Academic literature on the topic 'OMP biogenesis'
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Journal articles on the topic "OMP biogenesis"
Costello, Shawn M., Ashlee M. Plummer, Patrick J. Fleming, and Karen G. Fleming. "Dynamic periplasmic chaperone reservoir facilitates biogenesis of outer membrane proteins." Proceedings of the National Academy of Sciences 113, no. 33 (August 1, 2016): E4794—E4800. http://dx.doi.org/10.1073/pnas.1601002113.
Full textAlbrecht, Reinhard, Monika Schütz, Philipp Oberhettinger, Michaela Faulstich, Ivan Bermejo, Thomas Rudel, Kay Diederichs, and Kornelius Zeth. "Structure of BamA, an essential factor in outer membrane protein biogenesis." Acta Crystallographica Section D Biological Crystallography 70, no. 6 (May 30, 2014): 1779–89. http://dx.doi.org/10.1107/s1399004714007482.
Full textKonovalova, Anna, Marcin Grabowicz, Carl J. Balibar, Juliana C. Malinverni, Ronald E. Painter, Daniel Riley, Paul A. Mann, et al. "Inhibitor of intramembrane protease RseP blocks the σE response causing lethal accumulation of unfolded outer membrane proteins." Proceedings of the National Academy of Sciences 115, no. 28 (June 25, 2018): E6614—E6621. http://dx.doi.org/10.1073/pnas.1806107115.
Full textVolokhina, Elena B., Frank Beckers, Jan Tommassen, and Martine P. Bos. "The β-Barrel Outer Membrane Protein Assembly Complex of Neisseria meningitidis." Journal of Bacteriology 191, no. 22 (September 18, 2009): 7074–85. http://dx.doi.org/10.1128/jb.00737-09.
Full textHart, Elizabeth M., Angela M. Mitchell, Anna Konovalova, Marcin Grabowicz, Jessica Sheng, Xiaoqing Han, Frances P. Rodriguez-Rivera, et al. "A small-molecule inhibitor of BamA impervious to efflux and the outer membrane permeability barrier." Proceedings of the National Academy of Sciences 116, no. 43 (October 7, 2019): 21748–57. http://dx.doi.org/10.1073/pnas.1912345116.
Full textHorne, Jim E., and Sheena E. Radford. "A growing toolbox of techniques for studying β-barrel outer membrane protein folding and biogenesis." Biochemical Society Transactions 44, no. 3 (June 9, 2016): 802–9. http://dx.doi.org/10.1042/bst20160020.
Full textWeirich, Johanna, Cornelia Bräutigam, Melanie Mühlenkamp, Mirita Franz-Wachtel, Boris Macek, Ina Meuskens, Mikael Skurnik, et al. "Identifying components required for OMP biogenesis as novel targets for antiinfective drugs." Virulence 8, no. 7 (February 6, 2017): 1170–88. http://dx.doi.org/10.1080/21505594.2016.1278333.
Full textTata, Muralidhar, Santosh Kumar, Sarah R. Lach, Shreya Saha, Elizabeth M. Hart, and Anna Konovalova. "High-throughput suppressor screen demonstrates that RcsF monitors outer membrane integrity and not Bam complex function." Proceedings of the National Academy of Sciences 118, no. 32 (August 4, 2021): e2100369118. http://dx.doi.org/10.1073/pnas.2100369118.
Full textSoltes, Garner R., Jaclyn Schwalm, Dante P. Ricci, and Thomas J. Silhavy. "The Activity of Escherichia coli Chaperone SurA Is Regulated by Conformational Changes Involving a Parvulin Domain." Journal of Bacteriology 198, no. 6 (January 4, 2016): 921–29. http://dx.doi.org/10.1128/jb.00889-15.
Full textMarx, Dagan C., Ashlee M. Plummer, Anneliese M. Faustino, Taylor Devlin, Michaela A. Roskopf, Mathis J. Leblanc, Henry J. Lessen, et al. "SurA is a cryptically grooved chaperone that expands unfolded outer membrane proteins." Proceedings of the National Academy of Sciences 117, no. 45 (October 22, 2020): 28026–35. http://dx.doi.org/10.1073/pnas.2008175117.
Full textDissertations / Theses on the topic "OMP biogenesis"
Namdari, Fatémeh. "Caractérisation fonctionnelle de BamB, protéine impliquée dans la biogénèse de la membrane externe et la virulence de Salmonella." Thesis, Tours, 2013. http://www.theses.fr/2013TOUR4005/document.
Full textBamB is an outer-membrane lipoprotein belonging to the BAM complex (β-Barrel Assembly Machinery). In Salmonella, it is involved in the assembly of outer membrane proteins (OMP), in antibiotic susceptibility, in the transcriptional control of the three Type-Three-Secretion-Systems (T3SS) related genes and also in virulence. In E. coli, BamB interacts directly with the BamA protein. Moreover, BamB has been shown to have a serine-threonin kinase activity in this bacterium. In order to better characterize the roles of the BamB protein, our purposes were to study (1) the impact of the alteration of the interaction of BamB with the BAM complex or of its cytoplasmic sequestration and (2) its putative kinase activity in Salmonella. Our results show that some of the BamB roles are dissociable and that the BamA/BamB interaction is not required for T3SS expression, Salmonella virulence or OMP assembly in the outer membrane. Currently, neither a kinase activity nor a cytoplasmic activity has been clearly demonstrated for this protein
Book chapters on the topic "OMP biogenesis"
Bodelón, Gustavo, Elvira Marín, and Luis Ángel Fernández. "Analyzing the Role of Periplasmic Folding Factors in the Biogenesis of OMPs and Members of the Type V Secretion System." In Methods in Molecular Biology, 77–110. New York, NY: Springer New York, 2015. http://dx.doi.org/10.1007/978-1-4939-2871-2_7.
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