ArticleMolecular cell2012
A class of allosteric caspase inhibitors identified by high-throughput screening.
Article in Molecular cell, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 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
23 citing papers in PubMed, 46 citations in OpenAlex.
- Leveraging Deep Learning to Construct a Programmed Cell Death-Driven Prognostic Signature in Acute Myeloid Leukemia.Current issues in molecular biology · 2026Article
- MEF-AlloSite: an accurate and robust Multimodel Ensemble Feature selection for the Allosteric Site identification model.Journal of cheminformatics · 2024Article
- The landscape of programmed cell death-related lncRNAs in Alzheimer's disease and Parkinson's disease.Apoptosis : an international journal on programmed cell death · 2024Article
- Regulation of Peptidase Activity beyond the Active Site in Human Health and Disease.International journal of molecular sciences · 2023Review
- Allosteric Tuning of Caspase-7: Establishing the Nexus of Structure and Catalytic Power.Chemistry (Weinheim an der Bergstrasse, Germany) · 2023Article
- Essential Oils and Their Compounds as Potential Anti-Influenza Agents.Molecules (Basel, Switzerland) · 2022Review
- The impact of cycleanine in cancer research: a computational study.Journal of molecular modeling · 2022Article
- Mapping oncogenic protein interactions for precision medicine.International journal of cancer · 2022Review
- Mechanisms of Gasdermin Recognition by Proteases.Journal of molecular biology · 2022Review
- Microfluidic deep mutational scanning of the human executioner caspases reveals differences in structure and regulation.Cell death discovery · 2022Article
- The Role of Caspase-2 in Regulating Cell Fate.Cells · 2020Review
- Tri-arginine exosite patch of caspase-6 recruits substrates for hydrolysis.The Journal of biological chemistry · 2019Article
- Kaempferol mitigates Endoplasmic Reticulum Stress Induced Cell Death by targeting caspase 3/7.Scientific reports · 2018Article
- Allosteric Tuning of Caspase-7: A Fragment-Based Drug Discovery Approach.Angewandte Chemie (International ed. in English) · 2017Article
- ASD v3.0: unraveling allosteric regulation with structural mechanisms and biological networks.Nucleic acids research · 2016Article
- Mechanism-based management for mucositis: option for treating side effects without compromising the efficacy of cancer therapy.OncoTargets and therapy · 2016Review
- Small Molecule Active Site Directed Tools for Studying Human Caspases.Chemical reviews · 2015Review
- Computational Advances for the Development of Allosteric Modulators and Bitopic Ligands in G Protein-Coupled Receptors.The AAPS journal · 2015Review
- Structure-based inhibition of protein-protein interactions.European journal of medicinal chemistry · 2015Review
- Compounds with anti-influenza activity: present and future of strategies for the optimal treatment and management of influenza. Part II: Future compounds against influenza virus.Journal of preventive medicine and hygiene · 2014Review
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
Abstract
Caspase inhibition is a promising approach for treating multiple diseases. Using a reconstituted assay and high-throughput screening, we identified a group of nonpeptide caspase inhibitors. These inhibitors share common chemical scaffolds, suggesting the same mechanism of action. They can inhibit apoptosis in various cell types induced by multiple stimuli; they can also inhibit caspase-1-mediated interleukin generation in macrophages, indicating potential anti-inflammatory application. While these compounds inhibit all the tested caspases, kinetic analysis indicates they do not compete for the catalytic sites of the enzymes. The cocrystal structure of one of these compounds with caspase-7 reveals that it binds to the dimerization interface of the caspase, another common structural element shared by all active caspases. Consistently, biochemical analysis demonstrates that the compound abates caspase-8 dimerization. Based on these kinetic, biochemical, and structural analyses, we suggest that these compounds are allosteric caspase inhibitors that function through binding to the dimerization interface of caspases.
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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.