Evidence map›Paper›PMID 26915475›Full record

ArticleAngewandte Chemie (International ed. in English)2016

Orthogonal Protein Assembly on DNA Nanostructures Using Relaxases.

Sandra Sagredo, Tobias Pirzer, Ali Aghebat Rafat, Marisa A Goetzfried, Gabriel Moncalian, Friedrich C Simmel, Fernando de la Cruz

Open access · hybridAbstract read
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
3.8field-weighted citation impact, top 6% 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

17 citing papers in PubMed, 46 citations in OpenAlex.

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  4. The crystal structure of the human smacovirus 1 Rep domain.Acta crystallographica. Section F, Structural biology communications · 2023
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  16. Orthogonal Protein Assembly on DNA Nanostructures Using Relaxases.Angewandte Chemie (International ed. in English) · 2016
    Article
  17. 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

7 authors at 2 institutions in 2 countries.

Sandra SagredoDepartamento de Biología Molecular e Instituto de Biomedicina y Biotecnología de Cantabria, Universidad de Cantabria-Consejo Superior de Investigaciones Científicas-SODERCAN, Albert Einstein 22, 39011, Santander, Spain.
Tobias PirzerPhysik-Department E14 and ZNN/WSI, TU Munich, Am Coulombwall 4a, 85748, Garching, Germany.
Ali Aghebat RafatPhysik-Department E14 and ZNN/WSI, TU Munich, Am Coulombwall 4a, 85748, Garching, Germany.
Marisa A GoetzfriedPhysik-Department E14 and ZNN/WSI, TU Munich, Am Coulombwall 4a, 85748, Garching, Germany.
Gabriel MoncalianDepartamento de Biología Molecular e Instituto de Biomedicina y Biotecnología de Cantabria, Universidad de Cantabria-Consejo Superior de Investigaciones Científicas-SODERCAN, Albert Einstein 22, 39011, Santander, Spain.
Friedrich C SimmelPhysik-Department E14 and ZNN/WSI, TU Munich, Am Coulombwall 4a, 85748, Garching, Germany. simmel@tum.de.ORCID http://orcid.org/0000-0003-3829-3446
Fernando de la CruzDepartamento de Biología Molecular e Instituto de Biomedicina y Biotecnología de Cantabria, Universidad de Cantabria-Consejo Superior de Investigaciones Científicas-SODERCAN, Albert Einstein 22, 39011, Santander, Spain. delacruz@unican.es.
Technical University of Munich · DEUniversidad de Cantabria · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

DNA-binding proteins are promising reagents for the sequence-specific modification of DNA-based nanostructures. Here, we investigate the utility of a series of relaxase proteins-TrwC, TraI, and MobA-for nanofunctionalization. Relaxases are involved in the conjugative transfer of plasmids between bacteria, and bind to their DNA target sites via a covalent phosphotyrosine linkage. We study the binding of the relaxases to two standard DNA origami structures-rodlike six-helix bundles and flat rectangular origami sheets. We find highly orthogonal binding of the proteins with binding yields of 40-50 % per binding site, which is comparable to other functionalization methods. The yields differ for the two origami structures and also depend on the position of the binding sites. Due to their specificity for a single-stranded DNA target, their orthogonality, and their binding properties, relaxases are a uniquely useful addition to the toolbox available for the modification of DNA nanostructures with proteins.

Indexed as

DNAMicroscopy, Electron, TransmissionNanostructuresProteinsDNAProteinsbacterial conjugationbioconjugationDNA nanotechnologyDNA origamirelaxase

Identifiers

PMID26915475
PMCPMC5067690
OpenAlexW2329033822

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.