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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
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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
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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
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Myeloid C-type lectins in innate immunity

Nature 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
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C-type lectin-like domains

Current Opinion in Structural Biology, 1999
Carbohydrate-recognition domains of C-type (Ca2+-dependent) animal lectins serve as prototypes for an important family of protein modules. Only some domains in this family bind Ca2+ or sugars. A comparison of recent structures of C-type lectin-like domains reveals diversity in the modular fold, particularly in the region associated with Ca2+ and sugar ...
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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
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The C-Type Lectin Receptors

C-type lectins (CTLs) form a broad and diverse protein superfamily with the ability to identify a wide array of ligands with their characteristic C-type lectin-like domains (CTLDs), thus governing a broad spectrum of physiological functions. CTLD-containing proteins (CTLDcps) are now classified into 17 groups based on their phylogeny and overall domain
Kasturi, Ganguly, Taruna, Madan
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C-type Lectins in Immunity to Lung Pathogens

2020
The respiratory tract is tasked with responding to a constant and vast influx of foreign agents. It acts as an important first line of defense in the innate immune system and as such plays a crucial role in preventing the entry of invading pathogens.
Raymond, Benjamin   +2 more
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Insect C-type lectins in innate immunity

Developmental & Comparative Immunology, 2018
C-type lectins (CTLs) are a family of proteins that contain characteristic modules of carbohydrate-recognition domains (CRDs) and they possess the binding activity to ligands in a calcium-dependent manner. CTLs play important roles in animal immune responses, and in insects, they are involved in opsonization, nodule formation, agglutination ...
Xiaofeng Xia   +3 more
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The C‐type lectin superfamily in the immune system

Immunological Reviews, 1998
Summary: Protein‐carbohydrate interactions serve multiple functions in the immune system. Many animal lectins (sugar‐binding proteins) mediate both pathogen recognition and cell‐cell interactions using structurally related Ca2+‐dependent carbohydrate‐recognition domains (C‐type CRDs).
W I, Weis, M E, Taylor, K, Drickamer
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