Статті в журналах з теми "Toxin-antitoxin (TA) system"
Оформте джерело за APA, MLA, Chicago, Harvard та іншими стилями
Ознайомтеся з топ-50 статей у журналах для дослідження на тему "Toxin-antitoxin (TA) system".
Біля кожної праці в переліку літератури доступна кнопка «Додати до бібліографії». Скористайтеся нею – і ми автоматично оформимо бібліографічне посилання на обрану працю в потрібному вам стилі цитування: APA, MLA, «Гарвард», «Чикаго», «Ванкувер» тощо.
Також ви можете завантажити повний текст наукової публікації у форматі «.pdf» та прочитати онлайн анотацію до роботи, якщо відповідні параметри наявні в метаданих.
Переглядайте статті в журналах для різних дисциплін та оформлюйте правильно вашу бібліографію.
Wilbaux, Myriam, Natacha Mine, Anne-Marie Guérout, Didier Mazel, and Laurence Van Melderen. "Functional Interactions between Coexisting Toxin-Antitoxin Systems of the ccd Family in Escherichia coli O157:H7." Journal of Bacteriology 189, no. 7 (January 26, 2007): 2712–19. http://dx.doi.org/10.1128/jb.01679-06.
Повний текст джерелаSingletary, Larissa A., Janet L. Gibson, Elizabeth J. Tanner, Gregory J. McKenzie, Peter L. Lee, Caleb Gonzalez, and Susan M. Rosenberg. "An SOS-Regulated Type 2 Toxin-Antitoxin System." Journal of Bacteriology 191, no. 24 (October 16, 2009): 7456–65. http://dx.doi.org/10.1128/jb.00963-09.
Повний текст джерелаNi, Songwei, Baiyuan Li, Kaihao Tang, Jianyun Yao, Thomas K. Wood, Pengxia Wang, and Xiaoxue Wang. "Conjugative plasmid-encoded toxin–antitoxin system PrpT/PrpA directly controls plasmid copy number." Proceedings of the National Academy of Sciences 118, no. 4 (January 22, 2021): e2011577118. http://dx.doi.org/10.1073/pnas.2011577118.
Повний текст джерелаRathore, Jitendra Singh, and Lalit Kumar Gautam. "Expression, Purification, and Functional Analysis of Novel RelE Operon fromX. nematophila." Scientific World Journal 2014 (2014): 1–7. http://dx.doi.org/10.1155/2014/428159.
Повний текст джерелаPiscotta, Frank J., Philip D. Jeffrey, and A. James Link. "ParST is a widespread toxin–antitoxin module that targets nucleotide metabolism." Proceedings of the National Academy of Sciences 116, no. 3 (December 31, 2018): 826–34. http://dx.doi.org/10.1073/pnas.1814633116.
Повний текст джерелаAlkhalili, Rawana, Joel Wallenius, and Björn Canbäck. "Towards Exploring Toxin-Antitoxin Systems in Geobacillus: A Screen for Type II Toxin-Antitoxin System Families in a Thermophilic Genus." International Journal of Molecular Sciences 20, no. 23 (November 22, 2019): 5869. http://dx.doi.org/10.3390/ijms20235869.
Повний текст джерелаTu, Chih-Han, Michelle Holt, Shengfeng Ruan, and Christina Bourne. "Evaluating the Potential for Cross-Interactions of Antitoxins in Type II TA Systems." Toxins 12, no. 6 (June 26, 2020): 422. http://dx.doi.org/10.3390/toxins12060422.
Повний текст джерелаHabib, Gul, Qing Zhu, and Baolin Sun. "Bioinformatics and Functional Assessment of Toxin-Antitoxin Systems in Staphylococcus aureus." Toxins 10, no. 11 (November 14, 2018): 473. http://dx.doi.org/10.3390/toxins10110473.
Повний текст джерелаPathak, Chinar, Hookang Im, Sun-bok Jang, Yeon-Jin Yang, Hye-Jin Yoon, Hong-Man Kim, Ae-Ran Kwon, and Bong-Jin Lee. "Toxins from TA system of Helicobacter pylori and insight into mRNase activity." Acta Crystallographica Section A Foundations and Advances 70, a1 (August 5, 2014): C828. http://dx.doi.org/10.1107/s2053273314091712.
