| Year |
Citation |
Score |
| 2019 |
Rosales-Hurtado M, Meffre P, Szurmant H, Benfodda Z. Synthesis of histidine kinase inhibitors and their biological properties. Medicinal Research Reviews. PMID 31802520 DOI: 10.1002/Med.21651 |
0.304 |
|
| 2019 |
Croce G, Gueudré T, Ruiz Cuevas MV, Keidel V, Figliuzzi M, Szurmant H, Weigt M. A multi-scale coevolutionary approach to predict interactions between protein domains. Plos Computational Biology. 15: e1006891. PMID 31634362 DOI: 10.1371/Journal.Pcbi.1006891 |
0.387 |
|
| 2019 |
Szurmant H. Evolutionary couplings of amino acid residues reveal structure and function of bacterial signaling proteins. Molecular Microbiology. PMID 31102561 DOI: 10.1111/Mmi.14282 |
0.368 |
|
| 2017 |
Szurmant H, Weigt M. Inter-residue, inter-protein and inter-family coevolution: bridging the scales. Current Opinion in Structural Biology. 50: 26-32. PMID 29101847 DOI: 10.1016/J.Sbi.2017.10.014 |
0.32 |
|
| 2017 |
Uguzzoni G, John Lovis S, Oteri F, Schug A, Szurmant H, Weigt M. Large-scale identification of coevolution signals across homo-oligomeric protein interfaces by direct coupling analysis. Proceedings of the National Academy of Sciences of the United States of America. PMID 28289198 DOI: 10.1073/Pnas.1615068114 |
0.367 |
|
| 2017 |
Uguzzoni G, Lovis SJ, Oteri F, Szurmant H, Martin W, Schug A. Prediction of Protein and RNA Structures by Co-Evolution: Going Beyond Anecdotal Cases towards Large-Scale Biophysical Journal. 112. DOI: 10.1016/J.Bpj.2016.11.326 |
0.324 |
|
| 2016 |
Boibessot T, Zschiedrich CP, Lebeau A, Bénimèlis D, Dunyach-Rémy C, Lavigne JP, Szurmant H, Benfodda Z, Meffre P. The rational design, synthesis and antimicrobial properties of thiophene derivatives that inhibit bacterial histidine kinases. Journal of Medicinal Chemistry. PMID 27575438 DOI: 10.1021/Acs.Jmedchem.6B00580 |
0.371 |
|
| 2016 |
Zschiedrich CP, Keidel V, Szurmant H. Molecular mechanisms of two-component signal transduction. Journal of Molecular Biology. PMID 27519796 DOI: 10.1016/J.Jmb.2016.08.003 |
0.333 |
|
| 2016 |
Feinauer C, Szurmant H, Weigt M, Pagnani A. Inter-Protein Sequence Co-Evolution Predicts Known Physical Interactions in Bacterial Ribosomes and the Trp Operon. Plos One. 11: e0149166. PMID 26882169 DOI: 10.1371/Journal.Pone.0149166 |
0.339 |
|
| 2013 |
Wu R, Gu M, Wilton R, Babnigg G, Kim Y, Pokkuluri PR, Szurmant H, Joachimiak A, Schiffer M. Insight into the sporulation phosphorelay: crystal structure of the sensor domain of Bacillus subtilis histidine kinase, KinD. Protein Science : a Publication of the Protein Society. 22: 564-76. PMID 23436677 DOI: 10.1002/Pro.2237 |
0.426 |
|
| 2013 |
Szurmant H, Hoch JA. Statistical analyses of protein sequence alignments identify structures and mechanisms in signal activation of sensor histidine kinases. Molecular Microbiology. 87: 707-12. PMID 23279101 DOI: 10.1111/Mmi.12128 |
0.443 |
|
| 2013 |
Schug A, Verma A, Weigt M, Szurmant H. Integrating Genomic Information with Molecular Simulation for Protein Dynamics Biophysical Journal. 104: 2-2. DOI: 10.1016/J.Bpj.2012.11.1202 |
0.389 |
|
| 2012 |
Dago AE, Schug A, Procaccini A, Hoch JA, Weigt M, Szurmant H. Structural basis of histidine kinase autophosphorylation deduced by integrating genomics, molecular dynamics, and mutagenesis. Proceedings of the National Academy of Sciences of the United States of America. 109: E1733-42. PMID 22670053 DOI: 10.1073/Pnas.1201301109 |
