Promising antibacterials for LLM of Staphylococcus aureus using virtual screening, molecular docking, dynamics, and MMPBSA

References

• Abraham, M. J., & Gready, J. E. (2011). Optimization of parameters for molecular dynamics simulation using smooth particle‐mesh Ewald in GROMACS 4.5. Journal of Computational Chemistry, 32(9), 2031–2040. https://doi.org/10.1002/jcc.21773
   PubMed Web of Science ®Google Scholar
• Berendsen, H. J., Postma, J. v., van Gunsteren, W. F., DiNola, A., & Haak, J. R. (1984). Molecular dynamics with coupling to an external bath. The Journal of Chemical Physics, 81(8), 3684–3690. https://doi.org/10.1063/1.448118
   Web of Science ®Google Scholar
• Berger-Bächi, B., Strässle, A., Gustafson, J. E., & Kayser, F. H. (1992). Mapping and characterization of multiple chromosomal factors involved in methicillin resistance in Staphylococcus aureus. Antimicrobial Agents and Chemotherapy, 36(7), 1367–1373. https://doi.org/10.1128/AAC.36.7.1367
   PubMed Web of Science ®Google Scholar
• Couto, I., Melo-Cristino, J., Fernandes, M. L., Garcia, T., Serrano, N., Salgado, M. J., Torres-Pereira, A., Sanches, I. S., & de Lencastre, H. (1995). Unusually large number of methicillin-resistant Staphylococcus aureus clones in a Portuguese hospital. Journal of Clinical Microbiology, 33(8), 2032–2035. https://doi.org/10.1128/jcm.33.8.2032-2035.1995
   PubMed Web of Science ®Google Scholar
• Dalal, V., Golemi-Kotra, D., & Kumar, P. (2022). Quantum mechanics/molecular mechanics studies on the catalytic mechanism of a novel esterase (FmtA) of Staphylococcus aureus. Journal of Chemical Information and Modeling, 62(10), 2409–2420. https://doi.org/10.1021/acs.jcim.2c00057
   PubMed Web of Science ®Google Scholar
• Dalal, V., Kumar, P., Rakhaminov, G., Qamar, A., Fan, X., Hunter, H., Tomar, S., Golemi-Kotra, D., & Kumar, P. (2019). Repurposing an ancient protein core structure: Structural studies on FmtA, a novel esterase of Staphylococcus aureus. Journal of Molecular Biology, 431(17), 3107–3123. https://doi.org/10.1016/j.jmb.2019.06.019
   PubMed Web of Science ®Google Scholar
• Dalal, V., Dhankhar, P., Singh, V., Rakhaminov, G., Golemi-Kotra, D., & Kumar, P. (2021). Structure-based identification of potential drugs against FmtA of Staphylococcus aureus: Virtual screening, molecular dynamics, MM-GBSA, and QM/MM. The protein journal, 40(2), 148–165.
   Google Scholar
• Dallakyan, S., & Olson, A. J. (2015). Small-molecule library screening by docking with PyRx Chemical biology (pp. 243–250). Springer.
   Google Scholar
• De Lencastre, H., De Jonge, B., Matthews, P. R., & Tomasz, A. (1994). Molecular aspects of methicillin resistance in Staphylococcus aureus. The Journal of Antimicrobial Chemotherapy, 33(1), 7–24. https://doi.org/10.1093/jac/33.1.7
   PubMed Web of Science ®Google Scholar
• DeLano, W. L. (2002). The pymol molecular graphics system (2002). http://www.pymol.org
   Google Scholar
• Dhankhar, P., Dalal, V., Mahto, J. K., Gurjar, B. R., Tomar, S., Sharma, A. K., & Kumar, P. (2020). Characterization of dye-decolorizing peroxidase from Bacillus subtilis. Archives of Biochemistry and Biophysics, 693, 108590. https://doi.org/10.1016/j.abb.2020.108590
   PubMed Web of Science ®Google Scholar
• Dhankhar, P., Dalal, V., Singh, V., Sharma, A. K., & Kumar, P. (2021). Structure of dyedecolorizing peroxidase from Bacillus subtilis in complex with veratryl alcohol. International Journal of Biological Macromolecules, 193, 601–608.
