Evidence map›Paper›PMID 9111328›Full record

ArticleMolecular and cellular biology1997

Interaction between the human nuclear cap-binding protein complex and hnRNP F.

C Gamberi, E Izaurralde, C Beisel, I W Mattaj

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
1.6field-weighted citation impact, top 16% 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

29 citing papers in PubMed, 51 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.

C GamberiEuropean Molecular Biology Laboratory, Heidelberg, Germany.
E Izaurralde
C Beisel
I W Mattaj
European Molecular Biology Laboratory · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

hnRNP F was identified in a screen for proteins that interact with human CBP80 and CBP20, the components of the nuclear cap-binding complex (CBC). In vitro interaction studies showed that hnRNP F can bind to both CBP20 and CBP80 individually. hnRNP F and CBC bind independently to RNA, but hnRNP F binds preferentially to CBC-RNA complexes rather than to naked RNA. The hnRNP H protein, which is 78% identical to hnRNP F and also interacts with both CBP80 and CBP20 in vitro, does not discriminate between naked RNA and CBC-RNA complexes, showing that this effect is specific. Depletion of hnRNP F from HeLa cell nuclear extract decreases the efficiency of pre-mRNA splicing, a defect which can be partially compensated by addition of recombinant hnRNP F. Thus, hnRNP F is required for efficient pre-mRNA splicing in vitro and may participate in the effect of CBC on pre-mRNA splicing.

Indexed as

Amino Acid SequenceCross-Linking ReagentsElectrophoresis, Polyacrylamide GelHeLa CellsHeterogeneous-Nuclear Ribonucleoprotein Group F-HHeterogeneous-Nuclear RibonucleoproteinsHumansMacromolecular SubstancesMolecular Sequence DataRibonucleoproteinsRNA-Binding ProteinsRNA Cap-Binding ProteinsRNA CapsRNA, Heterogeneous NuclearCross-Linking ReagentsHeterogeneous-Nuclear Ribonucleoprotein Group F-HHeterogeneous-Nuclear RibonucleoproteinsMacromolecular SubstancesRibonucleoproteinsRNA-Binding ProteinsRNA Cap-Binding ProteinsRNA CapsRNA, Heterogeneous Nuclear

Identifiers

PMID9111328
PMCPMC232108
OpenAlexW2170003425

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.