Статті в журналах з теми "(p)ppGpp Synthetases"
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Ознайомтеся з топ-50 статей у журналах для дослідження на тему "(p)ppGpp Synthetases".
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Ababneh, Qutaiba O., and Jennifer K. Herman. "RelA Inhibits Bacillus subtilis Motility and Chaining." Journal of Bacteriology 197, no. 1 (October 20, 2014): 128–37. http://dx.doi.org/10.1128/jb.02063-14.
Повний текст джерелаTozawa, Yuzuru, Akira Nozawa, Takuya Kanno, Takakuni Narisawa, Shinji Masuda, Koji Kasai, and Hideaki Nanamiya. "Calcium-activated (p)ppGpp Synthetase in Chloroplasts of Land Plants." Journal of Biological Chemistry 282, no. 49 (October 15, 2007): 35536–45. http://dx.doi.org/10.1074/jbc.m703820200.
Повний текст джерелаSidorov, Roman Yu, and Alexander G. Tkachenko. "DMNP, a Synthetic Analog of Erogorgiaene, Inhibits the ppGpp Synthetase Activity of the Small Alarmone Synthetase RelZ." BIO Web of Conferences 57 (2023): 08002. http://dx.doi.org/10.1051/bioconf/20235708002.
Повний текст джерелаLemos, José A., Marcelle M. Nascimento, Vanessa K. Lin, Jacqueline Abranches, and Robert A. Burne. "Global Regulation by (p)ppGpp and CodY in Streptococcus mutans." Journal of Bacteriology 190, no. 15 (June 6, 2008): 5291–99. http://dx.doi.org/10.1128/jb.00288-08.
Повний текст джерелаJimmy, Steffi, Chayan Kumar Saha, Tatsuaki Kurata, Constantine Stavropoulos, Sofia Raquel Alves Oliveira, Alan Koh, Albinas Cepauskas, et al. "A widespread toxin−antitoxin system exploiting growth control via alarmone signaling." Proceedings of the National Academy of Sciences 117, no. 19 (April 28, 2020): 10500–10510. http://dx.doi.org/10.1073/pnas.1916617117.
Повний текст джерелаNatori, Yousuke, Kazumi Tagami, Kana Murakami, Sawako Yoshida, Osamu Tanigawa, Yoonsuh Moh, Kenta Masuda, et al. "Transcription Activity of Individual rrn Operons in Bacillus subtilis Mutants Deficient in (p)ppGpp Synthetase Genes, relA, yjbM, and ywaC." Journal of Bacteriology 191, no. 14 (May 15, 2009): 4555–61. http://dx.doi.org/10.1128/jb.00263-09.
Повний текст джерелаZhu, Jiawen, Tengfei Zhang, Zhipeng Su, Lu Li, Dong Wang, Ran Xiao, Muye Teng, Meifang Tan, and Rui Zhou. "(p)ppGpp synthetases regulate the pathogenesis of zoonotic Streptococcus suis." Microbiological Research 191 (October 2016): 1–11. http://dx.doi.org/10.1016/j.micres.2016.05.007.
Повний текст джерелаWang, Xin, Yiluo Cheng, Wenting Zhang, Qin Lu, Guoyuan Wen, Qingping Luo, Huabin Shao, Zishu Pan, and Tengfei Zhang. "(p)ppGpp synthetases are required for the pathogenicity of Salmonella Pullorum in chickens." Microbiological Research 245 (April 2021): 126685. http://dx.doi.org/10.1016/j.micres.2020.126685.
Повний текст джерелаWang, Xin, Yiluo Cheng, Wenting Zhang, Qin Lu, Guoyuan Wen, Qingping Luo, Huabin Shao, Zishu Pan, and Tengfei Zhang. "(p)ppGpp synthetases are required for the pathogenicity of Salmonella Pullorum in chickens." Microbiological Research 245 (April 2021): 126685. http://dx.doi.org/10.1016/j.micres.2020.126685.
Повний текст джерелаZhu, Jiawen, Tengfei Zhang, Zhipeng Su, Liping Feng, Hanyang Liu, Zhenying Xu, Yongsheng Wu, Ting Gao, Huabin Shao, and Rui Zhou. "Co-regulation of CodY and (p)ppGpp synthetases on morphology and pathogenesis of Streptococcus suis." Microbiological Research 223-225 (June 2019): 88–98. http://dx.doi.org/10.1016/j.micres.2019.04.001.
