Evidence map›Paper›PMID 19895111›Full record

ArticleJournal of biomedical optics

Characterization of an orange acceptor fluorescent protein for sensitized spectral fluorescence resonance energy transfer microscopy using a white-light laser.

Yuansheng Sun, Cynthia F Booker, Sangeeta Kumari, Richard N Day, Mike Davidson, Ammasi Periasamy

Abstract readEvaluation Study
In one paragraph

Article in Journal of biomedical optics. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing 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

20 citing papers in PubMed.

  1. Article
  2. Article
  3. MultiplexedContrast media & molecular imaging · 2020
    Article
  4. Cyclic-di-GMP regulation promotes survival of a slow-replicating subpopulation of intracellularProceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Hypoxia-induced changes in protein s-nitrosylation in female mouse brainstem.American journal of respiratory cell and molecular biology · 2015
    Article
  10. Article
  11. Article
  12. Förster resonance energy transfer microscopy and spectroscopy for localizing protein-protein interactions in living cells.Cytometry. Part A : the journal of the International Society for Analytical Cytology · 2013
    Review
  13. Review
  14. Article
  15. Red fluorescent proteins: advanced imaging applications and future design.Angewandte Chemie (International ed. in English) · 2012
    Review
  16. Fluorescent proteins for FRET microscopy: monitoring protein interactions in living cells.BioEssays : news and reviews in molecular, cellular and developmental biology · 2012
    Review
  17. Article
  18. Article
  19. Article
  20. FRET microscopy in 2010: the legacy of Theodor Förster on the 100th anniversary of his birth.Chemphyschem : a European journal of chemical physics and physical chemistry · 2011
    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

6 authors.

Yuansheng SunUniversity of Virginia, Department of Biology, W. M. Keck Center for Cellular Imaging, McCormick Road, Charlottesville, Virginia 22904, USA.
Cynthia F Booker
Sangeeta Kumari
Richard N Day
Mike Davidson
Ammasi Periasamy

Funding

Tunable White Light Laser Confocal/Spectral Imaging MicroscopyS10RR025616 · NCRR · UNIVERSITY OF VIRGINIA · PI PERIASAMY, AMMASI · 2009 to 2009
$500k
NCRR NIH HHS RR025616NCRR NIH HHS S10 RR025616
6 · The paper itself

Abstract

Orange fluorescent proteins (FPs) are attractive candidates as Forster resonance energy transfer (FRET) partners, bridging the gap between green and red/far-red FPs, but they pose significant challenges using common fixed laser wavelengths. We investigated monomeric Kusabira orange 2 (mKO2) FP as a FRET acceptor for monomeric teal FP (mTFP) as donor on a FRET standard construct using a fixed-distance amino acid linker, expressed in live cells. We quantified the apparent FRET efficiency (E%) of this construct, using sensitized spectral FRET microscopy on the Leica TCS SP5 X imaging system equipped with a white-light laser that allows choosing any excitation wavelength from 470 to 670 nm in 1-nm increments. The E% obtained in sensitized spectral FRET microscopy was then confirmed with fluorescence lifetime measurements. Our results demonstrate that mKO2 and mTFP are good FRET partners given proper imaging setups. mTFP was optimally excited by the Argon 458 laser line, and the 540-nm wavelength excitation for mKO2 was chosen from the white-light laser. The white-light laser generally extends the usage of orange and red/far-red FPs in sensitized FRET microscopy assays by tailoring excitation and emission precisely to the needs of the FRET pair.

Indexed as

LasersAnimalsCell LineEquipment DesignEquipment Failure AnalysisFluorescence Resonance Energy TransferLuminescent ProteinsMiceMicroscopy, FluorescencePituitary GlandRed Fluorescent ProteinReproducibility of ResultsSensitivity and SpecificityLuminescent ProteinsRed Fluorescent Protein

Identifiers

PMID19895111
PMCPMC2774974

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.