The gasdermins, a protein family executing cell death and inflammation

By Petr Brož, P. Pelegrín, F. Shao. Nature reviews. Immunology, 2019

1,405 citations recorded by the source corpus.

Subfields: Immunology, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/bbb5dc8e7c77bbe183fb20bb98717b79285c1c36

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In Immunology

1. V. Deretic
2. F. Shao

In Molecular Biology

1. V. Deretic
2. Jingjin Ding
3. Kun Wang
4. F. Shao
5. T. Kanneganti
6. Edward A. Miao

Citations in the corpus

• A guide to cell death pathways (2023, neutral): “Activated caspase-1 and caspase-11 can mediate the cleavage of gasdermin D (GSDMD) to remove an autoinhibitory carboxy-terminal domain from GSDMD, enabling the N-terminal fragment to form pores on the plasma membrane and resulting in pyroptosis 101,106–108 .”
• Pyroptosis in inflammatory diseases and cancer (2022, background): “Recently, Zhou et al found that GZMA derived from cytotoxic T lymphocytes cleaves GSDMB to form pores in the membrane, resulting in pyroptosis of GSDMB-expressing cancer cells [50].”
• Structural Mechanism for GSDMD Targeting by Autoprocessed Caspases in Pyroptosis. (2020, background): “GSDMD belongs to a gasdermin family that also includes GSDMA, GSDMB, GSDMC, GSDME, and DFNB59 (Broz et al., 2019).”
• Role of pyroptosis in inflammation and cancer (2022, background): “Gasdermins have strong sequence similarities with the autosomal DFNA5 (dominant nonsyndromic sensory nerve 5) gene that codes for a protein associated with human autosomal dominant nonsyndromic hearing loss [22, 24].”
• Granzyme A from cytotoxic lymphocytes cleaves GSDMB to trigger pyroptosis in target cells (2020, background): “Supporting the redefinition of pyroptosis, four other gasdermins (GSDMA, GSDMB, GSDMC, and GSDME) share the autoinhibited pore-forming domain but not the caspase-1/11 cleavage site (24, 28, 31).”
• Autophagy in inflammation, infection, and immunometabolism (2021, background): “, 2017) before GSDMD-pores and pyroptosis start to dominate in their release (Broz et al., 2020; Kayagaki et al., 2015; Shi et al., 2015), which appears to be a preferred way for IL-1β release by neutrophils (Karmakar et al.”