Mausita Karmakar, Martin Minns, Elyse N Greenberg, Jose Diaz-Aponte, Kersi Pestonjamasp, Jennifer L Johnson, Joseph K Rathkey, Derek W Abbott, Kun Wang, Feng Shao, Sergio D Catz, George R Dubyak, Eric Pearlman. Nat Commun 2020
Times Cited: 94
Times Cited: 94
Times Cited
Times Co-cited
Similarity
Cleavage of GSDMD by inflammatory caspases determines pyroptotic cell death.
Jianjin Shi, Yue Zhao, Kun Wang, Xuyan Shi, Yue Wang, Huanwei Huang, Yinghua Zhuang, Tao Cai, Fengchao Wang, Feng Shao. Nature 2015
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Inflammasome-activated gasdermin D causes pyroptosis by forming membrane pores.
Xing Liu, Zhibin Zhang, Jianbin Ruan, Youdong Pan, Venkat Giri Magupalli, Hao Wu, Judy Lieberman. Nature 2016
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Caspase-11 cleaves gasdermin D for non-canonical inflammasome signalling.
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Pore-forming activity and structural autoinhibition of the gasdermin family.
Jingjin Ding, Kun Wang, Wang Liu, Yang She, Qi Sun, Jianjin Shi, Hanzi Sun, Da-Cheng Wang, Feng Shao. Nature 2016
Jingjin Ding, Kun Wang, Wang Liu, Yang She, Qi Sun, Jianjin Shi, Hanzi Sun, Da-Cheng Wang, Feng Shao. Nature 2016
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The Pore-Forming Protein Gasdermin D Regulates Interleukin-1 Secretion from Living Macrophages.
Charles L Evavold, Jianbin Ruan, Yunhao Tan, Shiyu Xia, Hao Wu, Jonathan C Kagan. Immunity 2018
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Noncanonical inflammasome signaling elicits gasdermin D-dependent neutrophil extracellular traps.
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The neutrophil NLRC4 inflammasome selectively promotes IL-1β maturation without pyroptosis during acute Salmonella challenge.
Kaiwen W Chen, Christina J Groß, Flor Vásquez Sotomayor, Katryn J Stacey, Jurg Tschopp, Matthew J Sweet, Kate Schroder. Cell Rep 2014
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Chemotherapy drugs induce pyroptosis through caspase-3 cleavage of a gasdermin.
Yupeng Wang, Wenqing Gao, Xuyan Shi, Jingjin Ding, Wang Liu, Huabin He, Kun Wang, Feng Shao. Nature 2017
Yupeng Wang, Wenqing Gao, Xuyan Shi, Jingjin Ding, Wang Liu, Huabin He, Kun Wang, Feng Shao. Nature 2017
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Gasdermin D is an executor of pyroptosis and required for interleukin-1β secretion.
Wan-ting He, Haoqiang Wan, Lichen Hu, Pengda Chen, Xin Wang, Zhe Huang, Zhang-Hua Yang, Chuan-Qi Zhong, Jiahuai Han. Cell Res 2015
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The gasdermins, a protein family executing cell death and inflammation.
Petr Broz, Pablo Pelegrín, Feng Shao. Nat Rev Immunol 2020
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Pathogen blockade of TAK1 triggers caspase-8-dependent cleavage of gasdermin D and cell death.
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ESCRT-dependent membrane repair negatively regulates pyroptosis downstream of GSDMD activation.
Sebastian Rühl, Kateryna Shkarina, Benjamin Demarco, Rosalie Heilig, José Carlos Santos, Petr Broz. Science 2018
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Gasdermin D plays a vital role in the generation of neutrophil extracellular traps.
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GSDMD membrane pore formation constitutes the mechanism of pyroptotic cell death.
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Caspase-8 induces cleavage of gasdermin D to elicit pyroptosis during Yersinia infection.
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Non-canonical inflammasome activation targets caspase-11.
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Gasdermin E suppresses tumour growth by activating anti-tumour immunity.
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Gasdermin pores permeabilize mitochondria to augment caspase-3 activation during apoptosis and inflammasome activation.
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GsdmD p30 elicited by caspase-11 during pyroptosis forms pores in membranes.
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FDA-approved disulfiram inhibits pyroptosis by blocking gasdermin D pore formation.
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Inflammatory caspases are innate immune receptors for intracellular LPS.
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Granzyme A from cytotoxic lymphocytes cleaves GSDMB to trigger pyroptosis in target cells.
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Pyroptosis: Gasdermin-Mediated Programmed Necrotic Cell Death.
Jianjin Shi, Wenqing Gao, Feng Shao. Trends Biochem Sci 2017
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Pyroptosis and Apoptosis Pathways Engage in Bidirectional Crosstalk in Monocytes and Macrophages.
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Caspase-1 initiates apoptosis in the absence of gasdermin D.
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Cryo-EM structure of the gasdermin A3 membrane pore.
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Co-cited is the co-citation frequency, indicating how many articles cite the article together with the query article. Similarity is the co-citation as percentage of the times cited of the query article or the article in the search results, whichever is the lowest. These numbers are calculated for the last 100 citations when articles are cited more than 100 times.