H
Hugh D. Sisler
Researcher at University of Maryland, College Park
Publications - 51
Citations - 2728
Hugh D. Sisler is an academic researcher from University of Maryland, College Park. The author has contributed to research in topics: Ergosterol & Sterol. The author has an hindex of 30, co-authored 51 publications receiving 2689 citations. Previous affiliations of Hugh D. Sisler include Lawrence University & Dow Chemical Company.
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Journal ArticleDOI
Inhibition of protein synthesis in vitro by cycloheximide
Malcolm R. Siegel,Hugh D. Sisler +1 more
TL;DR: The data presented here will show that incorporation of leucine labelled with carbon-14 into protein in a cell-free system from Saccharomyces pastorianus is inhibited by low concentrations of cycloheximide.
Journal ArticleDOI
Site of action of cycloheximide in cells of Saccharomyces pastorianus: II. The nature of inhibition of protein synthesis in a cell-free system
Malcolm R. Siegel,Hugh D. Sisler +1 more
TL;DR: The data indicate that the antibiotic Cycloheximide does not interfere with amino acid activation or transfer of activated amino acids to soluble-RNA, and the site of action apparently involves the transfer of amino acyl-soluble-RNA to the ribosomes and subsequent protein formation.
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Site of action of cycloheximide in cells of Saccharomyces pastorianus. 3. Further studies on the mechanism of action and the mechanism of resistance in saccharomyces species.
Malcolm R. Siegel,Hugh D. Sisler +1 more
TL;DR: Kinetics of cycloheximide-inhibited transfer of amino acids from soluble RNA to protein in a system from Saccharomyces pastorianus was further investigated and showed that resistance or susceptibility of the system to cyclo heximide is determined by the ribosomes and not by the supernatant enzymes.
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Benomyl and methyl-2-benzimidazolecarbamate (MBC): Biochemical, cytological and chemical aspects of toxicity to Ustilago maydis and Saccharomyces cerevesiae☆
TL;DR: Action of methyl-2-benzimidazolecarbamate (MBC), a breakdown product of benomyl, was studied in synchronous cultures of Ustilago maydis and Saccharomyces cerevesiae, showing markedly resembles mitotic arrest caused by colchicine and isopropyl N-phenylcarbamate in higher plants and griseofulvin in the fungus Aspergillus nidulans.
Journal ArticleDOI
Site of action of cycloheximide in cells of saccharomyces pastorianus. i. effect of the antibiotic on cellular metabolism.
Malcolm R. Siegel,Hugh D. Sisler +1 more
TL;DR: It is concluded that the primary action of cycloheximide is the inhibition of protein synthesis and that alterations in cellular metabolism in treated cells is a reflection of disrupted protein synthesis.