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http://purl.uniprot.org/citations/15843462http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15843462http://www.w3.org/2000/01/rdf-schema#comment"Drosophila knockout mutants have placed peptidoglycan recognition proteins (PGRPs) in the two major pathways controlling immune gene expression. We now examine PGRP affinities for peptidoglycan. PGRP-SA and PGRP-LCx are bona fide pattern recognition receptors, and PGRP-SA, the peptidoglycan receptor of the Toll/Dif pathway, has selective affinity for different peptidoglycans. PGRP-LCx, the default peptidoglycan receptor of the Imd/Relish pathway, has strong affinity for all polymeric peptidoglycans tested and for monomeric peptidoglycan. PGRP-LCa does not have affinity for polymeric or monomeric peptidoglycan. Instead, PGRP-LCa can form heterodimers with LCx when the latter is bound to monomeric peptidoglycan. Hence, PGRP-LCa can be said to function as an adaptor, thus adding a new function to a member of the PGRP family."xsd:string
http://purl.uniprot.org/citations/15843462http://purl.org/dc/terms/identifier"doi:10.1073/pnas.0407559102"xsd:string
http://purl.uniprot.org/citations/15843462http://purl.uniprot.org/core/author"Goldman W.E."xsd:string
http://purl.uniprot.org/citations/15843462http://purl.uniprot.org/core/author"Schultz N."xsd:string
http://purl.uniprot.org/citations/15843462http://purl.uniprot.org/core/author"Karlsson J."xsd:string
http://purl.uniprot.org/citations/15843462http://purl.uniprot.org/core/author"Steiner H."xsd:string
http://purl.uniprot.org/citations/15843462http://purl.uniprot.org/core/author"Mellroth P."xsd:string
http://purl.uniprot.org/citations/15843462http://purl.uniprot.org/core/author"Hakansson J."xsd:string
http://purl.uniprot.org/citations/15843462http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/15843462http://purl.uniprot.org/core/name"Proc Natl Acad Sci U S A"xsd:string
http://purl.uniprot.org/citations/15843462http://purl.uniprot.org/core/pages"6455-6460"xsd:string
http://purl.uniprot.org/citations/15843462http://purl.uniprot.org/core/title"Ligand-induced dimerization of Drosophila peptidoglycan recognition proteins in vitro."xsd:string
http://purl.uniprot.org/citations/15843462http://purl.uniprot.org/core/volume"102"xsd:string
http://purl.uniprot.org/citations/15843462http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/15843462
http://purl.uniprot.org/citations/15843462http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/15843462
http://purl.uniprot.org/uniprot/Q9GNK5#attribution-D8EA9734BD3D040AD4846DD0BEE8C576http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/15843462
http://purl.uniprot.org/uniprot/Q9VYX7#attribution-D8EA9734BD3D040AD4846DD0BEE8C576http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/15843462
http://purl.uniprot.org/uniprot/#_A0A0B4KHY4-mappedCitation-15843462http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/15843462
http://purl.uniprot.org/uniprot/#_A0A0S0WMR4-mappedCitation-15843462http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/15843462
http://purl.uniprot.org/uniprot/#_E1JHK1-mappedCitation-15843462http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/15843462
http://purl.uniprot.org/uniprot/#_E1JHK2-mappedCitation-15843462http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/15843462
http://purl.uniprot.org/uniprot/#_A0A2U8U0I3-mappedCitation-15843462http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/15843462
http://purl.uniprot.org/uniprot/#_A0A2U8U141-mappedCitation-15843462http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/15843462
http://purl.uniprot.org/uniprot/#_E1JI87-mappedCitation-15843462http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/15843462