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The Mechanism by which Cycloheximide and Related Glutarimide Antibiotics Inhibit Peptide Synthesis on Reticulocyte Ribosomes

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Obrig, Tom G., Culp, William J., McKeehan, Wallace L., Hardesty, Boyd·1971·Journal of Biological Chemistry

Abstract

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. They inhibit binding of deacylated tRNAphe to reticulocyte ribosomes in the absence of transfer enzymes at concentrations similar to those that inhibit peptide initiation. These concentrations are below those required for comparable inhibition of peptide extension or transfer enzyme II-dependent translocation of peptidyl-tRNA from the acceptor to the donor ribosomal sites and appear to provide the basis for differential inhibition of peptide initiation and extension.

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Metadata

Authors
Obrig, T. G., Culp, W. J., McKeehan, W. L., & Hardesty, B.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1971-01
Volume
246
Issue
1
Pages
174-181
ISSN
0021-9258 (ISSN-L)
OpenAlex
W1491060698
Cited by
512
References
0
FWCI
10.41
Type
journal article
Language
en
Open access
hybrid

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CoChat. (2026). Citation check: The Mechanism by which Cycloheximide and Related Glutarimide Antibiotics Inhibit Peptide Synthesis on Reticulocyte Ribosomes. https://app.cochat.ai/papers/10.1016/s0021-9258(18)62546-3
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Obrig, T. G., Culp, W. J., McKeehan, W. L., & Hardesty, B. (1971). The Mechanism by which Cycloheximide and Related Glutarimide Antibiotics Inhibit Peptide Synthesis on Reticulocyte Ribosomes. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(18)62546-3

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.