Journal articles on the topic 'Anti–σ factor Interactions'
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Jamithireddy, Anil Kumar, Ashish Runthala та Balasubramanian Gopal. "Evaluation of specificity determinants in Mycobacterium tuberculosis σ/anti-σ factor interactions". Biochemical and Biophysical Research Communications 521, № 4 (2020): 900–906. http://dx.doi.org/10.1016/j.bbrc.2019.10.198.
Full textShukla, Jinal, Radhika Gupta, Krishan Gopal Thakur, Rajesh Gokhale та B. Gopal. "Structural basis for the redox sensitivity of theMycobacterium tuberculosisSigK–RskA σ–anti-σ complex". Acta Crystallographica Section D Biological Crystallography 70, № 4 (2014): 1026–36. http://dx.doi.org/10.1107/s1399004714000121.
Full textKwak, Min-Kyu, Han-Bong Ryu, Sung-Hyun Song, Jin-Won Lee та Sa-Ouk Kang. "Anti-σ factor YlaD regulates transcriptional activity of σ factor YlaC and sporulation via manganese-dependent redox-sensing molecular switch in Bacillus subtilis". Biochemical Journal 475, № 13 (2018): 2127–51. http://dx.doi.org/10.1042/bcj20170911.
Full textAnthony, Jennifer R., Jack D. Newman та Timothy J. Donohue. "Interactions Between the Rhodobacter sphaeroides ECF Sigma Factor, σ E , and its Anti-sigma Factor, ChrR". Journal of Molecular Biology 341, № 2 (2004): 345–60. http://dx.doi.org/10.1016/j.jmb.2004.06.018.
Full textWettstadt, Sarah, Francisco J. Marcos-Torres, Joaquín R. Otero-Asman, Alicia García-Puente, Álvaro Ortega та María A. Llamas. "Bacterial TonB-dependent transducers interact with the anti-σ factor in absence of the inducing signal protecting it from proteolysis". PLOS Biology 22, № 12 (2024): e3002920. https://doi.org/10.1371/journal.pbio.3002920.
Full textCartagena, Alexis Jaramillo, Amy B. Banta, Nikhil Sathyan та ін. "Structural basis for transcription activation by Crl through tethering of σS and RNA polymerase". Proceedings of the National Academy of Sciences 116, № 38 (2019): 18923–27. http://dx.doi.org/10.1073/pnas.1910827116.
Full textThakur, Krishan Gopal, Anagha Madhusudan Joshi та B. Gopal. "Structural and Biophysical Studies on Two Promoter Recognition Domains of the Extra-cytoplasmic Function σ Factor σC from Mycobacterium tuberculosis". Journal of Biological Chemistry 282, № 7 (2006): 4711–18. http://dx.doi.org/10.1074/jbc.m606283200.
Full textKarlinsey, Joyce E., and Kelly T. Hughes. "Genetic Transplantation: Salmonella enterica Serovar Typhimurium as a Host To Study Sigma Factor and Anti-Sigma Factor Interactions in GeneticallyIntractable Systems." Journal of Bacteriology 188, no. 1 (2006): 103–14. http://dx.doi.org/10.1128/jb.188.1.103-114.2006.
Full textCavaliere, Paola, та Françoise Norel. "Recent advances in the characterization of Crl, the unconventional activator of the stress sigma factor σS/RpoS". Biomolecular Concepts 7, № 3 (2016): 197–204. http://dx.doi.org/10.1515/bmc-2016-0006.
Full textHo, Khang, та Rasika M. Harshey. "Membrane-associated σ factors disrupt rRNA operon clustering in Escherichia coli". PLOS Biology 23, № 4 (2025): e3003113. https://doi.org/10.1371/journal.pbio.3003113.
Full textTamizi, Amin-Asyraf, Norliza Abu-Bakar, Aimera-Farhana Samsuddin, Lina Rozano, Rohaiza Ahmad-Redzuan, and Abdul-Munir Abdul-Murad. "Characterisation and Mutagenesis Study of An Alternative Sigma Factor Gene (hrpL) from Erwinia mallotivora Reveal Its Central Role in Papaya Dieback Disease." Biology 9, no. 10 (2020): 323. http://dx.doi.org/10.3390/biology9100323.
Full textPaul, Deborupa, and Sanmitra Ghosh. "An overview of heat-stress response regulation in Gram-negative bacteria considering Escherichia coli as a model organism." Journal of Experimental Biology and Agricultural Sciences 10, no. 1 (2022): 190–200. http://dx.doi.org/10.18006/2022.10(1).190.200.