Повний текст джерелаChoi, Wonho, Yoshihiro Yamaguchi, Ji-Young Park, Sang-Hyun Park, Hyeok-Won Lee, Byung-Kwan Lim, Michael Otto, Masayori Inouye, Min-Ho Yoon, and Jung-Ho Park. "Functional Characterization of the mazEF Toxin-Antitoxin System in the Pathogenic Bacterium Agrobacterium tumefaciens." Microorganisms 9, no. 5 (May 20, 2021): 1107. http://dx.doi.org/10.3390/microorganisms9051107.
Повний текст джерелаDaimon, Yasushi, Shin-ichiro Narita та Yoshinori Akiyama. "Activation of Toxin-Antitoxin System Toxins Suppresses Lethality Caused by the Loss of σEin Escherichia coli". Journal of Bacteriology 197, № 14 (27 квітня 2015): 2316–24. http://dx.doi.org/10.1128/jb.00079-15.
Повний текст джерелаLee, Ki-Young, and Bong-Jin Lee. "Dynamics-Based Regulatory Switches of Type II Antitoxins: Insights into New Antimicrobial Discovery." Antibiotics 12, no. 4 (March 23, 2023): 637. http://dx.doi.org/10.3390/antibiotics12040637.
Повний текст джерелаKasari, Villu, Kristi Kurg, Tõnu Margus, Tanel Tenson, and Niilo Kaldalu. "The Escherichia coli mqsR and ygiT Genes Encode a New Toxin-Antitoxin Pair." Journal of Bacteriology 192, no. 11 (March 16, 2010): 2908–19. http://dx.doi.org/10.1128/jb.01266-09.
Повний текст джерелаSoutourina, Olga. "Type I Toxin-Antitoxin Systems in Clostridia." Toxins 11, no. 5 (May 6, 2019): 253. http://dx.doi.org/10.3390/toxins11050253.
Повний текст джерелаSala, Ambre Julie, Patricia Bordes, Sara Ayala, Nawel Slama, Samuel Tranier, Michèle Coddeville, Anne-Marie Cirinesi, Marie-Pierre Castanié-Cornet, Lionel Mourey, and Pierre Genevaux. "Directed evolution of SecB chaperones toward toxin-antitoxin systems." Proceedings of the National Academy of Sciences 114, no. 47 (November 7, 2017): 12584–89. http://dx.doi.org/10.1073/pnas.1710456114.
Повний текст джерелаKang, Sung-Min, Do-Hee Kim, Chenglong Jin, and Bong-Jin Lee. "A Systematic Overview of Type II and III Toxin-Antitoxin Systems with a Focus on Druggability." Toxins 10, no. 12 (December 4, 2018): 515. http://dx.doi.org/10.3390/toxins10120515.
Повний текст джерелаSaavedra De Bast, Manuel, Natacha Mine, and Laurence Van Melderen. "Chromosomal Toxin-Antitoxin Systems May Act as Antiaddiction Modules." Journal of Bacteriology 190, no. 13 (April 25, 2008): 4603–9. http://dx.doi.org/10.1128/jb.00357-08.
Повний текст джерелаHill, Virginia, Hatice Akarsu, Rubén Sánchez Barbarroja, Valentina L. Cippà, Peter Kuhnert, Martin Heller, Laurent Falquet, et al. "Minimalistic mycoplasmas harbor different functional toxin-antitoxin systems." PLOS Genetics 17, no. 10 (October 21, 2021): e1009365. http://dx.doi.org/10.1371/journal.pgen.1009365.
Повний текст джерелаKamruzzaman, Muhammad, Alma Y. Wu, and Jonathan R. Iredell. "Biological Functions of Type II Toxin-Antitoxin Systems in Bacteria." Microorganisms 9, no. 6 (June 11, 2021): 1276. http://dx.doi.org/10.3390/microorganisms9061276.
