Статті в журналах з теми "RRNA Methyltransferase"
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Ознайомтеся з топ-50 статей у журналах для дослідження на тему "RRNA Methyltransferase".
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Corrêa, Laís L., Marta A. Witek, Natalia Zelinskaya, Renata C. Picão, and Graeme L. Conn. "Heterologous Expression and Functional Characterization of the Exogenously Acquired Aminoglycoside Resistance Methyltransferases RmtD, RmtD2, and RmtG." Antimicrobial Agents and Chemotherapy 60, no. 1 (November 9, 2015): 699–702. http://dx.doi.org/10.1128/aac.02482-15.
Повний текст джерелаSavic, Miloje, S. Sunita, Natalia Zelinskaya, Pooja M. Desai, Rachel Macmaster, Kellie Vinal, and Graeme L. Conn. "30S Subunit-Dependent Activation of the Sorangium cellulosum So ce56 Aminoglycoside Resistance-Conferring 16S rRNA Methyltransferase Kmr." Antimicrobial Agents and Chemotherapy 59, no. 5 (March 2, 2015): 2807–16. http://dx.doi.org/10.1128/aac.00056-15.
Повний текст джерелаNosrati, Meisam, Debayan Dey, Atousa Mehrani, Sarah E. Strassler, Natalia Zelinskaya, Eric D. Hoffer, Scott M. Stagg, Christine M. Dunham, and Graeme L. Conn. "Functionally critical residues in the aminoglycoside resistance-associated methyltransferase RmtC play distinct roles in 30S substrate recognition." Journal of Biological Chemistry 294, no. 46 (October 8, 2019): 17642–53. http://dx.doi.org/10.1074/jbc.ra119.011181.
Повний текст джерелаChen, Hao, Zhennan Shi, Jiaojiao Guo, Kao-jung Chang, Qianqian Chen, Cong-Hui Yao, Marcia C. Haigis, and Yang Shi. "The human mitochondrial 12S rRNA m4C methyltransferase METTL15 is required for mitochondrial function." Journal of Biological Chemistry 295, no. 25 (May 5, 2020): 8505–13. http://dx.doi.org/10.1074/jbc.ra119.012127.
Повний текст джерелаRowe, Sebastian J., Ryan J. Mecaskey, Mohamed Nasef, Rachel C. Talton, Rory E. Sharkey, Joshua C. Halliday, and Jack A. Dunkle. "Shared requirements for key residues in the antibiotic resistance enzymes ErmC and ErmE suggest a common mode of RNA recognition." Journal of Biological Chemistry 295, no. 51 (October 5, 2020): 17476–85. http://dx.doi.org/10.1074/jbc.ra120.014280.
Повний текст джерелаMcGann, Patrick, Sarah Chahine, Darius Okafor, Ana C. Ong, Rosslyn Maybank, Yoon I. Kwak, Kerry Wilson, Michael Zapor, Emil Lesho, and Mary Hinkle. "Detecting 16S rRNA Methyltransferases in Enterobacteriaceae by Use of Arbekacin." Journal of Clinical Microbiology 54, no. 1 (November 4, 2015): 208–11. http://dx.doi.org/10.1128/jcm.02642-15.
Повний текст джерелаvan Tran, Nhan, Felix G. M. Ernst, Ben R. Hawley, Christiane Zorbas, Nathalie Ulryck, Philipp Hackert, Katherine E. Bohnsack, et al. "The human 18S rRNA m6A methyltransferase METTL5 is stabilized by TRMT112." Nucleic Acids Research 47, no. 15 (July 22, 2019): 7719–33. http://dx.doi.org/10.1093/nar/gkz619.
Повний текст джерелаWhite, Joshua, Zhihua Li, Richa Sardana, Janusz M. Bujnicki, Edward M. Marcotte, and Arlen W. Johnson. "Bud23 Methylates G1575 of 18S rRNA and Is Required for Efficient Nuclear Export of Pre-40S Subunits." Molecular and Cellular Biology 28, no. 10 (March 10, 2008): 3151–61. http://dx.doi.org/10.1128/mcb.01674-07.
Повний текст джерелаRuszkowska, Agnieszka. "METTL16, Methyltransferase-Like Protein 16: Current Insights into Structure and Function." International Journal of Molecular Sciences 22, no. 4 (February 22, 2021): 2176. http://dx.doi.org/10.3390/ijms22042176.
