ArticleOrganometallics2011
Organometallic Pyridylnaphthalimide Complexes as Protein Kinase Inhibitors.
Article in Organometallics, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 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.
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Who cites it
5 citing papers in PubMed.
- Proteome-Wide Target Identification Using Reactive Metallo-Scaffolds (r-mS): A Platform for Metallodrug Discovery.Angewandte Chemie (International ed. in English) · 2026Article
- An iridium(iii)-based irreversible protein-protein interaction inhibitor of BRD4 as a potent anticancer agent.Chemical science · 2015Article
- Non-ATP-Mimetic Organometallic Protein Kinase Inhibitor.ChemistryOpen · 2013Article
- Bioactive cyclometalated phthalimides: design, synthesis and kinase inhibition.Dalton transactions (Cambridge, England : 2003) · 2012Article
- The art of filling protein pockets efficiently with octahedral metal complexes.Angewandte Chemie (International ed. in English) · 2012Article
Corrections and comments
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Authors and funding
7 authors.
Funding
Abstract
A new metal-containing scaffold for the design of protein kinase inhibitors is introduced. Key feature is a 3-(2-pyridyl)-1,8-naphthalimide "pharmacophore chelate ligand" which is designed to form two hydrogen bonds with the hinge region of the ATP-binding site and is at the same time capable of serving as a stable bidentate ligand through C-H-activation at the 4-position of the electron-deficient naphthalene moiety. This C-H-activation leads to a reduced demand for coordinating heteroatoms and thus sets the basis for a very efficient three-step synthesis starting from 1,8-naphthalic anhydride. The versatility of this ligand is demonstrated with the discovery of a ruthenium complex that functions as a nanomolar inhibitor for myosin light-chain kinase (MYLK or MLCK).
Identifiers
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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.