Evidence map›Paper›PMID 26501285›Full record

ReviewSensors (Basel, Switzerland)2015

Fluorescent proteins as genetically encoded FRET biosensors in life sciences.

Bernhard Hochreiter, Alan Pardo Garcia, Johannes A Schmid

Abstract readReview
In one paragraph

Review in Sensors (Basel, Switzerland), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 79 papers.

0numbers the graph read from it
0cells of the map it votes in
79citing 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

79 citing papers in PubMed.

  1. Article
  2. Review
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  15. Review
  16. Choosing the Probe for Single-Molecule Fluorescence Microscopy.International journal of molecular sciences · 2022
    Review
  17. Conserved histidine and tyrosine determine spectral responses through the water network in Deinococcus radiodurans phytochrome.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2022
    Article
  18. Article
  19. Detecting Förster resonance energy transfer in living cells by conventional and spectral flow cytometry.Cytometry. Part A : the journal of the International Society for Analytical Cytology · 2022
    Article
  20. Real-time detection of response regulator phosphorylation dynamics in live bacteria.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article

19 more citing papers are in PubMed but not listed here.

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.

Bernhard HochreiterInstitute for Vascular Biology and Thrombosis Research, Medical University Vienna, Schwarzspanierstraße17, Vienna A-1090, Austria. bernhard.hochreiter@meduniwien.ac.at.
Alan Pardo GarciaInstitute for Vascular Biology and Thrombosis Research, Medical University Vienna, Schwarzspanierstraße17, Vienna A-1090, Austria. alanpardogarcia@gmail.com.
Johannes A SchmidInstitute for Vascular Biology and Thrombosis Research, Medical University Vienna, Schwarzspanierstraße17, Vienna A-1090, Austria. johannes.schmid@meduniwien.ac.at.

Funding

Austrian Science Fund FWF F 5407Austrian Science Fund FWF P 27842
6 · The paper itself

Abstract

Fluorescence- or Förster resonance energy transfer (FRET) is a measurable physical energy transfer phenomenon between appropriate chromophores, when they are in sufficient proximity, usually within 10 nm. This feature has made them incredibly useful tools for many biomedical studies on molecular interactions. Furthermore, this principle is increasingly exploited for the design of biosensors, where two chromophores are linked with a sensory domain controlling their distance and thus the degree of FRET. The versatility of these FRET-biosensors made it possible to assess a vast amount of biological variables in a fast and standardized manner, allowing not only high-throughput studies but also sub-cellular measurements of biological processes. In this review, we aim at giving an overview over the recent advances in genetically encoded, fluorescent-protein based FRET-biosensors, as these represent the largest and most vividly growing group of FRET-based sensors. For easy understanding, we are grouping them into four categories, depending on their molecular mechanism. These are based on: (a) cleavage; (b) conformational-change; (c) mechanical force and (d) changes in the micro-environment. We also address the many issues and considerations that come with the development of FRET-based biosensors, as well as the possibilities that are available to measure them.

Indexed as

Biosensing TechniquesFluorescence Resonance Energy TransferFluorescent DyesLuminescent ProteinsFluorescent DyesLuminescent ProteinsbiosensorsfluorescenceFRETimaging

Identifiers

PMID26501285
PMCPMC4634415

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.