Статті в журналах з теми "TRNAfMet"
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Steiner-Mosonyi, Marta, Carole Creuzenet, Robert A. B. Keates, Benjamin R. Strub, and Dev Mangroo. "ThePseudomonas aeruginosaInitiation Factor IF-2 Is Responsible for Formylation-independent Protein Initiation inP. aeruginosa." Journal of Biological Chemistry 279, no. 50 (September 22, 2004): 52262–69. http://dx.doi.org/10.1074/jbc.m408086200.
Повний текст джерелаLi, Yan, William B. Holmes, Dean R. Appling, and Uttam L. RajBhandary. "Initiation of Protein Synthesis in Saccharomyces cerevisiae Mitochondria without Formylation of the Initiator tRNA." Journal of Bacteriology 182, no. 10 (May 15, 2000): 2886–92. http://dx.doi.org/10.1128/jb.182.10.2886-2892.2000.
Повний текст джерелаFratte, Sonia Delle, Chiara Piubelli, and Enrico Domenici. "Development of a High-Throughput Scintillation Proximity Assay for the Identification of C-Domain Translational Initiation Factor 2 Inhibitors." Journal of Biomolecular Screening 7, no. 6 (December 2002): 541–46. http://dx.doi.org/10.1177/1087057102238628.
Повний текст джерелаSchmitt, Emmanuelle, Michel Panvert, Sylvain Blanquet, and Yves Mechulam. "Crystal structure of methionyl-tRNAfMet transformylase complexed with the initiator formyl-methionyl-tRNAfMet." EMBO Journal 17, no. 23 (December 1, 1998): 6819–26. http://dx.doi.org/10.1093/emboj/17.23.6819.
Повний текст джерелаPolishchuk, L. V. "Nucleotide sequences of tRNA-methonine genes of Streptomyces globisporus 1912-2, identified in silico." Visnik ukrains'kogo tovaristva genetikiv i selekcioneriv 14, no. 1 (June 20, 2016): 58–62. http://dx.doi.org/10.7124/visnyk.utgis.14.1.545.
Повний текст джерелаNomura, Teruaki, Nobuyuki Fujita, and Akira Ishihama. "Promoter selectivity ofEscherichia coliRNA polymerase: alteration by fMet-tRNAfMet." Nucleic Acids Research 14, no. 17 (1986): 6857–70. http://dx.doi.org/10.1093/nar/14.17.6857.
Повний текст джерелаRodnina, M. V., Y. P. Semenkov, and W. Wintermeyer. "Purification of fMET-tRNAfMET by Fast Protein Liquid Chromatography." Analytical Biochemistry 219, no. 2 (June 1994): 380–81. http://dx.doi.org/10.1006/abio.1994.1282.
Повний текст джерелаFerguson, Blair Q., and David C. H. Yang. "Topographic modeling of free and methionyl-tRNA synthetase-bound tRNAfMet by singlet-singlet energy transfer: bending of the 3'-terminal arm in tRNAfMet." Biochemistry 25, no. 21 (October 1986): 6572–78. http://dx.doi.org/10.1021/bi00369a035.
Повний текст джерелаDuroc, Yann, Carmela Giglione, and Thierry Meinnel. "Mutations in Three Distinct Loci Cause Resistance to Peptide Deformylase Inhibitors in Bacillus subtilis." Antimicrobial Agents and Chemotherapy 53, no. 4 (January 26, 2009): 1673–78. http://dx.doi.org/10.1128/aac.01340-08.
Повний текст джерелаGuenneugues, Marc, Enrico Caserta, Letizia Brandi, Roberto Spurio, Sylvie Meunier, Cynthia L. Pon, Rolf Boelens, and Claudio O. Gualerzi. "Mapping the fMet-tRNAfMet binding site of initiation factor IF2." EMBO Journal 19, no. 19 (October 2, 2000): 5233–40. http://dx.doi.org/10.1093/emboj/19.19.5233.
