Evidence map›Paper›PMID 9671805›Full record

ArticleNucleic acids research1998

TRIP: a novel double stranded RNA binding protein which interacts with the leucine rich repeat of flightless I.

S A Wilson, E C Brown, A J Kingsman, S M Kingsman

Open access · bronzeAbstract read
In one paragraph

Article in Nucleic acids research, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed, 1 pooled it
0.8field-weighted citation impact, top 28% 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

21 citing papers in PubMed, 1 synthesis or guideline pooled it, 51 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Review
  4. Review
  5. Article
  6. Review
  7. Article
  8. Noncoding RNAs and LRRFIP1 regulate TNF expression.Journal of immunology (Baltimore, Md. : 1950) · 2014
    Article
  9. Molecular basis of DNA recognition in the immune system.Journal of immunology (Baltimore, Md. : 1950) · 2013
    Review
  10. Article
  11. Article
  12. Article
  13. Leucine-rich repeat (in Flightless I) interacting protein-1 regulates a rapid type I interferon response.Journal of interferon & cytokine research : the official journal of the International Society for Interferon and Cytokine Research · 2010
    Article
  14. Article
  15. Catenin' on to nucleic acid sensing.Nature immunology · 2010
    Article
  16. Mutually exclusive interactions drive handover of mRNA from export adaptors to TAP.Proceedings of the National Academy of Sciences of the United States of America · 2008
    Article
  17. Article
  18. Article
  19. Article
  20. Article
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.

S A WilsonDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.
E C Brown
A J Kingsman
S M Kingsman
University of Oxford · GB

Funding

Wellcome Trust
6 · The paper itself

Abstract

A northwestern screen of a CHO-K1 cell line cDNA library with radiolabelled HIV-1 TAR RNA identified a novel TAR RNA interacting protein, TRIP. The human trip cDNA was also cloned and its expression is induced by phorbol esters. The N-terminus of TRIP shows high homology to the coiled coil domain of FLAP, a protein which binds the leucine-rich repeat (LRR) of Flightless I (FLI) and the interaction of TRIP with the FLI LRR has been confirmed in vitro . TRIP does not bind single stranded DNA or RNA significantly and binds double stranded DNA weakly. In contrast, TRIP binds double stranded RNA with high affinity and two molecules of TRIP bind the TAR stem. The RNA binding domain has been identified and encompasses a lysine-rich motif. A TRIP-GFP fusion is localised in the cytoplasm and excluded from the nucleus. FLI has a C-terminal gelsolin-like domain which binds actin and therefore the association of TRIP with the FLI LRR may provide a link between the actin cytoskeleton and RNA in mammalian cells.

Indexed as

GelsolinReceptors, Cytoplasmic and NuclearAmino Acid SequenceAnimalsBase SequenceBinding SitesCell Line, TransformedCHO CellsCloning, MolecularCOS CellsCricetinaeCytoplasmDNA PrimersGene ExpressionHeLa CellsHIV-1DNA PrimersFLII protein, humanGelsolinLeucineLRRFIP1 protein, humanMicrofilament ProteinsMitogensPhorbol EstersProteinsReceptors, Cytoplasmic and NuclearRNA-Binding ProteinsRNA, Double-StrandedTrans-Activators

Identifiers

PMID9671805
PMCPMC147727
OpenAlexW2019572414

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.