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Multisite phosphorylation of a synthetic peptide derived from the carboxyl terminus of the ribosomal protein S6 (open access)

Multisite phosphorylation of a synthetic peptide derived from the carboxyl terminus of the ribosomal protein S6

Article synthesizing and testing the synthetic peptide AKRRRLSSLRASTSKSESSQK (56-21) which corresponds to the carboxyl-terminal 21 amino acids of human ribosomal protein S6 as a substrate for S6/H4 kinase purified from human placenta. The data suggests that multiple S6 kinases may be required to phosphorylate S6 at all five sites which are modified in vivo.
Date: January 5, 1991
Creator: Brandon, Stanley D. & Masaracchia, Ruthann A.
System: The UNT Digital Library
Quantitative Studies of Inhibitors of ADP-ribosylation in Vitro and in Vivo (open access)

Quantitative Studies of Inhibitors of ADP-ribosylation in Vitro and in Vivo

Article evaluating the selectivity of compounds originally identified as inhibitors of poly(ADP-ribose) polymerase on members of the three classes of enzymes. The results suggest that micromolar levels of the benzamides in the culture medium should allow selective inhibition of poly(ADP-ribose) metabolism in intact cells. Furthermore, comparative quantitative inhibition studies should prove useful for assigning the biological effects of these inhibitors as an effect on either poly(ADP-ribose) or mono(ADP-ribose) metabolism.
Date: March 15, 1989
Creator: Rankin, Patrick W.; Jacobson, Elaine L.; Benjamin, Robert C.; Moss, Joel & Jacobson, Myron K.
System: The UNT Digital Library