Evidence map›Paper›PMID 22396229›Full record

ReviewBioEssays : news and reviews in molecular, cellular and developmental biology2012

Fluorescent proteins for FRET microscopy: monitoring protein interactions in living cells.

Richard N Day, Michael W Davidson

Erratum issuedAbstract readReview
In one paragraph

Review in BioEssays : news and reviews in molecular, cellular and developmental biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 55 papers.

0numbers the graph read from it
0cells of the map it votes in
55citing 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

55 citing papers in PubMed.

  1. Review
  2. Macromolecular High-Affinity Binding Probed by Advanced Fluorescence Techniques.Chembiochem : a European journal of chemical biology · 2025
    Review
  3. Article
  4. Review
  5. Article
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  11. Article
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4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

2 authors.

Richard N DayDepartment of Cellular and Integrative Physiology, Indiana University School of Medicine, Indianapolis, IN, USA. rnday@iupui.edu
Michael W Davidson

Funding

PROBE DELIVERY COREP30DK079312 · NIDDK · INDIANA UNIV-PURDUE UNIV AT INDIANAPOLIS · PI DUNN, KENNETH W · 2007 to 2021
$17.1M
SPECIFIC REPRESSION OF PROLACTIN GENE EXPRESSIONR01DK043701 · NIDDK · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI DAY, RICHARD N · 1994 to 2012
$3.4M
NIDDK NIH HHS 2R01DK43701NIDDK NIH HHS P30 DK079312NIDDK NIH HHS R01 DK043701
6 · The paper itself

Abstract

The discovery and engineering of novel fluorescent proteins (FPs) from diverse organisms is yielding fluorophores with exceptional characteristics for live-cell imaging. In particular, the development of FPs for fluorescence (or Förster) resonance energy transfer (FRET) microscopy is providing important tools for monitoring dynamic protein interactions inside living cells. The increased interest in FRET microscopy has driven the development of many different methods to measure FRET. However, the interpretation of FRET measurements is complicated by several factors including the high fluorescence background, the potential for photoconversion artifacts and the relatively low dynamic range afforded by this technique. Here, we describe the advantages and disadvantages of four methods commonly used in FRET microscopy. We then discuss the selection of FPs for the different FRET methods, identifying the most useful FP candidates for FRET microscopy. The recent success in expanding the FP color palette offers the opportunity to explore new FRET pairs.

Indexed as

Fluorescent DyesGreen Fluorescent ProteinsBiosensing TechniquesFluorescence Resonance Energy TransferMicroscopy, FluorescenceMolecular ImagingPhotobleachingFluorescent DyesGreen Fluorescent Proteins

Identifiers

PMID22396229
PMCPMC3517158

What OpenQuestion holds

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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.