Повний текст джерелаSteinchen, Wieland, Jan S. Schuhmacher, Florian Altegoer, Christopher D. Fage, Vasundara Srinivasan, Uwe Linne, Mohamed A. Marahiel, and Gert Bange. "Catalytic mechanism and allosteric regulation of an oligomeric (p)ppGpp synthetase by an alarmone." Proceedings of the National Academy of Sciences 112, no. 43 (October 12, 2015): 13348–53. http://dx.doi.org/10.1073/pnas.1505271112.
Повний текст джерелаMwangi, Michael M., Choonkeun Kim, Marilyn Chung, Jennifer Tsai, Govindan Vijayadamodar, Michelle Benitez, Thomas P. Jarvie, Lei Du та Alexander Tomasz. "Whole-Genome Sequencing Reveals a Link Between β-Lactam Resistance and Synthetases of the Alarmone (p)ppGpp inStaphylococcus aureus". Microbial Drug Resistance 19, № 3 (червень 2013): 153–59. http://dx.doi.org/10.1089/mdr.2013.0053.
Повний текст джерелаDasgupta, Shreya, Pallabi Basu, Ritesh Ranjan Pal, Satyabrata Bag, and Rupak K. Bhadra. "Genetic and mutational characterization of the small alarmone synthetase gene relV of Vibrio cholerae." Microbiology 160, no. 9 (September 1, 2014): 1855–66. http://dx.doi.org/10.1099/mic.0.079319-0.
Повний текст джерелаGaca, Anthony O., Pavel Kudrin, Cristina Colomer-Winter, Jelena Beljantseva, Kuanqing Liu, Brent Anderson, Jue D. Wang, et al. "From (p)ppGpp to (pp)pGpp: Characterization of Regulatory Effects of pGpp Synthesized by the Small Alarmone Synthetase of Enterococcus faecalis." Journal of Bacteriology 197, no. 18 (June 29, 2015): 2908–19. http://dx.doi.org/10.1128/jb.00324-15.
Повний текст джерелаBeljantseva, Jelena, Pavel Kudrin, Liis Andresen, Victoria Shingler, Gemma C. Atkinson, Tanel Tenson, and Vasili Hauryliuk. "Negative allosteric regulation of Enterococcus faecalis small alarmone synthetase RelQ by single-stranded RNA." Proceedings of the National Academy of Sciences 114, no. 14 (March 20, 2017): 3726–31. http://dx.doi.org/10.1073/pnas.1617868114.
Повний текст джерелаOkada, Yumiko, Sou-ichi Makino, Toru Tobe, Nobuhiko Okada, and Shouji Yamazaki. "Cloning of rel from Listeria monocytogenes as an Osmotolerance Involvement Gene." Applied and Environmental Microbiology 68, no. 4 (April 2002): 1541–47. http://dx.doi.org/10.1128/aem.68.4.1541-1547.2002.
Повний текст джерелаLee, Jae-Woo, Young-Ha Park, and Yeong-Jae Seok. "Rsd balances (p)ppGpp level by stimulating the hydrolase activity of SpoT during carbon source downshift inEscherichia coli." Proceedings of the National Academy of Sciences 115, no. 29 (June 18, 2018): E6845—E6854. http://dx.doi.org/10.1073/pnas.1722514115.
Повний текст джерелаVan der Henst, Mathilde, Elodie Carlier, and Xavier De Bolle. "Intracellular Growth and Cell Cycle Progression are Dependent on (p)ppGpp Synthetase/Hydrolase in Brucella abortus." Pathogens 9, no. 7 (July 14, 2020): 571. http://dx.doi.org/10.3390/pathogens9070571.
Повний текст джерелаBrandi, Anna, Mara Giangrossi, Attilio Fabbretti, and Maurizio Falconi. "The hns Gene of Escherichia coli Is Transcriptionally Down-Regulated by (p)ppGpp." Microorganisms 8, no. 10 (October 10, 2020): 1558. http://dx.doi.org/10.3390/microorganisms8101558.
