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Cited by 537

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A conserved double-stranded RNA-binding domain.

Open access
St Johnston, D, Brown, N H, Gall, J G, Jantsch, M·1992·Proceedings of the National Academy of Sciences

Abstract

We have identified a double-stranded (ds)RNA-binding domain in each of two proteins: the product of the Drosophila gene staufen, which is required for the localization of maternal mRNAs, and a protein of unknown function, Xlrbpa, from Xenopus. The amino acid sequences of the binding domains are similar to each other and to additional domains in each protein. Database searches identified similar domains in several other proteins known or thought to bind dsRNA, including human dsRNA-activated inhibitor (DAI), human trans-activating region (TAR)-binding protein, and Escherichia coli RNase III. By analyzing in detail one domain in staufen and one in Xlrbpa, we delimited the minimal region that binds dsRNA. On the basis of the binding studies and computer analysis, we have derived a consensus sequence that defines a 65- to 68-amino acid dsRNA-binding domain.

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Metadata

Authors
St Johnston, D., Brown, N. H., Gall, J. G., & Jantsch, M.
Venue
Proceedings of the National Academy of Sciences
Published
1992-11-15
Volume
89
Issue
22
Pages
10979-10983
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W2128674562
Cited by
537
References
1
FWCI
8.53
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: A conserved double-stranded RNA-binding domain. https://app.cochat.ai/papers/10.1073/pnas.89.22.10979
The paper
St Johnston, D., Brown, N. H., Gall, J. G., & Jantsch, M. (1992). A conserved double-stranded RNA-binding domain. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.89.22.10979

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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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