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Cited by 260

The DOI matches its Crossref record; 19 of the 19 references it cites were found in a registry or an index.

Protein Displacement by DExH/D "RNA Helicases" Without Duplex Unwinding

Fairman, Margaret E., Maroney, Patricia A., Wang, Wen, Bowers, Heath A., Gollnick, Paul, Nilsen, Timothy W., Jankowsky, Eckhard·2004·Science

Abstract

Members of the DExH/D superfamily of nucleic acid–activated nucleotide triphosphatases are essential for virtually all aspects of RNA metabolism, including pre–messenger RNA splicing, RNA interference, translation, and nucleocytoplasmic trafficking. Physiological substrates for these enzymes are thought to be regions of double-stranded RNA, because several DExH/D proteins catalyze strand separation in vitro. These “RNA helicases” can also disrupt RNA-protein interactions, but it is unclear whether this activity is coupled to duplex unwinding. Here we demonstrate that two unrelated DExH/D proteins catalyze protein displacement independently of duplex unwinding. Therefore, the essential functions of DExH/D proteins are not confined to RNA duplexes but can be exerted on a wide range of ribonucleoprotein substrates.

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Metadata

Authors
Fairman, M. E., Maroney, P. A., Wang, W., Bowers, H. A., Gollnick, P., Nilsen, T. W., & Jankowsky, E.
Venue
Science
Published
2004-04-30
Volume
304
Issue
5671
Pages
730-734
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W2051537724
Cited by
260
References
19
FWCI
9.73
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Protein Displacement by DExH/D "RNA Helicases" Without Duplex Unwinding. https://app.cochat.ai/papers/10.1126/science.1095596
The paper
Fairman, M. E., Maroney, P. A., Wang, W., Bowers, H. A., Gollnick, P., Nilsen, T. W., & Jankowsky, E. (2004). Protein Displacement by DExH/D "RNA Helicases" Without Duplex Unwinding. Science. https://doi.org/10.1126/science.1095596

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