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Determination of Gasdermin Pores

2023
The 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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Transcriptional and Epigenetic Regulation of Gasdermins

Journal of Molecular Biology, 2022
Gasdermins (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.
Emilie, Bourdonnay, Thomas, Henry
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Inflammasome and gasdermin signaling in neutrophils

Molecular Microbiology, 2022
AbstractInflammasomes 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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Inducing Pyroptosis via Gasdermin B and Gasdermin E Cleavage

2023
Gasdermin 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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Gasdermin D kills bacteria

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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Epigenetic and transcriptional control of gasdermins

Seminars in Immunology, 2023
Cells 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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Coral gasdermin triggers pyroptosis

Science Immunology, 2020
Coral gasdermin is activated by caspase 3 and involved in pathogen-induced coral death.
Shuai Jiang   +4 more
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Association between Gasdermin A, Gasdermin B Polymorphisms and Allergic Rhinitis Amongst Jordanians

Endocrine, Metabolic & Immune Disorders - Drug Targets, 2021
Background: 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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Recognition of gasdermins by proteases

The Journal of Immunology, 2021
Abstract The recognition and cleavage of gasdermin family members by proteases trigger the activation of the pore-forming activities of gasdermins. A prominent example is the targeting of gasdermin D (GSDMD) by inflammatory caspases-1/4/5/11 as an essential step in initiating pyroptosis following inflammasome activation.
Tsan Sam Xiao   +2 more
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Evolution of the gasdermin family and pyroptosis

Developmental & Comparative Immunology, 2023
Gasdermins have been identified as playing a prominent role in the innate immune response as the executors of a specific type of cell death called pyroptosis. Specific proteolytic cleavage of gasdermins generates an N-terminal that oligomerizes and forms pores in the cell membrane.
Angosto-Bazarra, Diego   +2 more
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