Evidence map›Paper›PMID 10757789›Full record

ArticleMolecular and cellular biology2000

Identification and characterization of a novel serine-arginine-rich splicing regulatory protein.

D C Barnard, J G Patton

Abstract read
In one paragraph

Article in Molecular and cellular biology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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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

22 citing papers in PubMed.

  1. SR proteins in cancer: function, regulation, and small inhibitor.Cellular & molecular biology letters · 2024
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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.

D C BarnardDepartment of Molecular Biology, Vanderbilt University, Nashville, Tennessee 37235, USA.
J G Patton

Funding

REGULATION OF ALPHA TROPOMYOSIN SPLICINGR01GM050418 · NIGMS · VANDERBILT UNIVERSITY · PI PATTON, JAMES G. · 1994 to 1997
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NIGMS NIH HHS GM50418
6 · The paper itself

Abstract

We have identified an 86-kDa protein containing a single amino-terminal RNA recognition motif and two carboxy-terminal domains rich in serine-arginine (SR) dipeptides. Despite structural similarity to members of the SR protein family, p86 is clearly unique. It is not found in standard SR protein preparations, does not precipitate in the presence of high magnesium concentrations, is not recognized by antibodies specific for SR proteins, and cannot complement splicing-defective S100 extracts. However, we have found that p86 can inhibit the ability of purified SR proteins to activate splicing in S100 extracts and can even inhibit the in vitro and in vivo activation of specific splice sites by a subset of SR proteins, including ASF/SF2, SC35, and SRp55. In contrast, p86 activates splicing in the presence of SRp20. Thus, it appears that pairwise combination of p86 with specific SR proteins leads to altered splicing efficiency and differential splice site selection. In all cases, such regulation requires the presence of the two RS domains and a unique intervening EK-rich region, which appear to mediate direct protein-protein contact between these family members. Full-length p86, but not a mutant lacking the RS-EK-RS domains, was found to preferentially interact with itself, SRp20, ASF/SF2, SRp55, and, to a slightly lesser extent, SC35. Because of the primary sequence and unique properties of p86, we have named this protein SRrp86 for SR-related protein of 86 kDa.

Indexed as

RNA-Binding ProteinsAmino Acid SequenceArginineBlotting, WesternCarrier ProteinsChromatography, AffinityGenetic Complementation TestMolecular Sequence DataNuclear ProteinsProtein BindingProtein Structure, TertiaryRecombinant ProteinsRNARNA SplicingS100 ProteinsSequence Analysis, DNAArginineCarrier ProteinsNuclear ProteinsRecombinant ProteinsRNARNA-Binding ProteinsS100 ProteinsSerineSerine-Arginine Splicing FactorsSREK1 protein, human

Identifiers

PMID10757789
PMCPMC85584

What OpenQuestion holds

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Registered trials

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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.