Evidence map›Paper›PMID 39167037›Full record

ArticleProtein science : a publication of the Protein Society2024

Tunable crystalline assemblies using surface-engineered protein cages.

Marcel Lach, Michael Rütten, Tobias Beck

Abstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Article
  2. Tunable crystalline assemblies using surface-engineered protein cages.Protein science : a publication of the Protein Society · 2024
    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

3 authors.

Marcel LachDepartment of Chemistry, Institute of Physical Chemistry, University of Hamburg, Hamburg, Germany.
Michael RüttenDepartment of Chemistry, Institute of Physical Chemistry, University of Hamburg, Hamburg, Germany.
Tobias BeckDepartment of Chemistry, Institute of Physical Chemistry, University of Hamburg, Hamburg, Germany.ORCID 0000-0001-7398-3982

Funding

Deutsche ForschungsgemeinschaftFonds der Chemischen Industrie
6 · The paper itself

Abstract

Assembly of nanoparticles into superlattices yields nanomaterials with novel properties. We have recently shown that engineered protein cages are excellent building blocks for the assembly of inorganic nanoparticles into highly structured hybrid materials, with unprecedented precision. In this study, we show that the protein matrix, composed of surface-charged protein cages, can be readily tuned to achieve a number of different crystalline assemblies. Simply by altering the assembly conditions, different types of crystalline structures were produced, without the need to further modify the cages. Future work can utilize these new protein scaffolds to create nanoparticle superlattices with various assembly geometries and thus tune the functionality of these hybrid materials.

Indexed as

Protein EngineeringCrystallizationModels, MolecularNanoparticlesProteinsSurface PropertiesProteinscrystallizationelectrostatic assemblyhybrid protein materialsprotein cages

Identifiers

PMID39167037
PMCPMC11337932

What OpenQuestion holds

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LicenceCC BY-NC
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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.