ArticleJournal of medicinal chemistry2011
Analogues and derivatives of oncrasin-1, a novel inhibitor of the C-terminal domain of RNA polymerase II and their antitumor activities.
Article in Journal of medicinal chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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.
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
17 citing papers in PubMed.
- High Target Homology Does Not Guarantee Inhibition: Aminothiazoles Emerge as Inhibitors ofACS infectious diseases · 2024Article
- Design, synthesis, and evaluation of novelJournal of enzyme inhibition and medicinal chemistry · 2020Article
- Automated synthesis ofEJNMMI radiopharmacy and chemistry · 2020Article
- Identification and targeting of selective vulnerability rendered by tamoxifen resistance.Breast cancer research : BCR · 2020Article
- Regulation of the Ras-Related Signaling Pathway by Small Molecules Containing an Indole Core Scaffold: A Potential Antitumor Therapy.Frontiers in pharmacology · 2020Review
- Article
- Structure-based design of new poly (ADP-ribose) polymerase (PARP-1) inhibitors.Molecular diversity · 2017Article
- Simultaneous determination and validation of oncrasin-266 and its metabolites by HPLC-MS/MS: Application to a pharmacokinetic study.Journal of chromatography. B, Analytical technologies in the biomedical and life sciences · 2016Article
- RAS signaling and anti-RAS therapy: lessons learned from genetically engineered mouse models, human cancer cells, and patient-related studies.Acta biochimica et biophysica Sinica · 2016Review
- Predictive biomarkers in precision medicine and drug development against lung cancer.Chinese journal of cancer · 2015Review
- Expression of sulfotransferase SULT1A1 in cancer cells predicts susceptibility to the novel anticancer agent NSC-743380.Oncotarget · 2015Article
- Development of synthetic lethality anticancer therapeutics.Journal of medicinal chemistry · 2014Review
- Prodrug oncrasin-266 improves the stability, pharmacokinetics, and safety of NSC-743380.Bioorganic & medicinal chemistry · 2014Article
- Targeted regulation of PI3K/Akt/mTOR/NF-κB signaling by indole compounds and their derivatives: mechanistic details and biological implications for cancer therapy.Anti-cancer agents in medicinal chemistry · 2013Review
- Microwave-assisted synthesis of 3-nitroindoles from N-aryl enamines via intramolecular arene-alkene coupling.Organic letters · 2013Article
- Antitumor activity of a novel STAT3 inhibitor and redox modulator in non-small cell lung cancer cells.Biochemical pharmacology · 2012Article
- Antitumor activity of a novel oncrasin analogue is mediated by JNK activation and STAT3 inhibition.PloS one · 2011Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors.
Funding
Abstract
To optimize the antitumor activity of oncrasin-1, a small molecule RNA polymerase II inhibitor, we evaluated 69 oncrasin-1 analogues for their cytotoxic activity against normal human epithelial cells and K-Ras mutant tumor cells. About 40 of those compounds were as potent as or more potent than oncrasin-1 in tumor cells and had a minimal cytotoxic effect on normal cells. Structure-activity relationship analysis revealed that most of the active compounds contained either a hydroxymethyl group or an aldehyde group as a substitute at the 3-position of the indole. Both electron-donating and electron-withdrawing groups in the benzene ring were well tolerated. The hydroxymethyl compounds ranged from equipotent with to 100 times as potent as the corresponding aldehyde compounds. We tested three active analogues' effect on RNA polymerase phosphorylation and found that they all inhibited phosphorylation of the C-terminal domain of RNA polymerase II, suggesting that the active compounds might act through the same mechanisms as oncrasin-1.
Indexed as
Identifiers
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.