   Google Scholar
• Dhankhar, P., Dalal, V., & Kumar, V. (2021). Screening of Severe Acute Respiratory Syndrome Coronavirus 2 RNA-Dependent RNA Polymerase Inhibitors Using Computational Approach. Journal of Computational Biology, 28(12), 1228–1247.
   Google Scholar
• Dhankhar, P., Dalal, V., Golemi-Kotra, D., & Kumar, P. (2020). In-silico approach to identify novel potent inhibitors against GraR of S. aureus. Frontiers in Bioscience-Landmark, 25(7), 1337–1360.
   Google Scholar
• Fan, X., Liu, Y., Smith, D., Konermann, L., Siu, K. M., & Golemi-Kotra, D. (2007). Diversity of penicillin-binding proteins. The Journal of Biological Chemistry, 282(48), 35143–35152. https://doi.org/10.1074/jbc.M706296200
   PubMed Web of Science ®Google Scholar
• FONTANA, R. (1985). Penicillin-binging proteins and the intrinsic resistance to βlactams in Gram-positive cocci. The Journal of Antimicrobial Chemotherapy, 16(4), 412–416. https://doi.org/10.1093/jac/16.4.412
   PubMed Web of Science ®Google Scholar
• Gupta, D. N., Dalal, V., Savita, B. K., Dhankhar, P., Ghosh, D. K., Kumar, P., & Sharma, A. K. (2021). In-silico screening and identification of potential inhibitors against 2Cys peroxiredoxin of Candidatus Liberibacter asiaticus. Journal of Biomolecular Structure and Dynamics, 1–15. https://doi.org/10.1080/07391102.2021.1916597
   Google Scholar
• Gustafson, J., Strässle, A., Hächler, H., Kayser, F. H., & Berger-Bächi, B. (1994). The femC locus of Staphylococcus aureus required for methicillin resistance includes the glutamine synthetase operon. Journal of Bacteriology, 176(5), 1460–1467. https://doi.org/10.1128/jb.176.5.1460-1467.1994
   PubMed Web of Science ®Google Scholar
• Hess, B., Bekker, H., Berendsen, H. J., & Fraaije, J. G. (1997). LINCS: A linear constraint solver for molecular simulations. Journal of Computational Chemistry, 18(12), 1463–1472. https://doi.org/10.1002/(SICI)1096-987X(199709)18:12<1463::AID-JCC4>3.0.CO;2-H
   Web of Science ®Google Scholar
• Hiramatsu, K. (2001). Vancomycin-resistant Staphylococcus aureus: A new model of antibiotic resistance. The Lancet. Infectious Diseases, 1(3), 147–155. https://doi.org/10.1016/S1473-3099(01)00091-3
   PubMedGoogle Scholar
• Hiramatsu, K., Cui, L., Kuroda, M., & Ito, T. (2001). The emergence and evolution of methicillin-resistant Staphylococcus aureus. Trends in Microbiology, 9(10), 486–493. https://doi.org/10.1016/S0966-842X(01)02175-8
   PubMed Web of Science ®Google Scholar
• Holden, M. T. G., Feil, E. J., Lindsay, J. A., Peacock, S. J., Day, N. P. J., Enright, M. C., Foster, T. J., Moore, C. E., Hurst, L., Atkin, R., Barron, A., Bason, N., Bentley, S. D., Chillingworth, C., Chillingworth, T., Churcher, C., Clark, L., Corton, C., Cronin, A., … Parkhill, J. (2004). Complete genomes of two clinical Staphylococcus aureus strains: Evidence for the rapid evolution of virulence and drug resistance. Proceedings of the National Academy of Sciences of the United States of America, 101(26), 9786–9791. https://doi.org/10.1073/pnas.0402521101
   PubMed Web of Science ®Google Scholar
