The DOI matches its Crossref record; 23 of the 23 references it cites were found in a registry or an index.
Role of RNase H in hybrid-arrested translation by antisense oligonucleotides.
Open accessAbstract
The mechanism of hybrid-arrested translation by antisense oligodeoxynucleotides has been investigated with the rabbit reticulocyte lysate system. The oligonucleotides studied were directed against different regions of mouse alpha- or beta-globin mRNAs. Freshly prepared reticulocyte lysates were found to contain 1-2% of the level of RNase H in nucleated cells. This level of activity was sufficient to cleave nearly 100% of the targeted mRNA at the site of hybridization with a complementary oligodeoxynucleotide in 1 hr under conditions of active translation. Using poly(rA).oligo(dT) as a competitive inhibitor of the enzyme, hybrid arrest by oligodeoxynucleotides complementary to the sequence spanning the initiation codon or to a sequence in the coding region was found to be due entirely to cleavage of mRNA by RNase H. Hybridization of oligodeoxynucleotides adjacent to the cap site of beta-globin mRNA, but not the alpha-globin mRNA, also inhibited protein synthesis directly. Even in this case, however, cleavage of the mRNA by RNase H was the predominant pathway of inhibition.
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Cites
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Cited by
Antisense Oligonucleotides as Therapeutic Agents—Is the Bullet Really Magical?
Stein, C. A., & Cheng, Y.-C. (1993) · Science · doi:10.1126/science.8351515 · Cited by 1,303
Morpholino Antisense Oligomers: Design, Preparation, and Properties
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Antidepressants and Hypothalamic-Pituitary-Adrenocortical Regulation
HOLSBOER, F., & BARDEN, N. (1996) · Endocrine Reviews · doi:10.1210/edrv-17-2-187 · Cited by 852
Phosphorothioates, Essential Components of Therapeutic Oligonucleotides
Eckstein, F. (2014) · Nucleic Acid Therapeutics · doi:10.1089/nat.2014.0506 · Cited by 684
Kozak, M. (1989) · Molecular and Cellular Biology · doi:10.1128/mcb.9.11.5134 · Cited by 630
Metadata
- Authors
- Walder, R. Y., & Walder, J. A.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1988-07
- Volume
- 85
- Issue
- 14
- Pages
- 5011-5015
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2063915751
- Cited by
- 450
- References
- 23
- FWCI
- 7.24
- Type
- journal article
- Language
- en
- Open access
- green
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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