Evidence map›Paper›PMID 30533492›Full record

ArticleBiophysics reports2018

Significant expansion and red-shifting of fluorescent protein chromophore determined through computational design and genetic code expansion.

Li Wang, Xian Chen, Xuzhen Guo, Jiasong Li, Qi Liu, Fuying Kang, Xudong Wang, Cheng Hu, Haiping Liu, Weimin Gong and 3 more

Open access · diamondAbstract read
In one paragraph

Article in Biophysics reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
1.0field-weighted citation impact, top 16% 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

6 citing papers in PubMed, 10 citations in OpenAlex.

  1. Article
  2. Article
  3. Pharmacological action ofFrontiers in pharmacology · 2023
    Review
  4. Article
  5. Article
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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

13 authors at 5 institutions in 1 country.

Li Wang *1Institute of Biophysics, Chinese Academy of Sciences, Beijing, 100101 China.
Xian Chen *3Key Laboratory of Physics and Technology for Advanced Batteries (Ministry of Education), Department of Physics, Jilin University, Changchun, 130012 China.
Xuzhen Guo *1Institute of Biophysics, Chinese Academy of Sciences, Beijing, 100101 China.
Jiasong Li1Institute of Biophysics, Chinese Academy of Sciences, Beijing, 100101 China.
Qi Liu1Institute of Biophysics, Chinese Academy of Sciences, Beijing, 100101 China.
Fuying Kang1Institute of Biophysics, Chinese Academy of Sciences, Beijing, 100101 China.
Xudong Wang *1Institute of Biophysics, Chinese Academy of Sciences, Beijing, 100101 China.
Cheng Hu1Institute of Biophysics, Chinese Academy of Sciences, Beijing, 100101 China.
Haiping Liu1Institute of Biophysics, Chinese Academy of Sciences, Beijing, 100101 China.
Weimin Gong1Institute of Biophysics, Chinese Academy of Sciences, Beijing, 100101 China.
Wei Zhuang4State Key Laboratory of Structural Chemistry, Fujian Institute of Research on the Structure of Matter, Chinese Academy of Sciences, Fuzhou, 350002 China.
Xiaohong Liu1Institute of Biophysics, Chinese Academy of Sciences, Beijing, 100101 China.
Jiangyun Wang1Institute of Biophysics, Chinese Academy of Sciences, Beijing, 100101 China.
Chinese Academy of Sciences · CNInstitute of Biophysics · CNFujian Institute of Research on the Structure of Matter · CNJilin University · CNUniversity of Chinese Academy of Sciences · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

abstractFluorescent proteins (FPs) with emission wavelengths in the far-red and infrared regions of the spectrum provide powerful tools for deep-tissue and super-resolution imaging. The development of red-shifted FPs has evoked widespread interest and continuous engineering efforts. In this article, based on a computational design and genetic code expansion, we report a rational approach to significantly expand and red-shift the chromophore of green fluorescent protein (GFP). We applied computational calculations to predict the excitation and emission wavelengths of a FP chromophore harboring unnatural amino acids (UAA) and identify in silico an appropriate UAA, 2-amino-3-(6-hydroxynaphthalen-2-yl)propanoic acid (naphthol-Ala). Our methodology allowed us to formulate a GFP variant (cpsfGFP-66-Naphthol-Ala) with red-shifted absorbance and emission spectral maxima exceeding 60 and 130 nm, respectively, compared to those of GFP. The GFP chromophore is formed through autocatalytic post-translational modification to generate a planar 4-( GRAPHICAL ABSTRACT:

Indexed as

Computational designGreen fluorescent proteinRed-shiftUnnatural amino acids

Identifiers

PMID30533492
PMCPMC6245237
OpenAlexW2899777855

What OpenQuestion holds

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LicenceCC BY
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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.