Full textRédly, Gyula Alan, and Keith Poole. "FpvIR Control of fpvA Ferric Pyoverdine Receptor Gene Expression in Pseudomonas aeruginosa: Demonstration of an Interaction between FpvI and FpvR and Identification of Mutations in Each Compromising This Interaction." Journal of Bacteriology 187, no. 16 (2005): 5648–57. http://dx.doi.org/10.1128/jb.187.16.5648-5657.2005.
Full textDelumeau, Olivier, Richard J. Lewis та Michael D. Yudkin. "Protein-Protein Interactions That Regulate the Energy Stress Activation of σB in Bacillus subtilis". Journal of Bacteriology 184, № 20 (2002): 5583–89. http://dx.doi.org/10.1128/jb.184.20.5583-5589.2002.
Full textNambigari, Navaneetha. "Cancer Therapeutics: Structure-Based Drug Design of Inhibitors for a Novel Angiogenic Growth Factor." Mathematical Biology and Bioinformatics 18, no. 1 (2023): 72–88. http://dx.doi.org/10.17537/2023.18.72.
Full textDehbi, Mohammed, Gregory Moeck, Francis F. Arhin, et al. "Inhibition of Transcription in Staphylococcus aureus by a Primary Sigma Factor-Binding Polypeptide from Phage G1." Journal of Bacteriology 191, no. 12 (2009): 3763–71. http://dx.doi.org/10.1128/jb.00241-09.
Full textGriffiths-Jones, D., Y. Sylvestre Garcia, D. Ryder, et al. "POS0850 A PHASE II RANDOMISED CONTROLLED TRIAL OF ORAL PREDNISOLONE IN EARLY DIFFUSE CUTANEOUS SYSTEMIC SCLEROSIS (PRedSS)." Annals of the Rheumatic Diseases 81, Suppl 1 (2022): 717.2–718. http://dx.doi.org/10.1136/annrheumdis-2022-eular.694.
Full textMcGuffie, Bryan A., Isabelle Vallet-Gely та Simon L. Dove. "σ Factor and Anti-σ Factor That Control Swarming Motility and Biofilm Formation in Pseudomonas aeruginosa". Journal of Bacteriology 198, № 5 (2015): 755–65. http://dx.doi.org/10.1128/jb.00784-15.
Full textCampbell, Elizabeth A., Shoko Masuda, Jing L. Sun та ін. "Crystal Structure of the Bacillus stearothermophilus Anti-σ Factor SpoIIAB with the Sporulation σ Factor σF". Cell 108, № 6 (2002): 795–807. http://dx.doi.org/10.1016/s0092-8674(02)00662-1.
Full textMaillard, Antoine P., Eric Girard, Widade Ziani, Isabelle Petit-Härtlein, Richard Kahn та Jacques Covès. "The Crystal Structure of the Anti-σ Factor CnrY in Complex with the σ Factor CnrH Shows a New Structural Class of Anti-σ Factors Targeting Extracytoplasmic Function σ Factors". Journal of Molecular Biology 426, № 12 (2014): 2313–27. http://dx.doi.org/10.1016/j.jmb.2014.04.003.
Full textLachowicz, Mirosław, Henryk Leszczyński, and Elżbieta Puźniakowska–Gałuch. "Diffusive and Anti-Diffusive Behavior for Kinetic Models of Opinion Dynamics." Symmetry 11, no. 8 (2019): 1024. http://dx.doi.org/10.3390/sym11081024.
Full textWerstiuk, Nick Henry, та Jiangong Ma. "An AM1 calculational study of the Diels–Alder addition of maleic anhydride to C5-substituted pentamethylcyclopentadienes and 2,5-dimethylthiophene oxide. An attempt to ascertain the factors controlling the π-facial selectivities and relative reactivities". Canadian Journal of Chemistry 72, № 12 (1994): 2493–505. http://dx.doi.org/10.1139/v94-316.
Full textYamato, Takehiko, Hideo Kamimura, and Hirohisa Tsuzuki. "ipso-Nitration of tert-butyl[n.2]metacyclophanes; through-space electronic interactions between two benzene rings." Canadian Journal of Chemistry 76, no. 7 (1998): 997–1005. http://dx.doi.org/10.1139/v98-111.
Full textPaudel, Hari Ram, Lucas José Karas та Judy I.-Chia Wu. "On the reciprocal relationship between σ-hole bonding and (anti)aromaticity gain in ketocyclopolyenes". Organic & Biomolecular Chemistry 18, № 27 (2020): 5125–29. http://dx.doi.org/10.1039/d0ob01076f.
