Journal articles on the topic 'AgrC'
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Yu, Tao, Xiaojie Jiang, Xiaobo Xu, et al. "Cross-Phosphorylation between AgrC Histidine Kinase and the Noncognate Response Regulator Lmo1172 in Listeria monocytogenes under Benzalkonium Chloride Stress." Microorganisms 12, no. 2 (2024): 392. http://dx.doi.org/10.3390/microorganisms12020392.
Full textZhang, Linsheng, and Guangyong Ji. "Identification of a Staphylococcal AgrB Segment(s) Responsible for Group-Specific Processing of AgrD by Gene Swapping." Journal of Bacteriology 186, no. 20 (2004): 6706–13. http://dx.doi.org/10.1128/jb.186.20.6706-6713.2004.
Full textZhu, Yan-Yan, Qiong Jin, Zhao-Jie Wang, et al. "Tripterhyponoid A from Tripterygium hypoglaucum Inhibiting MRSA by Multiple Mechanisms." Molecules 30, no. 12 (2025): 2539. https://doi.org/10.3390/molecules30122539.
Full textQian, Lijuan, Yuxin He, Wenzhe Lian, et al. "AgrC biotinylation inhibits Staphylococcus aureus infection." PLOS ONE 20, no. 4 (2025): e0318695. https://doi.org/10.1371/journal.pone.0318695.
Full textNiyigaba, Jean, Jessica Ya Sun, Daiyan Peng, and Clemence Uwimbabazi. "Agriculture and Green Economy for Environmental Kuznets Curve Adoption in Developing Countries: Insights from Rwanda." Sustainability 12, no. 24 (2020): 10381. http://dx.doi.org/10.3390/su122410381.
Full textRieu, Aurélie, Stéphanie Weidmann, Dominique Garmyn, Pascal Piveteau, and Jean Guzzo. "agr System of Listeria monocytogenes EGD-e: Role in Adherence and Differential Expression Pattern." Applied and Environmental Microbiology 73, no. 19 (2007): 6125–33. http://dx.doi.org/10.1128/aem.00608-07.
Full textLade, Harshad, Sung Hee Chung, Yeonhee Lee, et al. "Thymol Reduces agr-Mediated Virulence Factor Phenol-Soluble Modulin Production in Staphylococcus aureus." BioMed Research International 2022 (May 9, 2022): 1–14. http://dx.doi.org/10.1155/2022/8221622.
Full textMcNamara, Peter J., and John J. Iandolo. "Genetic Instability of the Global Regulator agrExplains the Phenotype of the xpr Mutation inStaphylococcus aureus KSI9051." Journal of Bacteriology 180, no. 10 (1998): 2609–15. http://dx.doi.org/10.1128/jb.180.10.2609-2615.1998.
Full textvan Leeuwen, Willem, Wendy van Nieuwenhuizen, Christel Gijzen, Henri Verbrugh, and Alex van Belkum. "Population Studies of Methicillin-Resistant and -Sensitive Staphylococcus aureus Strains Reveal a Lack of Variability in the agrD Gene, Encoding a Staphylococcal Autoinducer Peptide." Journal of Bacteriology 182, no. 20 (2000): 5721–29. http://dx.doi.org/10.1128/jb.182.20.5721-5729.2000.
Full textSung, Julia M. L., Peter D. Chantler, and David H. Lloyd. "Accessory Gene Regulator Locus of Staphylococcus intermedius." Infection and Immunity 74, no. 5 (2006): 2947–56. http://dx.doi.org/10.1128/iai.74.5.2947-2956.2006.
Full textXie, Qian, Mareike M. Wiedmann, Aishan Zhao, et al. "Discovery of quorum quenchers targeting the membrane-embedded sensor domain of the Staphylococcus aureus receptor histidine kinase, AgrC." Chemical Communications 56, no. 76 (2020): 11223–26. http://dx.doi.org/10.1039/d0cc04873a.
Full textSomerville, Greg A., Stephen B. Beres, J. Ross Fitzgerald, et al. "In Vitro Serial Passage of Staphylococcus aureus: Changes in Physiology, Virulence Factor Production, and agr Nucleotide Sequence." Journal of Bacteriology 184, no. 5 (2002): 1430–37. http://dx.doi.org/10.1128/jb.184.5.1430-1437.2002.
Full textSrivastava, S. K., K. Rajasree, A. Fasim, G. Arakere, and B. Gopal. "Influence of the AgrC-AgrA Complex on the Response Time of Staphylococcus aureus Quorum Sensing." Journal of Bacteriology 196, no. 15 (2014): 2876–88. http://dx.doi.org/10.1128/jb.01530-14.
