Evidence map›Paper›PMID 19968300›Full record

ArticleJournal of the American Chemical Society2010

Activatable magnetic resonance imaging agents for myeloperoxidase sensing: mechanism of activation, stability, and toxicity.

Elisenda Rodríguez, Mark Nilges, Ralph Weissleder, John W Chen

Erratum issuedOpen access · greenAbstract read
In one paragraph

Article in Journal of the American Chemical Society, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 55 papers.

0numbers the graph read from it
0cells of the map it votes in
55citing papers in PubMed
3.6field-weighted citation impact, top 7% 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

55 citing papers in PubMed, 111 citations in OpenAlex.

  1. An HRedox biology · 2026
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  11. Pathologically triggeredActa pharmaceutica Sinica. B · 2023
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  14. Review
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  17. Article
  18. An activatable PET imaging radioprobe is a dynamic reporter of myeloperoxidase activity in vivo.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  19. Molecular Magnetic Resonance Imaging Using a Redox-Active Iron Complex.Journal of the American Chemical Society · 2019
    Article
  20. Article
4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

4 authors at 3 institutions in 1 country.

Elisenda RodríguezCenter for Molecular Imaging Research, Department of Radiology, Massachusetts General Hospital, Boston, Massachusetts 02114, USA.
Mark Nilges
Ralph Weissleder
John W Chen
Massachusetts General Hospital · USCenter for Systems Biology · USUniversity of Illinois Urbana-Champaign · US

Funding

MR imaging of myeloperoxidase activityR01HL078641 · NHLBI · MASSACHUSETTS GENERAL HOSPITAL · PI WEISSLEDER, RALPH · 2004 to 2007
$1.5M
Molecular imaging of vascular pathologyK08HL081170 · NHLBI · MASSACHUSETTS GENERAL HOSPITAL · PI CHEN, JOHN W · 2006 to 2010
$666k
NHLBI NIH HHS K08 HL081170NHLBI NIH HHS K08HL081170NHLBI NIH HHS R01 HL078641NHLBI NIH HHS R01-HL078641
6 · The paper itself

Abstract

Myeloperoxidase (MPO) is increasingly being recognized as an important factor in many inflammatory diseases, particularly cardiovascular and neurological diseases. MPO-specific imaging agents would thus be highly useful to diagnose early disease, monitor disease progression, and quantify treatment effects. This study reports in vitro and in vivo characterizations of the mechanism of interaction between MPO and paramagnetic enzyme substrates based on physical and biological measurements. We show that these agents are activated through a radical mechanism, which can combine to form oligomers and, in the presence of tyrosine-containing peptide, bind to proteins. We further identified two new imaging agents, which represent the near extremes in either oligomerization (mono-5HT-DTPA-Gd) or protein-binding in their activation mechanism (bis-o-dianisidine-DTPA-Gd). On the other hand, we found that the agent bis-5HT-DTPA-Gd utilizes both mechanisms when activated. These properties yield distinct in vivo pharmacokinetics profiles for each of these agents that may be exploited for different applications. Specificity studies show that only MPO, but not eosinophil peroxidase, can highly activate these agents, and that MPO activity as low as 0.005 U/mg of tissue can be detected. Gd kinetic lability and cytotoxicity studies further confirm stability of the Gd ion and low toxicity for the 5HT-based agents, suggesting that these agents are suitable for translational in vivo studies.

Indexed as

AnimalsElectron Spin Resonance SpectroscopyGadoliniumKineticsMagnetic Resonance ImagingMiceNIH 3T3 CellsOrganometallic CompoundsOxidation-ReductionPeroxidaseProteinsTyrosineGadoliniumOrganometallic CompoundsPeroxidaseProteinsTyrosine

Identifiers

PMID19968300
PMCPMC2802665
OpenAlexW2012053461

What OpenQuestion holds

Textmetadata
LicenceTDM
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.