Full textSorenson, Margareta K., Soumya S. Ray та Seth A. Darst. "Crystal Structure of the Flagellar σ/Anti-σ Complex σ28/FlgM Reveals an Intact σ Factor in an Inactive Conformation". Molecular Cell 14, № 1 (2004): 127–38. http://dx.doi.org/10.1016/s1097-2765(04)00150-9.
Full textHubin, Elizabeth A., Aline Tabib-Salazar, Laurence J. Humphrey, et al. "Structural, functional, and genetic analyses of the actinobacterial transcription factor RbpA." Proceedings of the National Academy of Sciences 112, no. 23 (2015): 7171–76. http://dx.doi.org/10.1073/pnas.1504942112.
Full textCampbell, Elizabeth A., та Seth A. Darst. "The anti-σ factor SpoIIAB forms a 2:1 complex with σF, contacting multiple conserved regions of the σ factor". Journal of Molecular Biology 300, № 1 (2000): 17–28. http://dx.doi.org/10.1006/jmbi.2000.3838.
Full textMasuda, Shoko, Katsuhiko S. Murakami, Sheng Wang та ін. "Crystal Structures of the ADP and ATP Bound Forms of the Bacillus Anti-σ Factor SpoIIAB in Complex with the Anti-anti-σ SpoIIAA". Journal of Molecular Biology 340, № 5 (2004): 941–56. http://dx.doi.org/10.1016/j.jmb.2004.05.040.
Full textLedermann, Raphael, Ilka Bartsch, Barbara Müller, Janine Wülser, and Hans-Martin Fischer. "A Functional General Stress Response of Bradyrhizobium diazoefficiens Is Required for Early Stages of Host Plant Infection." Molecular Plant-Microbe Interactions® 31, no. 5 (2018): 537–47. http://dx.doi.org/10.1094/mpmi-11-17-0284-r.
Full textWeinhold, Frank. "Anti-Electrostatic Pi-Hole Bonding: How Covalency Conquers Coulombics." Molecules 27, no. 2 (2022): 377. http://dx.doi.org/10.3390/molecules27020377.
Full textKodgire, Prashant, and K. Krishnamurthy Rao. "hag expression in Bacillus subtilis is both negatively and positively regulated by ScoC." Microbiology 155, no. 1 (2009): 142–49. http://dx.doi.org/10.1099/mic.0.021899-0.
Full textGuzina, Jelena, та Marko Djordjevic. "Promoter Recognition by Extracytoplasmic Function σ Factors: Analyzing DNA and Protein Interaction Motifs". Journal of Bacteriology 198, № 14 (2016): 1927–38. http://dx.doi.org/10.1128/jb.00244-16.
Full textHo, Theresa D., та Craig D. Ellermeier. "PrsW Is Required for Colonization, Resistance to Antimicrobial Peptides, and Expression of Extracytoplasmic Function σ Factors in Clostridium difficile". Infection and Immunity 79, № 8 (2011): 3229–38. http://dx.doi.org/10.1128/iai.00019-11.
Full textKallifidas, Dimitris, Derek Thomas, Phillip Doughty та Mark S. B. Paget. "The σ R regulon of Streptomyces coelicolor A3(2) reveals a key role in protein quality control during disulphide stress". Microbiology 156, № 6 (2010): 1661–72. http://dx.doi.org/10.1099/mic.0.037804-0.
Full textROBERTS, H. L. L., L. CHANG, and C. D. ROBERTS. "IMPACT OF DYNAMICAL CHIRAL SYMMETRY BREAKING ON MESON STRUCTURE AND INTERACTIONS." International Journal of Modern Physics A 26, no. 03n04 (2011): 371–77. http://dx.doi.org/10.1142/s0217751x11051688.
Full textMeng, Ying, and Qiman Liu. "New Insights into Adsorption Properties of the Tubular Au26 from AIMD Simulations and Electronic Interactions." Molecules 28, no. 7 (2023): 2916. http://dx.doi.org/10.3390/molecules28072916.
Full textStockwell, S. B., L. Reutimann, and M. L. Guerinot. "A Role for Bradyrhizobium japonicum ECF16 Sigma Factor EcfS in the Formation of a Functional Symbiosis with Soybean." Molecular Plant-Microbe Interactions® 25, no. 1 (2012): 119–28. http://dx.doi.org/10.1094/mpmi-07-11-0188.
