Evidence map›Paper›PMID 12496124›Full record

ArticleBiophysical journal2002

Picosecond-hetero-FRET microscopy to probe protein-protein interactions in live cells.

Marc Tramier, Isabelle Gautier, Tristan Piolot, Sylvie Ravalet, Klaus Kemnitz, Jacques Coppey, Christiane Durieux, Vincent Mignotte, Maïté Coppey-Moisan

Open access · bronzeAbstract readEvaluation Study
In one paragraph

Article in Biophysical journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
10.1field-weighted citation impact, top 2% 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

48 citing papers in PubMed, 131 citations in OpenAlex.

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  20. Fluorescence lifetime imaging microscopy of intracellular glucose dynamics.Journal of diabetes science and technology · 2012
    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

9 authors at 4 institutions in 2 countries.

Marc TramierInstitut Jacques Monod, UMR 7592, CNRS, Universités P6/P7, 2 place Jussieu, 75251 Paris Cedex 05, France.
Isabelle Gautier
Tristan Piolot
Sylvie Ravalet
Klaus Kemnitz
Jacques Coppey
Christiane Durieux
Vincent Mignotte
Maïté Coppey-Moisan
Centre National de la Recherche Scientifique · FREuroPhoton (Germany) · DEInstitut Jacques Monod · FRMaternité Port Royal · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

By using a novel time- and space-correlated single-photon counting detector, we show that fluorescence resonance energy transfer (FRET) between cyan fluorescent protein (CFP) and yellow fluorescent protein (YFP) fused to herpes simplex virus thymidine kinase (TK) monomers can be used to reveal homodimerization of TK in the nucleus and cytoplasm of live cells. However, the quantification of energy transfer was limited by the intrinsic biexponential fluorescence decay of the donor CFP (lifetimes of 1.3 +/- 0.2 ns and 3.8 +/- 0.4 ns) and by the possibility of homodimer formation between two TK-CFP. In contrast, the heterodimerization of the transcriptional factor NF-E2 in the nucleus of live cells was quantified from the analysis of the fluorescence decays of GFP in terms of 1) FRET efficiency between GFP and DsRed chromophores fused to p45 and MafG, respectively, the two subunits of NF-E2 (which corresponds to an interchromophoric distance of 39 +/- 1 A); and 2) fractions of GFP-p45 bound to DsRed-MafG (constant in the nucleus, varying in the range of 20% to 70% from cell to cell). The picosecond resolution of the fluorescence kinetics allowed us to discriminate between very short lifetimes of immature green species of DsRed-MafG and that of GFP-p45 involved in FRET with DsRed-MafG.

Indexed as

AnimalsBacterial ProteinsChlorocebus aethiopsDNA-Binding ProteinsErythroid-Specific DNA-Binding FactorsFluorescence Resonance Energy TransferGreen Fluorescent ProteinsHeLa CellsHerpesvirus 1, HumanHumansLuminescent ProteinsMacromolecular SubstancesNF-E2 Transcription FactorNF-E2 Transcription Factor, p45 SubunitProteinsRecombinant Fusion ProteinsBacterial ProteinsDNA-Binding ProteinsErythroid-Specific DNA-Binding Factorsfluorescent protein 583Green Fluorescent ProteinsLuminescent ProteinsMacromolecular SubstancesNFE2 protein, humanNF-E2 Transcription FactorNF-E2 Transcription Factor, p45 SubunitProteinsRecombinant Fusion ProteinsThymidine KinaseTranscription Factorsyellow fluorescent protein, Bacteria

Identifiers

PMID12496124
PMCPMC1302432
OpenAlexW2033052788

What OpenQuestion holds

Textmetadata
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.