Evidence map›Paper›PMID 11991645›Full record

ArticleRNA (New York, N.Y.)2002

Regulation of alternative splicing by SRrp86 through coactivation and repression of specific SR proteins.

Daron C Barnard, Jun Li, Rui Peng, James G Patton

Open access · greenAbstract read
In one paragraph

Article in RNA (New York, N.Y.), 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
0.9field-weighted citation impact, top 27% 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

10 citing papers in PubMed, 26 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.

Daron C BarnardDepartment of Molecular Biology, Vanderbilt University, Nashville, Tennessee 37235, USA.
Jun Li
Rui Peng
James G Patton
Vanderbilt University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

SRrp86 is an 86-kDa member of the SR protein superfamily that is unique in that it can alter splice site selection by regulating the activity of other SR proteins. To study the function of SRrp86, inducible cell lines were created in which the concentration of SRrp86 could be varied and its effects on alternative splicing determined. Here, we show that SRrp86 can activate SRp20 and repress SC35 in a dose-dependent manner both in vitro and in vivo. These effects are apparently mediated through direct protein-protein interaction, as pull-down assays showed that SRrp86 interacts with both SRp20 and SC35. Consistent with the hypothesis that relatively modest changes in the concentration or activity of one or more splicing factors can combinatorially regulate overall splicing, protein expression patterns of SRrp86, SRp20, and SC35 reveal that each tissue maintains a unique ratio of these factors. Regulation of SR protein activity, coupled with regulated protein expression, suggest that SRrp86 may play a crucial role in determining tissue specific patterns of alternative splicing.

Indexed as

Alternative Splicing3' Untranslated Regions5' Untranslated RegionsAnimalsBlotting, WesternCarrier ProteinsCells, CulturedHeLa CellsHumansNuclear ProteinsOrgan SpecificityPhosphoproteinsRatsRNA-Binding ProteinsSerine-Arginine Splicing Factors3' Untranslated Regions5' Untranslated RegionsCarrier ProteinsNuclear ProteinsPhosphoproteinsRNA-Binding ProteinsSerine-Arginine Splicing FactorsSREK1 protein, humanSrek1 protein, ratSRSF3 protein, human

Identifiers

PMID11991645
PMCPMC1370273
OpenAlexW2123621813

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.