Evidence map›Paper›PMID 21684671›Full record

ArticleBiophysical chemistry2011

Human U2B″ protein binding to snRNA stemloops.

Sandra G Williams, Kathleen B Hall

Open access · greenAbstract read
In one paragraph

Article in Biophysical chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
0.9field-weighted citation impact, top 26% 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

12 citing papers in PubMed, 17 citations in OpenAlex.

  1. RNA-Binding Proteins in Dinoflagellates.International journal of molecular sciences · 2026
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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

2 authors at 1 institution in 1 country.

Sandra G WilliamsDepartment of Biochemistry and Molecular Biophysics, Washington University Medical School, St Louis, MO 63110, United States.
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
The contribution of protein conformational instability to RNA bindingF31GM089576 · NIGMS · WASHINGTON UNIVERSITY · PI WILLIAMS, SANDRA GISELA · 2009 to 2010
$55k
NIGMS NIH HHS F31 GM089576NIGMS NIH HHS R01 GM096444
6 · The paper itself

Abstract

The human U2B″ protein is one of the unique proteins that comprise the U2 snRNP, but it is also a representative of the U1A/U2B″ protein family. In the U2 snRNP, it is bound to Stem-Loop IV (SLIV) of the U2 snRNA. We find that in vitro it binds not only to human SLIV, but also to Stem-Loop II (SLII) from human U1 snRNA and to Drosophila U2 snRNA SLIV. The thermodynamics of these binding interactions show a striking similarity, leading to the conclusion that U2B″ has a relaxed specificity for its RNA targets. The binding properties of U2B″ are distinct from those of human U1A and of Drosophila SNF, despite its high homology to those proteins, and so provide important new information on how this protein family has modulated its target preferences.

Indexed as

Amino Acid SequenceAnimalsBase SequenceDrosophilaHumansModels, MolecularMolecular Sequence DataNucleic Acid ConformationProtein BindingRNA, Small NuclearsnRNP Core ProteinsThermodynamicsRNA, Small NuclearsnRNP Core ProteinsSNRPB2 protein, humanU1 small nuclear RNAU2 small nuclear RNA

Identifiers

PMID21684671
PMCPMC3166965
OpenAlexW2101244998

What OpenQuestion holds

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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.