Evidence map›Paper›PMID 27559380›Full record

ArticleBeilstein journal of organic chemistry2016

Artificial Diels-Alderase based on the transmembrane protein FhuA.

Hassan Osseili, Daniel F Sauer, Klaus Beckerle, Marcus Arlt, Tomoki Himiyama, Tino Polen, Akira Onoda, Ulrich Schwaneberg, Takashi Hayashi, Jun Okuda

Abstract read
In one paragraph

Article in Beilstein journal of organic chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

4 citing papers in PubMed.

  1. Article
  2. Review
  3. Review
  4. 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

10 authors.

Hassan Osseili *Institute of Inorganic Chemistry, RWTH Aachen University, Landoltweg 1, 52056 Aachen, Germany.
Daniel F Sauer *Institute of Inorganic Chemistry, RWTH Aachen University, Landoltweg 1, 52056 Aachen, Germany.
Klaus BeckerleInstitute of Inorganic Chemistry, RWTH Aachen University, Landoltweg 1, 52056 Aachen, Germany.
Marcus ArltInstitute of Biotechnology, RWTH Aachen University, Worringer Weg 1, 52056 Aachen, Germany.
Tomoki HimiyamaDepartment of Applied Chemistry, Graduate School of Engineering, Osaka University, 2-1 Yamadaoka, Suita 565-0871, Japan.
Tino PolenInstitute of Bio- and Geosciences IBG-1: Biotechnology, Forschungszentrum Jülich GmbH, 52425 Jülich, Germany.
Akira OnodaDepartment of Applied Chemistry, Graduate School of Engineering, Osaka University, 2-1 Yamadaoka, Suita 565-0871, Japan.
Ulrich SchwanebergInstitute of Biotechnology, RWTH Aachen University, Worringer Weg 1, 52056 Aachen, Germany.
Takashi HayashiDepartment of Applied Chemistry, Graduate School of Engineering, Osaka University, 2-1 Yamadaoka, Suita 565-0871, Japan.
Jun OkudaInstitute of Inorganic Chemistry, RWTH Aachen University, Landoltweg 1, 52056 Aachen, Germany.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Copper(I) and copper(II) complexes were covalently linked to an engineered variant of the transmembrane protein Ferric hydroxamate uptake protein component A (FhuA ΔCVF(tev)). Copper(I) was incorporated using an N-heterocyclic carbene (NHC) ligand equipped with a maleimide group on the side arm at the imidazole nitrogen. Copper(II) was attached by coordination to a terpyridyl ligand. The spacer length was varied in the back of the ligand framework. These biohybrid catalysts were shown to be active in the Diels-Alder reaction of a chalcone derivative with cyclopentadiene to preferentially give the endo product.

Indexed as

artificial Diels-Alderasebiohybrid catalysiscopper enyzmemembrane protein

Identifiers

PMID27559380
PMCPMC4979952

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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.