Full textHastie, Jessica L., Kyle B. Williams, Carolina Sepúlveda, Jon C. Houtman, Katrina T. Forest та Craig D. Ellermeier. "Evidence of a Bacterial Receptor for Lysozyme: Binding of Lysozyme to the Anti-σ Factor RsiV Controls Activation of the ECF σ Factor σV". PLoS Genetics 10, № 10 (2014): e1004643. http://dx.doi.org/10.1371/journal.pgen.1004643.
Full textBeaucher, Jocelyn, Sébastien Rodrigue, Pierre-Étienne Jacques, Issar Smith, Ryszard Brzezinski та Luc Gaudreau. "Novel Mycobacterium tuberculosis anti-σ factor antagonists control σF activity by distinct mechanisms". Molecular Microbiology 45, № 6 (2002): 1527–40. http://dx.doi.org/10.1046/j.1365-2958.2002.03135.x.
Full textLuebke, Justin L., Daniel S. Eaton, Joseph R. Sachleben та Sean Crosson. "Allosteric control of a bacterial stress response system by an anti-σ factor". Molecular Microbiology 107, № 2 (2017): 164–79. http://dx.doi.org/10.1111/mmi.13868.
Full textAldridge, Phillip, Joyce E. Karlinsey, Eric Becker, Fabienne F. V. Chevance та Kelly T. Hughes. "Flk prevents premature secretion of the anti-σ factor FlgM into the periplasm". Molecular Microbiology 61, № 1 (2006): 269. http://dx.doi.org/10.1111/j.1365-2958.2006.05201.x.
Full textWecke, Tina, Birgit Veith, Armin Ehrenreich, and Thorsten Mascher. "Cell Envelope Stress Response in Bacillus licheniformis: Integrating Comparative Genomics, Transcriptional Profiling, and Regulon Mining To Decipher a Complex Regulatory Network." Journal of Bacteriology 188, no. 21 (2006): 7500–7511. http://dx.doi.org/10.1128/jb.01110-06.
Full textZavodovsky, B. V., Yu R. Akhverdyan, E. V. Papichev, Yu V. Polyakova, and L. E. Sivordova. "Relationship between the level of antibodies to the RA-33 antigen and the course of rheumatoid arthritis." YAKUT MEDICAL JOURNAL 88, no. 4 (2024): 9–12. https://doi.org/10.25789/ymj.2024.88.02.
Full textFang, Chengli, Lingting Li, Liqiang Shen, et al. "Structures and mechanism of transcription initiation by bacterial ECF factors." Nucleic Acids Research 47, no. 13 (2019): 7094–104. http://dx.doi.org/10.1093/nar/gkz470.
Full textKim, Yunok, Jaeseung Yoo, Donghyuk Jang, et al. "Further utilization of a Mn redox reaction via control of structural disorder in olivine systems." Journal of Materials Chemistry A 6, no. 28 (2018): 13743–50. http://dx.doi.org/10.1039/c8ta03631d.
Full textAlhadlaq, Meshari Ahmed, Jeffrey Green, and Bassam K. Kudhair. "Analysis of Kytococcus sedentarius Strain Isolated from a Dehumidifier Operating in a University Lecture Theatre: Systems for Aerobic Respiration, Resisting Osmotic Stress, and Sensing Nitric Oxide." Microbial Physiology 31, no. 2 (2021): 135–45. http://dx.doi.org/10.1159/000512751.
Full textBanerjee, Rajdeep, Paulami Rudra, Abinit Saha, and Jayanta Mukhopadhyay. "Recombinant Reporter Assay Using Transcriptional Machinery of Mycobacterium tuberculosis." Journal of Bacteriology 197, no. 3 (2014): 646–53. http://dx.doi.org/10.1128/jb.02445-14.
Full textVIOLA, MARIA GRAZIA. "ON A SUBFACTOR CONSTRUCTION OF A FACTOR NON-ANTIISOMORPHIC TO ITSELF." International Journal of Mathematics 15, no. 08 (2004): 833–54. http://dx.doi.org/10.1142/s0129167x04002570.
Full textTorres-Gómez, Héctor, Constantin Daniliuc, Dirk Schepmann, Erik Laurini, Sabrina Pricl та Bernhard Wünsch. "Propellanes as Rigid Scaffolds for the Stereodefined Attachment of σ-Pharmacophoric Structural Elements to Achieve σ Affinity". International Journal of Molecular Sciences 22, № 11 (2021): 5685. http://dx.doi.org/10.3390/ijms22115685.
Full textHarbottle, John, and Nikolay Zenkin. "Ureidothiophene inhibits interaction of bacterial RNA polymerase with –10 promotor element." Nucleic Acids Research 48, no. 14 (2020): 7914–23. http://dx.doi.org/10.1093/nar/gkaa591.
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