Evidence map›Paper›PMID 26241391›Full record

ArticleBiotechnology and bioengineering2016

Electrochemical activation of engineered protein switches.

Jay H Choi, Maya Zayats, Peter C Searson, Marc Ostermeier

Abstract read
In one paragraph

Article in Biotechnology and bioengineering, 2016. 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. 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

4 authors.

Jay H ChoiDepartment of Chemical and Biomolecular Engineering, Johns Hopkins University, 3400 N. Charles St., Baltimore, Maryland, 21218.
Maya ZayatsDepartment of Materials Science and Engineering, Johns Hopkins University, 3400 N. Charles St., Baltimore, Maryland, 21218. oster@jhu.edu.
Peter C SearsonDepartment of Materials Science and Engineering, Johns Hopkins University, 3400 N. Charles St., Baltimore, Maryland, 21218.
Marc OstermeierDepartment of Chemical and Biomolecular Engineering, Johns Hopkins University, 3400 N. Charles St., Baltimore, Maryland, 21218.

Funding

Translational Research Central ServicesP30CA006973 · NCI · JOHNS HOPKINS UNIVERSITY · PI Rosalie Wollett · 1985 to 2026
$208.6M
The Combinatorial Design of Protein Molecular SwitchesR01GM066972 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI OSTERMEIER, MARC A · 2003 to 2016
$4.0M
NCI NIH HHS P30 CA006973NIGMS NIH HHS R01 GM066972
6 · The paper itself

Abstract

Engineered protein switches have a large dynamic range, high specificity for the activating ligand, and a modular architecture, and have been explored for a wide range of applications including biosensors and therapeutics. The ability to externally control switch function is important in extending applications for protein switches. We recently demonstrated that the on/off state could be controlled by the redox state of disulfide bonds introduced into the switches at select locations. Here, we demonstrate that an electrochemical signal can be used as an exogenous input to control switch function via reduction of the engineered disulfide bonds. This study suggests that disulfide-containing protein switch is a potentially useful platform for bioelectronic sensors with remote control of the sensing ability.

Indexed as

Protein ConformationProtein EngineeringDisulfidesOxidation-ReductionProteinsDisulfidesProteinsallosterydisulfide bondelectrochemical reductionprotein engineeringprotein switch

Identifiers

PMID26241391
PMCPMC4721505

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.