ReviewJournal of molecular biology2022
Mechanisms of Gasdermin Recognition by Proteases.
Review in Journal of molecular biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 27 citations in OpenAlex.
- Theme and variations: activation and regulation of gasdermin-mediated inflammation.Biochemical Society transactions · 2026Review
- Targeting pyroptosis in periodontitis: mechanisms and therapeutic strategies.Frontiers in immunology · 2026Review
- Differentiating the Substrate Profiles of Inflammatory Caspases Using Extended Förster Resonance Energy Transfer-Based Peptide Substrates.Chembiochem : a European journal of chemical biology · 2026Article
- Chemically induced dimerization of GSDMD C-terminal domain blocks GSDMD N-terminal domain-mediated pyroptosis.Cell death discovery · 2025Article
- Matrix-M adjuvant triggers inflammasome activation and enables antigen cross-presentation through induction of lysosomal membrane permeabilization.NPJ vaccines · 2025Article
- Modeling Necroptotic and Pyroptotic Signaling inBiomolecules · 2025Review
- Mechanisms of RCD-1 pore formation and membrane bending.Nature communications · 2025Article
- Gasdermin D (GSDM D) as a Potential Diagnostic Biomarker in Bladder Cancer: New Perspectives in Detection.Cancers · 2024Article
- Expansion of the Structure-Activity Relationship Profile of Triaminopyrimidines as Inhibitors of Caspase-1.Chemical biology & drug design · 2024Article
- Nonallosteric activation of posttranslational modification enzymes by active site-directed inhibitors.Computational and structural biotechnology journal · 2024Article
- Mechanisms regulating host cell death duringmBio · 2024Review
- Pyroptosis: Induction and inhibition strategies for immunotherapy of diseases.Acta pharmaceutica Sinica. B · 2024Review
- Gasdermins: a dual role in pyroptosis and tumor immunity.Frontiers in immunology · 2024Review
- Structural and functional insights into GSDMB isoforms complex roles in pathogenesis.Cell cycle (Georgetown, Tex.) · 2023Review
- Pyroptosis and the cellular consequences of gasdermin pores.Seminars in immunology · 2023Review
- The Pyroptotic and Nonpyroptotic Roles of Gasdermins in Modulating Cancer Progression and Their Perspectives on Cancer Therapeutics.Archivum immunologiae et therapiae experimentalis · 2023Review
- Pyroptosis in neutrophils: Multimodal integration of inflammasome and regulated cell death signaling pathways.Immunological reviews · 2023Review
- Regulation of gasdermins in pyroptosis and cytokine release.Advances in immunology · 2023Article
- Regulation of Synovial γδ T Cell Ligand Expression by Mitochondrial Reactive Oxygen Species and Gasdermin-D.Journal of immunology (Baltimore, Md. : 1950) · 2023Article
- No longer married to inflammasome signaling: the diverse interacting pathways leading to pyroptotic cell death.The Biochemical journal · 2022Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Members of the gasdermin family contain positively charged N-terminal domains (NTDs) capable of binding phospholipids and assembling membrane pores, and C-terminal domains (CTDs) that bind the NTDs to prevent pore formation in the resting states. The flexible NTD-CTD linker regions of gasdermins are highly variable in length and sequences, which may be attributable to gasdermin recognition by diverse proteases. In addition, protease cleavage within the NTDs is known to inactivate several gasdermin family members. Recognition and cleavage of the gasdermin family members by different proteases share common and distinct features at the protease active sites, as well as exosites recently identified for the inflammatory caspases. Utilization of exosites may strengthen enzyme-substrate interaction, improve efficiency of proteolysis, and enhance substrate selectivity. It remains to be determined if the dual site recognition of gasdermin D (GSDMD) by the inflammatory caspases is employed by other GSDMD-targeting proteases, or is involved in proteolytic processing of other gasdermins. Biochemical and structural approaches will be instrumental in revealing how potential exosites in diverse proteases engage different gasdermin substrates. Different features of gasdermin sequence, structure, expression characteristics, and post-translational modifications may dictate distinct mechanisms of protease-dependent activation or inactivation. Such diverse mechanisms may underlie the divergent physiological and pathological functions of gasdermins, and furnish opportunities for therapeutic targeting of gasdermins in infectious diseases and inflammatory disorders.
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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.