Повний текст джерелаAbranches, Jacqueline, Alaina R. Martinez, Jessica K. Kajfasz, Violeta Chávez, Danielle A. Garsin, and José A. Lemos. "The Molecular Alarmone (p)ppGpp Mediates Stress Responses, Vancomycin Tolerance, and Virulence in Enterococcus faecalis." Journal of Bacteriology 191, no. 7 (January 23, 2009): 2248–56. http://dx.doi.org/10.1128/jb.01726-08.
Повний текст джерелаMartínez-Costa, Oscar H., Miguel A. Fernández-Moreno, and Francisco Malpartida. "The relA/spoT-Homologous Gene inStreptomyces coelicolor Encodes Both Ribosome-Dependent (p)ppGppSynthesizing and -Degrading Activities." Journal of Bacteriology 180, no. 16 (August 15, 1998): 4123–32. http://dx.doi.org/10.1128/jb.180.16.4123-4132.1998.
Повний текст джерелаMouery, Kyle, Bethany A. Rader, Erin C. Gaynor, and Karen Guillemin. "The Stringent Response Is Required for Helicobacter pylori Survival of Stationary Phase, Exposure to Acid, and Aerobic Shock." Journal of Bacteriology 188, no. 15 (August 1, 2006): 5494–500. http://dx.doi.org/10.1128/jb.00366-06.
Повний текст джерелаRonneau, Séverin, and Régis Hallez. "Make and break the alarmone: regulation of (p)ppGpp synthetase/hydrolase enzymes in bacteria." FEMS Microbiology Reviews 43, no. 4 (March 27, 2019): 389–400. http://dx.doi.org/10.1093/femsre/fuz009.
Повний текст джерелаTian, Chengzhe, Mohammad Roghanian, Mikkel Girke Jørgensen, Kim Sneppen, Michael Askvad Sørensen, Kenn Gerdes, and Namiko Mitarai. "Rapid Curtailing of the Stringent Response by Toxin-Antitoxin Module-Encoded mRNases." Journal of Bacteriology 198, no. 14 (May 2, 2016): 1918–26. http://dx.doi.org/10.1128/jb.00062-16.
Повний текст джерелаHolley, Concerta, Dharanesh Gangaiah, Wei Li, Kate R. Fortney, Diane M. Janowicz, Sheila Ellinger, Beth Zwickl, Barry P. Katz, and Stanley M. Spinola. "A (p)ppGpp-Null Mutant of Haemophilus ducreyi Is Partially Attenuated in Humans Due to Multiple Conflicting Phenotypes." Infection and Immunity 82, no. 8 (June 9, 2014): 3492–502. http://dx.doi.org/10.1128/iai.01994-14.
Повний текст джерелаCoppa, Crescenzo, Luca Sorrentino, Monica Civera, Marco Minneci, Francesca Vasile, and Sara Sattin. "New Chemotypes for the Inhibition of (p)ppGpp Synthesis in the Quest for New Antimicrobial Compounds." Molecules 27, no. 10 (May 12, 2022): 3097. http://dx.doi.org/10.3390/molecules27103097.
Повний текст джерелаGermain, Elsa, Mohammad Roghanian, Kenn Gerdes, and Etienne Maisonneuve. "Stochastic induction of persister cells by HipA through (p)ppGpp-mediated activation of mRNA endonucleases." Proceedings of the National Academy of Sciences 112, no. 16 (April 6, 2015): 5171–76. http://dx.doi.org/10.1073/pnas.1423536112.
Повний текст джерелаManuel, Jerrylynn, Chrystal Berry, Carrie Selin, W. G. Dilantha Fernando, and Teresa R. de Kievit. "Repression of the Antifungal Activity of Pseudomonas sp. Strain DF41 by the Stringent Response." Applied and Environmental Microbiology 77, no. 16 (June 24, 2011): 5635–42. http://dx.doi.org/10.1128/aem.02875-10.
Повний текст джерелаMerrikh, Houra, Alexander E. Ferrazzoli, and Susan T. Lovett. "Growth Phase and (p)ppGpp Control of IraD, a Regulator of RpoS Stability, in Escherichia coli." Journal of Bacteriology 191, no. 24 (October 9, 2009): 7436–46. http://dx.doi.org/10.1128/jb.00412-09.
Повний текст джерелаZhou, Yan Ning, William G. Coleman, Zhaoxu Yang, Yi Yang, Nathaniel Hodgson, Fuxiang Chen, and Ding Jun Jin. "Regulation of Cell Growth during Serum Starvation and Bacterial Survival in Macrophages by the Bifunctional Enzyme SpoT in Helicobacter pylori." Journal of Bacteriology 190, no. 24 (October 3, 2008): 8025–32. http://dx.doi.org/10.1128/jb.01134-08.
