Evidence map›Paper›PMID 20682277›Full record

ArticleBiophysical journal2010

Brightness analysis by Z-scan fluorescence fluctuation spectroscopy for the study of protein interactions within living cells.

Patrick J Macdonald, Yun Chen, Xiao Wang, Yan Chen, Joachim D Mueller

Abstract read
In one paragraph

Article in Biophysical journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing 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

30 citing papers in PubMed.

  1. Analysis of Arc/Arg3.1 Oligomerization In Vitro and in Living Cells.International journal of molecular sciences · 2024
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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

5 authors.

Patrick J MacdonaldSchool of Physics and Astronomy, University of Minnesota, Minneapolis, Minnesota, USA.
Yun Chen
Xiao Wang
Yan Chen
Joachim D Mueller

Funding

In vivo Fluorescence Fluctuation Spectroscopy - Administrative SupplementR01GM064589 · NIGMS · UNIVERSITY OF MINNESOTA TWIN CITIES · PI MUELLER, JOACHIM D · 2002 to 2019
$4.6M
NIGMS NIH HHS GM64589NIGMS NIH HHS R01 GM064589
6 · The paper itself

Abstract

Fluorescence fluctuation spectroscopy (FFS) quantifies interactions of fluorescently labeled proteins inside living cells by brightness analysis. Conventional FFS implicitly requires that the sample thickness exceeds the size of the observation volume. This condition is not always fulfilled when measuring cells. Cytoplasmic sections, especially, can be thinner than the axial size of the observation volume. The finite sample thickness introduces a brightness bias which, if not recognized, leads to an erroneous interpretation of the data. To avoid this artifact, we introduce z-scan FFS which consists of a fluorescence intensity z scan through the sample followed by an FFS measurement. To model the experimental z-scan data, a new PSF model had to be introduced. We use the intensity z scan together with the PSF model to determine the geometry of the sample and then extract the brightness from the FFS data. Cells expressing EGFP serve as a model system for testing the experimental approach. We demonstrate that z-scan FFS abolishes the brightness artifact and use the method to determine the oligomerization of cytoplasmic nuclear transport factor 2.

Indexed as

AnimalsCell SurvivalChlorocebus aethiopsCOS CellsGreen Fluorescent ProteinsHumansModels, BiologicalNucleocytoplasmic Transport ProteinsPregnancy ProteinsProtein BindingSpectrometry, Fluorescenceenhanced green fluorescent proteinGreen Fluorescent ProteinsNucleocytoplasmic Transport ProteinsNUTF2 protein, humanPregnancy Proteins

Identifiers

PMID20682277
PMCPMC2913191

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.