Evidence map›Paper›PMID 26246319›Full record

ArticleScientific reports2015

Ultrafast excited-state dynamics and fluorescence deactivation of near-infrared fluorescent proteins engineered from bacteriophytochromes.

Jingyi Zhu, Daria M Shcherbakova, Yusaku Hontani, Vladislav V Verkhusha, John T M Kennis

Abstract read
In one paragraph

Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing 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

11 citing papers in PubMed.

  1. Article
  2. Article
  3. Protein-chromophore interactions controlling photoisomerization in red/green cyanobacteriochromes.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2022
    Article
  4. Article
  5. Choosing Fluorescent Probes and Labeling Systems.Methods in molecular biology (Clifton, N.J.) · 2021
    Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
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.

Jingyi ZhuBiophysics Section, Department of Physics and Astronomy, Faculty of Sciences, VU University, De Boelelaan 1081, 1081 HV, Amsterdam, The Netherlands.
Daria M ShcherbakovaDepartment of Anatomy and Structural Biology, Albert Einstein College of Medicine Bronx, Bronx, New York 10461, USA.
Yusaku HontaniBiophysics Section, Department of Physics and Astronomy, Faculty of Sciences, VU University, De Boelelaan 1081, 1081 HV, Amsterdam, The Netherlands.
Vladislav V Verkhusha1] Department of Anatomy and Structural Biology, Albert Einstein College of Medicine Bronx, Bronx, New York 10461, USA [2] Department of Biochemistry and Developmental Biology, Faculty of Medicine, University of Helsinki, Helsinki 00290, Finland.
John T M KennisBiophysics Section, Department of Physics and Astronomy, Faculty of Sciences, VU University, De Boelelaan 1081, 1081 HV, Amsterdam, The Netherlands.

Funding

In Vivo Multiphoton Based Imaging of Complex Cancer Cell BehaviorR01CA164468 · NCI · ALBERT EINSTEIN COLLEGE OF MEDICINE, INC · PI VERKHUSHA, VLADISLAV · 2011 to 2015
$3.8M
Molecular Fluorescent ToolkitR01GM073913 · NIGMS · ALBERT EINSTEIN COLLEGE OF MEDICINE, INC · PI VERKHUSHA, VLADISLAV · 2006 to 2014
$2.4M
Engineering bacterial phytochromes for near-infrared imaging in mammalsR01GM108579 · NIGMS · ALBERT EINSTEIN COLLEGE OF MEDICINE, INC · PI VERKHUSHA, VLADISLAV · 2014 to 2017
$1.3M
NCI NIH HHS CA164468NCI NIH HHS R01 CA164468NIGMS NIH HHS GM073913NIGMS NIH HHS GM108579NIGMS NIH HHS R01 GM073913NIGMS NIH HHS R01 GM108579
6 · The paper itself

Abstract

Near-infrared fluorescent proteins, iRFPs, are recently developed genetically encoded fluorescent probes for deep-tissue in vivo imaging. Their functions depend on the corresponding fluorescence efficiencies and electronic excited state properties. Here we report the electronic excited state deactivation dynamics of the most red-shifted iRFPs: iRFP702, iRFP713 and iRFP720. Complementary measurements by ultrafast broadband fluorescence and absorption spectroscopy show that single exponential decays of the excited state with 600~700 ps dominate in all three iRFPs, while photoinduced isomerization was completely inhibited. Significant kinetic isotope effects (KIE) were observed with a factor of ~1.8 in D2O, and are interpreted in terms of an excited-state proton transfer (ESPT) process that deactivates the excited state in competition with fluorescence and chromophore mobility. On this basis, new approaches for rational molecular engineering may be applied to iRFPs to improve their fluorescence.

Indexed as

Bacterial ProteinsLuminescent ProteinsSpectrometry, FluorescenceBacterial ProteinsLuminescent Proteins

Identifiers

PMID26246319
PMCPMC4526943

What OpenQuestion holds

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LicenceCC BY
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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.