Evidence map›Paper›PMID 22009680›Full record

ArticleNucleic acids research2012

Analysis of the interaction with the hepatitis C virus mRNA reveals an alternative mode of RNA recognition by the human La protein.

Luigi Martino, Simon Pennell, Geoff Kelly, Tam T T Bui, Olga Kotik-Kogan, Stephen J Smerdon, Alex F Drake, Stephen Curry, Maria R Conte

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
3.1field-weighted citation impact, top 8% of its field
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

39 citing papers in PubMed, 51 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Structure ofRNA biology · 2021
    Article
  5. Review
  6. Review
  7. Review
  8. Review
  9. Review
  10. Hepatitis C Virus Translation Regulation.International journal of molecular sciences · 2020
    Review
  11. Article
  12. Article
  13. Structural basis for recognition of human 7SK long noncoding RNA by the La-related protein Larp7.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  14. Article
  15. Article
  16. Review
  17. eLife · 2017
    Article
  18. Article
  19. 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

9 authors at 2 institutions in 1 country.

Luigi MartinoRandall Division of Cell and Molecular Biophysics, King's College London, New Hunt's House, Guy's Campus, London SE1 1UL, UK.
Simon Pennell
Geoff Kelly
Tam T T Bui
Olga Kotik-Kogan
Stephen J Smerdon
Alex F Drake
Stephen Curry
Maria R Conte
King's College London · GBImperial College London · GB

Funding

Biotechnology and Biological Sciences Research Council BB/E02209X/1Department of Health U117584228Medical Research Council MC_U117533887Medical Research Council MC_U117584228Wellcome Trust 075295/A/04/ZWellcome Trust 085944/Z/08/Z
6 · The paper itself

Abstract

Human La protein is an essential factor in the biology of both coding and non-coding RNAs. In the nucleus, La binds primarily to 3' oligoU containing RNAs, while in the cytoplasm La interacts with an array of different mRNAs lacking a 3' UUU(OH) trailer. An example of the latter is the binding of La to the IRES domain IV of the hepatitis C virus (HCV) RNA, which is associated with viral translation stimulation. By systematic biophysical investigations, we have found that La binds to domain IV using an RNA recognition that is quite distinct from its mode of binding to RNAs with a 3' UUU(OH) trailer: although the La motif and first RNA recognition motif (RRM1) are sufficient for high-affinity binding to 3' oligoU, recognition of HCV domain IV requires the La motif and RRM1 to work in concert with the atypical RRM2 which has not previously been shown to have a significant role in RNA binding. This new mode of binding does not appear sequence specific, but recognizes structural features of the RNA, in particular a double-stranded stem flanked by single-stranded extensions. These findings pave the way for a better understanding of the role of La in viral translation initiation.

Indexed as

AutoantigensBinding SitesHepacivirusHumansModels, MolecularNucleic Acid ConformationProtein BindingRibonucleoproteinsRNA, MessengerRNA PrecursorsRNA, TransferRNA, ViralSS-B AntigenAutoantigensRibonucleoproteinsRNA, MessengerRNA PrecursorsRNA, TransferRNA, ViralSS-B Antigen

Identifiers

PMID22009680
PMCPMC3273827
OpenAlexW2093994360

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
Read underepoch 390

Registered trials

None linked

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.