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RIPK1 counteracts ZBP1-mediated necroptosis to inhibit inflammation

Author

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  • Juan Lin

    (Institute for Genetics, Centre for Molecular Medicine (CMMC), and Cologne Excellence Cluster on Cellular Stress Responses in Aging-Associated Diseases (CECAD), University of Cologne)

  • Snehlata Kumari

    (Institute for Genetics, Centre for Molecular Medicine (CMMC), and Cologne Excellence Cluster on Cellular Stress Responses in Aging-Associated Diseases (CECAD), University of Cologne)

  • Chun Kim

    (Institute for Genetics, Centre for Molecular Medicine (CMMC), and Cologne Excellence Cluster on Cellular Stress Responses in Aging-Associated Diseases (CECAD), University of Cologne)

  • Trieu-My Van

    (Institute for Genetics, Centre for Molecular Medicine (CMMC), and Cologne Excellence Cluster on Cellular Stress Responses in Aging-Associated Diseases (CECAD), University of Cologne)

  • Laurens Wachsmuth

    (Institute for Genetics, Centre for Molecular Medicine (CMMC), and Cologne Excellence Cluster on Cellular Stress Responses in Aging-Associated Diseases (CECAD), University of Cologne)

  • Apostolos Polykratis

    (Institute for Genetics, Centre for Molecular Medicine (CMMC), and Cologne Excellence Cluster on Cellular Stress Responses in Aging-Associated Diseases (CECAD), University of Cologne)

  • Manolis Pasparakis

    (Institute for Genetics, Centre for Molecular Medicine (CMMC), and Cologne Excellence Cluster on Cellular Stress Responses in Aging-Associated Diseases (CECAD), University of Cologne)

Abstract

The enzyme RIPK1 functions through its RHIM domain to prevent ZBP1-mediated activation of RIPK3–MLKL-dependent necroptosis, thus preventing perinatal lethality and skin inflammation in adult mice.

Suggested Citation

  • Juan Lin & Snehlata Kumari & Chun Kim & Trieu-My Van & Laurens Wachsmuth & Apostolos Polykratis & Manolis Pasparakis, 2016. "RIPK1 counteracts ZBP1-mediated necroptosis to inhibit inflammation," Nature, Nature, vol. 540(7631), pages 124-128, December.
    • Handle: RePEc:nat:nature:v:540:y:2016:i:7631:d:10.1038_nature20558
    DOI: 10.1038/nature20558
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    Cited by:

    1. Yanxiang Meng & Sarah E. Garnish & Katherine A. Davies & Katrina A. Black & Andrew P. Leis & Christopher R. Horne & Joanne M. Hildebrand & Hanadi Hoblos & Cheree Fitzgibbon & Samuel N. Young & Toby Di, 2023. "Phosphorylation-dependent pseudokinase domain dimerization drives full-length MLKL oligomerization," Nature Communications, Nature, vol. 14(1), pages 1-18, December.

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