• Katayama, Y., Ito, T., & Hiramatsu, K. (2000). A new class of genetic element, staphylococcus cassette chromosome mec, encodes methicillin resistance in Staphylococcus aureus. Antimicrobial Agents and Chemotherapy, 44(6), 1549–1555. https://doi.org/10.1128/AAC.44.6.1549-1555.2000
   PubMed Web of Science ®Google Scholar
• Kesari, P., Pratap, S., Dhankhar, P., Dalal, V., Mishra, M., Singh, P. K., Chauhan, H., & Kumar, P. (2020). Structural characterization and in-silico analysis of Momordica charantia 7S globulin for stability and ACE inhibition. Scientific Reports, 10(1), 1–13. https://doi.org/10.1038/s41598-020-58138-9
   PubMed Web of Science ®Google Scholar
• Komatsuzawa, H., Sugai, M., Ohta, K., Fujiwara, T., Nakashima, S., Suzuki, J., Lee, C. Y., & Suginaka, H. (1997). Cloning and characterization of the fmt gene which affects the methicillin resistance level and autolysis in the presence of Triton X-100 in methicillin-resistant Staphylococcus aureus. Antimicrobial Agents and Chemotherapy, 41(11), 2355–2361. https://doi.org/10.1128/AAC.41.11.2355
   PubMed Web of Science ®Google Scholar
• Kornblum, J., Hartman, B., Novick, R., & Tomasz, A. (1986). Conversion of a homogeneously methicillin-resistant strain of Staphylococcus aureus to heterogeneous resistance by Tn551-mediated insertional inactivation. European Journal of Clinical Microbiology, 5(6), 714–718. https://doi.org/10.1007/BF02013311
   PubMedGoogle Scholar
• Kumar, P., Dalal, V., Kokane, A., Singh, S., Lonare, S., Kaur, H., Ghosh, D. K., Kumar, P. & Sharma, A. K. (2020). Mutation studies and structure-based identification of potential inhibitor molecules against periplasmic amino acid binding protein of Candidatus Liberibacter asiaticus (CLasTcyA). International journal of biological macromolecules, 147, 1228–1238.
   Google Scholar
• Kumari, R., & Dalal, V. (2021). Identification of potential inhibitors for LLM of Staphylococcus aureus: Structure-based pharmacophore modeling, molecular dynamics, and binding free energy studies. Journal of Biomolecular Structure and Dynamics, 1–15. https://doi.org/10.1080/07391102.2021.1936179
   Google Scholar
• Kumari, N., Dalal, V., Kumar, P., & Rath, S. N. (2022). Antagonistic interaction between TTA-A2 and paclitaxel for anti-cancer effects by complex formation with T-type calcium channel. Journal of Biomolecular Structure and Dynamics, 40(6), 2395-2406. https://doi.org/10.1080/07391102.2020.1839558
   PubMed Web of Science ®Google Scholar
• Kumari, R., Dhankhar, P., & Dalal, V. (2021). Structure-based mimicking of hydroxylated biphenyl congeners (OHPCBs) for human transthyretin, an important enzyme of thyroid hormone system. Journal of Molecular Graphics and Modelling, 105, 107870. https://doi.org/10.1016/j.jmgm.2021.107870
   PubMed Web of Science ®Google Scholar
• Kumari, R., Kumar, R., Consortium, O. S. D. D., & Lynn, A. (2014). g_mmpbsa– A GROMACS tool for high-throughput MM-PBSA calculations. Journal of Chemical Information and Modeling, 54(7), 1951–1962. https://doi.org/10.1021/ci500020m
   PubMed Web of Science ®Google Scholar
• Kumari, R., Rathi, R., Pathak, S. R., & Dalal, V. (2022). Structural-based virtual screening and identification of novel potent antimicrobial compounds against YsxC of Staphylococcus aureus. Journal of Molecular Structure, 1255, 132476.