Повний текст джерелаLee, Min Woo, Elizabeth E. Rogers, and Drake C. Stenger. "Xylella fastidiosa Plasmid-Encoded PemK Toxin Is an Endoribonuclease." Phytopathology® 102, no. 1 (January 2012): 32–40. http://dx.doi.org/10.1094/phyto-05-11-0150.
Повний текст джерелаNorouzi, Masoumeh, Abbas Maleki, Elham Aboualigalehdari, and Sobhan Ghafourian. "Type II toxin- antitoxin systems in clinical isolates of antibiotic resistant Acinetobacter baumannii." Genetika 54, no. 2 (2022): 625–32. http://dx.doi.org/10.2298/gensr2202625n.
Повний текст джерелаChlebicka, Kinga, Emilia Bonar, Piotr Suder, Emeline Ostyn, Brice Felden, Benedykt Wladyka, and Marie-Laure Pinel-Marie. "Impacts of the Type I Toxin–Antitoxin System, SprG1/SprF1, on Staphylococcus aureus Gene Expression." Genes 12, no. 5 (May 18, 2021): 770. http://dx.doi.org/10.3390/genes12050770.
Повний текст джерелаAgarwal, Sakshi, Arun Sharma, Rania Bouzeyen, Amar Deep, Harsh Sharma, Kiran K. Mangalaparthi, Keshava K. Datta, et al. "VapBC22 toxin-antitoxin system from Mycobacterium tuberculosis is required for pathogenesis and modulation of host immune response." Science Advances 6, no. 23 (June 2020): eaba6944. http://dx.doi.org/10.1126/sciadv.aba6944.
Повний текст джерелаYao, Jianyun, Xiangkai Zhen, Kaihao Tang, Tianlang Liu, Xiaolong Xu, Zhe Chen, Yunxue Guo, et al. "Novel polyadenylylation-dependent neutralization mechanism of the HEPN/MNT toxin/antitoxin system." Nucleic Acids Research 48, no. 19 (October 12, 2020): 11054–67. http://dx.doi.org/10.1093/nar/gkaa855.
Повний текст джерелаShapira, Shiran, Ilana Boustanai, Dina Kazanov, Marina Ben Shimon, Ahmad Fokra, and Nadir Arber. "Innovative dual system approach for selective eradication of cancer cells using viral-based delivery of natural bacterial toxin–antitoxin system." Oncogene 40, no. 31 (June 25, 2021): 4967–79. http://dx.doi.org/10.1038/s41388-021-01792-8.
Повний текст джерелаBodogai, Monica, Szilamér Ferenczi, Denys Bashtovyy, Paul Miclea, Péter Papp, and Ilona Dusha. "The ntrPR Operon of Sinorhizobium meliloti Is Organized and Functions as a Toxin-Antitoxin Module." Molecular Plant-Microbe Interactions® 19, no. 7 (July 2006): 811–22. http://dx.doi.org/10.1094/mpmi-19-0811.
Повний текст джерелаZielenkiewicz, Urszula, Magdalena Kowalewska, Celina Kaczor, and Piotr Cegłowski. "In Vivo Interactions between Toxin-Antitoxin Proteins Epsilon and Zeta of Streptococcal Plasmid pSM19035 in Saccharomyces cerevisiae." Journal of Bacteriology 191, no. 11 (April 3, 2009): 3677–84. http://dx.doi.org/10.1128/jb.01763-08.
Повний текст джерелаValizadeh, Nasrin, Firuzeh Valian, Nourkhoda Sadeghifard, Shahriar Karami, Iraj Pakzad, Hossein Kazemian, and Sobhan Ghafourian. "The Role of Peganum harmala Ethanolic Extract and Type II Toxin Antitoxin System in Biofilm Formation." Drug Research 67, no. 07 (March 20, 2017): 385–87. http://dx.doi.org/10.1055/s-0043-102060.
Повний текст джерелаTamman, Hedvig, Andres Ainelo, Mari Tagel, and Rita Hõrak. "Stability of the GraA Antitoxin Depends on Growth Phase, ATP Level, and Global Regulator MexT." Journal of Bacteriology 198, no. 5 (December 14, 2015): 787–96. http://dx.doi.org/10.1128/jb.00684-15.
