{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Rambaruth ND"],"funding":["Biotechnology and Biological Sciences Research Council"],"pagination":["6670-82"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC4533885"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["20(4)"],"pubmed_abstract":["Mincle, the macrophage-inducible C-type lectin also known as CLEC-4E, binds to the mycobacterial glycolipid trehalose dimycolate and initiates a signaling cascade by serving as a receptor for Mycobacterium tuberculosis and other pathogenic mycobacterial species. Studies of the biological functions of human mincle often rely on mouse models, based on the assumption that the biological properties of the mouse receptor mimic those of the human protein. Experimental support for this assumption has been obtained by expression of the carbohydrate-recognition domain of mouse mincle and characterization of its interaction with small molecule analogs of trehalose dimycolate. The results confirm that the ligand-binding properties of mouse mincle closely parallel those of the human receptor. These fi"],"journal":["Molecules (Basel, Switzerland)"],"pubmed_title":["Mouse mincle: characterization as a model for human mincle and evolutionary implications."],"pmcid":["PMC4533885"],"funding_grant_id":["BB/K007718/1"],"pubmed_authors":["Taylor ME","Rambaruth ND","Marlor H","Drickamer K","Jegouzo SA"],"additional_accession":[]},"is_claimable":false,"name":"Mouse mincle: characterization as a model for human mincle and evolutionary implications.","description":"Mincle, the macrophage-inducible C-type lectin also known as CLEC-4E, binds to the mycobacterial glycolipid trehalose dimycolate and initiates a signaling cascade by serving as a receptor for Mycobacterium tuberculosis and other pathogenic mycobacterial species. Studies of the biological functions of human mincle often rely on mouse models, based on the assumption that the biological properties of the mouse receptor mimic those of the human protein. Experimental support for this assumption has been obtained by expression of the carbohydrate-recognition domain of mouse mincle and characterization of its interaction with small molecule analogs of trehalose dimycolate. The results confirm that the ligand-binding properties of mouse mincle closely parallel those of the human receptor. These fi","dates":{"release":"2015-01-01T00:00:00Z","publication":"2015 Apr","modification":"2025-04-04T09:39:30.983Z","creation":"2019-03-27T00:10:11Z"},"accession":"S-EPMC4533885","cross_references":{"pubmed":["25884549"],"doi":["10.3390/molecules20046670"]}}