| http://purl.uniprot.org/citations/11773072 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/11773072 | http://www.w3.org/2000/01/rdf-schema#comment | "The bactericidal/permeability increasing (BPI) and lipopolysaccharide (LPS)-binding (LBP) proteins are closely related two-domain proteins in which LPS binding is mediated by the NH(2)-terminal domain. To further define the role of the COOH-terminal domain of these proteins in delivery of LPS to specific host acceptors, we have compared interactions of LBP, BPI, LBP(N)-BPI(C) (NH(2)-terminal domain of LBP, COOH-terminal domain of BPI), and BPI(N)-LBP(C) with purified (3)H-LPS and, subsequently, with purified leukocytes and soluble (s)CD14. The COOH-terminal domain of LBP promotes delivery of LPS to CD14 on both polymorphonuclear leukocytes and monocytes resulting in cell activation. In the presence of Ca(2+) and Mg(2+), LBP and BPI each promote aggregation of LPS to protein-LPS aggregates of increased size (apparent M(r) > 20 x 10(6) Da), but only LPS associated with LBP and BPI(N)-LBP(C) is disaggregated in the presence of CD14. BPI and LBP(N)-BPI(C) promote apparently CD14-independent LPS association to monocytes without cell activation. These findings demonstrate that the carboxyl-terminal domain of these closely related endotoxin-binding proteins dictates the route and host responses to complexes they form with endotoxin."xsd:string |
| http://purl.uniprot.org/citations/11773072 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m109622200"xsd:string |
| http://purl.uniprot.org/citations/11773072 | http://purl.uniprot.org/core/author | "Elsbach P."xsd:string |
| http://purl.uniprot.org/citations/11773072 | http://purl.uniprot.org/core/author | "Weiss J.P."xsd:string |
| http://purl.uniprot.org/citations/11773072 | http://purl.uniprot.org/core/author | "Eastvold J."xsd:string |
| http://purl.uniprot.org/citations/11773072 | http://purl.uniprot.org/core/author | "Gioannini T.L."xsd:string |
| http://purl.uniprot.org/citations/11773072 | http://purl.uniprot.org/core/author | "Iovine N."xsd:string |
| http://purl.uniprot.org/citations/11773072 | http://purl.uniprot.org/core/date | "2002"xsd:gYear |
| http://purl.uniprot.org/citations/11773072 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
| http://purl.uniprot.org/citations/11773072 | http://purl.uniprot.org/core/pages | "7970-7978"xsd:string |
| http://purl.uniprot.org/citations/11773072 | http://purl.uniprot.org/core/title | "The carboxyl-terminal domain of closely related endotoxin-binding proteins determines the target of protein-lipopolysaccharide complexes."xsd:string |
| http://purl.uniprot.org/citations/11773072 | http://purl.uniprot.org/core/volume | "277"xsd:string |
| http://purl.uniprot.org/citations/11773072 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/11773072 |
| http://purl.uniprot.org/citations/11773072 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/11773072 |
| http://purl.uniprot.org/uniprot/#_P18428-mappedCitation-11773072 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/11773072 |
| http://purl.uniprot.org/uniprot/#_Q8TCF0-mappedCitation-11773072 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/11773072 |
| http://purl.uniprot.org/uniprot/P18428 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/11773072 |
| http://purl.uniprot.org/uniprot/Q8TCF0 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/11773072 |