Evidence map›Paper›PMID 9405646›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1997

A multimeric complex and the nuclear targeting of the Drosophila Rel protein Dorsal.

J Yang, R Steward

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1997. 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
1.3field-weighted citation impact, top 19% 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, 38 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Mosquito immune defenses against Plasmodium infection.Developmental and comparative immunology · 2010
    Review
  6. Article
  7. Article
  8. A heterotrimeric death domain complex in Toll signaling.Proceedings of the National Academy of Sciences of the United States of America · 2002
    Article
  9. Article
  10. Maternal control of the Drosophila dorsal-ventral body axis.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

2 authors at 2 institutions in 1 country.

J YangWaksman Institute and Department of Molecular Biology and Biochemistry, Rutgers University, Piscataway, NJ 08855, USA.
R Steward
Princeton University · USRutgers, The State University of New Jersey · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The intracellular part of the Rel signal transduction pathway in Drosophila is encoded by Toll, tube, pelle, dorsal, and cactus, and it functions to form the dorsal-ventral axis in the Drosophila embryo. Upon activation of the transmembrane receptor Toll, Dorsal dissociates from its cytoplasmic inhibitor Cactus and enters the nucleus. Tube and Pelle are required to relay the signal from Toll to the Dorsal-Cactus complex. In a yeast two-hybrid assay, we found that both Tube and Pelle interact with Dorsal. We confirmed these interactions in an in vitro binding assay. Tube interacts with Dorsal via its C-terminal domain, whereas full-length Pelle is required for Dorsal binding. Tube and Pelle bind Dorsal in the N-terminal domain 1 of the Dorsal Rel homology region rather than at the Cactus binding site. Domain 1 has been found to be necessary for Dorsal nuclear targeting. Genetic experiments indicate that Tube-Dorsal interaction is necessary for normal signal transduction. We propose a model in which Tube, Pelle, Cactus, and Dorsal form a multimeric complex that represents an essential aspect of signal transduction.

Indexed as

Drosophila ProteinsReceptors, Cell SurfaceSignal TransductionAnimalsCell NucleusDNA-Binding ProteinsDrosophilaInsect ProteinsMembrane GlycoproteinsNF-kappa BNuclear ProteinsPhosphoproteinsProtein Serine-Threonine KinasesToll-Like ReceptorsTranscription Factorscact protein, Drosophiladl protein, DrosophilaDNA-Binding ProteinsDrosophila ProteinsInsect ProteinsMembrane GlycoproteinsNF-kappa BNuclear ProteinsPhosphoproteinspll protein, DrosophilaProtein Serine-Threonine KinasesReceptors, Cell SurfaceTl protein, DrosophilaToll-Like ReceptorsTranscription Factors

Identifiers

PMID9405646
PMCPMC25042
OpenAlexW2021105570

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.