Evidence map›Paper›PMID 23012481›Full record

ArticleRNA (New York, N.Y.)2012

Intrinsic flexibility of snRNA hairpin loops facilitates protein binding.

Michael Rau, W Tom Stump, Kathleen B Hall

Open access · bronzeAbstract read
In one paragraph

Article in RNA (New York, N.Y.), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.1field-weighted citation impact, top 24% 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

13 citing papers in PubMed, 16 citations in OpenAlex.

  1. Review
  2. Blind tests of RNA-protein binding affinity prediction.Proceedings of the National Academy of Sciences of the United States of America · 2019
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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.

Michael RauDepartment of Biochemistry and Molecular Biophysics, Washington University Medical School, St. Louis, Missouri 63110, USA.
W Tom Stump
Kathleen B Hall
Washington University in St. Louis · US

Funding

Coevolution of snrnp U1A/U2B proteins and snRNA stemloopsR01GM096444 · NIGMS · WASHINGTON UNIVERSITY · PI HALL, KATHLEEN B · 2011 to 2014
$1.4M
NIGMS NIH HHS R01 GM096444
6 · The paper itself

Abstract

Stem-loop II of U1 snRNA and Stem-loop IV of U2 snRNA typically have 10 or 11 nucleotides in their loops. The fluorescent nucleobase 2-aminopurine was used as a substitute for the adenines in each loop to probe the local and global structures and dynamics of these unusually long loops. Using steady-state and time-resolved fluorescence, we find that, while the bases in the loops are stacked, they are able to undergo significant local motion on the picosecond/nanosecond timescale. In addition, the loops have a global conformational change at low temperatures that occurs on the microsecond timescale, as determined using laser T-jump experiments. Nucleobase and loop motions are present at temperatures far below the melting temperature of the hairpin stem, which may facilitate the conformational change required for specific protein binding to these RNA loops.

Indexed as

Inverted Repeat Sequences2-AminopurineAnimalsBase SequenceDrosophilaDrosophila ProteinsFluorescence PolarizationFluorescent DyesHumansModels, MolecularNucleic Acid ConformationProtein BindingRabbitsRibonucleoproteinsRNA, Small NuclearSpectrometry, Fluorescence2-AminopurineDrosophila ProteinsFluorescent DyesRibonucleoproteinsRNA, Small NuclearU1 small nuclear RNAU2 small nuclear RNA

Identifiers

PMID23012481
PMCPMC3479389
OpenAlexW2108404575

What OpenQuestion holds

Textmetadata
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.