Повний текст джерелаDonga, Robert A., Tak-Hang Chan, and Masad J. Damha. "Ion-tagged synthesis of an oligoribonucleotide pentamer — The continuing versatility of TBDMS chemistry." Canadian Journal of Chemistry 85, no. 4 (April 1, 2007): 274–82. http://dx.doi.org/10.1139/v07-022.
Повний текст джерелаJurėnas, Dukas, Sneha Chatterjee, Albert Konijnenberg, Frank Sobott, Louis Droogmans, Abel Garcia-Pino, and Laurence Van Melderen. "AtaT blocks translation initiation by N-acetylation of the initiator tRNAfMet." Nature Chemical Biology 13, no. 6 (April 3, 2017): 640–46. http://dx.doi.org/10.1038/nchembio.2346.
Повний текст джерелаSchmitt, Emmanuelle, Yves Mechulam, Marc Ruff, Andre Mitschler, Dino Moras, and Sylvain Blanquet. "Crystallization and preliminary X-ray analysis ofEscherichia coli methionyl–tRNAfMet formyltransferase." Proteins: Structure, Function, and Genetics 25, no. 1 (May 1996): 139–41. http://dx.doi.org/10.1002/prot.14.
Повний текст джерелаMeunier, S. "Structure of the fMet-tRNAfMet-binding domain of B.stearothermophilus initiation factor IF2." EMBO Journal 19, no. 8 (April 17, 2000): 1918–26. http://dx.doi.org/10.1093/emboj/19.8.1918.
Повний текст джерелаGuillon, Jean-Michel, Thierry Meinnel, Yves Mechulam, Christine Lazennec, Sylvain Blanquet, and Guy Fayat. "Nucleotides of tRNA governing the specificity of Escherichia coli methionyl-tRNAfMet formyltransferase." Journal of Molecular Biology 224, no. 2 (March 1992): 359–67. http://dx.doi.org/10.1016/0022-2836(92)91000-f.
Повний текст джерелаSchmitt, Emmanuelle, Yves Mechulam, Marc Ruff, Andre Mitschler, Dino Moras, and Sylvain Blanquet. "Crystallization and preliminary x‐ray analysis of Escherichia coli methionyl‐tRNAfMet formyltransferase." Proteins: Structure, Function, and Genetics 25, no. 1 (May 1996): 139–41. http://dx.doi.org/10.1002/(sici)1097-0134(199605)25:1<139::aid-prot14>3.3.co;2-z.
Повний текст джерелаBiedenbänder, Thomas, Vanessa de Jesus, Martina Schmidt-Dengler, Mark Helm, Björn Corzilius, and Boris Fürtig. "RNA modifications stabilize the tertiary structure of tRNAfMet by locally increasing conformational dynamics." Nucleic Acids Research 50, no. 4 (February 7, 2022): 2334–49. http://dx.doi.org/10.1093/nar/gkac040.
Повний текст джерелаRoy, Bappaditya, Qi Liu, Shinichiro Shoji, and Kurt Fredrick. "IF2 and unique features of initiator tRNAfMet help establish the translational reading frame." RNA Biology 15, no. 4-5 (November 13, 2017): 604–13. http://dx.doi.org/10.1080/15476286.2017.1379636.
Повний текст джерелаPande, Chandramohan, and Arnold Wishnia. "Characterization of the fluorescent bimane derivative of E. coli initiator transfer RNA (tRNAfMet)." Biochemical and Biophysical Research Communications 127, no. 1 (February 1985): 49–55. http://dx.doi.org/10.1016/s0006-291x(85)80124-8.
Повний текст джерелаMeinnel, Thierry, Yves Mechulam, Sylvain Blanquet, and Guy Fayat. "Binding of the anticodon domain of tRNAfMet to Escherichia coli methionyl-tRNA synthetase." Journal of Molecular Biology 220, no. 2 (July 1991): 205–8. http://dx.doi.org/10.1016/0022-2836(91)90003-o.
Повний текст джерелаTakahiro, Nagase, Ishii Shunsuke, and Imamoto Fumio. "Differential transcriptional control of the two tRNAfMet genes of Escherichia coli K-12." Gene 67, no. 1 (July 1988): 49–57. http://dx.doi.org/10.1016/0378-1119(88)90007-8.
