Evidence map›Paper›PMID 20597503›Full record

ArticleJournal of the American Chemical Society2010

Selective 2'-hydroxyl acylation analyzed by protection from exoribonuclease.

Kady-Ann Steen, Arun Malhotra, Kevin M Weeks

Abstract read
In one paragraph

Article in Journal of the American Chemical Society, 2010. 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
2.8field-weighted citation impact, top 9% 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

24 citing papers in PubMed, 40 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. High-throughput determination of RNA structures.Nature reviews. Genetics · 2018
    Review
  5. Single-molecule FRET studies on the cotranscriptional folding of a thiamine pyrophosphate riboswitch.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Folding and ligand recognition of the TPP riboswitch aptamer at single-molecule resolution.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  16. Article
  17. Article
  18. Article
  19. The mechanisms of RNA SHAPE chemistry.Journal of the American Chemical Society · 2012
    Article
  20. Folding energy landscape of the thiamine pyrophosphate riboswitch aptamer.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
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

3 authors at 1 institution in 1 country.

Kady-Ann SteenDepartment of Chemistry, University of North Carolina, Chapel Hill, North Carolina 27599-3290, USA.
Arun Malhotra
Kevin M Weeks
University of Miami · US

Funding

Retroviral Genomic RNA Dimer Structure and FunctionR01GM064803 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI WEEKS, KEVIN M · 2002 to 2016
$3.7M
Structural studies of exoribonucleasesR01GM069972 · NIGMS · UNIVERSITY OF MIAMI SCHOOL OF MEDICINE · PI MALHOTRA, ARUN · 2003 to 2007
$1.4M
NIGMS NIH HHS GM69972NIGMS NIH HHS R01 GM064803NIGMS NIH HHS R01 GM069972
6 · The paper itself

Abstract

Selective 2'-hydroxyl acylation analyzed by primer extension (SHAPE) is a powerful approach for characterizing RNA structure and dynamics at single-nucleotide resolution. However, SHAPE technology is limited, sometimes severely, because primer extension detection obscures structural information for approximately 15 nts at the 5' end and 40-60 nts at the 3' end of the RNA. Moreover, detection by primer extension is more complex than the actual structure-selective chemical interrogation step. Here we quantify covalent adducts in RNA directly by adduct-inhibited exoribonuclease degradation. RNA 2'-O-adducts block processivity of a 3'-->5' exoribonuclease, RNase R, to produce fragments that terminate three nucleotides 3' of the modification site. We analyzed the structure of the native thiamine pyrophosphate (TPP) riboswitch aptamer domain and identified large changes in local nucleotide dynamics and global RNA structure upon ligand binding. In addition to numerous changes that can be attributed to ligand recognition, we identify a single nucleotide bulge register shift, distant from the binding site, that stabilizes the ligand-bound structure. Selective 2'-hydroxyl acylation analyzed by protection from exoribonuclease (RNase-detected SHAPE) should prove broadly useful for facile structural analysis of small noncoding RNAs and for RNAs that have functionally critical structures at their 5' and 3' ends.

Indexed as

AcylationBase SequenceCatalytic DomainExoribonucleasesHydroxidesModels, MolecularNucleic Acid ConformationRNASubstrate SpecificityExoribonucleaseshydroxide ionHydroxidesRNA

Identifiers

PMID20597503
PMCPMC2912424
OpenAlexW1983479792

What OpenQuestion holds

Textmetadata
LicenceTDM
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.