Evidence map›Paper›PMID 28147274›Full record

ArticleCell reports2017

Mechanism of β-actin mRNA Recognition by ZBP1.

Giuseppe Nicastro, Adela M Candel, Michael Uhl, Alain Oregioni, David Hollingworth, Rolf Backofen, Stephen R Martin, Andres Ramos

Abstract read
In one paragraph

Article in Cell reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed, 1 pooled it
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

40 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
  2. Synaptic Proteostasis in Health and Disease.Journal of neurochemistry · 2026
    Review
  3. Review
  4. Article
  5. Cracking the (zip)code of dynein-dependent RNA localization.Nature structural & molecular biology · 2026
    Article
  6. Review
  7. Article
  8. Review
  9. Review
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. The importance of mRNA (New York, N.Y.) · 2023
    Article
  20. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors.

Giuseppe NicastroMacromolecular Structure Laboratory, The Francis Crick Institute, London NW1 1AT, UK.
Adela M CandelAt the former MRC National Institute for Medical Research, Mill Hill, London.
Michael UhlBioinformatics Group, Department of Computer Science, University of Freiburg, 79110 Freiburg, Germany.
Alain OregioniMRC Biomedical NMR Centre, The Francis Crick Institute, London NW1 1AT, UK.
David HollingworthMycobacterial Systems Biology Laboratory, The Francis Crick Institute, London NW1 1AT, UK.
Rolf BackofenBioinformatics Group, Department of Computer Science, University of Freiburg, 79110 Freiburg, Germany; Centre for Biological Signaling Studies (BIOSS), University of Freiburg, 79110 Freiburg, Germany.
Stephen R MartinStructural Biology Science Technology Platform, The Francis Crick Institute, London NW1 1AT, UK.
Andres RamosInstitute of Structural and Molecular Biology, University College London, London WC1E 6XA, UK; The Francis Crick Institute, London NW1 1AT, UK. Electronic address: a.ramos@ucl.ac.uk.

Funding

Cancer Research UK FC001029Medical Research Council MC_PC_13051Medical Research Council MC_U117533887Medical Research Council MC_U117574558Medical Research Council U117574558
6 · The paper itself

Abstract

Zipcode binding protein 1 (ZBP1) is an oncofetal RNA-binding protein that mediates the transport and local translation of β-actin mRNA by the KH3-KH4 di-domain, which is essential for neuronal development. The high-resolution structures of KH3-KH4 with their respective target sequences show that KH4 recognizes a non-canonical GGA sequence via an enlarged and dynamic hydrophobic groove, whereas KH3 binding to a core CA sequence occurs with low specificity. A data-informed kinetic simulation of the two-step binding reaction reveals that the overall reaction is driven by the second binding event and that the moderate affinities of the individual interactions favor RNA looping. Furthermore, the concentration of ZBP1, but not of the target RNA, modulates the interaction, which explains the functional significance of enhanced ZBP1 expression during embryonic development.

Indexed as

ActinsAmino Acid SequenceAnimalsAvian ProteinsChickensEmbryonic DevelopmentRNARNA-Binding ProteinsRNA, MessengerActinsAvian ProteinsRNARNA-Binding ProteinsRNA, MessengerZBP1 protein, Gallus gallusbinding mechanismIMP1mRNA local translationneuronal developmentneuronal mRNA granulesNMRprotein-RNA interactionsZBP1

Identifiers

PMID28147274
PMCPMC5300891

What OpenQuestion holds

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.