Evidence map›Paper›PMID 20096786›Full record

ReviewMethods (San Diego, Calif.)2010

The design of Förster (fluorescence) resonance energy transfer (FRET)-based molecular sensors for Ran GTPase.

Petr Kaláb, Jon Soderholm

Open access · greenAbstract readReview
In one paragraph

Review in Methods (San Diego, Calif.), 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.8field-weighted citation impact, top 16% 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

16 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
  2. Review
  3. Using FLIM-FRET for Characterizing Spatial Interactions in the Spindle.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  4. eLife · 2020
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. How cells process information: quantification of spatiotemporal signaling dynamics.Protein science : a publication of the Protein Society · 2012
    Review
  13. Article
  14. How kinesin-2 forms a stalk.Molecular biology of the cell · 2011
    Article
  15. Article
  16. 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 at 2 institutions in 2 countries.

Petr KalábNational Cancer Institute, NIH, Bethesda, MD 20892-4256, USA. kalab@mail.nih.gov
Jon Soderholm
National Institutes of Health · USYonsei University · KR

Funding

Cellular functions of Ran GTPaseZIABC011084 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI KALAB, PETR · 2009 to 2016
$4.3M
Studying the Role of Ran in MitosisR01GM065232 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI HEALD, REBECCA W, WEIS, KARSTEN · 2003 to 2011
$2.4M
Intramural NIH HHS ZIA BC011084NIGMS NIH HHS R01GM065232
6 · The paper itself

Abstract

The application of FRET-based molecular biosensors provided confirmation of the central model of Ran GTPase function and led to important new insights into its physiological role. In many fields of cell biology, methods employing FRET are a standard approach that is becoming increasingly accessible due to advances in instrumentation and available fluorophores. However, the optimal design of a FRET sensor remains to be the cornerstone of any successful FRET application. Utilizing the recent literature on FRET applications and our studies on Ran, we outline the basic considerations involved in designing molecular FRET sensors. We point to several broadly applicable principles that were used in many different FRET sensors that can detect a wide range of molecular events. Using the FRET sensors for Ran that we created as examples, we then focus on the practical aspects of FRET assays. We describe the preparation of a bipartite FRET sensor consisting of ECFP-Ran and EYFP-importin beta and its validation as a reporter for FRET-based high throughput screening in small molecule libraries. Finally, we review the design and optimization of monomolecular FRET sensors that monitor the RanGTP-RanBP1 interaction, and of sensors detecting the RanGTP-regulated importin beta cargo release.

Indexed as

AnimalsBiosensing TechniquesFluorescence Resonance Energy TransferHumansNuclear ProteinsNuclear Proteinsran-binding protein 1

Identifiers

PMID20096786
PMCPMC2884063
OpenAlexW2033468005

What OpenQuestion holds

Textmetadata
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.