Evidence map›Paper›PMID 29877078›Full record

ArticleACS sensors2018

Expanding the Scope of Protein-Detecting Electrochemical DNA "Scaffold" Sensors.

Di Kang, Claudio Parolo, Sheng Sun, Nathan E Ogden, Frederick W Dahlquist, Kevin W Plaxco

Open access · greenAbstract read
In one paragraph

Article in ACS sensors, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.2field-weighted citation impact, top 11% 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

18 citing papers in PubMed, 45 citations in OpenAlex.

  1. Review
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  3. Article
  4. Rationally Designed DNA-Based Scaffolds and Switching Probes for Protein Sensing.Advances in biochemical engineering/biotechnology · 2024
    Review
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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 1 institution in 1 country.

Di Kang
Claudio Parolo
Sheng Sun
Nathan E Ogden
Frederick W Dahlquist
University of California, Santa Barbara · US

Funding

MECHANISTIC STUDIES OF BACTERIAL CHEMOTAXISR01GM059544 · NIGMS · UNIVERSITY OF OREGON · PI DAHLQUIST, FREDERICK W. · 1999 to 2018
$4.8M
The thermodynamics of protein-surface interactionsR01GM118560 · NIGMS · UNIVERSITY OF CALIFORNIA SANTA BARBARA · PI PLAXCO, KEVIN W · 2017 to 2020
$1.4M
A new approach to quantitative, point-of-care serologyR01AI107936 · NIAID · UNIVERSITY OF CALIFORNIA SANTA BARBARA · PI PLAXCO, KEVIN W · 2014 to 2017
$1.4M
NIAID NIH HHS R01 AI107936NIGMS NIH HHS R01 GM059544NIGMS NIH HHS R01 GM118560
6 · The paper itself

Abstract

The ability to measure the levels of diagnostically relevant proteins, such as antibodies, directly at the point of care could significantly impact healthcare. Thus motivated, we explore here the E-DNA "scaffold" sensing platform, a rapid, convenient, single-step means to this end. These sensors comprise a rigid nucleic acid "scaffold" attached via a flexible linker to an electrode and modified on its distal end with a redox reporter and a protein binding "recognition element". The binding of a targeted protein reduces the efficiency with which the redox reporter approaches the electrode, resulting in an easily measured signal change when the sensor is interrogated voltammetrically. Previously we have demonstrated scaffold sensors employing a range of low molecular weight haptens and linear peptides as their recognition elements. Expanding on this here we have characterized sensors employing much larger recognition elements (up to and including full length proteins) in order to (1) define the range of recognition elements suitable for use in the platform; (2) better characterize the platform's signaling mechanism to aid its design and optimization; and (3) demonstrate the analytical performance of sensors employing full-length proteins as recognition elements. In doing so we have enlarged the range of molecular targets amenable to this rapid and convenient sensing platform.

Indexed as

Biosensing TechniquesDNAElectrochemical TechniquesEquipment DesignEscherichia coli ProteinsGreen Fluorescent ProteinsHistidine KinaseHIV Core Protein p24Limit of DetectionMethyl-Accepting Chemotaxis ProteinsMolecular WeightNitrilotriacetic AcidProteinscheA protein, E coliDNAEscherichia coli ProteinsGreen Fluorescent ProteinsHistidine KinaseHIV Core Protein p24Methyl-Accepting Chemotaxis ProteinsNitrilotriacetic AcidProteinsantibody detectionDNAelectrochemical biosensorproteinprotein detection

Identifiers

PMID29877078
PMCPMC6519109
OpenAlexW2805756211

What OpenQuestion holds

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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.