ArticleImmunity2020
Immune Sensing of Cell Death through Recognition of Histone Sequences by C-Type Lectin-Receptor-2d Causes Inflammation and Tissue Injury.
Article in Immunity, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.
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Who cites it
50 citing papers in PubMed, 86 citations in OpenAlex.
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- Characterization of NLRP3 Inflammasome-Associated Hub Genes in the Progression of Diabetic Nephropathy.Immunity, inflammation and disease · 2026Article
- C-type lectin-like domain family 2 (CLEC2D) promotes proliferation and migration of breast cancer and serves as a poor prognostic factor.Breast cancer (Tokyo, Japan) · 2026Article
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- Research progress on the cross-regulation between ferroptosis and immunogenic cell death in tumor micro-environment.Frontiers in oncology · 2025Review
- Single-cell RNA sequencing of peripheral blood links cell-type-specific regulation of splicing to autoimmune and inflammatory diseases.Nature genetics · 2024Article
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- DAMP sensing and sterile inflammation: intracellular, intercellular and inter-organ pathways.Nature reviews. Immunology · 2024Review
- Innate immune sensing of cell death in disease and therapeutics.Nature cell biology · 2024Review
- Systemic mechanisms of necrotic cell debris clearance.Cell death & disease · 2024Review
- Extracellular histones promote TWIK2-dependent potassium efflux and associated NLRP3 activation in alveolar macrophages during sepsis-induced lung injury.Inflammation research : official journal of the European Histamine Research Society ... [et al.] · 2024Article
- naRNA-LL37 composite DAMPs define sterile NETs as self-propagating drivers of inflammation.EMBO reports · 2024Article
- C-type lectin 2D (CLEC2D) is upregulated in clear cell renal cell carcinoma (ccRCC) tissues and predicts poor prognosis.Heliyon · 2024Article
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3 authors at 1 institution in 1 country.
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Abstract
The immune system monitors the health of cells and is stimulated by necrosis. Here we examined the receptors and ligands driving this response. In a targeted screen of C-type lectin receptors, a Clec2d reporter responded to lysates from necrotic cells. Biochemical purification identified histones, both free and bound to nucleosomes or neutrophil extracellular traps, as Clec2d ligands. Clec2d recognized poly-basic sequences in histone tails and this recognition was sensitive to post-translational modifications of these sequences. As compared with WT mice, Clec2d
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