Neutrophil granules: a library of innate immunity proteins.
By N. Borregaard, O. Sørensen, K. Theilgaard-Mönch. Trends in immunology, 2007
741 citations recorded by the source corpus.
Subfields: Immunology, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/e20a1865af7117bf9ad2cdcf8b02cede33d703bc
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Citations in the corpus
- Arginase I–Producing Myeloid-Derived Suppressor Cells in Renal Cell Carcinoma Are a Subpopulation of Activated Granulocytes (2009, neutral): “removal and the resolution of inflammation (22, 23).”
- Arginase: an emerging key player in the mammalian immune system (2009, background): “Arginase I shares this feature with other important constitutive PMN proteins or peptides involved in inflammation and microbial defense like human cationic anti-microbial protein of 18 kDa (hCAP18), neutrophil gelatinase-associated lipocalin (NGAL), bactericidal/ permeability-increasing protein (BP”
- Blood-brain barrier pathophysiology in traumatic brain injury (2011, background): “Similar results were obtained in Mmp9−/− mice or in chimeras, in which bone marrow from MMP9-deficient mice was transplanted into wildtype animals [196].”
- Neutrophils, from marrow to microbes. (2010, background): “…cells (TREM-1) (by ligands not yet identified; Ford and McVicar, 2009), which is upregulated (Bouchon et al., 2000, 2001) and signals through DAP12 (presented earlier) (Bouchon et al., 2000; Tessarz and Cerwenka, 2008), may lead to degranulation and transcriptional activity (Bouchon et al., 2000).”
- Diverse novel functions of neutrophils in immunity, inflammation, and beyond (2013, background): “The interaction between human neutrophils and DCs has been proposed to be at least in part mediated by a unique interaction between DC-SIGN and Mac-1 on the neutrophil surface (van Gisbergen et al., 2005a,b; Boudaly, 2009; Yang et al., 2009; Fig.”
- Leukocyte migration into inflamed tissues. (2014, background): “Specifically, because blood leukocytes are a rich source of preformed granular chemoattractants, such as cathepsin G, LL-37, and azurocidin (Borregaard et al., 2007; Soehnlein et al., 2008), and can also release lipid and protein chemotactic molecules (e.”