Evidence map›Paper›PMID 22366230›Full record

ArticleMethods (San Diego, Calif.)2012

Fluorogen activating proteins in flow cytometry for the study of surface molecules and receptors.

Matthew J Saunders, Christopher Szent-Gyorgyi, Gregory W Fisher, Jonathan W Jarvik, Marcel P Bruchez, Alan S Waggoner

Open access · greenAbstract read
In one paragraph

Article in Methods (San Diego, Calif.), 2012. 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
1.2field-weighted citation impact, top 22% of its field
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, 20 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. γ2 GABAFrontiers in cellular neuroscience · 2018
    Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Localization microscopy using noncovalent fluorogen activation by genetically encoded fluorogen-activating proteins.Chemphyschem : a European journal of chemical physics and physical chemistry · 2014
    Article
  14. Article
  15. 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

6 authors at 2 institutions in 1 country.

Matthew J SaundersMolecular Biosensor and Imaging Center, Carnegie Mellon University, 4400 Fifth Ave., Pittsburgh, PA 15213, USA. matsaun@andrew.cmu.edu
Christopher Szent-Gyorgyi
Gregory W Fisher
Jonathan W Jarvik
Marcel P Bruchez
Alan S Waggoner
Carnegie Mellon University · USImaging Center · US

Funding

FLUORESCENT PROBES &IMAGING FOR NETWORKS &PATHWAY(RMI)U54RR022241 · NCRR · MELLON PITTS CORPORATION (MPC CORP) · PI WAGGONER, ALAN S. · 2005 to 2011
$19.9M
Fluorescent Biosensors for Networks and PathwaysU54GM103529 · NIGMS · CARNEGIE-MELLON UNIVERSITY · PI WAGGONER, ALAN S. · 2012 to 2013
$6.3M
Bright Blinking Probes for Fast Multicolor Superresolution Imaging in Live CellsR01GM086237 · NIGMS · CARNEGIE-MELLON UNIVERSITY · PI BRUCHEZ, MARCEL P · 2009 to 2010
$347k
NCRR NIH HHS U54 RR022241NCRR NIH HHS U54RR022241NIGMS NIH HHS R01 1R01GM086237NIGMS NIH HHS R01 GM086237NIGMS NIH HHS U54 GM103529
6 · The paper itself

Abstract

The use of fluorescent proteins, particularly when genetically fused to proteins of biological interest, have greatly advanced many flow cytometry research applications. However, there remains a major limitation to this methodology in that only total cellular fluorescence is measured. Commonly used fluorescent proteins (e.g., EGFP and its variants) are fluorescent whether the fusion protein exists on the surface or in sub-cellular compartments. A flow cytometer cannot distinguish between these separate sources of fluorescence. This can be of great concern when using flow cytometry, plate readers or microscopy to quantify cell surface receptors or other surface proteins genetically fused to fluorescent proteins. Recently developed fluorogen activating proteins (FAPs) solve many of these issues by allowing the selective visualization of only those cell surface proteins that are exposed to the extracellular milieu. FAPs are GFP-sized single chain antibodies that specifically bind to and generate fluorescence from otherwise non-fluorescent dyes ('activate the fluorogen'). Like the fluorescent proteins, FAPs can be genetically fused to proteins of interest. When exogenously added fluorogens bind FAPs, fluorescence immediately increases by as much as 20,000-fold, rendering the FAP fusion proteins highly fluorescent. Moreover, since fluorogens can be made membrane impermeant, fluorescence can be limited to only those receptors expressed on the cell surface. Using cells expressing beta-2 adrenergic receptor (β2AR) fused at its N-terminus to a FAP, flow cytometry based receptor internalization assays have been developed and characterized. The fluorogen/FAP system is ideally suited to the study of cell surface proteins by fluorescence and avoids drawbacks of using receptor/fluorescent protein fusions, such as internal accumulation. We also briefly comment on extending FAP-based technologies to the study of events occurring inside of the cell as well.

Indexed as

Adrenergic beta-2 Receptor AntagonistsAdrenergic beta-AgonistsAnimalsBiological AssayCell LineCell MembraneFlow CytometryFluorescenceFluorescent DyesGreen Fluorescent ProteinsHumansIsoproterenolKineticsMicePropranololProtein BindingAdrenergic beta-2 Receptor AntagonistsAdrenergic beta-AgonistsFluorescent DyesGreen Fluorescent ProteinsIsoproterenolPropranololReceptors, Adrenergic, beta-2Recombinant Fusion ProteinsSingle-Chain Antibodies

Identifiers

PMID22366230
PMCPMC3432715
OpenAlexW2074211893

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.