Evidence map›Paper›PMID 27713486›Full record

ArticleScientific reports2016

The phasor-FLIM fingerprints reveal shifts from OXPHOS to enhanced glycolysis in Huntington Disease.

Sara Sameni, Adeela Syed, J Lawrence Marsh, Michelle A Digman

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
2.8field-weighted citation impact, top 10% 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

37 citing papers in PubMed, 57 citations in OpenAlex.

  1. Article
  2. Article
  3. Label-free metabolic imaging ofFrontiers in cellular and infection microbiology · 2025
    Article
  4. Phasor-FLIM and SHG imaging for quantitative analysis of lung cancer autofluorescence.Computational and structural biotechnology journal · 2025
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  13. Label-free spatially maintained measurements of metabolic phenotypes in cells.Frontiers in bioengineering and biotechnology · 2023
    Article
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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

4 authors at 2 institutions in 1 country.

Sara SameniLaboratory for Fluorescence Dynamics, UC Irvine, CA, USA.
Adeela SyedDepartment of Developmental and Cell Biology, UC Irvine, CA, USA.
J Lawrence MarshDepartment of Developmental and Cell Biology, UC Irvine, CA, USA.
Michelle A DigmanLaboratory for Fluorescence Dynamics, UC Irvine, CA, USA.
University of California, Irvine · USFluorescence Innovations (United States) · US

Funding

TRD4: Phasor analysisP41GM103540 · NIGMS · UNIVERSITY OF CALIFORNIA-IRVINE · PI GRATTON, ENRICO · 2012 to 2020
$12.5M
NIGMS NIH HHS P41 GM103540
6 · The paper itself

Abstract

Huntington disease (HD) is an autosomal neurodegenerative disorder caused by the expansion of Polyglutamine (polyQ) in exon 1 of the Huntingtin protein. Glutamine repeats below 36 are considered normal while repeats above 40 lead to HD. Impairment in energy metabolism is a common trend in Huntington pathogenesis; however, this effect is not fully understood. Here, we used the phasor approach and Fluorescence Lifetime Imaging Microscopy (FLIM) to measure changes between free and bound fractions of NADH as a indirect measure of metabolic alteration in living cells. Using Phasor-FLIM, pixel maps of metabolic alteration in HEK293 cell lines and in transgenic Drosophila expressing expanded and unexpanded polyQ HTT exon1 in the eye disc were developed. We found a significant shift towards increased free NADH, indicating an increased glycolytic state for cells and tissues expressing the expanded polyQ compared to unexpanded control. In the nucleus, a further lifetime shift occurs towards higher free NADH suggesting a possible synergism between metabolic dysfunction and transcriptional regulation. Our results indicate that metabolic dysfunction in HD shifts to increased glycolysis leading to oxidative stress and cell death. This powerful label free method can be used to screen native HD tissue samples and for potential drug screening.

Indexed as

GlycolysisAnimalsAnimals, Genetically ModifiedCell NucleusDrosophilaEyeGene Expression RegulationHEK293 CellsHumansHuntingtin ProteinHuntington DiseaseMicroscopy, FluorescenceNADOxidative StressPhosphorylationTrinucleotide Repeat ExpansionHTT protein, humanHuntingtin ProteinNAD

Identifiers

PMID27713486
PMCPMC5054433
OpenAlexW2529446065

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.