Evidence map›Paper›PMID 9848655›Full record

ArticleRNA (New York, N.Y.)1998

Separable roles in vivo for the two RNA binding domains of Drosophila A1-hnRNP homolog.

K Zu, M L Sikes, A L Beyer

Open access · bronzeAbstract read
In one paragraph

Article in RNA (New York, N.Y.), 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
0.5field-weighted citation impact, top 36% 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

13 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
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  5. Article
  6. Nuclear export of single native mRNA molecules observed by light sheet fluorescence microscopy.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  7. Article
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  12. Article
  13. Specification of the somatic musculature in Drosophila.Wiley interdisciplinary reviews. Developmental biology
    Review
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

3 authors at 2 institutions in 1 country.

K ZuDepartment of Microbiology, University of Virginia, Charlottesville 22908, USA.
M L Sikes
A L Beyer
University of Virginia · USStony Brook University · US

Funding

NIGMS NIH HHS GM-39271
6 · The paper itself

Abstract

We analyzed the roles of the three domains of a Drosophila hnRNP A1 homolog by expression of wild-type and mutant versions of HRB87F/hrp36 in Drosophila melanogaster. HRB87F/hrp36 is one of two Drosophila proteins that is most similar to mammalian A1 hnRNP, and like A1, consists of two copies of the RNA-binding domain (RBD) motif followed by a glycine-rich domain (GRD). The role of the domains in nuclear localization and RNA binding to polytene chromosomal sites was determined. RBD-1 and the GRD were largely responsible for both the cellular location of the protein and for the typical chromosomal distribution pattern of the protein at sites of PolII transcription. RBD-1 also provided a role in the exon-skipping activity of the protein that was not provided by RBD-2. On the other hand, RBD-2 and the GRD were responsible for the very limited chromosomal distribution pattern seen upon heat shock, when HRB87F/hrp36 is sequestered at heat-shock puff 93D, which encodes a long nucleus-restricted RNA. Thus, these studies indicate that the two RBDs function independently of each other but in concert with the GRD. In addition, the self-association property of the GRD was strikingly evident in these overexpressed proteins.

Indexed as

Heterogeneous-Nuclear Ribonucleoprotein Group A-BAlternative SplicingAnimalsBase SequenceCell NucleusDNA PrimersDrosophila melanogasterExonsGlycineHeat-Shock ResponseHeterogeneous Nuclear Ribonucleoprotein A1Heterogeneous-Nuclear RibonucleoproteinsRibonucleoproteinsRNA-Binding ProteinsDNA PrimersGlycineHeterogeneous Nuclear Ribonucleoprotein A1Heterogeneous-Nuclear Ribonucleoprotein Group A-BHeterogeneous-Nuclear RibonucleoproteinsRibonucleoproteinsRNA-Binding Proteins

Identifiers

PMID9848655
PMCPMC1369727
OpenAlexW2168710840

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.