Повний текст джерелаDi Pietro, E., J. Sirois, M. L. Tremblay, and R. E. MacKenzie. "Mitochondrial NAD-Dependent Methylenetetrahydrofolate Dehydrogenase-Methenyltetrahydrofolate Cyclohydrolase Is Essential for Embryonic Development." Molecular and Cellular Biology 22, no. 12 (June 15, 2002): 4158–66. http://dx.doi.org/10.1128/mcb.22.12.4158-4166.2002.
Повний текст джерелаFerguson, Blair Q., and David C. H. Yang. "tRNAfMet-induced conformational transition at the intersubunit domain of fluorescent-labeled methionyl-tRNA synthetase." Biochemistry 25, no. 10 (May 1986): 2743–48. http://dx.doi.org/10.1021/bi00358a001.
Повний текст джерелаAgrawal, Rajendra K., Christian M. T. Spahn, Pawel Penczek, Robert A. Grassucci, Knud H. Nierhaus, and Joachim Frank. "Visualization of Trna Movements on the Escherichia coli 70s Ribosome during the Elongation Cycle." Journal of Cell Biology 150, no. 3 (August 7, 2000): 447–60. http://dx.doi.org/10.1083/jcb.150.3.447.
Повний текст джерелаMayer, C. "Conformational change of Escherichia coli initiator methionyl-tRNAfMet upon binding to methionyl-tRNA formyl transferase." Nucleic Acids Research 30, no. 13 (July 1, 2002): 2844–50. http://dx.doi.org/10.1093/nar/gkf411.
Повний текст джерелаBonocora, Richard P., and David A. Shub. "A novel group I intron-encoded endonuclease specific for the anticodon region of tRNAfMet genes." Molecular Microbiology 39, no. 5 (February 24, 2004): 1299–306. http://dx.doi.org/10.1111/j.1365-2958.2001.02318.x.
Повний текст джерелаHansen, Peter Kamp, Brian F. C. Clark, and Hans Uffe Petersen. "Interaction between non-formylated initiator Met-tRNAfMet and the ribosomal A-site from Escherichia coli." Biochimie 69, no. 8 (August 1987): 871–77. http://dx.doi.org/10.1016/0300-9084(87)90214-8.
Повний текст джерелаJohansson, Magnus, Ka-Weng Ieong, Stefan Trobro, Peter Strazewski, Johan Åqvist, Michael Y. Pavlov, and Måns Ehrenberg. "pH-sensitivity of the ribosomal peptidyl transfer reaction dependent on the identity of the A-site aminoacyl-tRNA." Proceedings of the National Academy of Sciences 108, no. 1 (December 17, 2010): 79–84. http://dx.doi.org/10.1073/pnas.1012612107.
Повний текст джерелаGross, Martin, Mark S. Rubino, and Suzanne M. Hessefort. "The conversion of eIF-2·GDP to eIF-2·GTP by eIF-2B requires Met-tRNAfMet." Biochemical and Biophysical Research Communications 181, no. 3 (December 1991): 1500–1507. http://dx.doi.org/10.1016/0006-291x(91)92109-w.
Повний текст джерелаChan, Ka-Kong, Perry Rosen, Anthony Specian, Jr., Herbert Weissbach, and Carlos Spears. "Synthesis and Activity of a Tetrahydrofolate Inhibitor of the Enzyme N10-Formyl-H4-folate-Met-tRNAfMet Transformylase." HETEROCYCLES 24, no. 11 (1986): 3079. http://dx.doi.org/10.3987/r-1986-11-3079.
Повний текст джерелаPERREAULT, Jean-Pierre, Richard T. PON, Mei-yan JIANG, Nassim USMAN, Jana PIKA, Kelvin K. OGILVIE, and Robert CEDERGREN. "The synthesis and functional evaluation of RNA and DNA polymers having the sequence of Escherichia coli tRNAfMet." European Journal of Biochemistry 186, no. 1-2 (December 1989): 87–93. http://dx.doi.org/10.1111/j.1432-1033.1989.tb15181.x.
