Evidence map›Paper›PMID 23813736›Full record

ReviewCytometry. Part A : the journal of the International Society for Analytical Cytology2013

Förster resonance energy transfer microscopy and spectroscopy for localizing protein-protein interactions in living cells.

Yuansheng Sun, Christina Rombola, Vinod Jyothikumar, Ammasi Periasamy

Abstract readReview
In one paragraph

Review in Cytometry. Part A : the journal of the International Society for Analytical Cytology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing 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

44 citing papers in PubMed.

  1. Novel ErScientific reports · 2026
    Article
  2. Review
  3. Article
  4. Review
  5. Review
  6. Article
  7. Article
  8. An integrated structural model of the DNA damage-responsive H3K4me3 binding WDR76:SPIN1 complex with the nucleosome.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. bioRxiv : the preprint server for biology · 2023
    Article
  16. Article
  17. Review
  18. Mitochondria-localized AMPK responds to local energetics and contributes to exercise and energetic stress-induced mitophagy.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  19. Review
  20. 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

4 authors.

Yuansheng SunThe W.M. Keck Center for Cellular Imaging (KCCI), Department of Biology, Physical and Life Sciences Building, University of Virginia, Charlottesville, Virginia.
Christina Rombola
Vinod Jyothikumar
Ammasi Periasamy

Funding

S-nitrosothiol signaling in pulmonary epithelial cellsP01HL101871 · NHLBI · UNIVERSITY OF VIRGINIA · PI GASTON, BENJAMIN, LEWIS, STEPHEN JOHN · 2011 to 2015
$8.7M
Airway redox biochemistry as a deteriminant of asthma phenotype during adolescen*U10HL109250 · NHLBI · UNIVERSITY OF VIRGINIA · PI ERZURUM, SERPIL C., GASTON, BENJAMIN · 2011 to 2016
$4.2M
Zeiss 780 NLO High Sensitivity Multiphoton Microscopy SystemS10OD016446 · OD · UNIVERSITY OF VIRGINIA · PI PERIASAMY, AMMASI · 2013 to 2013
$600k
Frequency-domain Fluorescence Lifetime Imaging Microscopy (FD-FLIM)S10RR027409 · NCRR · UNIVERSITY OF VIRGINIA · PI PERIASAMY, AMMASI · 2010 to 2010
$347k
NCRR NIH HHS S10 RR027409NHLBI NIH HHS P01 HL101871NHLBI NIH HHS P01HL101871NHLBI NIH HHS U10 HL109250NIH HHS S10 OD016446
6 · The paper itself

Abstract

The fundamental theory of Förster resonance energy transfer (FRET) was established in the 1940s. Its great power was only realized in the past 20 years after different techniques were developed and applied to biological experiments. This success was made possible by the availability of suitable fluorescent probes, advanced optics, detectors, microscopy instrumentation, and analytical tools. Combined with state-of-the-art microscopy and spectroscopy, FRET imaging allows scientists to study a variety of phenomena that produce changes in molecular proximity, thereby leading to many significant findings in the life sciences. In this review, we outline various FRET imaging techniques and their strengths and limitations; we also provide a biological model to demonstrate how to investigate protein-protein interactions in living cells using both intensity- and fluorescence lifetime-based FRET microscopy methods.

Indexed as

FluorescenceFluorescence Resonance Energy TransferFluorescent DyesMicroscopy, FluorescenceProtein Interaction MappingProteinsSingle-Cell AnalysisFluorescent DyesProteinsFLIMFLIM-FRETFRETprotein-protein interactions

Identifiers

PMID23813736
PMCPMC3924896

What OpenQuestion holds

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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.