Full textWang, Li, Lin Qiao, Aike Li, et al. "Integrative Multiomics Analysis of the Heat Stress Response of Enterococcus faecium." Biomolecules 13, no. 3 (2023): 437. http://dx.doi.org/10.3390/biom13030437.
Full textWang, Lina, Chunshan Quan, Yongbin Xu, Xihui Li, Xiaojing Qu, and Shengdi Fan. "Construction of AgrC Proteoliposomes by Detergent-Mediated Method." Acta Chimica Sinica 72, no. 2 (2014): 233. http://dx.doi.org/10.6023/a13111123.
Full textJordani, Bárbara, Francisco Roger Carneiro Ribeiro, Valéria Costa de Oliveira, and Rodrigo Cesar Pierozan. "Efeito da saturação do agregado graúdo reciclado na resistência mecânica e durabilidade do concreto." Revista de Arquitetura IMED 13, no. 1 (2024): 70. https://doi.org/10.18256/2318-1109.2024.v13i1.5067.
Full textAllocca, V., F. Manna, and P. De Vita. "Estimating annual groundwater recharge coefficient for karst aquifers of the southern Apennines (Italy)." Hydrology and Earth System Sciences 18, no. 2 (2014): 803–17. http://dx.doi.org/10.5194/hess-18-803-2014.
Full textJarraud, S., G. J. Lyon, A. M. S. Figueiredo, et al. "Exfoliatin-Producing Strains Define a Fourthagr Specificity Group in Staphylococcus aureus." Journal of Bacteriology 182, no. 22 (2000): 6517–22. http://dx.doi.org/10.1128/jb.182.22.6517-6522.2000.
Full textZhang, Liying, Chunshan Quan, Xuning Zhang, Wen Xiong, and Shengdi Fan. "Proteoliposome‐based model for screening inhibitors targeting histidine kinase AgrC." Chemical Biology & Drug Design 93, no. 5 (2019): 712–23. http://dx.doi.org/10.1111/cbdd.13497.
Full textSteiner, Elisabeth, Jamie Scott, Nigel P. Minton, and Klaus Winzer. "AnagrQuorum Sensing System That Regulates Granulose Formation and Sporulation in Clostridium acetobutylicum." Applied and Environmental Microbiology 78, no. 4 (2011): 1113–22. http://dx.doi.org/10.1128/aem.06376-11.
Full textGeorge Cisar, Elizabeth A., Edward Geisinger, Tom W. Muir, and Richard P. Novick. "Symmetric signalling within asymmetric dimers of theStaphylococcus aureusreceptor histidine kinase AgrC." Molecular Microbiology 74, no. 1 (2009): 44–57. http://dx.doi.org/10.1111/j.1365-2958.2009.06849.x.
Full textWang, Lina, Chunshan Quan, Wen Xiong, Xiaojing Qu, Shengdi Fan, and Wenzhong Hu. "New insight into transmembrane topology of Staphylococcus aureus histidine kinase AgrC." Biochimica et Biophysica Acta (BBA) - Biomembranes 1838, no. 3 (2014): 988–93. http://dx.doi.org/10.1016/j.bbamem.2013.12.006.
Full textGeisinger, Edward, Elizabeth A. George, John Chen, Tom W. Muir, and Richard P. Novick. "Identification of ligand specificity determinants in AgrC, theStaphylococcus aureusquorum-sensing receptor." Journal of Biological Chemistry 287, no. 22 (2012): 18588. http://dx.doi.org/10.1074/jbc.a112.710227.
Full textGeisinger, Edward, Elizabeth A. George, Tom W. Muir, and Richard P. Novick. "Identification of Ligand Specificity Determinants in AgrC, theStaphylococcus aureusQuorum-sensing Receptor." Journal of Biological Chemistry 283, no. 14 (2008): 8930–38. http://dx.doi.org/10.1074/jbc.m710227200.
Full textLi, Wei, Xiaoyu Ma, Yumin Chen, et al. "Random Fuzzy Granular Decision Tree." Mathematical Problems in Engineering 2021 (June 9, 2021): 1–17. http://dx.doi.org/10.1155/2021/5578682.
Full textWang, Boyuan, Aishan Zhao, Qian Xie, et al. "Functional Plasticity of the AgrC Receptor Histidine Kinase Required for Staphylococcal Virulence." Cell Chemical Biology 24, no. 1 (2017): 76–86. http://dx.doi.org/10.1016/j.chembiol.2016.12.008.
