. Sci USA 109: E1733-42, 2012.

Diaz, A.R., Core, L., Jiang, M., Morelli, M., Chiang, C.H., Szurmant, H., and Perego, M. Bacillus subtilis RapA Phosphatase Domain Interaction with its Substrate, Phosphorylate Spo0F, and its Inhibitor, the PhrA peptide. J. Bacteriol. 194: 1378-88, 2012.

Fukushima, T., Furihata, I., Emmins, R., Daniel, R.A., Hoch, J.A., and Szurmant, H. A Role for the Essential YycG Sensor Histidine Kinase In Sensing Cell Division. Mol. Microbiol. 79: 503-22, 2011.

Procaccini, A., Lunt, B., Szurmant, H., Hwa, T., and Weigt, M. Dissecting the Specificity of Protein-Protein Interaction in Bacterial Two-Component Signaling: Orphans and Crosstalks. PLoS One 6: e19729, 2011.

Wilson, A.C. and Szurmant, H. Transposon Systems for Random Mutagenesis of Bacillus subtilis. Methods Mol. Biol. 765: 359-71, 2011.

Szurmant, H. and Hoch, J.A. Interaction Fidelity in Two-Component Signaling. Curr. Opin. Microbiol. 13: 190-7, 2010.

Schug, A., Weigt, M., Hoch, J.A., Onuchic, J.N., Hwa, T., and Szurmant, H. Computational Modeling of Phosphotransfer Complexes in Two-Component Signaling. Methods Enzymol. 471: 43-58, 2010.

Lunt, B., Szurmant, H., Procaccini, A., Hoch, J.A., Hwa, T., Weigt, M. Inference of Direct Residue Contacts in Two-Component Signaling. Methods Enzymol. 471: 17-41, 2010.

Chang, C., Tesar, C., Gu, M., Babnig, G., Joachimiak, A., Pokkuluri, P.R., Szurmant, H., and Schiffer, M. Periplasmic PAS Domains: A Dominant Structural Family Governing Signal Transduction. J. Bacteriol. 192: 1156-9, 2010.

Schug, A., Weigt, M., Onuchic, J.N., Hwa, T., and Szurmant, H. High Resolution Protein Complexes From Integrating Genomic Information With Molecular Simulation. Proc. Natl. Acad. Sci. USA 106: 22124-9, 2009.

Weigt, M., White, R. A., Szurmant, H., Hoch, J.A., and Hwa, T. Identification of Direct Residue Contacts in Protein-Protein Interaction By Message Passing. Proc. Natl. Acad. Sci. USA 106: 67-72, 2009.

Szurmant, H., Bobay, B.G., White, R. A., Sullivan, D.M., Thompson, R.J., Hwa, T., Hoch, J.A., and Cavanagh, J. Co-evolving Motions at Protein-Protein Interfaces of Two- Component Signaling Systems Identified by Covariance Analysis. Biochemistry, 47: 7782-4, 2008. Selected as “hot article” by the editorial board.

Fukushima, T., Szurmant, H., Kim, E.J., Perego, M., and Hoch, J.A. A Sensor Histidine Kinase Coordinates Cell Wall Architecture with Cell Division in Bacillus subtilis. Mol. Microbiol. 69: 621-32 (Including Cover Image), 2008.

Szurmant, H., Bu, L., Brooks, C.L., and Hoch, J.A. An Essential Sensor Histidine Kinase Controlled By Transmembrane Helix Interaction with its Auxiliary Proteins. Proc. Natl. Acad. Sci. USA 105: 5891-6, 2008.

Szurmant, H., White, R.A., and Hoch, J.A. Sensor Complexes Regulating Twocomponent Signal Transduction. Curr. Opin. Struct. Biol. 17: 706-15, 2007.

Santelli, E., Liddington, R.C., Mohan, M.A., Hoch, J.A., and Szurmant, H. The Crystal Structure of Bacillus subtilis YycI Reveals a Common Fold for Two Members of an Unusual Class of Histidine Kinase Regulatory Proteins. J. Bacteriol. 289: 3280-9, 2007.

Szurmant, H., Mohan, M.A., Imus, P.M., and Hoch, J.A. YycH and YycI Interact to Regulate the Essential YycFG Two-Component System. J. Bacteriol. 289: 3290-5, 2007.

White, R. A., Szurmant, H., Hoch, J.A., and Hwa, T. Features of Protein-protein Interactions in Two-Component Signaling Deduced from Genomic Libraries. Methods Enzymol. 422: 75-101, 2007.

Szurmant, H., Fukushima, T., M.A., and Hoch, J.A. The Essential YycFG Two- Component System in Bacillus subtilis. Methods Enzymol. 422: 396-417, 2007.

Szurmant, H., Zhao, H., Mohan, M.A., Hoch, J.A., and Varughese, K.I. The Crystal Structure of YycH Involved in the Regulation of the Essential YycFG Two-Component System in Bacillus subtilis reveals a Novel Tertiary Structure. Protein Sci. 15: 929-34 (Including Cover Image), 2006.

Wörner, K., Szurmant, H., Chiang, C., and Hoch, J.A. Phosphorylation and Functional Analysis of the Sporulation Initiation Factor Spo0A from Clostridium botulinum. Mol. Microbiol., 59: 1000-12, 2006.

Szurmant, H., Nelson, K., Kim, E.J., Perego, M., and Hoch, J.A. YycH Regulates the Activity of the Essential YycFG Two-Component System in Bacillus subtilis. J. Bacteriol. 187: 5419-26, 2005.

Szurmant, H. and Ordal, G.W. The Diversity in Chemotaxis Mechanisms among the Bacteria and Archaea. Microbiol. Mol. Biol. Rev. 68: 301-19, 2004.

Szurmant, H., Muff, T., and Ordal, G.W. Bacillus subtilis CheC and FliY are Members of a Novel Class of CheY-P Hydrolyzing Proteins in the Chemotactic Signal Transduction Cascade. J. Biol. Chem. 279: 21787-92, 2004.

Szurmant, H., Bunn, M.W., Cho, S.H., and Ordal, G.W. Ligand Induced Conformational Changes in the Bacillus subtilis Chemotaxis Receptor McpB Determined by Disulfide Crosslinking in vivo. J. Mol. Biol. 344: 919-28, 2004.

Szurmant, H., Bunn, M.W., Cannistraro, V.J., and Ordal, G.W. Bacillus subtilis Hydrolyzes CheY-P at the Place of its Action, the Flagellar Switch. J. Biol. Chem. 278: 48611-6, 2003.

Zimmer, M.A., Szurmant, H., Saulmon, M.M., Collins, M. A., Bant, J.S., and Ordal, G.W. The Role of Heterologous Receptors in McpB-Mediated Signaling in Bacillus subtilis Chemotaxis. Mol. Microbiol. 45: 555-69, 2002.