ArticleAngewandte Chemie (International ed. in English)2017
Allosteric Tuning of Caspase-7: A Fragment-Based Drug Discovery Approach.
Article in Angewandte Chemie (International ed. in English), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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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
7 citing papers in PubMed.
- Chemoproteomics Identifies State-Dependent and Proteoform-Selective Caspase-2 Inhibitors.Journal of the American Chemical Society · 2024Article
- Development of Allosteric NIK Ligands from Fragment-Based NMR Screening.ACS medicinal chemistry letters · 2023Article
- Allosteric Tuning of Caspase-7: Establishing the Nexus of Structure and Catalytic Power.Chemistry (Weinheim an der Bergstrasse, Germany) · 2023Article
- Fragment-Based Discovery of Novel Allosteric MEK1 Binders.ACS medicinal chemistry letters · 2021Article
- Synthesis, Characterization, and In Vivo Anti-Cancer Activity of New Metal Complexes Derived from Isatin-Molecules (Basel, Switzerland) · 2019Article
- Proteases: Pivot Points in Functional Proteomics.Methods in molecular biology (Clifton, N.J.) · 2019Review
- Allosteric Tuning of Caspase-7: A Fragment-Based Drug Discovery Approach.Angewandte Chemie (International ed. in English) · 2017Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
The caspase family of cysteine proteases are highly sought-after drug targets owing to their essential roles in apoptosis, proliferation, and inflammation pathways. High-throughput screening efforts to discover inhibitors have gained little traction. Fragment-based screening has emerged as a powerful approach for the discovery of innovative drug leads. This method has become a central facet of drug discovery campaigns in the pharmaceutical industry and academia. A fragment-based drug discovery campaign against human caspase-7 resulted in the discovery of a novel series of allosteric inhibitors. An X-ray crystal structure of caspase-7 bound to a fragment hit and a thorough kinetic characterization of a zymogenic form of the enzyme were used to investigate the allosteric mechanism of inhibition. This work further advances our understanding of the mechanisms of allosteric control of this class of pharmaceutically relevant enzymes, and provides a new path forward for drug discovery efforts.
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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.