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Human TH17 cells engage gasdermin E pores to release IL-1α on NLRP3 inflammasome activation
Nature Immunology, 2023 It has been shown that innate immune responses can adopt adaptive properties such as memory. Whether T cells utilize innate immune signaling pathways to diversify their repertoire of effector functions is unknown.
, Mahima Arunkumar
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Pore-forming activity and structural autoinhibition of the gasdermin family
Nature, 2016 Jingjin Ding, Wang Liu, Jianjin Shi
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Transcriptional and Epigenetic Regulation of Gasdermins
Journal of Molecular Biology, 2022Gasdermins (GSDM) are a family of six homologous proteins (GSDMA to E and Pejvakin) in humans. GSDMA-E are pore-forming proteins targeting the plasma membrane to trigger a rapid cell death termed pyroptosis or bacterial membranes to promote antibacterial immune defenses.
Thomas Henry, Emilie Bourdonnay
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Determination of Gasdermin Pores
2023The gasdermin family represents a type of membrane pore-forming proteins. The gasdermin family is extensively characterized as the executioner of pyroptotic cell death in mammals; recent studies suggest that gasdermin-like pore-forming proteins are also present in bacteria and fungi.
Kun, Wang, Jingjin, Ding, Feng, Shao
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Association between Gasdermin A, Gasdermin B Polymorphisms and Allergic Rhinitis Amongst Jordanians
Endocrine, Metabolic & Immune Disorders - Drug Targets, 2021Background: Gasdermin A (GSDMA) and Gasdermin B (GSDMB) have been associated with childhood and to a lesser extent with adult asthma in many populations. In this study, we investigate whether there is an association between GSDMA (rs7212938, T/G) and GSDMB (rs7216389, T/C) at locus 17q21.2 and risk of Allergic Rhinitis among Jordanians. Also, we aimed
Malek Zihlif +6 more
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Epigenetic and transcriptional control of gasdermins
Seminars in Immunology, 2023Cells undergo an inflammatory programmed lytic cell death called 'pyroptosis' (with the Greek roots 'fiery'), often featuring morphological hallmarks such as large ballooning protrusions and subsequent bursting. Originally described as a caspase-1-dependent cell death in response to bacterial infection, pyroptosis has since been re-defined in 2018 as a
Cristhian Cadena +3 more
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Inducing Pyroptosis via Gasdermin B and Gasdermin E Cleavage
2023Gasdermin B (GSDMB) and gasdermin E (GSDME) are two members of the gasdermin family, which shares a conservative gasdermin-N domain capable of executing pyroptotic cell death, through perforating the plasma membrane from inside of the cell. Both GSDMB and GSDME are autoinhibited in the resting stage and require proteolytic cleavage to unleash the pore ...
Zhiwei, Zhou, Yupeng, Wang, Feng, Shao
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Microbiological Research, 2023
The recognition of pathogen- or damage- associated molecular patterns (PAMPs/DAMPs) signals a series of coordinated responses as part of innate immunity or host cell defense during infection. The inflammasome is an assemblage of multiprotein complexes in the cytosol that activate inflammatory caspases and release pro-inflammatory mediators. This review
Abosede Salami +2 more
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The recognition of pathogen- or damage- associated molecular patterns (PAMPs/DAMPs) signals a series of coordinated responses as part of innate immunity or host cell defense during infection. The inflammasome is an assemblage of multiprotein complexes in the cytosol that activate inflammatory caspases and release pro-inflammatory mediators. This review
Abosede Salami +2 more
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Inflammasome and gasdermin signaling in neutrophils
Molecular Microbiology, 2022AbstractInflammasomes and gasdermins mount potent host defense pathways against invading microbial pathogens, however, dysregulation in these pathways can drive a variety of inflammatory disorders. Neutrophils, historically regarded as effector phagocytes that drive host defense via microbial killing, are now emerging as critical drivers of immunity in
See Jie Yow +2 more
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Science immunology
Plasma membrane perforation elicited by caspase cleavage of the gasdermin D (GSDMD) N-terminal domain (GSDMD-NT) triggers pyroptosis. The mechanisms underlying GSDMD membrane translocation and pore formation are not fully understood.
A. Balasubramanian +23 more
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Plasma membrane perforation elicited by caspase cleavage of the gasdermin D (GSDMD) N-terminal domain (GSDMD-NT) triggers pyroptosis. The mechanisms underlying GSDMD membrane translocation and pore formation are not fully understood.
A. Balasubramanian +23 more
semanticscholar +1 more source