Evidence map›Paper›PMID 29055415›Full record

ArticleThe Journal of investigative dermatology2017

Research Techniques Made Simple: Methodology and Applications of Förster Resonance Energy Transfer (FRET) Microscopy.

Joshua A Broussard, Kathleen J Green

Abstract read
In one paragraph

Article in The Journal of investigative dermatology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing 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

15 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Review
  6. Fluorescence-Based Protein Stability Monitoring-A Review.International journal of molecular sciences · 2024
    Review
  7. Advanced Microscopy Techniques for Molecular Biophysics.International journal of molecular sciences · 2023
    Review
  8. Review
  9. Article
  10. Synthetic Strategies for FRET-Enabled Carbohydrate Active Enzyme Probes.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  11. Fluorescent Indicators For Biological Imaging of Monatomic Ions.Frontiers in cell and developmental biology · 2022
    Review
  12. Review
  13. Article
  14. Homologous Recombination under the Single-Molecule Fluorescence Microscope.International journal of molecular sciences · 2019
    Review
  15. FRET Microscopy in Yeast.Biosensors · 2019
    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

2 authors.

Joshua A BroussardDepartment of Pathology, Northwestern University, Feinberg School of Medicine, Chicago, Illinois, USA; Department of Dermatology, Northwestern University, Feinberg School of Medicine, Chicago, Illinois, USA.
Kathleen J GreenDepartment of Pathology, Northwestern University, Feinberg School of Medicine, Chicago, Illinois, USA; Department of Dermatology, Northwestern University, Feinberg School of Medicine, Chicago, Illinois, USA. Electronic address: kgreen@northwestern.edu.

Funding

MOLECULAR GENETICS OF PEMPHIGUS FOLIACEUS ANTIGENR01AR041836 · NIAMS · NORTHWESTERN UNIVERSITY AT CHICAGO · PI Kathleen Janee Green · 1993 to 2026
$11.8M
Desmoplakin Assembly and Function in EpidermisR37AR043380 · NIAMS · NORTHWESTERN UNIVERSITY AT CHICAGO · PI GREEN, KATHLEEN JANEE · 2011 to 2020
$4.6M
Regulation of Desmosomal Cadherins in Oral CancerR01CA122151 · NCI · NORTHWESTERN UNIVERSITY AT CHICAGO · PI GREEN, KATHLEEN JANEE · 2006 to 2016
$2.6M
POST GRADUATE PROGRAM IN CUTANEOUS BIOLOGYT32AR007593 · NIAMS · NORTHWESTERN UNIVERSITY · PI GREEN, KATHLEEN JANEE · 1995 to 2004
$694k
NCI NIH HHS R01 CA122151NIAMS NIH HHS R01 AR041836NIAMS NIH HHS R37 AR043380NIAMS NIH HHS T32 AR007593
6 · The paper itself

Abstract

Classical biochemical techniques have contributed a great deal to our understanding of the mechanisms regulating fundamental biological processes. However, these approaches are typically end-point, population-based assays and are often insufficient in examining transient molecular events. Förster resonance energy transfer (FRET) microscopy is a powerful technique capable of investigating dynamic interactions between proteins and a plethora of biochemical signaling events based on the development of specific biosensors. This technique exploits the principle that when FRET occurs, energy from a donor fluorophore is transferred to an acceptor fluorophore only when certain conditions are met. These include dependence on both distance and fluorophore orientation. In this article, applications of FRET microscopy to protein interactions and modifications are discussed, and examples are given of the types of biosensors that can be developed. There are a number of methods to measure FRET. The most common modalities and specific advantages and shortcomings for each are reviewed. Finally, general considerations and guidelines for choosing a method are discussed.

Indexed as

Research DesignFluorescence Resonance Energy TransferHumansMicroscopyProteinsSensitivity and SpecificityProteins

Identifiers

PMID29055415
PMCPMC5800528

What OpenQuestion holds

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LicenceTDM
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.