About: C-Type Lectin Receptors

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Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	C-Type Lectin Receptors
Creator	Kanazawa, Nobuo
Source	PMC
abstract	C-type lectins, originally defined as proteins binding carbohydrates in a Ca(2+)-dependent manner, form a large family containing soluble and membrane-bound proteins. Among them, those expressed on phagocytes and working as pathogen pattern-recognition receptors were designated as C-type lectin receptors (CLRs), in accordance with Toll-like receptors (TLRs), NOD-like receptors (NLRs), and RIG-I–like receptors (RLRs). Most of the genes for CLRs are clustered in human chromosome 12 close to the natural killer gene complex. Similar to the killer lectin-like receptors whose genes are clustered in this complex, most of the CLRs induce activating or regulatory signal cascades in response to distinct pathogen- or self-derived components, through the immunoreceptor tyrosine-based activating or inhibitory motif, respectively. In this chapter, some representative CLRs are picked up and their structural features leading to the functional consequences are discussed, especially on the signaling cascades and pathogen interactions, including some impacts on cutaneous pathophysiology. These CLRs should provide targets to develop effective vaccination and therapeutics for distinct infectious and autoimmune/inflammatory diseases.
has issue date	2015-11-30(xsd:dateTime)
bibo:doi	10.1007/978-4-431-55855-2_17
has license	no-cc
sha1sum (hex)	b9b83b283be6f7a780dfb2f6f86df6e4cd119e7a
schema:url	https://doi.org/10.1007/978-4-431-55855-2_17
resource representing a document's title	C-Type Lectin Receptors
has PubMed Central identifier	PMC7121771
schema:publication	Immunology of the Skin
resource representing a document's body	covid:b9b83b283be6f7a780dfb2f6f86df6e4cd119e7a#body_text
is schema:about of	named entity 'lectins' named entity 'FORM' named entity 'SOLUBLE' named entity 'DEFINED' named entity 'CONTAINING' named entity 'BINDING' named entity 'PROTEINS' named entity 'LECTINS' named entity 'CARBOHYDRATES' named entity 'TYPE' named entity 'LECTIN' named entity 'TYPE' named entity 'DEPENDENT' named entity 'LARGE FAMILY' named entity 'RECEPTORS' named entity 'defined' named entity 'proteins' named entity 'proteins' named entity 'C-type lectins' named entity 'C-Type Lectin' named entity 'binding' named entity 'pDCs' named entity 'pathogen-associated molecular patterns' named entity 'mAb' named entity 'immunohistochemically' named entity 'Malt1' named entity 'pDCs' named entity 'langerin' named entity 'TNF-related apoptosis-inducing ligand' named entity 'DC-SIGN' named entity 'tyrosine' named entity 'glycoprotein gp120' named entity 'pDCs' named entity 'Candida albicans' named entity 'allele frequency' named entity 'FcRγ' named entity 'IL-23' named entity 'BDCA-2' named entity 'tuberculosis' named entity 'mincle' named entity 'DCs' named entity 'major histocompatibility complex' named entity 'adhesion molecules' named entity 'carbohydrates' named entity 'DCs' named entity 'ITAM' named entity 'murine' named entity 'myeloid cells' named entity 'mice' named entity 'DCIR' named entity 'mutation' named entity 'murine' named entity 'autoimmune' named entity 'CD94' named entity 'M. tuberculosis' named entity 'IL-12' named entity 'caspase recruitment domain' named entity 'CLRs' named entity 'lectin' named entity 'germinal center' named entity 'neutrophils' named entity 'Schistosoma mansoni' named entity 'CpG' named entity 'calcium influx' named entity 'autoimmune' named entity 'Cryptococcus neoformans' named entity 'CpG' named entity 'dectin-1' named entity 'monocytes' named entity 'Dectin' named entity 'Helicobacter pylori' named entity 'HCV' named entity 'PAMPs' named entity 'proline' named entity 'signaling cascade' named entity 'nitric oxide' named entity 'DCs' named entity 'DC-SIGN' named entity 'sialic acids' named entity 'virion' named entity 'HIV-1' named entity 'dectin' named entity 'FcR'

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