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Myeloid C-type lectins in innate immunity

open access: yesNature Immunology, 2006
C-type lectins expressed on myeloid cells comprise a family of proteins that share a common structural motif, and some act as receptors in pathogen recognition. But just as the presence of leucine-rich repeats alone is not sufficient to define a Toll-like receptor, the characterization of C-type lectin receptors in innate immunity requires the ...
Robinson, Matthew J   +4 more
openaire   +3 more sources

An evolutionary perspective on C‐type lectins in infection and immunity

open access: yesAnnals of the New York Academy of Sciences, 2012
Host–pathogen interactions have coevolved for many years. On the one hand, the human immune system consists of innate and adaptive immune cells that function to defeat pathogens, and on the other hand, pathogens have coevolved to use the system for their own propagation.
van den Berg, Linda M.   +2 more
openaire   +3 more sources
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Allostery in C-type lectins

Current Opinion in Structural Biology, 2020
C-type lectins are the largest and most diverse family of mammalian carbohydrate-binding proteins. They share a common protein fold, which provides the unifying basis for calcium-mediated carbohydrate recognition. Their involvement in a multitude of biological functions is remarkable.
Keller, B., Rademacher, C.
openaire   +3 more sources

Genomic analysis of C-type lectins

Biochemical Society Symposia, 2002
Many biological effects of complex carbohydrates are mediated by lectins that contain discrete carbohydrate-recognition domains. At least seven structurally distinct families of carbohydrate-recognition domains are found in lectins that are involved in intracellular trafficking, cell adhesion, cell–cell signalling, glycoprotein turnover and innate ...
Kurt, Drickamer, Andrew J, Fadden
openaire   +2 more sources

C-Type Lectin Receptors in Phagocytosis

2020
C-type lectin receptors (CLRs) are a family of transmembrane proteins having at least one C-type lectin-like domain (CTLD) on the cell surface and either a short intracellular signaling tail or a transmembrane domain that facilitates interaction with a second protein, often the Fc receptor common gamma chain (FcRγ), that mediates signaling.
Kai, Li, David M, Underhill
openaire   +2 more sources

C-type lectin receptors in antifungal immunity

Trends in Microbiology, 2008
Fungal infections represent a significant health burden, especially in immunocompromised individuals, yet many of the underlying immunological mechanisms involved in the recognition and control of these pathogens are unclear. The identification of the Toll-like receptors (TLRs) has shed new insights on innate microbial recognition and the initiation of
Janet A, Willment, Gordon D, Brown
openaire   +2 more sources

C-Type Lectins

2014
C-type lectins belong to a superfamily of receptors that share structural homology in their carbohydrate recognition domains and often bind to carbohydrates in a Ca-dependent fashion. Whereas endocytic C-type lectin receptors (CLRs) trigger the receptor-mediated endocytosis of soluble ligands, myeloid CLRs in innate immunity act as pattern recognition ...
Timo Johannssen   +3 more
openaire   +1 more source

C-Type Lectin Receptors in Antifungal Immunity

2020
Most fungal species are harmless to humans and some exist as commensals on mucocutaneous surfaces. Yet many fungi are opportunistic pathogens, causing life-threatening invasive infections when the immune system becomes compromised. The fungal cell wall contains conserved pathogen-associated molecular patterns (PAMPs), which allow the immune system to ...
Christina, Nikolakopoulou   +2 more
openaire   +2 more sources

Insect C-Type Lectins in Microbial Infections

2020
C-type lectins (CTLs) are a family of carbohydrate-recognition domain (CRD)-containing proteins that bind to ligands in a calcium-dependent manner. CTLs act as important components of insect innate immune responses, such as pattern recognition, agglutination, encapsulation, melanization, phagocytosis and prophenoloxidase activation, as well as gut ...
Yibin, Zhu, Xi, Yu, Gong, Cheng
openaire   +2 more sources

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