Evidence map›Paper›PMID 22973448›Full record

ArticlePloS one2012

Homodimerization of amyloid precursor protein at the plasma membrane: a homoFRET study by time-resolved fluorescence anisotropy imaging.

Viviane Devauges, Catherine Marquer, Sandrine Lécart, Jack-Christophe Cossec, Marie-Claude Potier, Emmanuel Fort, Klaus Suhling, Sandrine Lévêque-Fort

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
4.7field-weighted citation impact, top 5% 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

24 citing papers in PubMed, 44 citations in OpenAlex.

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  14. A Guide to Fluorescent Protein FRET Pairs.Sensors (Basel, Switzerland) · 2016
    Review
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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

8 authors at 5 institutions in 2 countries.

Viviane DevaugesInstitut des Sciences Moléculaires d'Orsay, CNRS UMR 8214, Univ. Paris Sud, Orsay, France.
Catherine Marquer
Sandrine Lécart
Jack-Christophe Cossec
Marie-Claude Potier
Emmanuel Fort
Klaus Suhling
Sandrine Lévêque-Fort
Inserm · FRInstitut des Sciences Moléculaires d'Orsay · FRKing's College London · GBSorbonne Université · FRUniversité Paris Cité · FR

Funding

Biotechnology and Biological Sciences Research Council BB/D011086/1
6 · The paper itself

Abstract

Classical FRET (Förster Resonance Energy Transfer) using two fluorescent labels (one for the donor and another one for the acceptor) is not efficient for studying the homodimerization of a protein as only half of the homodimers formed can be identified by this technique. We thus resorted to homoFRET detected by time-resolved Fluorescence Anisotropy IMaging (tr-FAIM). To specifically image the plasma membrane of living cells, an original combination of tr-FAIM and Total Internal Reflection Fluorescence Lifetime Imaging Microscope (TIRFLIM) was implemented. The correcting factor accounting for the depolarization due to the high numerical aperture (NA) objective, mandatory for TIRF microscopy, was quantified on fluorescein solutions and on HEK293 cells expressing enhanced Green Fluorescence Protein (eGFP). Homodimerization of Amyloid Precursor Protein (APP), a key mechanism in the etiology of Alzheimer's disease, was measured on this original set-up. We showed, both in epifluorescence and under TIRF excitation, different energy transfer rates associated with the homodimerization of wild type APP-eGFP or of a mutated APP-eGFP, which forms constitutive dimers. This original set-up thus offers promising prospects for future studies of protein homodimerization in living cells in control and pathological conditions.

Indexed as

Amyloid beta-Protein PrecursorCell MembraneDimerizationFluorescence PolarizationFluoroimmunoassayGreen Fluorescent ProteinsHEK293 CellsHumansSpectrometry, FluorescenceAmyloid beta-Protein Precursorenhanced green fluorescent proteinGreen Fluorescent Proteins

Identifiers

PMID22973448
PMCPMC3433432
OpenAlexW2013745373

What OpenQuestion holds

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LicenceCC BY
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.