The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.
Hfq and its constellation of RNA
Open accessAbstract
Hfq is an RNA-binding protein that is common to diverse bacterial lineages and has key roles in the control of gene expression. By facilitating the pairing of small RNAs with their target mRNAs, Hfq affects the translation and turnover rates of specific transcripts and contributes to complex post-transcriptional networks. These functions of Hfq can be attributed to its ring-like oligomeric architecture, which presents two non-equivalent binding surfaces that are capable of multiple interactions with RNA molecules. Distant homologues of Hfq occur in archaea and eukaryotes, reflecting an ancient origin for the protein family and hinting at shared functions. In this Review, we describe the salient structural and functional features of Hfq and discuss possible mechanisms by which this protein can promote RNA interactions to catalyse specific and rapid regulatory responses in vivo.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Quantifying E. coli Proteome and Transcriptome with Single-Molecule Sensitivity in Single Cells
Taniguchi, Y., Choi, P. J., Li, G.-W., Chen, H., Babu, M., Hearn, J., Emili, A., & Xie, X. S. (2010) · Science · doi:10.1126/science.1188308 · Cited by 1,982 · cited 1×
“However, most bacterial mRNAs are present in low number”
BackgroundInteraction network containing conserved and essential protein complexes in Escherichia coli
Butland, G., Peregrín-Alvarez, J. M., Li, J., Yang, W., Yang, X., Canadien, V., Starostine, A., Richards, D., Beattie, B., Krogan, N., et al. (2005) · Nature · doi:10.1038/nature03239 · Cited by 1,201
Identification of novel small RNAs using comparative genomics and microarrays
Wassarman, K. M., Repoila, F., Rosenow, C., Storz, G., & Gottesman, S. (2001) · Genes & Development · doi:10.1101/gad.901001 · Cited by 723
Global Functional Atlas of Escherichia coli Encompassing Previously Uncharacterized Proteins
Hu, P., Janga, S. C., Babu, M., Díaz-Mejía, J. J., Butland, G., Yang, W., Pogoutse, O., Guo, X., Phanse, S., Wong, P., et al. (2009) · PLoS Biology · doi:10.1371/journal.pbio.1000096 · Cited by 387
HITS-CLIP: panoramic views of protein-RNA regulation in living cells
Darnell, R. B. (2010) · WIREs RNA · doi:10.1002/wrna.31 · Cited by 382
Cited by
The Noncoding RNA Revolution—Trashing Old Rules to Forge New Ones
Cech, T. R., & Steitz, J. A. (2014) · Cell · doi:10.1016/j.cell.2014.03.008 · Cited by 2,524
Quorum sensing signal-response systems in Gram-negative bacteria
Papenfort, K., & Bassler, B. L. (2016) · Nature Reviews Microbiology · doi:10.1038/nrmicro.2016.89 · Cited by 2,256
Dual RNA-seq unveils noncoding RNA functions in host–pathogen interactions
Westermann, A. J., Förstner, K. U., Amman, F., Barquist, L., Chao, Y., Schulte, L. N., Müller, L., Reinhardt, R., Stadler, P. F., & Vogel, J. (2016) · Nature · doi:10.1038/nature16547 · Cited by 499
Self-citationHfq CLASH uncovers sRNA-target interaction networks linked to nutrient availability adaptation
Iosub, I. A., van Nues, R. W., McKellar, S. W., Nieken, K. J., Marchioretto, M., Sy, B., Tree, J. J., Viero, G., & Granneman, S. (2020) · eLife · doi:10.7554/elife.54655 · Cited by 98
sRNA-controlled iron sparing response in Staphylococci
Coronel-Tellez, R. H., Pospiech, M., Barrault, M., Liu, W., Bordeau, V., Vasnier, C., Felden, B., Sargueil, B., & Bouloc, P. (2022) · Nucleic Acids Research · doi:10.1093/nar/gkac648 · Cited by 43
“In Enterobacteriaceae, Hfq is an RNA chaperone required for sRNA-mediated regulations (70).”
Background
Metadata
- Authors
- Vogel, J., & Luisi, B. F.
- Venue
- Nature Reviews Microbiology
- Published
- 2011-08
- Volume
- 9
- Issue
- 8
- Pages
- 578-589
- ISSN
- 1740-1526 (ISSN-L)
- 1740-1534
- OpenAlex
- W2014372073
- Cited by
- 1,029
- References
- 5
- FWCI
- 6.96
- Type
- journal article
- Language
- en
- Open access
- green
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: Hfq and its constellation of RNA. https://app.cochat.ai/papers/10.1038/nrmicro2615
- The paper
- Vogel, J., & Luisi, B. F. (2011). Hfq and its constellation of RNA. Nature Reviews Microbiology. https://doi.org/10.1038/nrmicro2615
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
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.
