Evidence map›Paper›PMID 11121472›Full record

ArticleNucleic acids research2000

Role of SR protein modular domains in alternative splicing specificity in vivo.

W van Der Houven Van Oordt, K Newton, G R Screaton, J F Cáceres

Open access · bronzeAbstract read
In one paragraph

Article in Nucleic acids research, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
1.1field-weighted citation impact, top 23% 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

27 citing papers in PubMed, 57 citations in OpenAlex.

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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

4 authors at 1 institution in 1 country.

W van Der Houven Van OordtMRC Human Genetics Unit, Western General Hospital, Edinburgh EH4 2XU, UK and Molecular Immunology Group, Institute of Molecular Medicine, John Radcliffe Hospital, Headington, Oxford OX3 9DU, UK.
K Newton
G R Screaton
J F Cáceres
Western General Hospital · GB

Funding

Medical Research Council MC_U127584479Wellcome Trust
6 · The paper itself

Abstract

The SR proteins constitute a family of nuclear phosphoproteins which are required for constitutive splicing and also influence alternative splicing regulation. They have a modular structure consisting of one or two RNA recognition motifs (RRMs) and a C-terminal domain, rich in arginine and serine residues. The functional role of the different domains of SR proteins in constitutive splicing activity has been extensively studied in vitro; however, their contribution to alternative splicing specificity in vivo has not been clearly established. We sought to address how the modular domains of SR proteins contribute to alternative splicing specificity. The activity of a series of chimeric proteins consisting of domain swaps between different SR proteins showed that splice site selection is determined by the nature of the RRMs and that RRM2 of SF2/ASF has a dominant role and can confer specificity to a heterologous protein. In contrast, the identity of the RS domain is not important, as the RS domains are functionally interchangeable. The contribution of the RRMs to alternative splicing specificity in vivo suggests that sequence-specific RNA binding by SR proteins is required for this activity.

Indexed as

Alternative SplicingAdenovirus E1A ProteinsAmino Acid MotifsFibronectinsGenes, ReporterHeLa CellsHumansNuclear ProteinsPhosphoproteinsProtein Structure, TertiaryRecombinant Fusion ProteinsRNA-Binding ProteinsRNA, MessengerRNA PrecursorsSerine-Arginine Splicing FactorsSubstrate SpecificityAdenovirus E1A ProteinsFibronectinsNuclear ProteinsPhosphoproteinsRecombinant Fusion ProteinsRNA-Binding ProteinsRNA, MessengerRNA PrecursorsSerine-Arginine Splicing Factors

Identifiers

PMID11121472
PMCPMC115228
OpenAlexW2154700546

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.