Results 211 to 220 of about 30,240 (256)
Inflammatory and Immunological Basis of Periodontal Diseases
Journal of Periodontal Research, EarlyView.The periodontal lesion emerges as an evolving immunological battlefield, where host–microbiome interactions, dysregulated immune responses, fragile resolution mechanisms, and inflammophilic dysbiosis converge to shift the balance from homeostasis to unrestrained tissue destruction.
Giacomo Baima +3 more
wiley +1 more source
Autoimmunity and Periodontitis
Journal of Periodontal Research, EarlyView.In a microbe‐driven inflammatory environment, peptidyl‐arginine deiminase (PAD) enzymes from neutrophils and Porphyromonas gingivalis citrullinate both microbial and self‐antigens. B cell presentation of citrullinated or self‐mimicking epitopes activates T cells that assist B cells in antibody isotype switching, affinity maturation, epitope spreading ...
Massimo Costalonga +2 more
wiley +1 more source
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Myeloid C-type lectins in innate immunity
Nature Immunology, 2006C-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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Insect C-type lectins in innate immunity
Developmental & Comparative Immunology, 2018C-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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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.
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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.
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C-Type Lectin Receptors in Phagocytosis
2020C-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
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Genomic analysis of C-type lectins
Biochemical Society Symposia, 2002Many 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
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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 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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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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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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Insect C-Type Lectins in Microbial Infections
2020C-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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