Evidence map›Paper›PMID 30887622›Full record

ArticleAngewandte Chemie (International ed. in English)2019

Dissecting FOXP2 Oligomerization and DNA Binding.

Katharina Häußermann, Gavin Young, Philipp Kukura, Hendrik Dietz

Open access · hybridAbstract read
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
7.0field-weighted citation impact, top 4% 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

19 citing papers in PubMed, 36 citations in OpenAlex.

  1. Review
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  12. Label-free methods for opticalPhysical chemistry chemical physics : PCCP · 2021
    Review
  13. Article
  14. Standard operation procedure for switchSENSE DRX systems.European biophysics journal : EBJ · 2021
    Article
  15. Article
  16. Quantifying Protein-Protein Interactions by Molecular Counting with Mass Photometry.Angewandte Chemie (International ed. in English) · 2020
    Article
  17. Article
  18. Dissecting FOXP2 Oligomerization and DNA Binding.Angewandte Chemie (International ed. in English) · 2019
    Article
  19. 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 2 institutions in 2 countries.

Katharina HäußermannPhysik Department & Munich School of Bioengineering, Technische Universität München, Am Coulombwall 4a, 85784, Garching, Germany.
Gavin YoungDepartment of Chemistry, Physical and Theoretical Chemistry Laboratory, University of Oxford, South Parks Road, Oxford, OX1 3QZ, UK.
Philipp KukuraDepartment of Chemistry, Physical and Theoretical Chemistry Laboratory, University of Oxford, South Parks Road, Oxford, OX1 3QZ, UK.
Hendrik DietzPhysik Department & Munich School of Bioengineering, Technische Universität München, Am Coulombwall 4a, 85784, Garching, Germany.ORCID 0000-0003-1270-3662
Technical University of Munich · DEUniversity of Oxford · GB

Funding

Deutsche Forschungsgemeinschaft Leibniz ProgramDeutsche Forschungsgemeinschaft SFB863 TP A9European Research Council 256270European Research Council Consolidator Grant #724261 (to HD)European Research Council Starting Grant #337757 (to PK)
6 · The paper itself

Abstract

Protein-protein and protein-substrate interactions are critical to function and often depend on factors that are difficult to disentangle. Herein, a combined biochemical and biophysical approach, based on electrically switchable DNA biochips and single-molecule mass analysis, was used to characterize the DNA binding and protein oligomerization of the transcription factor, forkhead box protein P2 (FOXP2). FOXP2 contains domains commonly involved in nucleic-acid binding and protein oligomerization, such as a C

Indexed as

DimerizationProtein ConformationBinding SitesDNAForkhead Transcription FactorsHumansProtein BindingProtein DomainsDNAForkhead Transcription FactorsFOXP2 protein, humanbiochipsFOXP2mass photometryprotein-DNA interactionsprotein-protein interactions

Identifiers

PMID30887622
PMCPMC6986896
OpenAlexW2923914572

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.