Evidence map›Paper›PMID 33725379›Full record

ArticleAngewandte Chemie (International ed. in English)2021

Dynamic Protease Activation on a Multimeric Synthetic Protein Scaffold via Adaptable DNA-Based Recruitment Domains.

Tsuyoshi Mashima, Bas J H M Rosier, Koji Oohora, Tom F A de Greef, Takashi Hayashi, Luc Brunsveld

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2021. 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
0.6field-weighted citation impact, top 36% 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

3 citing papers in PubMed, 8 citations in OpenAlex.

  1. Programmable DNA Assemblies Reconstitute Supramolecular Protein Function.bioRxiv : the preprint server for biology · 2026
    Article
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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

6 authors at 2 institutions in 2 countries.

Tsuyoshi MashimaInstitute for Complex Molecular Systems and, Laboratory of Chemical Biology, Department of Biomedical Engineering, Eindhoven University of Technology, P.O. Box 513, 5600, MB, Eindhoven, The Netherlands.ORCID 0000-0002-2402-1573
Bas J H M RosierInstitute for Complex Molecular Systems and, Laboratory of Chemical Biology, Department of Biomedical Engineering, Eindhoven University of Technology, P.O. Box 513, 5600, MB, Eindhoven, The Netherlands.ORCID 0000-0002-0062-7087
Koji OohoraDepartment of Applied Chemistry, Graduate School of Engineering, Osaka University, Suita 565-0871, Osaka, Japan.ORCID 0000-0003-1155-6824
Tom F A de GreefInstitute for Complex Molecular Systems and, Laboratory of Chemical Biology, Department of Biomedical Engineering, Eindhoven University of Technology, P.O. Box 513, 5600, MB, Eindhoven, The Netherlands.ORCID 0000-0002-0714-5881
Takashi HayashiDepartment of Applied Chemistry, Graduate School of Engineering, Osaka University, Suita 565-0871, Osaka, Japan.ORCID 0000-0002-2215-935X
Luc BrunsveldInstitute for Complex Molecular Systems and, Laboratory of Chemical Biology, Department of Biomedical Engineering, Eindhoven University of Technology, P.O. Box 513, 5600, MB, Eindhoven, The Netherlands.ORCID 0000-0001-5675-511X
Eindhoven University of Technology · NLThe University of Osaka · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Hexameric hemoprotein (HTHP) is employed as a scaffold protein for the supramolecular assembly and activation of the apoptotic signalling enzyme caspase-9, using short DNA elements as modular recruitment domains. Caspase-9 assembly and activation on the HTHP platform due to enhanced proximity is followed by combinatorial inhibition at high scaffold concentrations. The DNA recruitment domains allow for reversible switching of the caspase-9 assembly and activity state using short modulatory DNA strands. Tuning of the recruitment domain affinity allows for generating kinetically trapped active enzyme complexes, as well as for dynamic repositioning of caspases over scaffold populations and inhibition using monovalent sink platforms. The conceptual combination of a highly structured multivalent protein platform with modular DNA recruitment domains provides emergent biomimicry properties with advanced levels of control over protein assembly.

Indexed as

Caspase 9DNAHumansKineticsModels, MolecularCASP9 protein, humanCaspase 9DNAartificial apoptosomeDNA nanotechnologyenzymesself-assemblysupramolecular chemistry

Identifiers

PMID33725379
PMCPMC8252739
OpenAlexW3138888298

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.