ReviewThe Biochemical journal2015
Comparative structural analysis of the caspase family with other clan CD cysteine peptidases.
Review in The Biochemical journal, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
49 citing papers in PubMed.
- Regulated Cell Death in Fungi, the Role of Metacaspases and Assay Techniques.Methods and protocols · 2026Review
- Cysteine proteases and how YabG fits into clan CD of the MEROPS database.Journal of bacteriology · 2025Review
- Caspase-mediated pathways in retinal ganglion cell injury: a novel therapeutic target for glaucoma.Frontiers in cell and developmental biology · 2025Review
- MicroED structure of the C11 cysteine protease clostripain.Journal of structural biology: X · 2024Article
- Fungal Apoptosis-Related Proteins.Microorganisms · 2024Review
- Chemoproteomics Identifies State-Dependent and Proteoform-Selective Caspase-2 Inhibitors.Journal of the American Chemical Society · 2024Article
- A Comprehensive Exploration of Caspase Detection Methods: From Classical Approaches to Cutting-Edge Innovations.International journal of molecular sciences · 2024Review
- Evolution of Caspases and the Invention of Pyroptosis.International journal of molecular sciences · 2024Review
- Expansion and diversity of caspases in Mytilus coruscus contribute to larval metamorphosis and environmental adaptation.BMC genomics · 2024Review
- Thermoprotection by a cell membrane-localized metacaspase in a green alga.The Plant cell · 2024Article
- Differential Expression of Stress Adaptation Genes in a DiatomInternational journal of molecular sciences · 2024Article
- Type III-B CRISPR-Cas cascade of proteolytic cleavages.Science (New York, N.Y.) · 2024Article
- Article
- CASP3 gene expression and the role of caspase 3 in the pathogenesis of depressive disorders.BMC psychiatry · 2023Article
- Roles of Cysteine Proteases in Biology and Pathogenesis of Parasites.Microorganisms · 2023Article
- Galectin-9 in Gastroenterological Cancer.International journal of molecular sciences · 2023Review
- RNA-activated protein cleavage with a CRISPR-associated endopeptidase.Science (New York, N.Y.) · 2022Article
- Structural and molecular determinants of Candida glabrata metacaspase maturation and activation by calcium.Communications biology · 2022Article
- Structural and functional studies of legumain-mycocypin complexes revealed a competitive, exosite-regulated mode of interaction.The Journal of biological chemistry · 2022Article
- Evolutionary Diversity and Function of Metacaspases in Plants: Similar to but Not Caspases.International journal of molecular sciences · 2022Review
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
Clan CD forms a structural group of cysteine peptidases, containing seven individual families and two subfamilies of structurally related enzymes. Historically, it is most notable for containing the mammalian caspases, on which the structures of the clan were founded. Interestingly, the caspase family is split into two subfamilies: the caspases, and a second subfamily containing both the paracaspases and the metacaspases. Structural data are now available for both the paracaspases and the metacaspases, allowing a comprehensive structural analysis of the entire caspase family. In addition, a relative plethora of structural data has recently become available for many of the other families in the clan, allowing both the structures and the structure-function relationships of clan CD to be fully explored. The present review compares the enzymes in the caspase subfamilies with each other, together with a comprehensive comparison of all the structural families in clan CD. This reveals a diverse group of structures with highly conserved structural elements that provide the peptidases with a variety of substrate specificities and activation mechanisms. It also reveals conserved structural elements involved in substrate binding, and potential autoinhibitory functions, throughout the clan, and confirms that the metacaspases are structurally diverse from the caspases (and paracaspases), suggesting that they should form a distinct family of clan CD peptidases.
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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.