Evidence map›Paper›PMID 30061991›Full record

ArticleChemical science2018

Total chemical synthesis and biophysical properties of a designed soluble 24 kDa amyloid analogue.

Régis Boehringer, Bruno Kieffer, Vladimir Torbeev

Abstract read
In one paragraph

Article in Chemical science, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
–field-weighted citation impact
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

3 citing papers in PubMed.

  1. Article
  2. Article
  3. Novel protein science enabled by total chemical synthesis.Protein science : a publication of the Protein Society · 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

3 authors.

Régis BoehringerInstitut de Science et d'Ingénierie Supramoléculaires (ISIS) , International Center for Frontier Research in Chemistry (icFRC) , University of Strasbourg , CNRS (UMR 7006) , Strasbourg , France . Email: torbeev@unistra.fr.ORCID 0000-0003-2344-1362
Bruno KiefferDepartment of Integrated Structural Biology , Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC) , INSERM (U964) , University of Strasbourg , CNRS (UMR 7104) , Illkirch , France.ORCID 0000-0002-2033-4679
Vladimir TorbeevInstitut de Science et d'Ingénierie Supramoléculaires (ISIS) , International Center for Frontier Research in Chemistry (icFRC) , University of Strasbourg , CNRS (UMR 7006) , Strasbourg , France . Email: torbeev@unistra.fr.ORCID 0000-0002-7865-1044

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Discovering molecular probes that specifically recognize distinct amyloid structures is highly important for physiological studies of protein-misfolding diseases as well as for the development of diagnostic reagents and inhibitors of amyloid self-assembly. Here, we demonstrate an approach that allows for identification of

Identifiers

PMID30061991
PMCPMC6049524

What OpenQuestion holds

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LicenceCC BY
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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.