ArticleChemMedChem2015
Investigating the Selectivity of Metalloenzyme Inhibitors in the Presence of Competing Metalloproteins.
Article in ChemMedChem, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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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.
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.
Who cites it
6 citing papers in PubMed, 17 citations in OpenAlex.
- Control of metalloenzyme activity using photopharmacophores.Coordination chemistry reviews · 2024Article
- Structure-Activity Relationships in Metal-Binding Pharmacophores for Influenza Endonuclease.Journal of medicinal chemistry · 2018Article
- Isosteres of hydroxypyridinethione as drug-like pharmacophores for metalloenzyme inhibition.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2018Article
- Dipicolinic Acid Derivatives as Inhibitors of New Delhi Metallo-β-lactamase-1.Journal of medicinal chemistry · 2017Article
- A Bioinorganic Approach to Fragment-Based Drug Discovery Targeting Metalloenzymes.Accounts of chemical research · 2017Article
- The effect of metalloprotein inhibitors on cellular metal ion content and distribution.Metallomics : integrated biometal science · 2017Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Metalloprotein inhibitors (MPi) are an important class of therapeutics for the treatment of a variety of diseases, including hypertension, cancer, and HIV/AIDS. However, despite their clinical success, there is an apprehension that MPi may be less selective than other small-molecule therapeutics and more prone to inhibit off-target metalloenzymes. We examined the issue of MPi specificity by investigating the selectivity of a variety of MPi against a representative panel of metalloenzymes in the presence of competing metalloproteins (metallothionein, myoglobin, carbonic anhydrase, and transferrin). Our findings reveal that a wide variety of MPi do not exhibit a decrease in inhibitory activity in the presence of large excesses of competing metalloproteins, suggesting that the competing proteins do not titrate the MPi away from its intended target. This study represents a rudimentary but important means to mimic the biological milieu, which contains other metalloproteins that could compete the MPi away from its target. The strategy used in this study may be a useful approach to examine the selectivity of other MPi in development.
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What OpenQuestion holds
Registered trials
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.