   Google Scholar
• Kurkcuoglu, Z., Koukos, P. I., Citro, N., Trellet, M. E., Rodrigues, J. P. G. L. M., Moreira, I. S., Roel-Touris, J., Melquiond, A. S. J., Geng, C., Schaarschmidt, J., Xue, L. C., Vangone, A., & Bonvin, A. M. J. J. (2018). Performance of HADDOCK and a simple contact-based protein–ligand binding affinity predictor in the D3R Grand Challenge 2. Journal of Computer-Aided Molecular Design, 32(1), 175–185. https://doi.org/10.1007/s10822-017-0049-y
   PubMed Web of Science ®Google Scholar
• Lindsay, J. A., & Holden, M. T. (2006). Understanding the rise of the superbug: Investigation of the evolution and genomic variation of Staphylococcus aureus. Functional & Integrative Genomics, 6(3), 186–201. https://doi.org/10.1007/s10142-005-0019-7
   PubMedGoogle Scholar
• Livermore, D. M. (2000). Antibiotic resistance in staphylococci. International Journal of Antimicrobial Agents, 16, 3–10. https://doi.org/10.1016/S0924-8579(00)00299-5
   PubMed Web of Science ®Google Scholar
• Lowy, F. D. (1998). Staphylococcus aureus infections. The New England Journal of Medicine, 339(8), 520–532. https://doi.org/10.1056/NEJM199808203390806
   PubMed Web of Science ®Google Scholar
• Lowy, F. D. (2003). Antimicrobial resistance: The example of Staphylococcus aureus. The Journal of Clinical Investigation, 111(9), 1265–1273. https://doi.org/10.1172/JCI18535
   PubMed Web of Science ®Google Scholar
• Lyon, B., Iuorio, J., May, J., & Skurray, R. (1984). Molecular epidemiology of multiresistant Staphylococcus aureus in Australian hospitals. Journal of Medical Microbiology, 17(1), 79–89. https://doi.org/10.1099/00222615-17-1-79
   PubMed Web of Science ®Google Scholar
• Maciejewski, M. W., Schuyler, A. D., Gryk, M. R., Moraru, I. I., Romero, P. R., Ulrich, E. L., Eghbalnia, H. R., Livny, M., Delaglio, F., & Hoch, J. C. (2017). NMRbox: A resource for biomolecular NMR computation. Biophysical Journal, 112(8), 1529–1534. https://doi.org/10.1016/j.bpj.2017.03.011
   PubMed Web of Science ®Google Scholar
• Maki, H., Yamaguchi, T., & Murakami, K. (1994). Cloning and characterization of a gene affecting the methicillin resistance level and the autolysis rate in Staphylococcus aureus. Journal of Bacteriology, 176(16), 4993–5000. https://doi.org/10.1128/jb.176.16.4993-5000.1994
   PubMed Web of Science ®Google Scholar
• Malik, A., Dalal, V., Ankri, S., & Tomar, S. (2019). Structural insights into Entamoeba histolytica arginase and structure‐based identification of novel non‐amino acid based inhibitors as potential antiamoebic molecules. The FEBS Journal, 286(20), 4135–4155. https://doi.org/10.1111/febs.14960
   PubMed Web of Science ®Google Scholar
• Memmi, G., Filipe, S. R., Pinho, M. G., Fu, Z., & Cheung, A. (2008). Staphylococcus aureus PBP4 is essential for β-lactam resistance in community-acquired methicillin-resistant strains. Antimicrobial Agents and Chemotherapy, 52(11), 3955–3966. https://doi.org/10.1128/AAC.00049-08
   PubMed Web of Science ®Google Scholar
• Morris, G. M., Huey, R., Lindstrom, W., Sanner, M. F., Belew, R. K., Goodsell, D. S., & Olson, A. J. (2009). AutoDock4 and AutoDockTools4: Automated docking with selective receptor flexibility. Journal of Computational Chemistry, 30(16), 2785–2791. https://doi.org/10.1002/jcc.21256
   PubMed Web of Science ®Google Scholar
• O’Boyle, N. M., Banck, M., James, C. A., Morley, C., Vandermeersch, T., & Hutchison, G. R. (2011). Open Babel: An open chemical toolbox. Journal of Cheminformatics, 3(1), 33. https://doi.org/10.1186/1758-2946-3-33
   PubMed Web of Science ®Google Scholar
• Ornelas-Soares, A., De Lencastre, H., De Jonge, B., & Tomasz, A. (1994). Reduced methicillin resistance in a new Staphylococcus aureus transposon mutant that incorporates muramyl dipeptides into the cell wall peptidoglycan. Journal of Biological Chemistry, 269(44), 27246–27250. https://doi.org/10.1016/S0021-9258(18)46975-X
   PubMed Web of Science ®Google Scholar
