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Cited by 366

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Evidence for reassociation of RNA-binding proteins after cell lysis: Implications for the interpretation of immunoprecipitation analyses

Open access
MILI, STAVROULA, STEITZ, JOAN A.·2004·RNA

Abstract

Immuno- and other affinity-purification approaches are commonly used to characterize the composition of ribonucleoprotein complexes. While associations detected by these procedures are often interpreted as reflecting in vivo interactions, it is also possible that they arise from reassociation of molecules after cell lysis. Here we used an experimental approach that allowed us to distinguish between these possibilities. Surprisingly, we show that the association of the RNA-binding protein HuR with its target mRNA, c-fos, as detected by co-immunoprecipitation, results largely from reassociation of molecules subsequent to cell lysis. The existence of such postlysis reassortments thus demonstrates that co-immunoprecipitation does not always recapitulate the in vivo state of ribonucleoprotein complexes.

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Metadata

Authors
MILI, S., & STEITZ, J. A.
Venue
RNA
Published
2004-09-23
Volume
10
Issue
11
Pages
1692-1694
ISSN
  • 1355-8382 (ISSN-L)
  • 1469-9001
OpenAlex
W2137969903
Cited by
366
References
1
FWCI
3.50
Type
journal article
Language
en
Open access
bronze

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CoChat. (2026). Citation check: Evidence for reassociation of RNA-binding proteins after cell lysis: Implications for the interpretation of immunoprecipitation analyses. https://app.cochat.ai/papers/10.1261/rna.7151404
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MILI, S., & STEITZ, J. A. (2004). Evidence for reassociation of RNA-binding proteins after cell lysis: Implications for the interpretation of immunoprecipitation analyses. RNA. https://doi.org/10.1261/rna.7151404

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