Повний текст джерелаL. Aishwarya, K. V., P. V. Geetha, M. Shanthi, and S. Uma. "Co occurrence of two 16S rRNA methyltrasferases along with NDM and OXA 48 like carbapenamases on a single plasmid in Klebsiella pneumoniae." Journal of Laboratory Physicians 11, no. 04 (October 2019): 305–11. http://dx.doi.org/10.4103/jlp.jlp_59_19.
Повний текст джерелаZong, Zhiyong, Sally R. Partridge, and Jonathan R. Iredell. "RmtC 16S rRNA Methyltransferase in Australia." Antimicrobial Agents and Chemotherapy 52, no. 2 (November 19, 2007): 794–95. http://dx.doi.org/10.1128/aac.01399-07.
Повний текст джерелаZhu, Chengming, Qi Yan, Chenchun Weng, Xinhao Hou, Hui Mao, Dun Liu, Xuezhu Feng, and Shouhong Guang. "Erroneous ribosomal RNAs promote the generation of antisense ribosomal siRNA." Proceedings of the National Academy of Sciences 115, no. 40 (September 17, 2018): 10082–87. http://dx.doi.org/10.1073/pnas.1800974115.
Повний текст джерелаGutierrez, Belen, Jose A. Escudero, Alvaro San Millan, Laura Hidalgo, Laura Carrilero, Cristina M. Ovejero, Alfonso Santos-Lopez, Daniel Thomas-Lopez, and Bruno Gonzalez-Zorn. "Fitness Cost and Interference of Arm/Rmt Aminoglycoside Resistance with the RsmF Housekeeping Methyltransferases." Antimicrobial Agents and Chemotherapy 56, no. 5 (February 13, 2012): 2335–41. http://dx.doi.org/10.1128/aac.06066-11.
Повний текст джерелаWachino, Jun-ichi, Keigo Shibayama, Hiroshi Kurokawa, Kouji Kimura, Kunikazu Yamane, Satowa Suzuki, Naohiro Shibata, Yasuyoshi Ike, and Yoshichika Arakawa. "Novel Plasmid-Mediated 16S rRNA m1A1408 Methyltransferase, NpmA, Found in a Clinically Isolated Escherichia coli Strain Resistant to Structurally Diverse Aminoglycosides." Antimicrobial Agents and Chemotherapy 51, no. 12 (September 17, 2007): 4401–9. http://dx.doi.org/10.1128/aac.00926-07.
Повний текст джерелаHusain, Nilofer, Karolina L. Tkaczuk, Rajesh T. Shenoy, Katarzyna H. Kaminska, Sonja Čubrilo, Gordana Maravić-Vlahoviček, Janusz M. Bujnicki, and J. Sivaraman. "Structural basis for the methylation of G1405 in 16S rRNA by aminoglycoside resistance methyltransferase Sgm from an antibiotic producer: a diversity of active sites in m 7 G methyltransferases." Nucleic Acids Research 38, no. 12 (February 27, 2010): 4120–32. http://dx.doi.org/10.1093/nar/gkq122.
Повний текст джерелаZou, Meijuan, Ying Mu, Xin Chai, Min Ouyang, Long-Jiang Yu, Lixin Zhang, Jörg Meurer, and Wei Chi. "The critical function of the plastid rRNA methyltransferase, CMAL, in ribosome biogenesis and plant development." Nucleic Acids Research 48, no. 6 (February 25, 2020): 3195–210. http://dx.doi.org/10.1093/nar/gkaa129.
Повний текст джерелаGranier, Sophie A., Laura Hidalgo, Alvaro San Millan, Jose Antonio Escudero, Belen Gutierrez, Anne Brisabois, and Bruno Gonzalez-Zorn. "ArmA Methyltransferase in a Monophasic Salmonella enterica Isolate from Food." Antimicrobial Agents and Chemotherapy 55, no. 11 (August 22, 2011): 5262–66. http://dx.doi.org/10.1128/aac.00308-11.
Повний текст джерелаHopkins, Katie L., Jose A. Escudero, Laura Hidalgo, and Bruno Gonzalez-Zorn. "16S rRNA Methyltransferase RmtC inSalmonella entericaSerovar Virchow." Emerging Infectious Diseases 16, no. 4 (April 2010): 712–15. http://dx.doi.org/10.3201/eid1604.090736.
