Evidence map›Paper›PMID 33845576›Full record

ArticleJournal of the American Chemical Society2021

A Coumarin-Porphyrin FRET Break-Apart Probe for Heme Oxygenase-1.

Edward R H Walter, Ying Ge, Justin C Mason, Joseph J Boyle, Nicholas J Long

Open access · hybridAbstract read
In one paragraph

Article in Journal of the American Chemical Society, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
4.5field-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

11 citing papers in PubMed, 69 citations in OpenAlex.

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  10. Enzyme-activated probes in optical imaging: a focus on atherosclerosis.Dalton transactions (Cambridge, England : 2003) · 2021
    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

5 authors at 2 institutions in 2 countries.

Edward R H WalterDepartment of Chemistry, Imperial College London, Molecular Sciences Research Hub, White City Campus, Wood Lane, London W12 0BZ, U.K.
Ying GeNational Lung and Heart Institute, Imperial College London, Du Cane Road, London W12 0NN, U.K.
Justin C MasonNational Lung and Heart Institute, Imperial College London, Du Cane Road, London W12 0NN, U.K.
Joseph J BoyleNational Lung and Heart Institute, Imperial College London, Du Cane Road, London W12 0NN, U.K.
Nicholas J LongDepartment of Chemistry, Imperial College London, Molecular Sciences Research Hub, White City Campus, Wood Lane, London W12 0BZ, U.K.ORCID 0000-0002-8298-938X
Lung Institute · USLondon Biofoundry · GB

Funding

British Heart Foundation FS/13/12/30037British Heart Foundation PG/17/71/33242British Heart Foundation PG/21/10422Medical Research Council MC_PC_19040
6 · The paper itself

Abstract

Heme oxygenase-1 (HO-1) is a vital enzyme in humans that primarily regulates free heme concentrations. The overexpression of HO-1 is commonly associated with cardiovascular and neurodegenerative diseases including atherosclerosis and ischemic stroke. Currently, there are no known chemical probes to detect HO-1 activity, limiting its potential as an early diagnostic/prognostic marker in these serious diseases. Reported here are the design, synthesis, and photophysical and biological characterization of a coumarin-porphyrin FRET break-apart probe to detect HO-1 activity,

Indexed as

CoumarinsEscherichia coliFluorescence Resonance Energy TransferHeme Oxygenase-1HumansPhotochemical ProcessesProtoporphyrinsSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationSpectrophotometry, UltravioletcoumarinCoumarinsHeme Oxygenase-1HMOX1 protein, humanprotoporphyrin IXProtoporphyrins

Identifiers

PMID33845576
PMCPMC8154531
OpenAlexW3155183246

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.