David C. Eustice
DuPont
15 Papers
482 Citations
David C. Eustice is an academic researcher from DuPont. The author has contributed to research in topics: Ribosome & Aminoglycoside. The author has an hindex of 12, co-authored 15 publications. Previous affiliations of David C. Eustice include Bayer Corporation & Bristol-Myers Squibb.
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Papers
Mechanism of action of DuP 721: inhibition of an early event during initiation of protein synthesis.
TL;DR: It is concluded that DuP 721 exerts its primary action at a step preceding the interaction of fMet-tRNA(fMet) and 30S ribosomal subunits with the initiator codon with the intent of inhibiting amino acid incorporation into proteins.
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Mechanisms of action of aminoglycoside antibiotics in eucaryotic protein synthesis.
TL;DR: It is found that the translocation of phe-tRNA on polyuridylate programmed ribosomes was susceptible to inhibition by paromomycin, and the in vitro translation of polysomes from two hygromycin B-resistant mutants was resistant to the inhibition of elongation caused by hygroitcin B.
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CD62/P-selectin binding sites for myeloid cells and sulfatides are overlapping.
Juergen Bajorath,Diane Hollenbaugh,Gordon King,William E. Harte,David C. Eustice,Richard P. Darveau,Alejandro Aruffo +6 more
TL;DR: The results suggest that the conservation of charged and hydrogen-bonding site chains is not sufficient to maintain the P-selectin function and that the exact stereochemistry provided by the side chains of residues lining the P -selectin binding pocket is critical for P- selectin binding.
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Altered 40 S ribosomal subunits in omnipotent suppressors of yeast
TL;DR: It is demonstrated that ribosomes from the four suppressors SUP35, SUP44, SUP45 and SUP46 translate polyuridylate templates in vitro with higher errors than ribosome from the normal stain, and that this misreading is substantially enhanced by the antibiotic paromomycin.
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The mechanism of action of DuP 721, a new antibacterial agent: effects on macromolecular synthesis.
TL;DR: In cell-free systems, DuP 721 concentrations up to 100 microM did not inhibit peptide chain elongation reactions under conditions where chloramphenicol, tetracycline and hygromycin B inhibited these reactions.
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