ArticleCell death and differentiation2014
Unnatural amino acids increase sensitivity and provide for the design of highly selective caspase substrates.
Article in Cell death and differentiation, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 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
46 citing papers in PubMed, 91 citations in OpenAlex.
- Engineering Cathepsin S Selective Chemical Probes and Antibody-Drug Conjugates through Substrate Profiling with Unnatural Amino Acids.Journal of medicinal chemistry · 2026Article
- Using a bioluminescence resonance energy transfer caspase biosensor to study caspase-3 cleavage site specificity.Bioscience reports · 2026Article
- Deep learning guided design of protease substrates.Nature communications · 2026Article
- Identifying protease-activated targets and exploring therapeutic applications.Expert opinion on therapeutic targets · 2025Review
- Exploring the involvement of serine proteases in neutrophil extracellular traps: a review of mechanisms and implications.Cell death & disease · 2025Review
- Use of protease substrate specificity screening in the rational design of selective protease inhibitors with unnatural amino acids: Application to HGFA, matriptase, and hepsin.Protein science : a publication of the Protein Society · 2024Article
- Review
- Article
- Non-Canonical Amino Acids in Analyses of Protease Structure and Function.International journal of molecular sciences · 2023Review
- Selective chemical reagents to investigate the role of caspase 6 in apoptosis in acute leukemia T cells.Chemical science · 2023Article
- Design and Synthesis of Ubiquitin-Based Chemical Tools with Unnatural Amino Acids for Selective Detection of Deubiquitinases.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Cell death in skin function, inflammation, and disease.The Biochemical journal · 2022Review
- Resurrection of an ancient inflammatory locus reveals switch to caspase-1 specificity on a caspase-4 scaffold.The Journal of biological chemistry · 2022Article
- Urinary detection of early responses to checkpoint blockade and of resistance to it via protease-cleaved antibody-conjugated sensors.Nature biomedical engineering · 2022Article
- Engineering caspase 7 as an affinity reagent to capture proteolytic products.The FEBS journal · 2021Article
- SARS-CoV-2 MNature chemical biology · 2021Article
- Editorial: Development and Applications of New Activity-Based Probes.Frontiers in chemistry · 2021Article
- Design of Optical-Imaging Probes by Screening of Diverse Substrate Libraries Directly in Disease-Tissue Extracts.Angewandte Chemie (International ed. in English) · 2020Article
- Cell death in chronic inflammation: breaking the cycle to treat rheumatic disease.Nature reviews. Rheumatology · 2020Review
- Noninvasive optical detection of granzyme B from natural killer cells with enzyme-activated fluorogenic probes.The Journal of biological chemistry · 2020Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
Traditional combinatorial peptidyl substrate library approaches generally utilize natural amino acids, limiting the usefulness of this tool in generating selective substrates for proteases that share similar substrate specificity profiles. To address this limitation, we synthesized a Hybrid Combinatorial Substrate Library (HyCoSuL) with the general formula of Ac-P4-P3-P2-Asp-ACC, testing the approach on a family of closely related proteases - the human caspases. The power of this library for caspase discrimination extends far beyond traditional PS-SCL approach, as in addition to 19 natural amino acids we also used 110 diverse unnatural amino acids that can more extensively explore the chemical space represented by caspase-active sites. Using this approach we identified and employed peptide-based substrates that provided excellent discrimination between individual caspases, allowing us to simultaneously resolve the individual contribution of the apical caspase-9 and the executioner caspase-3 and caspase-7 in the development of cytochrome-c-dependent apoptosis for the first time.
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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.