Повний текст джерелаOssa, Faisury, Michelle E. Diodati, Nora B. Caberoy, Krista M. Giglio, Mick Edmonds, Mitchell Singer, and Anthony G. Garza. "The Myxococcus xanthus Nla4 Protein Is Important for Expression of Stringent Response-Associated Genes, ppGpp Accumulation, and Fruiting Body Development." Journal of Bacteriology 189, no. 23 (September 28, 2007): 8474–83. http://dx.doi.org/10.1128/jb.00894-07.
Повний текст джерелаManav, Melek Cemre, Jelena Beljantseva, Martin S. Bojer, Tanel Tenson, Hanne Ingmer, Vasili Hauryliuk, and Ditlev E. Brodersen. "Structural basis for (p)ppGpp synthesis by theStaphylococcus aureussmall alarmone synthetase RelP." Journal of Biological Chemistry 293, no. 9 (January 11, 2018): 3254–64. http://dx.doi.org/10.1074/jbc.ra117.001374.
Повний текст джерелаAvarbock, Andrew, David Avarbock, Jiah-Shin Teh, Michael Buckstein, Zhi-mei Wang, and Harvey Rubin. "Functional Regulation of the Opposing (p)ppGpp Synthetase/Hydrolase Activities of RelMtbfromMycobacteriumtuberculosis†." Biochemistry 44, no. 29 (July 2005): 9913–23. http://dx.doi.org/10.1021/bi0505316.
Повний текст джерелаTagami, Kazumi, Hideaki Nanamiya, Yuka Kazo, Marie Maehashi, Shota Suzuki, Eri Namba, Masahiro Hoshiya, et al. "Expression of a small (p)ppGpp synthetase, YwaC, in the (p)ppGpp 0 mutant of Bacillus subtilis triggers YvyD‐dependent dimerization of ribosome." MicrobiologyOpen 1, no. 2 (April 3, 2012): 115–34. http://dx.doi.org/10.1002/mbo3.16.
Повний текст джерелаNanamiya, Hideaki, Koji Kasai, Akira Nozawa, Choong-Soo Yun, Takakuni Narisawa, Kana Murakami, Yousuke Natori, Fujio Kawamura, and Yuzuru Tozawa. "Identification and functional analysis of novel (p)ppGpp synthetase genes in Bacillus subtilis." Molecular Microbiology 67, no. 2 (December 7, 2007): 291–304. http://dx.doi.org/10.1111/j.1365-2958.2007.06018.x.
Повний текст джерелаMurdeshwar, M. S., and D. Chatterji. "MS_RHII-RSD, a Dual-Function RNase HII-(p)ppGpp Synthetase from Mycobacterium smegmatis." Journal of Bacteriology 194, no. 15 (May 25, 2012): 4003–14. http://dx.doi.org/10.1128/jb.00258-12.
Повний текст джерелаReiß, Swantje, Jan Pané-Farré, Stephan Fuchs, Patrice François, Manuel Liebeke, Jacques Schrenzel, Ulrike Lindequist, et al. "Global Analysis of the Staphylococcus aureus Response to Mupirocin." Antimicrobial Agents and Chemotherapy 56, no. 2 (November 21, 2011): 787–804. http://dx.doi.org/10.1128/aac.05363-11.
Повний текст джерелаZhang, Shuyu, та W. G. Haldenwang. "RelA Is a Component of the Nutritional Stress Activation Pathway of the Bacillus subtilis Transcription Factor σB". Journal of Bacteriology 185, № 19 (1 жовтня 2003): 5714–21. http://dx.doi.org/10.1128/jb.185.19.5714-5721.2003.
Повний текст джерелаYan, X., C. Zhao, A. Budin-Verneuil, A. Hartke, A. Rince, M. S. Gilmore, Y. Auffray, and V. Pichereau. "The (p)ppGpp synthetase RelA contributes to stress adaptation and virulence in Enterococcus faecalis V583." Microbiology 155, no. 10 (July 16, 2009): 3226–37. http://dx.doi.org/10.1099/mic.0.026146-0.
