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Gasdermin D Cleavage Assay Following Inflammasome Activation
2022Gasdermin D (GSDMD) is a recently identified pore-forming protein that is crucial for the execution of pyroptosis, a highly inflammatory form of cell death. GSDMD contains an N-terminal and a C-terminal domain that are separated by a proteolysis-sensitive linker.
Louisa Janice, Kamajaya, Dave, Boucher
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Versatility of gasdermin D beyond pyroptosis
Trends in Cell BiologyGasdermin D (GSDMD) has garnered significant attention primarily for the pore-forming role of its p30 N-terminal fragment (NT-p30) generated during pyroptosis, a proinflammatory form of cell death. However, emerging evidence suggests that the formation of GSDMD-NT pores is reversible, and the activation of GSDMD does not necessarily lead to pyroptosis.
Tianming Zhao, Zhexu Chi, Di Wang
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Mechanistic insights into gasdermin-mediated pyroptosis
Nature Reviews Molecular Cell BiologyPyroptosis, a novel mode of inflammatory cell death, is executed by membrane pore-forming gasdermin (GSDM) family members in response to extracellular or intracellular injury cues and is characterized by a ballooning cell morphology, plasma membrane rupture and the release of inflammatory mediators such as interleukin-1β (IL-1β), IL-18 and high ...
Yang Bai, Youdong Pan, Xing Liu
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Gasdermins in pyroptosis, inflammation, and cancer
Trends in Molecular MedicinePyroptosis is a type of programmed inflammatory cell death characterized by balloon-like swelling, membrane rupture, and the release of inflammatory cytokines and danger signals. Pyroptosis is directly triggered by activated gasdermins (GSDMs) which bind to membrane phospholipids, oligomerize, and form pores in cell membranes.
Rui Min +3 more
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New insights into Gasdermin D pore formation
Biochemical Society TransactionsGasdermin D (GSDMD) is a pore-forming protein that perforates the plasma membrane (PM) during pyroptosis, a pro-inflammatory form of cell death, to induce the unconventional secretion of inflammatory cytokines and, ultimately, cell lysis. GSDMD is activated by protease-mediated cleavage of its active N-terminal domain from the autoinhibitory C-terminal
Shirin Kappelhoff +2 more
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