0.432 |
|
| 2012 |
Diaz AR, Core LJ, Jiang M, Morelli M, Chiang CH, Szurmant H, Perego M. Bacillus subtilis RapA phosphatase domain interaction with its substrate, phosphorylated Spo0F, and its inhibitor, the PhrA peptide. Journal of Bacteriology. 194: 1378-88. PMID 22267516 DOI: 10.1128/Jb.06747-11 |
0.436 |
|
| 2012 |
Schug A, Weigt M, Szurmant H. Integrating Genomic Information with Molecular Simulation to Understand Protein Complex- and Active Conformation Formation in Two-Component Signal Transduction Biophysical Journal. 102: 45a. DOI: 10.1016/J.Bpj.2011.11.279 |
0.385 |
|
| 2011 |
Wilson AC, Szurmant H. Transposon-mediated random mutagenesis of Bacillus subtilis. Methods in Molecular Biology (Clifton, N.J.). 765: 359-71. PMID 21815103 DOI: 10.1007/978-1-61779-197-0_21 |
0.303 |
|
| 2011 |
Procaccini A, Lunt B, Szurmant H, Hwa T, Weigt M. Dissecting the specificity of protein-protein interaction in bacterial two-component signaling: orphans and crosstalks. Plos One. 6: e19729. PMID 21573011 DOI: 10.1371/Journal.Pone.0019729 |
0.372 |
|
| 2011 |
Fukushima T, Furihata I, Emmins R, Daniel RA, Hoch JA, Szurmant H. A role for the essential YycG sensor histidine kinase in sensing cell division. Molecular Microbiology. 79: 503-22. PMID 21219466 DOI: 10.1111/J.1365-2958.2010.07464.X |
0.374 |
|
| 2010 |
Schug A, Weigt M, Hoch JA, Onuchic JN, Hwa T, Szurmant H. Computational modeling of phosphotransfer complexes in two-component signaling. Methods in Enzymology. 471: 43-58. PMID 20946841 DOI: 10.1016/S0076-6879(10)71003-X |
0.359 |
|
| 2010 |
Lunt B, Szurmant H, Procaccini A, Hoch JA, Hwa T, Weigt M. Inference of direct residue contacts in two-component signaling. Methods in Enzymology. 471: 17-41. PMID 20946840 DOI: 10.1016/S0076-6879(10)71002-8 |
0.374 |
|
| 2010 |
Szurmant H, Hoch JA. Interaction fidelity in two-component signaling. Current Opinion in Microbiology. 13: 190-7. PMID 20133181 DOI: 10.1016/J.Mib.2010.01.007 |
0.391 |
|
| 2010 |
Chang C, Tesar C, Gu M, Babnigg G, Joachimiak A, Pokkuluri PR, Szurmant H, Schiffer M. Extracytoplasmic PAS-like domains are common in signal transduction proteins. Journal of Bacteriology. 192: 1156-9. PMID 20008068 DOI: 10.1128/Jb.01508-09 |
0.39 |
|
| 2009 |
Schug A, Weigt M, Onuchic JN, Hwa T, Szurmant H. High-resolution protein complexes from integrating genomic information with molecular simulation. Proceedings of the National Academy of Sciences of the United States of America. 106: 22124-9. PMID 20018738 DOI: 10.1073/Pnas.0912100106 |
0.376 |
|
| 2009 |
Weigt M, White RA, Szurmant H, Hoch JA, Hwa T. Identification of direct residue contacts in protein-protein interaction by message passing Proceedings of the National Academy of Sciences of the United States of America. 106: 67-72. PMID 19116270 DOI: 10.1073/Pnas.0805923106 |
0.366 |
|
| 2008 |
Szurmant H, Bobay BG, White RA, Sullivan DM, Thompson RJ, Hwa T, Hoch JA, Cavanagh J. Co-evolving motions at protein-protein interfaces of two-component signaling systems identified by covariance analysis. Biochemistry. 47: 7782-4. PMID 18588317 DOI: 10.1021/Bi8009604 |
0.373 |
|
| 2008 |
