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Gasdermins and cancers

Seminars in Immunology, 2023
The identification of gasdermin as the executor of pyroptosis has opened new avenues for the study of this process. Although pyroptosis research has mainly focused on immune cells since it was discovered three decades ago, accumulating evidence suggests that pyroptosis plays crucial roles in many biological processes.
Junwei Hou   +4 more
openaire   +2 more sources

Coral gasdermin triggers pyroptosis

Science Immunology, 2020
Coral gasdermin is activated by caspase 3 and involved in pathogen-induced coral death.
Shuai Jiang, Zhi Zhou, Li Sun
exaly   +3 more sources

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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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
openaire   +2 more sources

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
openaire   +2 more sources

Gasdermin and Gasdermin-Like Pore-Forming Proteins in Invertebrates, Fungi and Bacteria

Journal of Molecular Biology, 2022
The gasdermin family of pore-forming proteins (PFPs) has recently emerged as key molecular players controlling immune-related cell death in mammals. Characterized mammalian gasdermins are activated through proteolytic cleavage by caspases or serine proteases, which remove an inhibitory carboxy-terminal domain, allowing the pore-formation process ...
Asen, Daskalov, N Louise, Glass
openaire   +2 more sources

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
openaire   +2 more sources

Gasdermins and pyroptosis in the kidney

Nature Reviews Nephrology, 2023
Pyroptosis is a form of regulated cell death that is mediated by the membrane-targeting, pore-forming gasdermin family of proteins. Pyroptosis was initially described as a caspase 1- and inflammasome-dependent cell death pathway typified by the loss of membrane integrity and the secretion of cytokines such as IL-1β.
Esteban E. Elias   +2 more
openaire   +2 more sources

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
openaire   +2 more sources

Mechanisms of Gasdermin Recognition by Proteases

Journal of Molecular Biology, 2022
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
Zhonghua, Liu   +3 more
openaire   +2 more sources

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