Evidence map›Paper›PMID 21361282›Full record

ArticleJournal of the American Chemical Society2011

Control of the stability of a protein-RNA complex by the position of fluorine in a base analogue.

Yulia Benitex, Anne M Baranger

Erratum issuedOpen access · greenAbstract read
In one paragraph

Article in Journal of the American Chemical Society, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
1.6field-weighted citation impact, top 18% 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

2 citing papers in PubMed, 25 citations in OpenAlex.

  1. Article
  2. Fluorine bonding enhances the energetics of protein-lipid binding in the gas phase.Journal of the American Society for Mass Spectrometry · 2014
    Article
4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Yulia BenitexDepartment of Chemistry, Wesleyan University, Middletown, Connecticut 06459, United States.
Anne M Baranger
Wesleyan University · US

Funding

BIOORGANIC BASIS FOR RNA/PROTEIN STABILITYR01GM056857 · NIGMS · WESLEYAN UNIVERSITY · PI BARANGER, ANNE M · 1998 to 2006
$1.6M
NIGMS NIH HHS GM-056857NIGMS NIH HHS R01 GM056857
6 · The paper itself

Abstract

The effects of modifying the electronic characteristics of nonpolar base analogues substituted at positions involved in stacking interactions between SL2 RNA and the U1A protein are described. A surprisingly large difference in the stability between complexes formed with base analogues that differ only in the position of substitution of a single fluorine atom is observed. The results of high-level ab initio calculations of the interactions between the nonpolar base analogue and the amino acid side chain correlate with the experimentally observed trends in complex stability, which suggests that changes in stacking interactions that result from varying the position and degree of fluorine substitution contribute to the effects of fluorine substitution on the stability of the U1A-SL2 RNA complex.

Indexed as

Crystallography, X-RayFluorineModels, MolecularRNARNA-Binding ProteinsFluorineRNARNA-Binding Proteins

Identifiers

PMID21361282
PMCPMC3095225
OpenAlexW2008742361

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.