Повний текст джерелаXie, Zhoujie, Fengxia Qi, and Justin Merritt. "Development of a Tunable Wide-Range Gene Induction System Useful for the Study of Streptococcal Toxin-Antitoxin Systems." Applied and Environmental Microbiology 79, no. 20 (August 9, 2013): 6375–84. http://dx.doi.org/10.1128/aem.02320-13.
Повний текст джерелаHeaton, Brook E., Julien Herrou, Anne E. Blackwell, Vicki H. Wysocki, and Sean Crosson. "Molecular Structure and Function of the Novel BrnT/BrnA Toxin-Antitoxin System of Brucella abortus." Journal of Biological Chemistry 287, no. 15 (February 14, 2012): 12098–110. http://dx.doi.org/10.1074/jbc.m111.332163.
Повний текст джерелаBoss, Lidia, and Barbara Kędzierska. "Bacterial Toxin-Antitoxin Systems’ Cross-Interactions—Implications for Practical Use in Medicine and Biotechnology." Toxins 15, no. 6 (June 4, 2023): 380. http://dx.doi.org/10.3390/toxins15060380.
Повний текст джерелаJørgensen, Mikkel G., Deo P. Pandey, Milena Jaskolska, and Kenn Gerdes. "HicA of Escherichia coli Defines a Novel Family of Translation-Independent mRNA Interferases in Bacteria and Archaea." Journal of Bacteriology 191, no. 4 (December 5, 2008): 1191–99. http://dx.doi.org/10.1128/jb.01013-08.
Повний текст джерелаPark, Jin-Young, Hyo Jung Kim, Chinar Pathak, Hye-Jin Yoon, Do-Hee Kim, Sung Jean Park, and Bong-Jin Lee. "Induced DNA bending by unique dimerization of HigA antitoxin." IUCrJ 7, no. 4 (June 26, 2020): 748–60. http://dx.doi.org/10.1107/s2052252520006466.
Повний текст джерелаJin, Chenglong, Sung-Min Kang, Do-Hee Kim, and Bong-Jin Lee. "Structural and functional analysis of the Klebsiella pneumoniae MazEF toxin–antitoxin system." IUCrJ 8, no. 3 (March 5, 2021): 362–71. http://dx.doi.org/10.1107/s2052252521000452.
Повний текст джерелаKędzierska, Barbara, and Katarzyna Potrykus. "Minigene as a Novel Regulatory Element in Toxin-Antitoxin Systems." International Journal of Molecular Sciences 22, no. 24 (December 13, 2021): 13389. http://dx.doi.org/10.3390/ijms222413389.
Повний текст джерелаHosseini, Nava, Maryam Pourhajibagher, Nasim Chiniforush, Nazanin Hosseinkhan, Parizad Rezaie, and Abbas Bahador. "Modulation of Toxin-Antitoxin System Rnl AB Type II in Phage-Resistant Gammaproteobacteria Surviving Photodynamic Treatment." Journal of Lasers in Medical Sciences 10, no. 1 (December 15, 2018): 21–28. http://dx.doi.org/10.15171/jlms.2019.03.
Повний текст джерелаZhou, Jingyi, Shouyi Li, Haozhou Li, Yongxin Jin, Fang Bai, Zhihui Cheng, and Weihui Wu. "Identification of a Toxin–Antitoxin System That Contributes to Persister Formation by Reducing NAD in Pseudomonas aeruginosa." Microorganisms 9, no. 4 (April 2, 2021): 753. http://dx.doi.org/10.3390/microorganisms9040753.
Повний текст джерелаNigam, Akanksha, Adi Oron-Gottesman, and Hanna Engelberg-Kulka. "A Bias in the Reading of the Genetic Code of Escherichia coli is a Characteristic for Genes that Specify Stress-induced MazF-mediated Proteins." Current Genomics 21, no. 4 (August 8, 2020): 311–18. http://dx.doi.org/10.2174/1389202921999200606215305.
