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Boyd Hardesty

Researcher at University of Texas at Austin

Publications -  152
Citations -  6079

Boyd Hardesty is an academic researcher from University of Texas at Austin. The author has contributed to research in topics: Ribosome & Transfer RNA. The author has an hindex of 42, co-authored 152 publications receiving 5998 citations. Previous affiliations of Boyd Hardesty include University of Illinois at Chicago.

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BookDOI

Structure, function, and genetics of ribosomes

TL;DR: The papers in this book cover the Ribosome conference held at the University of Texas Marine Science Institute and topics covered include: Structure of ribosomes; Self-organization ofribosomal RNA; Structural dynamics of the translating ribosome; and Mechanism of Ribosomes Translocation.
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The Mechanism by which Cycloheximide and Related Glutarimide Antibiotics Inhibit Peptide Synthesis on Reticulocyte Ribosomes

TL;DR: Cycloheximide and related glutarimide antibiotics have been shown to affect binding, transfer enzyme II-dependent movement, and release of transfer RNA from the donor site of reticulocyte ribosomes, as well as both the initiation and extension of globin and phenylalanine peptides.
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The mechanism of sodium fluoride and cycloheximide inhibition of hemoglobin biosynthesis in the cell-free reticulocyte system.

TL;DR: Observations of the rate of amino acid incorporation indicate a sodium fluoride-sensitive reaction related to the initiation of new peptide chains on ribosomes that may bring about the increase in the proportion of monomeric ribosome because of a failure to re-form polysomes.
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Specificity of the protein kinase activity associated with the hemin-controlled repressor of rabbit reticulocyte.

TL;DR: Highly purified preparations of hemin-controlled repressor of rabbit reticulocyte contain a 3':5'-cyclic AMP-indenpendent protein kinase activity that phosphorylates the low-molecular-weight polypeptide chain of the initiation factor that forms a ternary complex with GTP and Met-tRNAf.
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The mechanism of cycloheximide inhibition of protein synthesis in rabbit reticulocytes.

TL;DR: Cycloheximide blocks the movement of peptidyl-tRNA from acceptor (aminoacyl) site to the donor (peptidyl) site on reticulocyte ribosomes and has no effect on the ribosome dependent GTPase activity of TF-II or on the peptide transferase reaction by which peptides on tRNA in the donor ribosomal site are transferred to an amino acid on t RNA in the acceptor site.