Published in J Biol Chem on August 25, 1988
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Steady state kinetic analysis of the mechanism of guanosine triphosphate hydrolysis catalyzed by Escherichia coli elongation factor G and the ribosome. Biochemistry (1976) 0.81
Isolation of physically and enzymically homogeneous Escherichia coli elongation factor G. Methods Enzymol (1979) 0.81
Selective chemical modification of Escherichia coli elongation factor G: butanedione modification of an arginine essential for nucleotide binding. Biochemistry (1977) 0.81
Selective chemical modification of Escherichia coli elongation factor G. N-Ethylmaleimide modification of a cysteine essential for nucleotide binding. J Biol Chem (1976) 0.80
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Chemical and physical studies on the structure of Escherichia coli elongation factor G. J Biol Chem (1975) 0.78
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Inactivation of Escherichia coli elongation factor Ts by the arginine-specific reagent butanedione. J Biol Chem (1979) 0.78
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A screening procedure for the intracellular expression of native proteins by Saccharomyces cerevisiae: discrimination of diphtheria toxin-resistant mutants. Yeast (1992) 0.75
Inactivation of Escherichia coli elongation factor Tu by the arginine-specific reagent butanedione. Arch Biochem Biophys (1980) 0.75
On the interaction of periodate oxidized GDP and its borohydride reduction product with the elongation factors Tu and G from Escherichia coli. FEBS Lett (1974) 0.75
Interactions of periodate-oxidized guanine nucleotides with Escherichia coli elongation factor G and the ribosome. Biochemistry (1974) 0.75