Evidence map›Paper›PMID 24756130›Full record

ArticleMolecules (Basel, Switzerland)2014

High efficiency acetylcholinesterase immobilization on DNA aptamer modified surfaces.

Orada Chumphukam, Thao T Le, Anthony E G Cass

Open access · goldAbstract read
In one paragraph

Article in Molecules (Basel, Switzerland), 2014. 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
1.0field-weighted citation impact, top 26% 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

1 citing paper in PubMed, 13 citations in OpenAlex.

  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

3 authors at 1 institution in 1 country.

Orada ChumphukamDepartment of Chemistry, Imperial College, London SW7 2AZ, UK.
Thao T LeDepartment of Chemistry, Imperial College, London SW7 2AZ, UK.
Anthony E G CassDepartment of Chemistry, Imperial College, London SW7 2AZ, UK. t.cass@imperial.ac.uk.
Imperial College London · GB

Funding

Biotechnology and Biological Sciences Research Council
6 · The paper itself

Abstract

We report here the in vitro selection of DNA aptamers for electric eel acetylcholinesterase (AChE). One selected aptamer sequence (R15/19) has a high affinity towards the enzyme (Kd=157±42 pM). Characterization of the aptamer showed its binding is not affected by low ionic strength (~20 mM), however significant reduction in affinity occurred at high ionic strength (~1.2 M). In addition, this aptamer does not inhibit the catalytic activity of AChE that we exploit through immobilization of the DNA on a streptavidin-coated surface. Subsequent immobilization of AChE by the aptamer results in a 4-fold higher catalytic activity when compared to adsorption directly on to plastic.

Indexed as

AcetylcholinesteraseAnimalsAptamers, NucleotideBase SequenceElectrophorusEnzymes, ImmobilizedFish ProteinsKineticsMolecular Sequence DataNucleic Acid ConformationOsmolar ConcentrationProtein BindingSELEX Aptamer TechniqueStreptavidinAcetylcholinesteraseAptamers, NucleotideEnzymes, ImmobilizedFish ProteinsStreptavidin

Identifiers

PMID24756130
PMCPMC6271157
OpenAlexW1977578269

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.