Повний текст джерелаBag, Satyabrata, Bhabatosh Das, Shreya Dasgupta, and Rupak K. Bhadra. "Mutational analysis of the (p)ppGpp synthetase activity of the Rel enzyme of Mycobacterium tuberculosis." Archives of Microbiology 196, no. 8 (May 24, 2014): 575–88. http://dx.doi.org/10.1007/s00203-014-0996-9.
Повний текст джерелаGropp, Michal, Yael Strausz, Miriam Gross, and Gad Glaser. "Regulation of Escherichia coli RelA Requires Oligomerization of the C-Terminal Domain." Journal of Bacteriology 183, no. 2 (January 15, 2001): 570–79. http://dx.doi.org/10.1128/jb.183.2.570-579.2001.
Повний текст джерелаKrishnan, Sushma, Anushya Petchiappan, Albel Singh, Apoorva Bhatt, and Dipankar Chatterji. "R-loop induced stress response by second (p)ppGpp synthetase inMycobacterium smegmatis: functional and domain interdependence." Molecular Microbiology 102, no. 1 (July 19, 2016): 168–82. http://dx.doi.org/10.1111/mmi.13453.
Повний текст джерелаChakraburtty, Rekha, Janet White, Eriko Takano, and Mervyn Bibb. "Cloning, characterization and disruption of a (p)ppGpp synthetase gene (relA) of Streptomyces coelicolor A3(2)." Molecular Microbiology 19, no. 2 (January 1996): 357–68. http://dx.doi.org/10.1046/j.1365-2958.1996.390919.x.
Повний текст джерелаGupta, Kuldeepkumar Ramnaresh, Gunjan Arora, Abid Mattoo, and Andaleeb Sajid. "Stringent Response in Mycobacteria: From Biology to Therapeutic Potential." Pathogens 10, no. 11 (November 1, 2021): 1417. http://dx.doi.org/10.3390/pathogens10111417.
Повний текст джерелаYang, Xiaoming, and Edward E. Ishiguro. "Involvement of the N Terminus of Ribosomal Protein L11 in Regulation of the RelA Protein of Escherichia coli." Journal of Bacteriology 183, no. 22 (November 15, 2001): 6532–37. http://dx.doi.org/10.1128/jb.183.22.6532-6537.2001.
Повний текст джерелаDas, Bhabatosh, Ritesh Ranjan Pal, Satyabrata Bag, and Rupak K. Bhadra. "Stringent response inVibrio cholerae: genetic analysis ofspoTgene function and identification of a novel (p)ppGpp synthetase gene." Molecular Microbiology 72, no. 2 (April 2009): 380–98. http://dx.doi.org/10.1111/j.1365-2958.2009.06653.x.
Повний текст джерелаPausch, Patrick, Maha Abdelshahid, Wieland Steinchen, Heinrich Schäfer, Fabio Lino Gratani, Sven-Andreas Freibert, Christiane Wolz, Kürşad Turgay, Daniel N. Wilson, and Gert Bange. "Structural Basis for Regulation of the Opposing (p)ppGpp Synthetase and Hydrolase within the Stringent Response Orchestrator Rel." Cell Reports 32, no. 11 (September 2020): 108157. http://dx.doi.org/10.1016/j.celrep.2020.108157.
Повний текст джерелаYang, Xiaoming, and Edward E. Ishiguro. "Dimerization of the RelA protein of Escherichia coli." Biochemistry and Cell Biology 79, no. 6 (December 1, 2001): 729–36. http://dx.doi.org/10.1139/o01-144.
Повний текст джерелаLemos, José A. C., Thomas A. Brown, and Robert A. Burne. "Effects of RelA on Key Virulence Properties of Planktonic and Biofilm Populations of Streptococcus mutans." Infection and Immunity 72, no. 3 (March 2004): 1431–40. http://dx.doi.org/10.1128/iai.72.3.1431-1440.2004.
Повний текст джерелаGratani, Fabio Lino, Petra Horvatek, Tobias Geiger, Marina Borisova, Christoph Mayer, Iwan Grin, Samuel Wagner, et al. "Regulation of the opposing (p)ppGpp synthetase and hydrolase activities in a bifunctional RelA/SpoT homologue from Staphylococcus aureus." PLOS Genetics 14, no. 7 (July 9, 2018): e1007514. http://dx.doi.org/10.1371/journal.pgen.1007514.
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