• Pandit, S., Dalal, V., & Mishra, G. (2018). Identification of novel phosphatidic acid binding domain on sphingosine kinase 1 of Arabidopsis thaliana. Plant Physiology and Biochemistry: PPB, 128, 178–184. https://doi.org/10.1016/j.plaphy.2018.04.039
   PubMed Web of Science ®Google Scholar
• Panlilio, A. L., Culver, D. H., Gaynes, R. P., Banerjee, S., Henderson, T. S., Tolson, J. S., … System, N. N. I. S. (1992). Methicillin-resistant Staphylococcus aureus in US hospitals, 1975–1991. Infection Control & Hospital Epidemiology, 13(10), 582–586. https://doi.org/10.2307/30148460
   PubMed Web of Science ®Google Scholar
• Parrinello, M., & Rahman, A. (1981). Polymorphic transitions in single crystals: A new molecular dynamics method. Journal of Applied Physics, 52(12), 7182–7190. https://doi.org/10.1063/1.328693
   Web of Science ®Google Scholar
• Peacock, S. J., & Paterson, G. K. (2015). Mechanisms of methicillin resistance in Staphylococcus aureus. Annual Review of Biochemistry, 84, 577–601. https://doi.org/10.1146/annurev-biochem-060614-034516
   PubMed Web of Science ®Google Scholar
• Pinho, M. G., de Lencastre, H., & Tomasz, A. (2001). An acquired and a native penicillin-binding protein cooperate in building the cell wall of drug-resistant staphylococci. Proceedings of the National Academy of Sciences, 98(19), 10886–10891. https://doi.org/10.1073/pnas.191260798
   PubMed Web of Science ®Google Scholar
• Pires, D. E., Blundell, T. L., & Ascher, D. B. (2015). pkCSM: Predicting small-molecule pharmacokinetic and toxicity properties using graph-based signatures. Journal of Medicinal Chemistry, 58(9), 4066–4072. https://doi.org/10.1021/acs.jmedchem.5b00104
   PubMed Web of Science ®Google Scholar
• Release, S. (2016). 2: Maestro. Schrödinger, LLC.
   Google Scholar
• Reynolds, P. E., & Fuller, C. (1986). Methicillin-resistant strains of Staphylococcus aureus; presence of identical additional penicillin-binding protein in all strains examined. FEMS Microbiology Letters, 33(2–3), 251–254. https://doi.org/10.1111/j.1574-6968.1986.tb01281.x
   Web of Science ®Google Scholar
• Saini, G., Dalal, V., Gupta, D. N., Sharma, N., Kumar, P., & Sharma, A. K. (2021). A molecular docking and dynamic approach to screen inhibitors against ZnuA1 of Candidatus Liberibacter asiaticus. Molecular Simulation, 47(6), 510-525. https://doi.org/10.1080/08927022.2021.1888948
   Google Scholar
• Saini, G., Dalal, V., Savita, B. K., Sharma, N., Kumar, P., & Sharma, A. K. (2019). Molecular docking and dynamic approach to virtual screen inhibitors against Esbp of Candidatus Liberibacter asiaticus. Journal of Molecular Graphics & Modelling, 92, 329–340. https://doi.org/10.1016/j.jmgm.2019.08.012
   PubMed Web of Science ®Google Scholar
• Schüttelkopf, A. W., & Van Aalten, D. M. (2004). PRODRG: A tool for high-throughput crystallography of protein–ligand complexes. Acta Crystallographica Section D Biological Crystallography, 60(8), 1355–1363. https://doi.org/10.1107/S0907444904011679
   PubMedGoogle Scholar
• Shopsin, B., Mathema, B., Martinez, J., Ha, E., Campo, M. L., Fierman, A., Krasinski, K., Kornblum, J., Alcabes, P., Waddington, M., Riehman, M., & Kreiswirth, B. N. (2000). Prevalence of methicillin-resistant and methicillin-susceptible Staphylococcus aureus in the community. The Journal of Infectious Diseases, 182(1), 359–362. https://doi.org/10.1086/315695
   PubMed Web of Science ®Google Scholar
• Singh, V., Dhankhar, P., Dalal, V., Tomar, S., & Kumar, P. (2022). In-silico functional and structural annotation of hypothetical protein from Klebsiella pneumonia: A potential drug target. Journal of Molecular Graphics and Modelling, 116, 108262.
   Google Scholar
• Singh, N., Dalal, V., & Kumar, P. (2018). Structure based mimicking of Phthalic acid esters (PAEs) and inhibition of hACMSD, an important enzyme of the tryptophan kynurenine metabolism pathway. International Journal of Biological Macromolecules, 108, 214–224.
