Evidence map›Paper›PMID 28530831›Full record

ArticleThe journal of physical chemistry letters2017

Blue-Shifted Green Fluorescent Protein Homologues Are Brighter than Enhanced Green Fluorescent Protein under Two-Photon Excitation.

Rosana S Molina, Tam M Tran, Robert E Campbell, Gerard G Lambert, Anya Salih, Nathan C Shaner, Thomas E Hughes, Mikhail Drobizhev

Open access · bronzeAbstract read
In one paragraph

Article in The journal of physical chemistry letters, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
4.6field-weighted citation impact, top 6% 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

23 citing papers in PubMed, 52 citations in OpenAlex.

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  6. A blue-shifted genetically encoded CabioRxiv : the preprint server for biology · 2023
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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

8 authors at 4 institutions in 3 countries.

Rosana S MolinaDepartment of Cell Biology & Neuroscience, Montana State University , Bozeman, Montana 59717, United States.ORCID http://orcid.org/0000-0001-7891-2462
Tam M TranDepartment of Chemistry, University of Alberta , Edmonton, Alberta T6G 2R3, Canada.
Robert E CampbellDepartment of Chemistry, University of Alberta , Edmonton, Alberta T6G 2R3, Canada.
Gerard G LambertScintillon Institute , San Diego, California 92121, United States.
Anya SalihWestern Sydney University , Penrith South DC, New South Wales 1797, Australia.
Nathan C ShanerScintillon Institute , San Diego, California 92121, United States.
Thomas E HughesDepartment of Cell Biology & Neuroscience, Montana State University , Bozeman, Montana 59717, United States.ORCID http://orcid.org/0000-0001-5880-9951
Mikhail DrobizhevDepartment of Cell Biology & Neuroscience, Montana State University , Bozeman, Montana 59717, United States.
Montana State University · USScintillon Institute · USUniversity of Alberta · CAWestern Sydney University · AU

Funding

Northern Lights collaboration for better 2-photon probesU01NS094246 · NINDS · MONTANA STATE UNIVERSITY - BOZEMAN · PI CAMPBELL, ROBERT E., DROBIZHEV, MIKHAIL · 2015 to 2017
$2.0M
Fluorescent proteins for superresolution imagingR01GM109984 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI SHANER, NATHAN CHRISTOPHER · 2014 to 2018
$1.8M
Probes for Luminescence-based Superresolution MicroscopyR01GM121944 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI SHANER, NATHAN CHRISTOPHER · 2017 to 2020
$1.3M
NIGMS NIH HHS R01 GM109984NIGMS NIH HHS R01 GM121944NINDS NIH HHS U01 NS094246
6 · The paper itself

Abstract

Fluorescent proteins (FPs) are indispensable markers for two-photon imaging of live tissue, especially in the brains of small model organisms. The quantity of physiologically relevant data collected, however, is limited by heat-induced damage of the tissue due to the high intensities of the excitation laser. We seek to minimize this damage by developing FPs with improved brightness. Among FPs with the same chromophore structure, the spectral properties can vary widely due to differences in the local protein environment. Using a physical model that describes the spectra of FPs containing the anionic green FP (GFP) chromophore, we predict that those that are blue-shifted in one-photon absorption will have stronger peak two-photon absorption cross sections. Following this prediction, we present 12 blue-shifted GFP homologues and demonstrate that they are up to 2.5 times brighter than the commonly used enhanced GFP (EGFP).

Indexed as

Hot TemperatureSpectrometry, FluorescenceColorFluorescent DyesGreen Fluorescent ProteinsLuminescent ProteinsModels, MolecularPhotonsenhanced green fluorescent proteinFluorescent DyesGreen Fluorescent ProteinsLuminescent Proteins

Identifiers

PMID28530831
PMCPMC5474692
OpenAlexW2619170026

What OpenQuestion holds

Textmetadata
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.