Szurmant H, Bu L, Brooks CL, Hoch JA. An essential sensor histidine kinase controlled by transmembrane helix interactions with its auxiliary proteins. Proceedings of the National Academy of Sciences of the United States of America. 105: 5891-6. PMID 18408157 DOI: 10.1073/Pnas.0800247105 |
0.392 |
|
| 2007 |
Szurmant H, White RA, Hoch JA. Sensor complexes regulating two-component signal transduction. Current Opinion in Structural Biology. 17: 706-15. PMID 17913492 DOI: 10.1016/J.Sbi.2007.08.019 |
0.345 |
|
| 2007 |
White RA, Szurmant H, Hoch JA, Hwa T. Features of Protein-Protein Interactions in Two-Component Signaling Deduced from Genomic Libraries Methods in Enzymology. 422: 75-101. PMID 17628135 DOI: 10.1016/S0076-6879(06)22004-4 |
0.386 |
|
| 2007 |
Szurmant H, Mohan MA, Imus PM, Hoch JA. YycH and YycI interact to regulate the essential YycFG two-component system in Bacillus subtilis. Journal of Bacteriology. 189: 3280-9. PMID 17307850 DOI: 10.1128/Jb.01936-06 |
0.388 |
|
| 2007 |
Santelli E, Liddington RC, Mohan MA, Hoch JA, Szurmant H. The crystal structure of Bacillus subtilis YycI reveals a common fold for two members of an unusual class of sensor histidine kinase regulatory proteins. Journal of Bacteriology. 189: 3290-5. PMID 17307848 DOI: 10.1128/Jb.01937-06 |
0.396 |
|
| 2006 |
Szurmant H, Zhao H, Mohan MA, Hoch JA, Varughese KI. 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 Science : a Publication of the Protein Society. 15: 929-34. PMID 16600972 DOI: 10.1110/Ps.052064406 |
0.385 |
|
| 2006 |
Wörner K, Szurmant H, Chiang C, Hoch JA. Phosphorylation and functional analysis of the sporulation initiation factor Spo0A from Clostridium botulinum. Molecular Microbiology. 59: 1000-12. PMID 16420367 DOI: 10.1111/J.1365-2958.2005.04988.X |
0.377 |
|
| 2005 |
Szurmant H, Nelson K, Kim EJ, Perego M, Hoch JA. YycH regulates the activity of the essential YycFG two-component system in Bacillus subtilis. Journal of Bacteriology. 187: 5419-26. PMID 16030236 DOI: 10.1128/Jb.187.15.5419-5426.2005 |
0.371 |
|
| 2004 |
Szurmant H, Bunn MW, Cho SH, Ordal GW. Ligand-induced conformational changes in the Bacillus subtilis chemoreceptor McpB determined by disulfide crosslinking in vivo. Journal of Molecular Biology. 344: 919-28. PMID 15544802 DOI: 10.1016/J.Jmb.2004.09.093 |
0.692 |
|
| 2004 |
Szurmant H, Ordal GW. Diversity in chemotaxis mechanisms among the bacteria and archaea. Microbiology and Molecular Biology Reviews : Mmbr. 68: 301-19. PMID 15187186 DOI: 10.1128/Mmbr.68.2.301-319.2004 |
0.623 |
|
| 2004 |
Szurmant H, Muff TJ, Ordal GW. Bacillus subtilis CheC and FliY are members of a novel class of CheY-P-hydrolyzing proteins in the chemotactic signal transduction cascade. The Journal of Biological Chemistry. 279: 21787-92. PMID 14749334 DOI: 10.1074/Jbc.M311497200 |
0.702 |
|
| 2003 |
Szurmant H, Bunn MW, Cannistraro VJ, Ordal GW. Bacillus subtilis hydrolyzes CheY-P at the location of its action, the flagellar switch. The Journal of Biological Chemistry. 278: 48611-6. PMID 12920116 DOI: 10.1074/Jbc.M306180200 |
0.66 |
|
| 2002 |
Zimmer MA, Szurmant H, Saulmon MM, Collins MA, Bant JS, Ordal GW. The role of heterologous receptors in McpB-mediated signalling in Bacillus subtilis chemotaxis. Molecular Microbiology. 45: 555-68. PMID 12123464 DOI: 10.1046/J.1365-2958.2002.03035.X |
0.651 |
|
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