Results 301 to 310 of about 237,325 (347)

Medial septum parvalbumin‐expressing inhibitory neurons are impaired in a mouse model of Dravet syndrome

open access: yesEpilepsia, EarlyView.
Abstract Objective Dravet syndrome (DS) is a severe neurodevelopmental disorder caused by pathogenic variants in the SCN1A gene, which encodes the voltage‐gated sodium channel Nav1.1 α subunit. Experiments in animal models of DS—including the haploinsufficient Scn1a+/− mouse—have identified impaired excitability of interneurons in the hippocampus and ...
Limei Zhu   +5 more
wiley   +1 more source

Blood group O expression in normal tissues and tumors

open access: yesThe FEBS Journal, EarlyView.
The H antigen (O blood group), the precursor to A and B blood groups, is expressed on human erythrocytes. Two novel monoclonal antibodies generated using sea lamprey immunization, Tn4‐31L and OmcFL3‐02, specifically detect the H antigen on glycan microarrays, glycoproteins, and human cells.
Ea Kristine Clarisse Tulin   +11 more
wiley   +1 more source

C-TYPE LECTIN-2D RECEPTOR CONTRIBUTES TO HISTONE-INDUCED VASCULAR BARRIER DYSFUNCTION DURING BURN INJURY. [PDF]

open access: yesShock
Yang X   +9 more
europepmc   +1 more source

Abnormalities in C-type lectin-like receptor 2 in a patient with Gorham-Stout disease: the first case report. [PDF]

open access: yesRes Pract Thromb Haemost
Oishi S   +5 more
europepmc   +1 more source
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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.
Christoph Rademacher   +2 more
openaire   +3 more sources

C-Type Lectins [PDF]

open access: possible, 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 ...
Stephanie Zimmermann   +3 more
openaire   +1 more source

The C‐type lectin‐like domain superfamily

open access: yesFEBS Journal, 2005
The superfamily of proteins containing C‐type lectin‐like domains (CTLDs) is a large group of extracellular Metazoan proteins with diverse functions. The CTLD structure has a characteristic double‐loop (‘loop‐in‐a‐loop’) stabilized by two highly conserved disulfide bridges located at the bases of the loops, as well as a set of conserved hydrophobic and
Alex N Zelensky, Jill E Gready
exaly   +5 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

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 ...
Andrew J. Fadden, Kurt Drickamer
openaire   +3 more sources

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