| pubmed-article:17417689 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17417689 | lifeskim:mentions | umls-concept:C0766850 | lld:lifeskim |
| pubmed-article:17417689 | pubmed:issue | 11 | lld:pubmed |
| pubmed-article:17417689 | pubmed:dateCreated | 2007-6-6 | lld:pubmed |
| pubmed-article:17417689 | pubmed:abstractText | Infection of bacteria triggers innate immune defense reactions in Drosophila. So far, the only bacterial component known to be recognized by the insect innate immune system is peptidoglycan, one of the most abundant constituents of the bacterial cell wall. Insects use peptidoglycan recognition proteins to detect peptidoglycan and to activate innate immune responses. Such specialized peptidoglycan receptors appear to have evolved from phage enzymes that hydrolyze bacterial cell walls. They are able to bind specific peptidoglycan molecules with distinct chemical moieties and activate innate immune pathways by interacting with other signaling proteins. Recent X-ray crystallographic studies of the peptidoglycan recognition proteins LCa, and LCx bound to peptidoglycan have provided structural insights into recognition of peptidoglycan and activation of innate immunity in insects. | lld:pubmed |
| pubmed-article:17417689 | pubmed:language | eng | lld:pubmed |
| pubmed-article:17417689 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17417689 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:17417689 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17417689 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17417689 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17417689 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17417689 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:17417689 | pubmed:issn | 1420-682X | lld:pubmed |
| pubmed-article:17417689 | pubmed:author | pubmed-author:DeisenhoferJJ | lld:pubmed |
| pubmed-article:17417689 | pubmed:author | pubmed-author:ChangC-ICI | lld:pubmed |
| pubmed-article:17417689 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:17417689 | pubmed:volume | 64 | lld:pubmed |
| pubmed-article:17417689 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17417689 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17417689 | pubmed:pagination | 1395-402 | lld:pubmed |
| pubmed-article:17417689 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
| pubmed-article:17417689 | pubmed:meshHeading | pubmed-meshheading:17417689... | lld:pubmed |
| pubmed-article:17417689 | pubmed:meshHeading | pubmed-meshheading:17417689... | lld:pubmed |
| pubmed-article:17417689 | pubmed:meshHeading | pubmed-meshheading:17417689... | lld:pubmed |
| pubmed-article:17417689 | pubmed:meshHeading | pubmed-meshheading:17417689... | lld:pubmed |
| pubmed-article:17417689 | pubmed:meshHeading | pubmed-meshheading:17417689... | lld:pubmed |
| pubmed-article:17417689 | pubmed:meshHeading | pubmed-meshheading:17417689... | lld:pubmed |
| pubmed-article:17417689 | pubmed:meshHeading | pubmed-meshheading:17417689... | lld:pubmed |
| pubmed-article:17417689 | pubmed:meshHeading | pubmed-meshheading:17417689... | lld:pubmed |
| pubmed-article:17417689 | pubmed:meshHeading | pubmed-meshheading:17417689... | lld:pubmed |
| pubmed-article:17417689 | pubmed:meshHeading | pubmed-meshheading:17417689... | lld:pubmed |
| pubmed-article:17417689 | pubmed:year | 2007 | lld:pubmed |
| pubmed-article:17417689 | pubmed:articleTitle | The peptidoglycan recognition proteins LCa and LCx. | lld:pubmed |
| pubmed-article:17417689 | pubmed:affiliation | Array Biopharma Inc, Boulder, CO 80301, USA. Chung-I.Chang@arraybiopharma.com | lld:pubmed |
| pubmed-article:17417689 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:17417689 | pubmed:publicationType | Review | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:17417689 | lld:pubmed |