Повний текст джерелаPelka, Heike, and LaDonne H. Schulman. "Study of the interaction of Escherichia coli methionyl-tRNA synthetase with tRNAfMet using chemical and enzymic probes." Biochemistry 25, no. 15 (July 1986): 4450–56. http://dx.doi.org/10.1021/bi00363a042.
Повний текст джерелаKrafft, Christoph, Annette Diehl, Stefan Laettig, Joachim Behlke, Udo Heinemann, Cynthia L. Pon, Claudio O. Gualerzi, and Heinz Welfle. "Interaction of fMet-tRNAfMet with the C-terminal domain of translational initiation factor IF2 from Bacillus stearothermophilus." FEBS Letters 471, no. 2-3 (April 10, 2000): 128–32. http://dx.doi.org/10.1016/s0014-5793(00)01377-6.
Повний текст джерелаWagner, T., C. Rundquist, M. Gross, and P. B. Sigler. "Structural features that underlie the use of bacterial Met-tRNAfMet primarily as an elongator in eukaryotic protein synthesis." Journal of Biological Chemistry 264, no. 31 (November 1989): 18506–11. http://dx.doi.org/10.1016/s0021-9258(18)51496-4.
Повний текст джерелаFerguson, Blair Q., and David C. H. Yang. "Localization of noncovalently bound ethidium in free and methionyl-tRNA synthetase bound tRNAfMet by singlet-singlet energy transfer." Biochemistry 25, no. 18 (September 1986): 5298–304. http://dx.doi.org/10.1021/bi00366a046.
Повний текст джерелаHountondji, Codjo, Sylvain Blanquet, and Florence Lederer. "Methionyl-tRNA synthetase from Escherichia coli: primary structure at the binding site for the 3'-end of tRNAfMet." Biochemistry 24, no. 5 (February 26, 1985): 1175–80. http://dx.doi.org/10.1021/bi00326a018.
Повний текст джерелаStolboushkina, Elena, Stanislav Nikonov, Natalia Zelinskaya, Valentina Arkhipova, Alexei Nikulin, Maria Garber, and Oleg Nikonov. "Crystal Structure of the Archaeal Translation Initiation Factor 2 in Complex with a GTP Analogue and Met-tRNAfMet." Journal of Molecular Biology 425, no. 6 (March 2013): 989–98. http://dx.doi.org/10.1016/j.jmb.2012.12.023.
Повний текст джерелаShu, H. H., C. A. Wise, G. D. Clark-Walker, and N. C. Martin. "A gene required for RNase P activity in Candida (Torulopsis) glabrata mitochondria codes for a 227-nucleotide RNA with homology to bacterial RNase P RNA." Molecular and Cellular Biology 11, no. 3 (March 1991): 1662–67. http://dx.doi.org/10.1128/mcb.11.3.1662-1667.1991.
Повний текст джерелаKrawczak, Felipe S., Marcelo B. Labruna, Joy A. Hecht, Christopher D. Paddock, and Sandor E. Karpathy. "Genotypic Characterization of Rickettsia bellii Reveals Distinct Lineages in the United States and South America." BioMed Research International 2018 (2018): 1–8. http://dx.doi.org/10.1155/2018/8505483.
Повний текст джерелаShu, H. H., C. A. Wise, G. D. Clark-Walker, and N. C. Martin. "A gene required for RNase P activity in Candida (Torulopsis) glabrata mitochondria codes for a 227-nucleotide RNA with homology to bacterial RNase P RNA." Molecular and Cellular Biology 11, no. 3 (March 1991): 1662–67. http://dx.doi.org/10.1128/mcb.11.3.1662.
Повний текст джерелаBattermann, Anja, Claudia Disse-Krömker, and Brigitte Dreiseikelmann. "A functional plasmid-borne rrn operon in soil isolates belonging to the genus Paracoccus." Microbiology 149, no. 12 (December 1, 2003): 3587–93. http://dx.doi.org/10.1099/mic.0.26608-0.
