Evidence map›Paper›PMID 36324888›Full record

ArticleFrontiers in bioengineering and biotechnology2022

Enhanced small green fluorescent proteins as a multisensing platform for biosensor development.

Guo-Teng Liang, Cuixin Lai, Zejun Yue, Hanbin Zhang, Danyang Li, Zhong Chen, Xingyu Lu, Liang Tao, Fedor V Subach, Kiryl D Piatkevich

Abstract read
In one paragraph

Article in Frontiers in bioengineering and biotechnology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing 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

17 citing papers in PubMed.

  1. Article
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  11. Rational Design of a Circularly Permuted Flavin-Based Fluorescent Protein.Chembiochem : a European journal of chemical biology · 2024
    Article
  12. Review
  13. Reengineering of a flavin-binding fluorescent protein using ProteinMPNN.Protein science : a publication of the Protein Society · 2024
    Article
  14. Article
  15. Article
  16. Article
  17. 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

10 authors.

Guo-Teng LiangSchool of Life Sciences, Westlake University, Hangzhou, Zhejiang, China.
Cuixin LaiSchool of Life Sciences, Westlake University, Hangzhou, Zhejiang, China.
Zejun YueSchool of Life Sciences, Westlake University, Hangzhou, Zhejiang, China.
Hanbin ZhangSchool of Life Sciences, Westlake University, Hangzhou, Zhejiang, China.
Danyang LiSchool of Life Sciences, Westlake University, Hangzhou, Zhejiang, China.
Zhong ChenKey Laboratory of Precise Synthesis of Functional Molecules of Zhejiang Province, School of Science, Instrumentation and Service Center for Molecular Sciences, Westlake University, Hangzhou, Zhejiang, China.
Xingyu LuKey Laboratory of Precise Synthesis of Functional Molecules of Zhejiang Province, School of Science, Instrumentation and Service Center for Molecular Sciences, Westlake University, Hangzhou, Zhejiang, China.
Liang TaoSchool of Life Sciences, Westlake University, Hangzhou, Zhejiang, China.
Fedor V SubachComplex of NBICS Technologies, National Research Center "Kurchatov Institute", Moscow, Russia.
Kiryl D PiatkevichSchool of Life Sciences, Westlake University, Hangzhou, Zhejiang, China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Engineered light, oxygen, and voltage (LOV)-based proteins are able to fluoresce without oxygen requirement due to the autocatalytic incorporation of exogenous flavin as a chromophore thus allowing for live cell imaging under hypoxic and anaerobic conditions. They were also discovered to have high sensitivity to transition metal ions and physiological flavin derivatives. These properties make flavin-binding fluorescent proteins (FPs) a perspective platform for biosensor development. However, brightness of currently available flavin-binding FPs is limited compared to GFP-like FPs creating a need for their further enhancement and optimization. In this study, we applied a directed molecular evolution approach to develop a pair of flavin-binding FPs, named miniGFP1 and miniGFP2. The miniGFP proteins are characterized by cyan-green fluorescence with excitation/emission maxima at 450/499 nm and a molecular size of ∼13 kDa. We carried out systematic benchmarking of miniGFPs in

Indexed as

copperflavinfluorescent protein biosensorhypoxialive cell imaging microscopy

Identifiers

PMID36324888
PMCPMC9618808

What OpenQuestion holds

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Registered trials

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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.