Evidence map›Paper›PMID 37431791›Full record

ReviewBiochemical Society transactions2023

Maximizing the performance of protein-based fluorescent biosensors.

Fu Chai, Dazhou Cheng, Yusuke Nasu, Takuya Terai, Robert E Campbell

Open access · hybridAbstract readReview
In one paragraph

Review in Biochemical Society transactions, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
6.8field-weighted citation impact, top 4% 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

9 citing papers in PubMed, 19 citations in OpenAlex.

  1. Development of a Photostable pH Biosensor Based on mStayGold.Chembiochem : a European journal of chemical biology · 2026
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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

5 authors at 3 institutions in 2 countries.

Fu ChaiDepartment of Chemistry, Graduate School of Science, The University of Tokyo, Tokyo 113-0033, Japan.
Dazhou ChengDepartment of Chemistry, Graduate School of Science, The University of Tokyo, Tokyo 113-0033, Japan.
Yusuke NasuDepartment of Chemistry, Graduate School of Science, The University of Tokyo, Tokyo 113-0033, Japan.
Takuya TeraiDepartment of Chemistry, Graduate School of Science, The University of Tokyo, Tokyo 113-0033, Japan.ORCID 0000-0002-3425-3589
Robert E CampbellDepartment of Chemistry, Graduate School of Science, The University of Tokyo, Tokyo 113-0033, Japan.ORCID 0000-0003-0604-092X
The University of Tokyo · JPJapan Science and Technology Agency · JPUniversity of Alberta · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Fluorescent protein (FP)-based biosensors are genetically encoded tools that enable the imaging of biological processes in the context of cells, tissues, or live animals. Though widely used in biological research, practically all existing biosensors are far from ideal in terms of their performance, properties, and applicability for multiplexed imaging. These limitations have inspired researchers to explore an increasing number of innovative and creative ways to improve and maximize biosensor performance. Such strategies include new molecular biology methods to develop promising biosensor prototypes, high throughput microfluidics-based directed evolution screening strategies, and improved ways to perform multiplexed imaging. Yet another approach is to effectively replace components of biosensors with self-labeling proteins, such as HaloTag, that enable the biocompatible incorporation of synthetic fluorophores or other ligands in cells or tissues. This mini-review will summarize and highlight recent innovations and strategies for enhancing the performance of FP-based biosensors for multiplexed imaging to advance the frontiers of research.

Indexed as

Biosensing TechniquesFluorescence Resonance Energy TransferAnimalsFluorescent DyesProteinsFluorescent DyesProteinsbiosensorschemical biologyfluorescence microscopyfluorescent proteinsprotein engineeringsignaling

Identifiers

PMID37431791
PMCPMC10586770
OpenAlexW4383872997

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

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.