Повний текст джерелаDavis, D. R., R. H. Griffey, Z. Yamaizumi, S. Nishimura, and C. D. Poulter. "15N-labeled tRNA. Identification of dihydrouridine in Escherichia coli tRNAfMet, tRNALys, and tRNAPhe by 1H-15N two-dimensional NMR." Journal of Biological Chemistry 261, no. 8 (March 1986): 3584–87. http://dx.doi.org/10.1016/s0021-9258(17)35686-7.
Повний текст джерелаBarraud, Pierre, Emmanuelle Schmitt, Yves Mechulam, Frédéric Dardel, and Carine Tisné. "A unique conformation of the anticodon stem-loop is associated with the capacity of tRNAfMet to initiate protein synthesis." Nucleic Acids Research 36, no. 15 (July 23, 2008): 4894–901. http://dx.doi.org/10.1093/nar/gkn462.
Повний текст джерелаGriffey, R. H., D. Davis, Z. Yamaizumi, S. Nishimura, A. Bax, B. Hawkins, and C. D. Poulter. "15N-labeled Escherichia coli tRNAfMet, tRNAGlu, tRNATyr, and tRNAPhe. Double resonance and two-dimensional NMR of N1-labeled pseudouridine." Journal of Biological Chemistry 260, no. 17 (August 1985): 9734–41. http://dx.doi.org/10.1016/s0021-9258(17)39300-6.
Повний текст джерелаLevin, Itay, Moshe Mevarech, and Bruce A. Palfey. "Characterization of a Novel Bifunctional Dihydropteroate Synthase/Dihydropteroate Reductase Enzyme from Helicobacter pylori." Journal of Bacteriology 189, no. 11 (April 6, 2007): 4062–69. http://dx.doi.org/10.1128/jb.01878-06.
Повний текст джерелаDžupponová, Veronika, Nataša Tomášková, Andrea Antošová, Erik Sedlák, and Gabriel Žoldák. "Salt-Specific Suppression of the Cold Denaturation of Thermophilic Multidomain Initiation Factor 2." International Journal of Molecular Sciences 24, no. 7 (April 5, 2023): 6787. http://dx.doi.org/10.3390/ijms24076787.
Повний текст джерелаMonestier, Auriane, Alexey Aleksandrov, Pierre-Damien Coureux, Michel Panvert, Yves Mechulam, and Emmanuelle Schmitt. "The structure of an E. coli tRNAfMet A1–U72 variant shows an unusual conformation of the A1–U72 base pair." RNA 23, no. 5 (January 31, 2017): 673–82. http://dx.doi.org/10.1261/rna.057877.116.
Повний текст джерелаKenri, Tsuyoshi, Fumio Imamoto, and Yasunobu Kano. "Construction and characterization of an Escherichia coli mutant deficient in the metY gene encoding tRNAf2Met: either tRNAf1Met or tRNAf2Met is required for cell growth." Gene 114, no. 1 (May 1992): 109–14. http://dx.doi.org/10.1016/0378-1119(92)90715-2.
Повний текст джерелаFerguson, Blair Q., and David C. H. Yang. "Methionyl-tRNA synthetase induced 3'-terminal and delocalized conformational transition in tRNAfMet: steady-state fluorescence of tRNA with a single fluorophore." Biochemistry 25, no. 3 (February 11, 1986): 529–39. http://dx.doi.org/10.1021/bi00351a002.
Повний текст джерелаFörster, Charlotte, Christoph Krafft, Heinz Welfle, Claudio O. Gualerzi, and Udo Heinemann. "Preliminary characterization by X-ray diffraction and Raman spectroscopy of a crystalline complex ofBacillus stearothermophilusinitiation factor 2 C-domain and fMet-tRNAfMet." Acta Crystallographica Section D Biological Crystallography 55, no. 3 (March 1, 1999): 712–16. http://dx.doi.org/10.1107/s0907444998014577.
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