Evidence map›Paper›PMID 31461959›Full record

ReviewInternational journal of molecular sciences2019

Circularly Permuted Fluorescent Protein-Based Indicators: History, Principles, and Classification.

Alexander I Kostyuk, Aleksandra D Demidovich, Daria A Kotova, Vsevolod V Belousov, Dmitry S Bilan

Abstract readReview
In one paragraph

Review in International journal of molecular sciences, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 69 papers.

0numbers the graph read from it
0cells of the map it votes in
69citing 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

69 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Protein Engineering for Spatiotemporally Resolved Cellular Monitoring.Annual review of analytical chemistry (Palo Alto, Calif.) · 2025
    Review
  11. Review
  12. An optical BOD biosensor based on intracellular ATP measurements in genetically modified Saccharomyces cerevisiae.Analytical sciences : the international journal of the Japan Society for Analytical Chemistry · 2025
    Article
  13. A novel protein for bioremediation of gadolinium waste.Protein science : a publication of the Protein Society · 2025
    Article
  14. Article
  15. Article
  16. Article
  17. Detection of circular permutations by Protein Language Models.Computational and structural biotechnology journal · 2025
    Article
  18. Article
  19. Article
  20. Review

9 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

5 authors.

Alexander I KostyukShemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Moscow 117997, Russia.
Aleksandra D DemidovichShemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Moscow 117997, Russia.
Daria A KotovaShemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Moscow 117997, Russia.
Vsevolod V BelousovShemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Moscow 117997, Russia.
Dmitry S BilanShemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Moscow 117997, Russia. d.s.bilan@gmail.com.

Funding

Russian Science Foundation 17-15-01175Российский Фонд Фундаментальных Исследований (РФФИ) 18-34-20032Российский Фонд Фундаментальных Исследований (РФФИ) 18-54-74003
6 · The paper itself

Abstract

Genetically encoded biosensors based on fluorescent proteins (FPs) are a reliable tool for studying the various biological processes in living systems. The circular permutation of single FPs led to the development of an extensive class of biosensors that allow the monitoring of many intracellular events. In circularly permuted FPs (cpFPs), the original N- and C-termini are fused using a peptide linker, while new termini are formed near the chromophore. Such a structure imparts greater mobility to the FP than that of the native variant, allowing greater lability of the spectral characteristics. One of the common principles of creating genetically encoded biosensors is based on the integration of a cpFP into a flexible region of a sensory domain or between two interacting domains, which are selected according to certain characteristics. Conformational rearrangements of the sensory domain associated with ligand interaction or changes in the cellular parameter are transferred to the cpFP, changing the chromophore environment. In this review, we highlight the basic principles of such sensors, the history of their creation, and a complete classification of the available biosensors.

Indexed as

Absorption, RadiationAnimalsBiosensing TechniquesGenes, ReporterGreen Fluorescent ProteinsHumansRecombinant ProteinsGreen Fluorescent ProteinsRecombinant Proteinscircularly permuted fluorescent proteinsgenetically encoded biosensors

Identifiers

PMID31461959
PMCPMC6747460

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.