Evidence map›Paper›PMID 29769518›Full record

ArticleNature communications2018

A cell-penetrating artificial metalloenzyme regulates a gene switch in a designer mammalian cell.

Yasunori Okamoto, Ryosuke Kojima, Fabian Schwizer, Eline Bartolami, Tillmann Heinisch, Stefan Matile, Martin Fussenegger, Thomas R Ward

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed
6.7field-weighted citation impact, top 2% 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

51 citing papers in PubMed, 131 citations in OpenAlex.

  1. Review
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  7. Exploring New Bioorthogonal Catalysts: Scaffold Diversity in Catalysis for Chemical Biology.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Review
  8. Article
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  11. Review
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  13. Nano letters · 2023
    Article
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  15. Review
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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

8 authors at 3 institutions in 2 countries.

Yasunori OkamotoDepartment of Chemistry, University of Basel, Mattenstrasse 24a, BPR 1096, CH-4058, Basel, Switzerland.ORCID http://orcid.org/0000-0002-2442-6079
Ryosuke KojimaDepartment of Biosystems Science and Engineering, ETH Zurich, Mattenstrasse 26, CH-4058, Basel, Switzerland.ORCID http://orcid.org/0000-0002-3792-9222
Fabian SchwizerDepartment of Chemistry, University of Basel, Mattenstrasse 24a, BPR 1096, CH-4058, Basel, Switzerland.
Eline BartolamiDepartment of Organic Chemistry, University of Geneva, CH-1211, Geneva, Switzerland.ORCID http://orcid.org/0000-0003-2187-6637
Tillmann HeinischDepartment of Chemistry, University of Basel, Mattenstrasse 24a, BPR 1096, CH-4058, Basel, Switzerland.
Stefan MatileDepartment of Organic Chemistry, University of Geneva, CH-1211, Geneva, Switzerland. Stefan.Matile@unige.ch.
Martin FusseneggerDepartment of Biosystems Science and Engineering, ETH Zurich, Mattenstrasse 26, CH-4058, Basel, Switzerland. martin.fussenegger@bsse.ethz.ch.ORCID http://orcid.org/0000-0001-8545-667X
Thomas R WardDepartment of Chemistry, University of Basel, Mattenstrasse 24a, BPR 1096, CH-4058, Basel, Switzerland. thomas.ward@unibas.ch.
University of Basel · CHETH Zurich · CHUniversity of Geneva · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Complementing enzymes in their native environment with either homogeneous or heterogeneous catalysts is challenging due to the sea of functionalities present within a cell. To supplement these efforts, artificial metalloenzymes are drawing attention as they combine attractive features of both homogeneous catalysts and enzymes. Herein we show that such hybrid catalysts consisting of a metal cofactor, a cell-penetrating module, and a protein scaffold are taken up into HEK-293T cells where they catalyze the uncaging of a hormone. This bioorthogonal reaction causes the upregulation of a gene circuit, which in turn leads to the expression of a nanoluc-luciferase. Relying on the biotin-streptavidin technology, variation of the biotinylated ruthenium complex: the biotinylated cell-penetrating poly(disulfide) ratio can be combined with point mutations on streptavidin to optimize the catalytic uncaging of an allyl-carbamate-protected thyroid hormone triiodothyronine. These results demonstrate that artificial metalloenzymes offer highly modular tools to perform bioorthogonal catalysis in live HEK cells.

Indexed as

BiotinBiotinylationCatalysisHEK293 CellsHumansMetalloendopeptidasesMolecular StructurePoint MutationRutheniumStereoisomerismStreptavidinTriiodothyronineBiotinMetalloendopeptidasesRutheniumStreptavidinTriiodothyronine

Identifiers

PMID29769518
PMCPMC5955986
OpenAlexW2804205785

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.