Evidence map›Paper›PMID 29642431›Full record

ArticleInternational journal of molecular sciences2018

The Recombinant Inhibitor of DNA Binding Id2 Forms Multimeric Structures via the Helix-Loop-Helix Domain and the Nuclear Export Signal.

Cornelia Roschger, Mario Schubert, Christof Regl, Ancuela Andosch, Augusto Marquez, Thomas Berger, Christian G Huber, Ursula Lütz-Meindl, Chiara Cabrele

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in International journal of molecular sciences, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.2field-weighted citation impact, top 48% 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

2 citing papers in PubMed, 2 citations in OpenAlex.

  1. Article
  2. bHLH-PAS Proteins: Their Structure and Intrinsic Disorder.International journal of molecular sciences · 2019
    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

9 authors at 1 institution in 1 country.

Cornelia RoschgerDepartment of Biosciences, University of Salzburg, Billrothstrasse 11 and Hellbrunner Strasse 34, 5020 Salzburg, Austria. cornelia.roschger@sbg.ac.at.
Mario SchubertDepartment of Biosciences, University of Salzburg, Billrothstrasse 11 and Hellbrunner Strasse 34, 5020 Salzburg, Austria. mario.schubert@sbg.ac.at.ORCID 0000-0003-0278-4091
Christof ReglDepartment of Biosciences, University of Salzburg, Billrothstrasse 11 and Hellbrunner Strasse 34, 5020 Salzburg, Austria. christof.regl@sbg.ac.at.
Ancuela AndoschDepartment of Biosciences, University of Salzburg, Billrothstrasse 11 and Hellbrunner Strasse 34, 5020 Salzburg, Austria. ancuela.andosch@sbg.ac.at.
Augusto MarquezDepartment of Chemistry and Physics of Materials, University of Salzburg, Jakob-Haringer Strasse 2a, 5020 Salzburg, Austria. augusto.marquez@imb-cnm.csic.es.ORCID 0000-0003-3074-7941
Thomas BergerDepartment of Chemistry and Physics of Materials, University of Salzburg, Jakob-Haringer Strasse 2a, 5020 Salzburg, Austria. thomas.berger@sbg.ac.at.ORCID 0000-0002-2062-5193
Christian G HuberDepartment of Biosciences, University of Salzburg, Billrothstrasse 11 and Hellbrunner Strasse 34, 5020 Salzburg, Austria. c.huber@sbg.ac.at.
Ursula Lütz-MeindlDepartment of Biosciences, University of Salzburg, Billrothstrasse 11 and Hellbrunner Strasse 34, 5020 Salzburg, Austria. ursula.luetz-meindl@sbg.ac.at.
Chiara CabreleDepartment of Biosciences, University of Salzburg, Billrothstrasse 11 and Hellbrunner Strasse 34, 5020 Salzburg, Austria. chiara.cabrele@sbg.ac.at.ORCID 0000-0002-7550-6896
University of Salzburg · AT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The inhibitor of DNA binding and cell differentiation 2 (Id2) is a helix-loop-helix (HLH) protein that acts as negative dominant regulator of basic-HLH transcription factors during development and in cancer. The structural properties of Id2 have been investigated so far by using synthetic or recombinant fragments reproducing single domains (N-terminus, HLH, C-terminus): the HLH domain tends to dimerize into a four-helix bundle, whereas the flanking regions are flexible. In this work, the intact protein was expressed in

Indexed as

Active Transport, Cell NucleusCircular DichroismEscherichia coliHelix-Loop-Helix MotifsHumansInclusion BodiesInhibitor of Differentiation Protein 2Models, MolecularNuclear Export SignalsProtein MultimerizationProtein Structure, SecondaryRecombinant ProteinsTranscription FactorsID2 protein, humanInhibitor of Differentiation Protein 2Nuclear Export SignalsRecombinant ProteinsTranscription Factorshelix-loop-helix domaininhibitor of DNA bindingintrinsic disorderprotein fibrilsprotein oligomerizationprotein self-assembly

Identifiers

PMID29642431
PMCPMC5979349
OpenAlexW2795848836

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.