Повний текст джерелаRichter, Uwe, Kristina Kühn, Sachiko Okada, Axel Brennicke, Andreas Weihe, and Thomas Börner. "A mitochondrial rRNA dimethyladenosine methyltransferase in Arabidopsis." Plant Journal 61, no. 4 (February 2010): 558–69. http://dx.doi.org/10.1111/j.1365-313x.2009.04079.x.
Повний текст джерелаGupta, Kirti, Ankit Gupta, and Saman Habib. "Characterization of a Plasmodium falciparum rRNA methyltransferase." Molecular and Biochemical Parasitology 223 (July 2018): 13–18. http://dx.doi.org/10.1016/j.molbiopara.2018.06.001.
Повний текст джерелаXu, Zhili, Heather C. O'Farrell, Jason P. Rife, and Gloria M. Culver. "A conserved rRNA methyltransferase regulates ribosome biogenesis." Nature Structural & Molecular Biology 15, no. 5 (April 6, 2008): 534–36. http://dx.doi.org/10.1038/nsmb.1408.
Повний текст джерелаTomikawa, Chie. "7-Methylguanosine Modifications in Transfer RNA (tRNA)." International Journal of Molecular Sciences 19, no. 12 (December 17, 2018): 4080. http://dx.doi.org/10.3390/ijms19124080.
Повний текст джерелаAbedeera, Sudeshi M., Caitlin M. Hawkins, and Sanjaya C. Abeysirigunawardena. "RsmG forms stable complexes with premature small subunit rRNA during bacterial ribosome biogenesis." RSC Advances 10, no. 38 (2020): 22361–69. http://dx.doi.org/10.1039/d0ra02732d.
Повний текст джерелаInoue, Koichi, Soumit Basu, and Masayori Inouye. "Dissection of 16S rRNA Methyltransferase (KsgA) Function in Escherichia coli." Journal of Bacteriology 189, no. 23 (September 21, 2007): 8510–18. http://dx.doi.org/10.1128/jb.01259-07.
Повний текст джерелаAtkinson, Gemma C., Lykke H. Hansen, Tanel Tenson, Anette Rasmussen, Finn Kirpekar, and Birte Vester. "Distinction between the Cfr Methyltransferase Conferring Antibiotic Resistance and the Housekeeping RlmN Methyltransferase." Antimicrobial Agents and Chemotherapy 57, no. 8 (June 10, 2013): 4019–26. http://dx.doi.org/10.1128/aac.00448-13.
Повний текст джерелаSergeeva, Olga, Philipp Sergeev, Pavel Melnikov, Tatiana Prikazchikova, Olga Dontsova, and Timofei Zatsepin. "Modification of Adenosine196 by Mettl3 Methyltransferase in the 5’-External Transcribed Spacer of 47S Pre-rRNA Affects rRNA Maturation." Cells 9, no. 4 (April 24, 2020): 1061. http://dx.doi.org/10.3390/cells9041061.
Повний текст джерелаHager, Jutta, Bart L. Staker, and Ursula Jakob. "Substrate Binding Analysis of the 23S rRNA Methyltransferase RrmJ." Journal of Bacteriology 186, no. 19 (October 1, 2004): 6634–42. http://dx.doi.org/10.1128/jb.186.19.6634-6642.2004.
Повний текст джерелаDunn, Sianadh, Olivia Lombardi, and Victoria H. Cowling. "c-Myc co-ordinates mRNA cap methylation and ribosomal RNA production." Biochemical Journal 474, no. 3 (January 20, 2017): 377–84. http://dx.doi.org/10.1042/bcj20160930.
Повний текст джерелаBueno, Maria Fernanda C., Gabriela R. Francisco, Jessica A. O'Hara, Doroti de Oliveira Garcia та Yohei Doi. "Coproduction of 16S rRNA Methyltransferase RmtD or RmtG with KPC-2 and CTX-M Group Extended-Spectrum β-Lactamases in Klebsiella pneumoniae". Antimicrobial Agents and Chemotherapy 57, № 5 (4 березня 2013): 2397–400. http://dx.doi.org/10.1128/aac.02108-12.