Full textAL-Sabaawy, Abeer Mahmood, Enas Abdul-muniem., AL-Layla, and Omar Ibrahim AL-Sabaawy. "Detection of bacterial infection of the eye chalazion in Mosul City." Science Archives 03, no. 04 (2022): 240–46. http://dx.doi.org/10.47587/sa.2022.3401.
Full textLina, Gerard, Sophie Jarraud, Guangyong Ji, et al. "Transmembrane topology and histidine protein kinase activity of AgrC, theagrsignal receptor inStaphylococcus aureus." Molecular Microbiology 28, no. 3 (1998): 655–62. http://dx.doi.org/10.1046/j.1365-2958.1998.00830.x.
Full textGreen, Macauley J., Ewan J. Murray, Paul Williams, Amir M. Ghaemmaghami, Jonathan W. Aylott, and Philip M. Williams. "Modelled-Microgravity Reduces Virulence Factor Production in Staphylococcus aureus through Downregulation of agr-Dependent Quorum Sensing." International Journal of Molecular Sciences 24, no. 21 (2023): 15997. http://dx.doi.org/10.3390/ijms242115997.
Full textQin, Xiang, Kavindra V. Singh, George M. Weinstock, and Barbara E. Murray. "Effects of Enterococcus faecalis fsrGenes on Production of Gelatinase and a Serine Protease and Virulence." Infection and Immunity 68, no. 5 (2000): 2579–86. http://dx.doi.org/10.1128/iai.68.5.2579-2586.2000.
Full textOliveira, Edenis Cesar. "Influência da variável ambiental no processo de escolha dos fornecedores: Um Estudo em Agroindústrias da Microrregião de Assis-SP." Revista Produção e Desenvolvimento 2, no. 2 (2016): 77–100. http://dx.doi.org/10.32358/rpd.2016.v2.117.
Full textXiang, Bingquan, Yujie Lei, Ya Chen, et al. "Mechanistic study on the inhibition of Staphylococcus epidermidis biofilm by agrC-specific binding polypeptide." Annals of Translational Medicine 8, no. 6 (2020): 337. http://dx.doi.org/10.21037/atm.2020.02.84.
Full textWang, Lina, Chunshan Quan, Baoquan Liu, et al. "Functional Reconstitution of Staphylococcus aureus Truncated AgrC Histidine Kinase in a Model Membrane System." PLoS ONE 8, no. 11 (2013): e80400. http://dx.doi.org/10.1371/journal.pone.0080400.
Full textHuang, Qian, Yihui Xie, Ziyu Yang, et al. "The cytoplasmic loops of AgrC contribute to the quorum-sensing activity of Staphylococcus aureus." Journal of Microbiology 59, no. 1 (2020): 92–100. http://dx.doi.org/10.1007/s12275-021-0274-x.
Full textDmitrenko, Olga, Andrey Chaplin, Anna Balbutskaya, Tamara Pkhakadze, and Sergey Alkhovsky. "In Silico Genome-Scale Analysis of Molecular Mechanisms Contributing to the Development of a Persistent Infection with Methicillin-Resistant Staphylococcus aureus (MRSA) ST239." International Journal of Molecular Sciences 23, no. 24 (2022): 16086. http://dx.doi.org/10.3390/ijms232416086.
Full textYang, Tian, Yftah Tal-Gan, Alexandra E. Paharik, Alexander R. Horswill, and Helen E. Blackwell. "Structure–Function Analyses of aStaphylococcus epidermidisAutoinducing Peptide Reveals Motifs Critical for AgrC-type Receptor Modulation." ACS Chemical Biology 11, no. 7 (2016): 1982–91. http://dx.doi.org/10.1021/acschembio.6b00120.
Full textChan, Weng C., Barry J. Coyle, and Paul Williams. "Virulence Regulation and Quorum Sensing in Staphylococcal Infections: Competitive AgrC Antagonists as Quorum Sensing Inhibitors§." Journal of Medicinal Chemistry 47, no. 19 (2004): 4633–41. http://dx.doi.org/10.1021/jm0400754.
Full textWang, Boyuan, Aishan Zhao, Richard P. Novick, and Tom W. Muir. "Activation and Inhibition of the Receptor Histidine Kinase AgrC Occurs through Opposite Helical Transduction Motions." Molecular Cell 53, no. 6 (2014): 929–40. http://dx.doi.org/10.1016/j.molcel.2014.02.029.
