FEBS Letters · 1979 · 69 citations · 13 references
Life SciencesBiochemistryBiologyProtein BiochemistryProtein TranslationStructural BiologyProtein Sequence AnalysisProtein StructureProtein SynthesisRibosome StructureTranslation ElongationTranslation In ProkaryotesBacterial Ribosome StructureProtein Sequence EvolutionRibosomal Protein StructureRibosomal Protein SynthesisRibosome Biogenesis In ProkaryotesTranslation Elongation In EukaryotesTranslation Elongation In Prokaryotes
Protein eL12/eL12-P from Artemia salina 80 S ribosomes plays a role in the elongation step of protein synthetic reactions [l-3]. It is an acidic protein which was shown [2,3] to be partially phosphorylated on a single serine residue. Like the homologous proteins from procaryotic organisms, eL12/eL12-P from A. dina occurs in more than one copy per large subunit [3]; the isolated protein dimerizes in aqueous solutions [ 31.
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Carl R. Woese, Linda J. Magrum, George E. Fox · Journal of Molecular Evolution · 1978 · 536 citations
Energetics and Structure of Halophilic Microorganisms
D. J. Kushner · FEBS Letters · 1980 · 383 citations
Cox Terhorst, W. Möller, Richard A. Laursen et al. · European Journal of Biochemistry · 1973 · 205 citations