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Cited by 450

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 access
Walder, R Y, Walder, J A·1988·Proceedings of the National Academy of Sciences

Abstract

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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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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CoChat. (2026). Citation check: Role of RNase H in hybrid-arrested translation by antisense oligonucleotides. https://app.cochat.ai/papers/10.1073/pnas.85.14.5011
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Walder, R. Y., & Walder, J. A. (1988). Role of RNase H in hybrid-arrested translation by antisense oligonucleotides. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.85.14.5011

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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.