Повний текст джерелаMcCulloch, Vicki, and Gerald S. Shadel. "Human Mitochondrial Transcription Factor B1 Interacts with the C-Terminal Activation Region of h-mtTFA and Stimulates Transcription Independently of Its RNA Methyltransferase Activity." Molecular and Cellular Biology 23, no. 16 (August 15, 2003): 5816–24. http://dx.doi.org/10.1128/mcb.23.16.5816-5824.2003.
Повний текст джерелаSharkey, Rory E., Johnny B. Herbert, Danielle A. McGaha, Vy Nguyen, Allyn J. Schoeffler, and Jack A. Dunkle. "Three critical regions of the erythromycin resistance methyltransferase, ErmE, are required for function supporting a model for the interaction of Erm family enzymes with substrate rRNA." RNA 28, no. 2 (November 18, 2021): 210–26. http://dx.doi.org/10.1261/rna.078946.121.
Повний текст джерелаLövgren, J. Mattias, and P. Mikael Wikström. "The rlmB Gene Is Essential for Formation of Gm2251 in 23S rRNA but Not for Ribosome Maturation inEscherichia coli." Journal of Bacteriology 183, no. 23 (December 1, 2001): 6957–60. http://dx.doi.org/10.1128/jb.183.23.6957-6960.2001.
Повний текст джерелаFarrow, Kylie A., Dena Lyras, Galina Polekhina, Katerina Koutsis, Michael W. Parker, and Julian I. Rood. "Identification of Essential Residues in the Erm(B) rRNA Methyltransferase of Clostridium perfringens." Antimicrobial Agents and Chemotherapy 46, no. 5 (May 2002): 1253–61. http://dx.doi.org/10.1128/aac.46.5.1253-1261.2002.
Повний текст джерелаSergeeva, O. V., D. E. Burakovsky, P. V. Sergiev, T. S. Zatsepin, M. Tomkuviene, S. Klimasauskas, and O. A. Dontsova. "Usage of rRNA-methyltransferase for site-specific fluorescent labeling." Moscow University Chemistry Bulletin 67, no. 2 (March 2012): 88–93. http://dx.doi.org/10.3103/s0027131412020058.
Повний текст джерелаKita, S., I. Tanaka, M. Yao, and Y. Tanaka. "Structural and functional analysis of rRNA methyltransferase fromStaphylococcus aureus." Acta Crystallographica Section A Foundations of Crystallography 67, a1 (August 22, 2011): C435—C436. http://dx.doi.org/10.1107/s0108767311089069.
Повний текст джерелаMann, Paul A., Liqun Xiong, Alexander S. Mankin, Andrew S. Chau, Cara A. Mendrick, David J. Najarian, Christina A. Cramer, et al. "EmtA, a rRNA methyltransferase conferring high-level evernimicin resistance." Molecular Microbiology 41, no. 6 (September 2001): 1349–56. http://dx.doi.org/10.1046/j.1365-2958.2001.02602.x.
Повний текст джерелаPintard, L. "MRM2 encodes a novel yeast mitochondrial 21S rRNA methyltransferase." EMBO Journal 21, no. 5 (March 1, 2002): 1139–47. http://dx.doi.org/10.1093/emboj/21.5.1139.
Повний текст джерелаGu, Xiang Rong, Claes Gustafsson, Jung Ku, Ming Yu, and Daniel V. Santi. "Identification of the 16S rRNA m5C967 Methyltransferase fromEscherichia coli†." Biochemistry 38, no. 13 (March 1999): 4053–57. http://dx.doi.org/10.1021/bi982364y.
Повний текст джерелаSu, Sai L., and David Dubnau. "Binding of Bacillus subtilis ermC' methyltransferase to 23S rRNA." Biochemistry 29, no. 25 (June 26, 1990): 6033–42. http://dx.doi.org/10.1021/bi00477a022.
Повний текст джерелаKumar, Atul, Santosh Kumar, and Bhupesh Taneja. "The structure of Rv2372c identifies an RsmE-like methyltransferase fromMycobacterium tuberculosis." Acta Crystallographica Section D Biological Crystallography 70, no. 3 (February 22, 2014): 821–32. http://dx.doi.org/10.1107/s1399004713033555.
