| pubmed-article:11401035 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11401035 | lifeskim:mentions | umls-concept:C0016452 | lld:lifeskim |
| pubmed-article:11401035 | lifeskim:mentions | umls-concept:C0524637 | lld:lifeskim |
| pubmed-article:11401035 | lifeskim:mentions | umls-concept:C0031308 | lld:lifeskim |
| pubmed-article:11401035 | lifeskim:mentions | umls-concept:C0017968 | lld:lifeskim |
| pubmed-article:11401035 | lifeskim:mentions | umls-concept:C0205263 | lld:lifeskim |
| pubmed-article:11401035 | lifeskim:mentions | umls-concept:C1314939 | lld:lifeskim |
| pubmed-article:11401035 | lifeskim:mentions | umls-concept:C1489709 | lld:lifeskim |
| pubmed-article:11401035 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:11401035 | pubmed:dateCreated | 2001-6-12 | lld:pubmed |
| pubmed-article:11401035 | pubmed:abstractText | A 40-kDa glycoprotein (gp40) was identified as a Con A-binding adhesive substance of the heliozoon Actinophrys sol for immobilizing and ingesting prey flagellates. Isolation and partial characterization of gp40 showed that: 1) gp40 is a major Con A-binding protein of Actinophrys with a molecular weight of 40 kDa, and is stored in secretory granules called extrusomes; 2) gp40 was purified by Con A-affinity chromatography, and the N-terminal amino acid sequence was determined as H2N-KVLK-FEDDFDTFDLQ; 3) prey flagellates became adhered to gp40-immobilized agarose beads; 4) phagocytosis of Actinophrys was induced against gp40-immobilized agarose beads; and 5) solubilized gp40 induced exocytosis of extrusomes and cell fusion of heliozoons. These results indicate that gp40 is a multi-functional secretory protein of Actinophrys, which is required in correct targeting of the heliozoon to food organisms as well as in self-recognition. | lld:pubmed |
| pubmed-article:11401035 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11401035 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11401035 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:11401035 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11401035 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11401035 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11401035 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11401035 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11401035 | pubmed:month | May | lld:pubmed |
| pubmed-article:11401035 | pubmed:issn | 1434-4610 | lld:pubmed |
| pubmed-article:11401035 | pubmed:author | pubmed-author:MurakamiHH | lld:pubmed |
| pubmed-article:11401035 | pubmed:author | pubmed-author:SuzakiTT | lld:pubmed |
| pubmed-article:11401035 | pubmed:author | pubmed-author:SakaguchiMM | lld:pubmed |
| pubmed-article:11401035 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11401035 | pubmed:volume | 152 | lld:pubmed |
| pubmed-article:11401035 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11401035 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11401035 | pubmed:pagination | 33-41 | lld:pubmed |
| pubmed-article:11401035 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
| pubmed-article:11401035 | pubmed:meshHeading | pubmed-meshheading:11401035... | lld:pubmed |
| pubmed-article:11401035 | pubmed:meshHeading | pubmed-meshheading:11401035... | lld:pubmed |
| pubmed-article:11401035 | pubmed:meshHeading | pubmed-meshheading:11401035... | lld:pubmed |
| pubmed-article:11401035 | pubmed:meshHeading | pubmed-meshheading:11401035... | lld:pubmed |
| pubmed-article:11401035 | pubmed:meshHeading | pubmed-meshheading:11401035... | lld:pubmed |
| pubmed-article:11401035 | pubmed:meshHeading | pubmed-meshheading:11401035... | lld:pubmed |
| pubmed-article:11401035 | pubmed:meshHeading | pubmed-meshheading:11401035... | lld:pubmed |
| pubmed-article:11401035 | pubmed:meshHeading | pubmed-meshheading:11401035... | lld:pubmed |
| pubmed-article:11401035 | pubmed:meshHeading | pubmed-meshheading:11401035... | lld:pubmed |
| pubmed-article:11401035 | pubmed:meshHeading | pubmed-meshheading:11401035... | lld:pubmed |
| pubmed-article:11401035 | pubmed:meshHeading | pubmed-meshheading:11401035... | lld:pubmed |
| pubmed-article:11401035 | pubmed:meshHeading | pubmed-meshheading:11401035... | lld:pubmed |
| pubmed-article:11401035 | pubmed:meshHeading | pubmed-meshheading:11401035... | lld:pubmed |
| pubmed-article:11401035 | pubmed:year | 2001 | lld:pubmed |
| pubmed-article:11401035 | pubmed:articleTitle | Involvement of a 40-kDa glycoprotein in food recognition, prey capture, and induction of phagocytosis in the protozoon Actinophrys sol. | lld:pubmed |
| pubmed-article:11401035 | pubmed:affiliation | Department of Biology, Faculty of Science, Kobe University, Japan. | lld:pubmed |
| pubmed-article:11401035 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11401035 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:11401035 | lld:pubmed |