Full textHansen, Anna Mette, Pai Peng, Mara Baldry, et al. "Lactam hybrid analogues of solonamide B and autoinducing peptides as potent S. aureus AgrC antagonists." European Journal of Medicinal Chemistry 152 (May 2018): 370–76. http://dx.doi.org/10.1016/j.ejmech.2018.04.053.
Full textSpiegel, Christopher, Stephan Josef Maria Steixner, and Débora C. Coraça-Huber. "Antibiofilm Activity of Omega-3 Fatty Acids and Its Influence on the Expression of Biofilm Formation Genes on Staphylococcus aureus." Antibiotics 11, no. 7 (2022): 932. http://dx.doi.org/10.3390/antibiotics11070932.
Full textQazi, Saara, Barry Middleton, Siti Hanna Muharram, et al. "N-Acylhomoserine Lactones Antagonize Virulence Gene Expression and Quorum Sensing in Staphylococcus aureus." Infection and Immunity 74, no. 2 (2006): 910–19. http://dx.doi.org/10.1128/iai.74.2.910-919.2006.
Full textVasquez, Joseph K., and Helen E. Blackwell. "Simplified Autoinducing Peptide Mimetics with Single-Nanomolar Activity Against the Staphylococcus aureus AgrC Quorum Sensing Receptor." ACS Infectious Diseases 5, no. 4 (2019): 484–92. http://dx.doi.org/10.1021/acsinfecdis.9b00002.
Full textZorzet, A., J. M. Andersen, A. I. Nilsson, N. F. Moller, and D. I. Andersson. "Compensatory mutations in agrC partly restore fitness in vitro to peptide deformylase inhibitor-resistant Staphylococcus aureus." Journal of Antimicrobial Chemotherapy 67, no. 8 (2012): 1835–42. http://dx.doi.org/10.1093/jac/dks168.
Full textTal-Gan, Yftah, Monika Ivancic, Gabriel Cornilescu, Tian Yang, and Helen E. Blackwell. "Highly Stable, Amide-Bridged Autoinducing Peptide Analogues that Strongly Inhibit the AgrC Quorum Sensing Receptor inStaphylococcus aureus." Angewandte Chemie International Edition 55, no. 31 (2016): 8913–17. http://dx.doi.org/10.1002/anie.201602974.
Full textTal-Gan, Yftah, Monika Ivancic, Gabriel Cornilescu, Tian Yang, and Helen E. Blackwell. "Highly Stable, Amide-Bridged Autoinducing Peptide Analogues that Strongly Inhibit the AgrC Quorum Sensing Receptor inStaphylococcus aureus." Angewandte Chemie 128, no. 31 (2016): 9059–63. http://dx.doi.org/10.1002/ange.201602974.
Full textBotelho, Ana M. N., Maiana O. C. Costa, Cristiana O. Beltrame, et al. "Complete Genome Sequence of the MRSA Isolate HC1335 from ST239 Lineage Displaying a Truncated AgrC Histidine Kinase Receptor." Genome Biology and Evolution 8, no. 10 (2016): 3187–92. http://dx.doi.org/10.1093/gbe/evw225.
Full textBroderick, Adam H., Danielle M. Stacy, Yftah Tal-Gan, Michael J. Kratochvil, Helen E. Blackwell, and David M. Lynn. "Surface Coatings that Promote Rapid Release of Peptide-Based AgrC Inhibitors for Attenuation of Quorum Sensing inStaphylococcus aureus." Advanced Healthcare Materials 3, no. 1 (2013): 97–105. http://dx.doi.org/10.1002/adhm.201300119.
Full textWang, Boyuan, Aishan Zhao, Richard P. Novick, and Tom W. Muir. "Key driving forces in the biosynthesis of autoinducing peptides required for staphylococcal virulence." Proceedings of the National Academy of Sciences 112, no. 34 (2015): 10679–84. http://dx.doi.org/10.1073/pnas.1506030112.
Full textWang, Lina, Chunshan Quan, Baoquan Liu, et al. "Green Fluorescent Protein (GFP)-Based Overexpression Screening and Characterization of AgrC, a Receptor Protein of Quorum Sensing in Staphylococcus aureus." International Journal of Molecular Sciences 14, no. 9 (2013): 18470–87. http://dx.doi.org/10.3390/ijms140918470.
Full textLiu, Jianan, Jinle Ma, Yingrui Wang, et al. "Synergistic Antibacterial Mechanism of Benzyl Isothiocyanate and Resveratrol Against Staphylococcus aureus Revealed by Transcriptomic Analysis and Their Application in Beef." Foods 14, no. 9 (2025): 1610. https://doi.org/10.3390/foods14091610.
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