Evidence map›Paper›PMID 24059509›Full record

ReviewBiochemical Society transactions2013

Rational design of FRET sensor proteins based on mutually exclusive domain interactions.

Maarten Merkx, Misha V Golynskiy, Laurens H Lindenburg, Jan L Vinkenborg

Abstract readReview
In one paragraph

Review in Biochemical Society transactions, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing 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

13 citing papers in PubMed.

  1. Review
  2. Review
  3. Review
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Synthetic biology devices for in vitro and in vivo diagnostics.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Review
  12. Article
  13. Engineering genetically encoded FRET sensors.Sensors (Basel, Switzerland) · 2014
    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

4 authors.

Maarten Merkx*Laboratory of Chemical Biology, Department of Biomedical Engineering, Eindhoven University of Technology, P.O. Box 513, 5600MB Eindhoven, The Netherlands.
Misha V Golynskiy
Laurens H Lindenburg
Jan L Vinkenborg

Funding

European Research Council 280255
6 · The paper itself

Abstract

Proteins that switch between distinct conformational states are ideal to monitor and control molecular processes within the complexity of biological systems. Inspired by the modular architecture of natural signalling proteins, our group explores generic design strategies for the construction of FRET-based sensor proteins and other protein switches. In the present article, I show that designing FRET sensors based on mutually exclusive domain interactions provides a robust method to engineer sensors with predictable properties and an inherently large change in emission ratio. The modularity of this approach should make it easily transferable to other applications of protein switches in fields ranging from synthetic biology, optogenetics and molecular diagnostics.

Indexed as

Biosensing TechniquesProtein EngineeringFluorescence Resonance Energy TransferProtein Interaction Domains and MotifsProteinsSynthetic BiologyProteins

Identifiers

PMID24059509
PMCPMC3822149

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.