Повний текст джерелаFritsche, Thomas R., Mariana Castanheira, George H. Miller, Ronald N. Jones, and Eliana S. Armstrong. "Detection of Methyltransferases Conferring High-Level Resistance to Aminoglycosides in Enterobacteriaceae from Europe, North America, and Latin America." Antimicrobial Agents and Chemotherapy 52, no. 5 (March 17, 2008): 1843–45. http://dx.doi.org/10.1128/aac.01477-07.
Повний текст джерелаWeitnauer, Gabriele, Sibylle Gaisser, Axel Trefzer, Sigrid Stockert, Lucy Westrich, Luis M. Quiros, Carmen Mendez, Jose A. Salas, and Andreas Bechthold. "An ATP-Binding Cassette Transporter and Two rRNA Methyltransferases Are Involved in Resistance to Avilamycin in the Producer Organism Streptomyces viridochromogenesTü57." Antimicrobial Agents and Chemotherapy 45, no. 3 (March 1, 2001): 690–95. http://dx.doi.org/10.1128/aac.45.3.690-695.2001.
Повний текст джерелаLyu, Guoliang, Le Zong, Chao Zhang, Xiaoke Huang, Wenbing Xie, Junnan Fang, Yiting Guan, et al. "Metastasis-related methyltransferase 1 (Merm1) represses the methyltransferase activity of Dnmt3a and facilitates RNA polymerase I transcriptional elongation." Journal of Molecular Cell Biology 11, no. 1 (March 21, 2018): 78–90. http://dx.doi.org/10.1093/jmcb/mjy023.
Повний текст джерелаLong, Katherine S., Jacob Poehlsgaard, Corinna Kehrenberg, Stefan Schwarz, and Birte Vester. "The Cfr rRNA Methyltransferase Confers Resistance to Phenicols, Lincosamides, Oxazolidinones, Pleuromutilins, and Streptogramin A Antibiotics." Antimicrobial Agents and Chemotherapy 50, no. 7 (July 2006): 2500–2505. http://dx.doi.org/10.1128/aac.00131-06.
Повний текст джерелаGustafsson, Claes, and Britt C. Persson. "Identification of the rrmA Gene Encoding the 23S rRNA m1G745 Methyltransferase in Escherichia coli and Characterization of an m1G745-Deficient Mutant." Journal of Bacteriology 180, no. 2 (January 15, 1998): 359–65. http://dx.doi.org/10.1128/jb.180.2.359-365.1998.
Повний текст джерелаYang, Weiwei, and Fupin Hu. "Research Updates of Plasmid-Mediated Aminoglycoside Resistance 16S rRNA Methyltransferase." Antibiotics 11, no. 7 (July 7, 2022): 906. http://dx.doi.org/10.3390/antibiotics11070906.
Повний текст джерелаSergeeva, O. V., I. V. Prokhorova, Y. Ordabaev, P. O. Tsvetkov, P. V. Sergiev, A. A. Bogdanov, A. A. Makarov, and O. A. Dontsova. "Properties of small rRNA methyltransferase RsmD: Mutational and kinetic study." RNA 18, no. 6 (April 25, 2012): 1178–85. http://dx.doi.org/10.1261/rna.032763.112.
Повний текст джерелаDemirci, H., L. H. G. Larsen, T. Hansen, A. Rasmussen, A. Cadambi, S. T. Gregory, F. Kirpekar, and G. Jogl. "Multi-site-specific 16S rRNA methyltransferase RsmF from Thermus thermophilus." RNA 16, no. 8 (June 17, 2010): 1584–96. http://dx.doi.org/10.1261/rna.2088310.
Повний текст джерелаLesnyak, Dmitry V., Jerzy Osipiuk, Tatiana Skarina, Petr V. Sergiev, Alexey A. Bogdanov, Aled Edwards, Alexei Savchenko, Andrzej Joachimiak, and Olga A. Dontsova. "Methyltransferase That Modifies Guanine 966 of the 16 S rRNA." Journal of Biological Chemistry 282, no. 8 (December 21, 2006): 5880–87. http://dx.doi.org/10.1074/jbc.m608214200.
Повний текст джерелаDenoya, C. D., and D. Dubnau. "Site and substrate specificity of the ermC 23S rRNA methyltransferase." Journal of Bacteriology 169, no. 8 (1987): 3857–60. http://dx.doi.org/10.1128/jb.169.8.3857-3860.1987.
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