GsdmD p30 elicited by caspase-11 during pyroptosis forms pores in membranes

By R. Aglietti, A. Estevez, Aaron Gupta, Monica L Gonzalez Ramirez, Peter S. Liu, N. Kayagaki, C. Ciferri, V. Dixit, E. Dueber. Proceedings of the National Academy of Sciences of the United States of America, 2016

816 citations recorded by the source corpus.

Subfields: Molecular Biology, Physiology, Public Health, Environmental and Occupational Health

View Paper: https://www.semanticscholar.org/paper/6cae9526e6414cff61dbbd507f90bb7d3cf232a9

How researchers see this paper

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In Molecular Biology

1. M. Lamkanfi
2. Edward A. Miao
3. F. Shao
4. S. B. Kovacs
5. N. Van Opdenbosch
6. Wenqing Gao
7. Douglas R. Green
8. S. Bunnell

In Physiology

1. M. Lamkanfi
2. Douglas R. Green

In Public Health, Environmental and Occupational Health

1. Douglas R. Green

Citations in the corpus

• Gasdermins: Effectors of pyroptosis (2017, background): “The liberated PFD then integrates into the cell membrane, where an estimated 16 PFD monomers oligomerize to form a large 10–15 nm diameter pore[15,18,19]; another group suggests 21 nm[20].”
• The pore forming protein gasdermin D regulates interleukin-1 secretion from living macrophages (2017, neutral): “Upon cleavage, the N-terminal fragment of GSDMD oligomerizes into ring-shaped structures in membranes (Aglietti et al., 2016; Ding et al., 2016; Liu et al., 2016; Sborgi et al., 2016).”