Evidence map›Paper›PMID 26727239›Full record

ArticleNature chemical biology2016

The solution structural ensembles of RNA kink-turn motifs and their protein complexes.

Xuesong Shi, Lin Huang, David M J Lilley, Pehr B Harbury, Daniel Herschlag

Abstract read
In one paragraph

Article in Nature chemical biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
–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

24 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. The roles of NOP56 in cancer and SCA36.Pathology oncology research : POR · 2023
    Review
  5. Article
  6. Recent advances in RNA structurome.Science China. Life sciences · 2022
    Review
  7. Article
  8. Article
  9. Site-specific covalent labeling of large RNAs with nanoparticles empowered by expanded genetic alphabet transcription.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  10. Article
  11. Article
  12. Article
  13. Sequence-dependent RNA helix conformational preferences predictably impact tertiary structure formation.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  14. The roles of structural dynamics in the cellular functions of RNAs.Nature reviews. Molecular cell biology · 2019
    Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Quantitative tests of a reconstitution model for RNA folding thermodynamics and kinetics.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors.

Xuesong ShiDepartment of Biochemistry, Stanford University, Stanford, California, USA.
Lin HuangNucleic Acid Structure Research Group, School of Life Sciences, University of Dundee, Dundee, UK.
David M J LilleyNucleic Acid Structure Research Group, School of Life Sciences, University of Dundee, Dundee, UK.
Pehr B HarburyDepartment of Biochemistry, Stanford University, Stanford, California, USA.
Daniel HerschlagDepartment of Biochemistry, Stanford University, Stanford, California, USA.

Funding

Time-resolved small angle X-ray scatteringP01GM066275 · NIGMS · STANFORD UNIVERSITY · PI HERSCHLAG, DANIEL · 2003 to 2017
$17.8M
NIH Director's Pioneer Award (RMI)DP1OD000429 · OD · STANFORD UNIVERSITY · PI HARBURY, PEHR A · 2005 to 2009
$3.8M
Biotechnology and Biological Sciences Research Council B17092Biotechnology and Biological Sciences Research Council BB/E001777/1Cancer Research UK 11722Cancer Research UK 18604Cancer Research UK A4959Cancer Research UK C28/A4959NIGMS NIH HHS P01 GM066275NIH HHS DP1 OD000429NIH HHS DP-OD000429-01Wellcome Trust 092056Wellcome Trust 092057
6 · The paper itself

Abstract

With the growing number of crystal structures of RNA and RNA-protein complexes, a critical next step is understanding the dynamic solution behavior of these entities in terms of conformational ensembles and energy landscapes. To this end, we have used X-ray scattering interferometry (XSI) to probe the ubiquitous RNA kink-turn motif and its complexes with the canonical kink-turn binding protein L7Ae. XSI revealed that the folded kink-turn is best described as a restricted conformational ensemble. The ions present in solution alter the nature of this ensemble, and protein binding can perturb the kink-turn ensemble without collapsing it to a unique state. This study demonstrates how XSI can reveal structural and ensemble properties of RNAs and RNA-protein complexes and uncovers the behavior of an important RNA-protein motif. This type of information will be necessary to understand, predict and engineer the behavior and function of RNAs and their protein complexes.

Indexed as

Nucleic Acid ConformationNucleotide MotifsBase SequenceInterferometryMolecular Dynamics SimulationMolecular Sequence DataRNAScattering, RadiationX-RaysRNA

Identifiers

PMID26727239
PMCPMC4755865

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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.