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Cited by 194

The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.

HSP90 Protein Stabilizes Unloaded Argonaute Complexes and Microscopic P-bodies in Human Cells

Open access
Johnston, Michael, Geoffroy, Marie-Claude, Sobala, Andrew, Hay, Ron, Hutvagner, Gyorgy·2010·Molecular Biology of the Cell

Abstract

Key components of the miRNA-mediated gene regulation pathway are localized in cytoplasmic processing bodies (P-bodies). Mounting evidence suggests that the presence of microscopic P-bodies are not always required for miRNA-mediated gene regulation. Here we have shown that geldanamycin, a well-characterized HSP90 inhibitor, abolishes P-bodies and significantly reduces Argonaute and GW182 protein levels but does not affect the miRNA level and the efficiency of miRNA-mediated gene repression; however, it significantly impairs siRNA loading and the efficacy of exogenous siRNA. Our data suggests that HSP90 protein chaperones Argonautes before binding RNA and may facilitate efficient loading of small RNA.

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Metadata

Authors
Johnston, M., Geoffroy, M.-C., Sobala, A., Hay, R., & Hutvagner, G.
Venue
Molecular Biology of the Cell
Published
2010-05
Volume
21
Issue
9
Pages
1462-1469
ISSN
  • 1059-1524 (ISSN-L)
  • 1939-4586
OpenAlex
W2140786935
Cited by
194
References
2
FWCI
7.33
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: HSP90 Protein Stabilizes Unloaded Argonaute Complexes and Microscopic P-bodies in Human Cells. https://app.cochat.ai/papers/10.1091/mbc.e09-10-0885
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Johnston, M., Geoffroy, M.-C., Sobala, A., Hay, R., & Hutvagner, G. (2010). HSP90 Protein Stabilizes Unloaded Argonaute Complexes and Microscopic P-bodies in Human Cells. Molecular Biology of the Cell. https://doi.org/10.1091/mbc.e09-10-0885

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