Evidence map›Paper›PMID 34934192›Full record

ArticleNature chemical biology2022

Mandipropamid as a chemical inducer of proximity for in vivo applications.

Michael J Ziegler, Klaus Yserentant, Valentin Dunsing, Volker Middel, Antoni J Gralak, Kaisa Pakari, Jörn Bargstedt, Christoph Kern, Annett Petrich, Salvatore Chiantia and 3 more

Open access · hybridAbstract read
In one paragraph

Article in Nature chemical biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
2.0field-weighted citation impact, top 12% 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

26 citing papers in PubMed, 37 citations in OpenAlex.

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  15. Photoactivatable Nanobody Conjugate Dimerizer Temporally Resolves Tiam1-Rac1 Signaling Axis.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024
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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

13 authors at 3 institutions in 2 countries.

Michael J Ziegler *Institute of Pharmacy and Molecular Biotechnology, Heidelberg University, Heidelberg, Germany.
Klaus Yserentant *Institute of Physical Chemistry, Heidelberg University, Heidelberg, Germany.ORCID http://orcid.org/0000-0001-9746-6912
Valentin DunsingInstitute of Biology and Biochemistry, University of Potsdam, Potsdam, Germany.
Volker MiddelInstitute of Biological and Chemical Systems (IBCS)-Biological Information Processing (BIP), Karlsruhe Institute of Technology (KIT), Eggenstein-Leopoldshafen, Germany.
Antoni J GralakInstitute of Pharmacy and Molecular Biotechnology, Heidelberg University, Heidelberg, Germany.
Kaisa PakariInstitute of Physical Chemistry, Heidelberg University, Heidelberg, Germany.ORCID http://orcid.org/0000-0001-8101-5252
Jörn BargstedtInstitute of Pharmacy and Molecular Biotechnology, Heidelberg University, Heidelberg, Germany.
Christoph KernInstitute of Pharmacy and Molecular Biotechnology, Heidelberg University, Heidelberg, Germany.
Annett PetrichInstitute of Biology and Biochemistry, University of Potsdam, Potsdam, Germany.
Salvatore ChiantiaInstitute of Biology and Biochemistry, University of Potsdam, Potsdam, Germany.
Uwe SträhleInstitute of Biological and Chemical Systems (IBCS)-Biological Information Processing (BIP), Karlsruhe Institute of Technology (KIT), Eggenstein-Leopoldshafen, Germany.ORCID http://orcid.org/0000-0002-4062-9431
Dirk-Peter HertenInstitute of Physical Chemistry, Heidelberg University, Heidelberg, Germany.ORCID http://orcid.org/0000-0002-3884-0262
Richard WombacherInstitute of Pharmacy and Molecular Biotechnology, Heidelberg University, Heidelberg, Germany. wombacher@mr.mpg.de.ORCID http://orcid.org/0000-0003-1267-5614
Heidelberg University · DEUniversity of Potsdam · DEKarlsruhe Institute of Technology · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Direct control of protein interactions by chemically induced protein proximity holds great potential for both cell and synthetic biology as well as therapeutic applications. Low toxicity, orthogonality and excellent cell permeability are important criteria for chemical inducers of proximity (CIPs), in particular for in vivo applications. Here, we present the use of the agrochemical mandipropamid (Mandi) as a highly efficient CIP in cell culture systems and living organisms. Mandi specifically induces complex formation between a sixfold mutant of the plant hormone receptor pyrabactin resistance 1 (PYR1) and abscisic acid insensitive (ABI). It is orthogonal to other plant hormone-based CIPs and rapamycin-based CIP systems. We demonstrate the applicability of the Mandi system for rapid and efficient protein translocation in mammalian cells and zebrafish embryos, protein network shuttling and manipulation of endogenous proteins.

Indexed as

Abscisic AcidAmidesAnimalsCarboxylic AcidsDimerizationFungicides, IndustrialZebrafishAbscisic AcidAmidesCarboxylic AcidsFungicides, Industrialmandipropamid

Identifiers

PMID34934192
PMCPMC8709788
OpenAlexW4200315554

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.