The C‐type lectin‐like domain superfamily
By A. Zelensky, Jill E. Gready. The FEBS Journal, 2005
1,351 citations recorded by the source corpus.
Subfields: Immunology, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/a163a96aa69334cd43273995f3165e10d473e6b9
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In Immunology
In Molecular Biology
Citations in the corpus
- Robust associations of four new chromosome regions from genome-wide analyses of type 1 diabetes (2007, background): “However, alignment of the domain across species suggested that this domain cannot be considered functional based on homology alon”
- Signalling through C-type lectin receptors: shaping immune responses (2009, background): “CLRs share at least one carbohydrate recognition domain, which is a compact structural module that contains conserved residue motifs and determines the carbohydrate specificity of the CL”
- Protein-glycan interactions in the control of innate and adaptive immune responses (2008, background): “C-type lectin receptors (CLRs) are calcium-dependent carbohydrate-binding proteins and consist of a large family of receptors (60–80) that is further divided into subfamilie”
- Insect immunity and its signalling: an overview (2010, background): “Analyses of the superfamily representation in several completely sequenced genomes have added 10 new groups (Zelensky and Gready, 2005).”
- Mincle is an ITAM-coupled activating receptor that senses damaged cells (2008, methodology): “(c,d) Immunoblot analysis of lysates of thioglycolate-elicited macrophages from wild-type mice (c) or FcgRI-FcgRIII double-deficient mice (Fcgr1–/–Fcgr3–/–) and FcRg-deficient mice, left unstimulated (0) or stimulated for 5 min with anti-Mincle and anti-rat IgG (5) (d).”