Evidence map›Paper›PMID 34231559›Full record

ArticleSoft matter2021

Decorated networks of native proteins: nanomaterials with tunable mesoscopic domain size.

Ioatzin Ríos de Anda, Angélique Coutable-Pennarun, Christopher Brasnett, Stephen Whitelam, Annela Seddon, John Russo, J L Ross Anderson, C Patrick Royall

Abstract read
In one paragraph

Article in Soft matter, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. 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

8 authors.

Ioatzin Ríos de AndaH.H. Wills Physics Laboratory, Tyndall Avenue, Bristol, BS8 1TL, UK. ioatzin.riosdeanda@bristol.ac.uk.
Angélique Coutable-Pennarun
Christopher Brasnett
Stephen Whitelam
Annela Seddon
John Russo
J L Ross Anderson
C Patrick Royall

Funding

Biotechnology and Biological Sciences Research Council BB/L01386X/1
6 · The paper itself

Abstract

Natural and artificial proteins with designer properties and functionalities offer unparalleled opportunity for functional nanoarchitectures formed through self-assembly. However, to exploit this potential we need to design the system such that assembly results in desired architecture forms while avoiding denaturation and therefore retaining protein functionality. Here we address this challenge with a model system of fluorescent proteins. By manipulating self-assembly using techniques inspired by soft matter where interactions between the components are controlled to yield the desired structure, we have developed a methodology to assemble networks of proteins of one species which we can decorate with another, whose coverage we can tune. Consequently, the interfaces between domains of each component can also be tuned, with potential applications for example in energy - or electron - transfer. Our model system of eGFP and mCherry with tuneable interactions reveals control over domain sizes in the resulting networks.

Indexed as

NanostructuresProteinsProteins

Identifiers

PMID34231559
PMCPMC8294043

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.