   PubMed Web of Science ®Google Scholar
• Singh, N., Dalal, V., & Kumar, P. (2020). Molecular docking and simulation analysis for elucidation of toxic effects of dicyclohexyl phthalate (DCHP) in glucocorticoid receptor-mediated adipogenesis. Molecular Simulation, 46(1), 9–21. https://doi.org/10.1080/08927022.2019.1662002
   Web of Science ®Google Scholar
• Singh, N., Dalal, V., Kumar, V., Sharma, M., & Kumar, P. (2019). Characterization of phthalate reductase from Ralstonia eutropha CH34 and in silico study of phthalate dioxygenase and phthalate reductase interaction. Journal of Molecular Graphics & Modelling, 90, 161–170. https://doi.org/10.1016/j.jmgm.2019.05.002
   PubMed Web of Science ®Google Scholar
• Singh, N., Dalal, V., Mahto, J. K., & Kumar, P. (2017). Biodegradation of phthalic acid esters (PAEs) and in silico structural characterization of mono-2-ethylhexyl phthalate (MEHP) hydrolase on the basis of close structural homolog. Journal of Hazardous Materials, 338, 11–22. https://doi.org/10.1016/j.jhazmat.2017.04.055
   PubMed Web of Science ®Google Scholar
• Suzuki, T., Campbell, J., Swoboda, J. G., Walker, S., & Gilmore, M. S. (2011). Role of wall teichoic acids in Staphylococcus aureus endophthalmitis. Investigative Ophthalmology & Visual Science, 52(6), 3187–3192. https://doi.org/10.1167/iovs.10-6558
   PubMed Web of Science ®Google Scholar
• Tong, S. Y., Davis, J. S., Eichenberger, E., Holland, T. L., & Fowler, V. G. Jr. (2015). Staphylococcus aureus infections: Epidemiology, pathophysiology, clinical manifestations, and management. Clinical Microbiology Reviews, 28(3), 603–661. https://doi.org/10.1128/CMR.00134-14
   PubMed Web of Science ®Google Scholar
• Trott, O., & Olson, A. J. (2010). AutoDock Vina: Improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading. Journal of Computational Chemistry, 31(2), 455–461. https://doi.org/10.1002/jcc.21334
   PubMed Web of Science ®Google Scholar
• Ubukata, K., Nonoguchi, R., Matsuhashi, M., & Konno, M. (1989). Expression and inducibility in Staphylococcus aureus of the mecA gene, which encodes a methicillin-resistant S. aureus-specific penicillin-binding protein. Journal of Bacteriology, 171(5), 2882–2885. https://doi.org/10.1128/jb.171.5.2882-2885.1989
   PubMed Web of Science ®Google Scholar
• Van Der Spoel, D., Lindahl, E., Hess, B., Groenhof, G., Mark, A. E., & Berendsen, H. J. (2005). GROMACS: Fast, flexible, and free. Journal of Computational Chemistry, 26(16), 1701–1718. https://doi.org/10.1002/jcc.20291
   PubMed Web of Science ®Google Scholar
• van Gunsteren, W. F., Billeter, S., Eising, A., Hünenberger, P., Krüger, P., Mark, A., & Tironi, I. (1996). Biomolecular simulation: The GROMOS96 manual and user guide. Vdf Hochschulverlag AG an Der ETH Zürich, Zürich, 86, 1–1044.
   Google Scholar
• Wielders, C. L. C., Vriens, M. R., Brisse, S., de Graaf-Miltenburg, L. A. M., Troelstra, A., Fleer, A., Schmitz, F. J., Verhoef, J., & Fluit, A. C. (2001). Evidence for in-vivo transfer of mecA DNA between strains of Staphylococcus aureus. The Lancet, 357(9269), 1674–1675. https://doi.org/10.1016/S0140-6736(00)04832-7
   PubMed Web of Science ®Google Scholar
• Wu, S., de Lencastre, H., Sali, A., & Tomasz, A. (1996). A phosphoglucomutase-like gene essential for the optimal expression of methicillin resistance in Staphylococcus aureus: Molecular cloning and DNA sequencing. Microbial Drug Resistance (Larchmont, N.Y.), 2(2), 277–286. https://doi.org/10.1089/mdr.1996.2.277
   PubMed Web of Science ®Google Scholar
• Wu, S., de Lencastre, H., & Tomasz, A. (1996). Sigma-B, a putative operon encoding alternate sigma factor of Staphylococcus aureus RNA polymerase: Molecular cloning and DNA sequencing. Journal of Bacteriology, 178(20), 6036–6042. https://doi.org/10.1128/jb.178.20.6036-6042.1996
   PubMed Web of Science ®Google Scholar