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Journal of Molecular Biology|May 25, 1983
Formation and properties of a covalent complex between elongation factor Tu and Phe-tRNA bearing a photoaffinity probe on its 3-(3-amino-3-carboxypropyl)uridine residueT Kao, D L Miller, M Abo, et al.Journal of the National Medical Association|July 1, 1987
Management of vascular traumaP R Cunningham, M CushmanRNA (New York, N.Y.)|July 17, 2001
A second function for pseudouridine synthases: A point mutant of RluD unable to form pseudouridines 1911, 1915, and 1917 in Escherichia coli 23S ribosomal RNA restores normal growth to an RluD-minus strainN S Gutgsell, M Del Campo, S Raychaudhuri, et al.Journal of Molecular Biology|January 5, 1984
Covalent crosslinking of Escherichia coli phenylalanyl-tRNA and valyl-tRNA to the ribosomal A site via photoaffinity probes attached to the 4-thiouridine residueL M Hsu, F L Lin, K Nurse, et al.The Journal of Biological Chemistry|August 25, 1984
High resolution localization of the tRNA anticodon interaction site on the Escherichia coli 30 S ribosomal subunitP Gornicki, K Nurse, W Hellmann, et al.Biochimie|October 1, 1987
Covalent cross-linking of AcVal-tRNA to Tetrahymena thermophila cytoplasmic ribosomes and two of its 17S rRNA mutantsK Nurse, J Colgan, R Denman, et al.Biochemistry|September 20, 1977
Synthesis and properties of nucleoside 5'-phosphoazidates derived from guanosine and adenosine nucleotides: effective on elongation factors G and Tu dependent reactionsS Chládek, K Quiggle, G Chinali, et al.Nucleic Acids Research|September 11, 1994
The single pseudouridine residue in Escherichia coli 16S RNA is located at position 516A Bakin, J A Kowalak, J A McCloskey, et al.Journal of Molecular Biology|October 5, 1988
Direct localization of the tRNA--anticodon interaction site on the Escherichia coli 30 S ribosomal subunit by electron microscopy and computerized image averagingT Wagenknecht, J Frank, M Boublik, et al.Biochemistry|November 14, 1997
Conformational analysis of Escherichia coli 30S ribosomes containing the single-base mutations G530U, U1498G, G1401C, and C1501G and the double-base mutation G1401C/C1501GH Moine, K Nurse, B Ehresmann, et al.Pageof 11