Evidence map›Paper›PMID 34458690›Full record

ArticleOSA continuum2021

Characterization of NADH fluorescence properties under one-photon excitation with respect to temperature, pH, and binding to lactate dehydrogenase.

Taylor M Cannon, Joao L Lagarto, Benjamin T Dyer, Edwin Garcia, Douglas J Kelly, Nicholas S Peters, Alexander R Lyon, Paul M W French, Chris Dunsby

Open access · goldAbstract read
In one paragraph

Article in OSA continuum, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
6.0field-weighted citation impact, top 4% 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

25 citing papers in PubMed, 43 citations in OpenAlex.

  1. Article
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  9. What Can Fluorescence Tell Us About Wine?International journal of molecular sciences · 2025
    Review
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  20. A short guide on blue fluorescent proteins: limits and perspectives.Applied microbiology and biotechnology · 2024
    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

9 authors at 2 institutions in 2 countries.

Taylor M CannonDepartment of Physics, Imperial College London, London, SW7 2AZ, UK.
Joao L LagartoDepartment of Physics, Imperial College London, London, SW7 2AZ, UK.ORCID https://orcid.org/0000-0001-9396-8923
Benjamin T DyerNational Heart and Lung Institute, Imperial College London, Du Cane Road, London, W12 0NN, UK.
Edwin GarciaDepartment of Physics, Imperial College London, London, SW7 2AZ, UK.
Douglas J KellyDepartment of Physics, Imperial College London, London, SW7 2AZ, UK.
Nicholas S PetersNational Heart and Lung Institute, Imperial College London, Du Cane Road, London, W12 0NN, UK.
Alexander R LyonNational Heart and Lung Institute, Imperial College London, Du Cane Road, London, W12 0NN, UK.
Paul M W FrenchDepartment of Physics, Imperial College London, London, SW7 2AZ, UK.
Chris DunsbyDepartment of Physics, Imperial College London, London, SW7 2AZ, UK.
Imperial College London · GBLung Institute · US

Funding

Biotechnology and Biological Sciences Research Council BB/E000495/1British Heart Foundation RG/16/3/32175
6 · The paper itself

Abstract

Reduced nicotinamide adenine dinucleotide (NADH) is the principal electron donor in glycolysis and oxidative metabolism and is thus recognized as a key biomarker for probing metabolic state. While the fluorescence characteristics of NADH have been investigated extensively, there are discrepancies in the published data due to diverse experimental conditions, instrumentation and microenvironmental parameters that can affect NADH fluorescence. Using a cuvette-based time-resolved spectrofluorimeter employing one-photon excitation at 375 nm, we characterized the fluorescence intensity, lifetime, spectral response, anisotropy and time-resolved anisotropy of NADH in aqueous solution under varying microenvironmental conditions, namely temperature, pH, and binding to lactate dehydrogenase (LDH). Our results demonstrate how temperature, pH, and binding partners each impact the fluorescence signature of NADH and highlight the complexity of the fluorescence data when different parameters produce competing effects. We hope that the data presented in this study will provide a reference for potential sources of variation in experiments measuring NADH fluorescence.

Identifiers

PMID34458690
PMCPMC8367293
OpenAlexW3160952001

What OpenQuestion holds

Textmetadata
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.