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Journal Article
Journal Article
Proceedings of the Royal Society. B, Biological sciences, ISSN 1471-2954, 2007, Volume 274, Issue 1617, pp. 1533 - 1539
... (the longest breath-holding dive recorded for a marine vertebrate). High levels of fidelity and the relatively discrete nature of the home ranges demonstrate that protection of key migratory pathways, foraging and over-wintering sites can serve as an important tool for the future conservation of marine turtles. 
Habitat conservation | Foraging | Satellite tracking | Turtles | Beaches | Female animals | Nesting sites | Loggerhead turtles | Environmental conservation | Sea turtles | Over-wintering | Fidelity | Caretta caretta | Migration | Chelonia mydas | LEATHERBACK TURTLES | foraging | LOCATION ACCURACY | fidelity | CHELONIA-MYDAS | LOGGERHEAD | over-wintering | EVOLUTIONARY BIOLOGY | FISHERIES | CARETTA-CARETTA | GREEN TURTLES | HABITAT | BIOLOGY | migration | SATELLITE-TRACKING | ECOLOGY | Animals | Turtles - physiology | Cyprus | Animal Migration | Female | Conservation of Natural Resources | Seasons | Telemetry | Homing Behavior - physiology
Journal Article
Nature (London), ISSN 1476-4687, 2017, Volume 546, Issue 7656, pp. 113 - 117
... A site for peptide-bond formation. EF-Tu-dependent aminoacyl-tRNA delivery, therefore, ensures the high fidelity of aminoacyl-tRNA selection [5, 6, 9... 
EF-TU | ANGSTROM RESOLUTION | ESCHERICHIA-COLI RIBOSOME | AMINOACYL-TRANSFER-RNA | CRYSTAL-STRUCTURE | MULTIDISCIPLINARY SCIENCES | ELECTRON-MICROSCOPY | ELONGATION-FACTOR-TU | GENETIC-CODE TRANSLATION | GTP HYDROLYSIS | 16S RIBOSOMAL-RNA | Anticodon - ultrastructure | Ribosome Subunits - chemistry | Protein Biosynthesis | Anticodon - chemistry | Ribosomes - metabolism | RNA, Ribosomal, 16S - ultrastructure | GTP Phosphohydrolases - ultrastructure | Guanosine Triphosphate - metabolism | RNA, Transfer, Amino Acyl - metabolism | Protein Domains | Codon - genetics | RNA, Transfer, Amino Acyl - ultrastructure | RNA, Ribosomal, 16S - metabolism | Anticodon - genetics | Ribosomes - chemistry | Models, Molecular | RNA, Transfer, Amino Acyl - genetics | Escherichia coli - chemistry | Peptide Elongation Factor Tu - ultrastructure | Cryoelectron Microscopy | Hydrolysis | Peptide Elongation Factor Tu - metabolism | Codon - ultrastructure | Ribosomes - ultrastructure | Codon - chemistry | GTP Phosphohydrolases - metabolism | Escherichia coli - genetics | Ribosome Subunits - ultrastructure | RNA, Ribosomal, 16S - genetics | Escherichia coli - ultrastructure | Ribosome Subunits - metabolism | RNA sequencing | Messenger RNA | Physiological aspects | Observations | Genetic translation | Methods | Transfer RNA | Binding | Fidelity | Anticodons | GTP | High resolution | tRNA | Molecular structure | Ricin | Ribosomes | Elongation factor EF-Tu | Decoding | Ribonucleic acid--RNA | Intermediates | Proteins | Docks | Microscopy | Elongated structure | Accommodation | Codons | Molecular biology | Binding sites | Elongation | Conformation
Journal Article
RNA Biology, ISSN 1547-6286, 07/2013, Volume 10, Issue 7, pp. 1073 - 1079
Journal Article