Evidence map›Paper›PMID 25860669›Full record

ArticleBiomedical microdevices2015

Engineered self-assembling monolayers for label free detection of influenza nucleoprotein.

Anton P Le Brun, Andrei Soliakov, Deepan S H Shah, Stephen A Holt, Alison McGill, Jeremy H Lakey

Open access · hybridAbstract read
In one paragraph

Article in Biomedical microdevices, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
1.4field-weighted citation impact, top 20% 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

5 citing papers in PubMed, 22 citations in OpenAlex.

  1. Fully Aqueous Self-Assembly of a Gold-Nanoparticle-Based Pathogen Sensor.International journal of molecular sciences · 2023
    Article
  2. Review
  3. Binding Revisited-Avidity in Cellular Function and Signaling.Frontiers in molecular biosciences · 2020
    Review
  4. Article
  5. Review
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 3 institutions in 2 countries.

Anton P Le BrunBragg Institute, Australian Nuclear Science and Technology Organisation, Locked Bag 2001, Kirrawee DC, NSW, 2232, Australia.
Andrei Soliakov
Deepan S H Shah
Stephen A Holt
Alison McGill
Jeremy H Lakey
Newcastle University · GBAustralian Nuclear Science and Technology Organisation · AUOrla Protein Technologies (United Kingdom) · GB

Funding

Wellcome Trust
6 · The paper itself

Abstract

Integrating nanotechnology into useable devices requires a combination of bottom up and top down methodology. Often the techniques to measure and control these different components are entirely different, so methods that can analyse the nanoscale component in situ are of increasing importance. Here we describe a strategy that employs a self-assembling monolayer of engineered protein chimeras to display an array of oriented antibodies (IgG) on a microelectronic device for the label free detection of influenza nucleoprotein. The structural and functional properties of the bio-interface were characterised by a range of physical techniques including surface plasmon resonance, quartz-crystal microbalance and neutron reflectometry. This combination of methods reveals a 13.5 nm thick engineered-monolayer that (i) self-assembles on gold surfaces, (ii) captures IgG with high affinity in a defined orientation and (iii) specifically recognises the influenza A nucleoprotein. Furthermore we also show that this non-covalent self-assembled structure can render the dissociation of bound IgG irreversible by chemical crosslinking in situ without affecting the IgG function. The methods can thus describe in detail the transition from soluble engineered molecules with nanometre dimensions to an array that demonstrates the principles of a working influenza sensor.

Indexed as

Equipment DesignEquipment Failure AnalysisHumansImmunoassayInfluenza, HumanMicro-Electrical-Mechanical SystemsNucleocapsid ProteinsProtein EngineeringReproducibility of ResultsRNA-Binding ProteinsSensitivity and SpecificityStaining and LabelingSurface Plasmon ResonanceViral Core ProteinsNP protein, Influenza A virusNucleocapsid ProteinsRNA-Binding ProteinsViral Core Proteins

Identifiers

PMID25860669
PMCPMC4392172
OpenAlexW2033419472

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.