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 джерелаZhou, Juan, Xue-Jian Du, Ying Liu, Zeng-Qiang Gao, Zhi Geng, Yu-Hui Dong, and Heng Zhang. "Insights into the Neutralization and DNA Binding of Toxin–Antitoxin System ParESO-CopASO by Structure-Function Studies." Microorganisms 9, no. 12 (December 3, 2021): 2506. http://dx.doi.org/10.3390/microorganisms9122506.
Повний текст джерелаKang, Sung-Min. "Mycobacterium tuberculosis Rv0229c Shows Ribonuclease Activity and Reveals Its Corresponding Role as Toxin VapC51." Antibiotics 12, no. 5 (May 1, 2023): 840. http://dx.doi.org/10.3390/antibiotics12050840.
Повний текст джерелаKang, Sung-Min, Ji Sung Koo, Chang-Min Kim, Do-Hee Kim, and Bong-Jin Lee. "mRNA Interferase Bacillus cereus BC0266 Shows MazF-Like Characteristics Through Structural and Functional Study." Toxins 12, no. 6 (June 8, 2020): 380. http://dx.doi.org/10.3390/toxins12060380.
Повний текст джерелаNonin-Lecomte, Sylvie, Laurence Fermon, Brice Felden, and Marie-Laure Pinel-Marie. "Bacterial Type I Toxins: Folding and Membrane Interactions." Toxins 13, no. 7 (July 14, 2021): 490. http://dx.doi.org/10.3390/toxins13070490.
Повний текст джерелаKim, Do-Hee, Sung-Min Kang, Sung-Min Baek, Hye-Jin Yoon, Dong Man Jang, Hyoun Sook Kim, Sang Jae Lee, and Bong-Jin Lee. "Role of PemI in the Staphylococcus aureus PemIK toxin–antitoxin complex: PemI controls PemK by acting as a PemK loop mimic." Nucleic Acids Research 50, no. 4 (February 10, 2022): 2319–33. http://dx.doi.org/10.1093/nar/gkab1288.
Повний текст джерелаJurėnas, Dukas, Laurence Van Melderen, and Abel Garcia-Pino. "Crystallization and X-ray analysis of all of the players in the autoregulation of theataRTtoxin–antitoxin system." Acta Crystallographica Section F Structural Biology Communications 74, no. 7 (June 26, 2018): 391–401. http://dx.doi.org/10.1107/s2053230x18007914.
Повний текст джерелаBajaj, R. Alexandra, Mark A. Arbing, Annie Shin, Duilio Cascio, and Linda Miallau. "Crystal structure of the toxin Msmeg_6760, the structural homolog ofMycobacterium tuberculosisRv2035, a novel type II toxin involved in the hypoxic response." Acta Crystallographica Section F Structural Biology Communications 72, no. 12 (November 19, 2016): 863–69. http://dx.doi.org/10.1107/s2053230x16017957.
Повний текст джерелаAriyachaokun, Kanchiyaphat, Anna D. Grabowska, Claude Gutierrez, and Olivier Neyrolles. "Multi-Stress Induction of the Mycobacterium tuberculosis MbcTA Bactericidal Toxin-Antitoxin System." Toxins 12, no. 5 (May 16, 2020): 329. http://dx.doi.org/10.3390/toxins12050329.
Повний текст джерелаWen, Wen, Banghui Liu, Lu Xue, Zhongliang Zhu, Liwen Niu, and Baolin Sun. "Autoregulation and Virulence Control by the Toxin-Antitoxin System SavRS inStaphylococcus aureus." Infection and Immunity 86, no. 5 (February 12, 2018): e00032-18. http://dx.doi.org/10.1128/iai.00032-18.
Повний текст джерелаLevante, Alessia, Camilla Lazzi, Giannis Vatsellas, Dimitris Chatzopoulos, Vasilis S. Dionellis, Periklis Makrythanasis, Erasmo Neviani, and Claudia Folli. "Genome Sequencing of five Lacticaseibacillus Strains and Analysis of Type I and II Toxin-Antitoxin System Distribution." Microorganisms 9, no. 3 (March 21, 2021): 648. http://dx.doi.org/10.3390/microorganisms9030648.
Повний текст джерела