| pubmed-article:8484779 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8484779 | lifeskim:mentions | umls-concept:C0079784 | lld:lifeskim |
| pubmed-article:8484779 | lifeskim:mentions | umls-concept:C1171362 | lld:lifeskim |
| pubmed-article:8484779 | lifeskim:mentions | umls-concept:C0441655 | lld:lifeskim |
| pubmed-article:8484779 | lifeskim:mentions | umls-concept:C0017262 | lld:lifeskim |
| pubmed-article:8484779 | lifeskim:mentions | umls-concept:C1515670 | lld:lifeskim |
| pubmed-article:8484779 | lifeskim:mentions | umls-concept:C0376315 | lld:lifeskim |
| pubmed-article:8484779 | lifeskim:mentions | umls-concept:C0591833 | lld:lifeskim |
| pubmed-article:8484779 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:8484779 | pubmed:dateCreated | 1993-6-1 | lld:pubmed |
| pubmed-article:8484779 | pubmed:abstractText | CSF-1 is a dimeric peptide growth factor, stabilized by disulfide bonds. We expressed mouse CSF-1 in bacteria as a fusion protein either with glutathione S-transferase (GST) or with a six histidine tag (His-tag). Large amounts of recombinant material were obtained and purified by a single affinity chromatography step. Purified CSF-1-His-tag monomers efficiently dimerized in vitro, but the presence of variable amounts of GST-moiety in CSF-1 preparations obtained by thrombin cleavage of GST-fusion proteins (thrombin-released CSF-1) interfered with dimerization. However, the thrombin-released CSF-1 monomers possessed agonistic activity, being capable of stimulating tyrosine phosphorylation of the CSF-1 receptor and of an array of cellular proteins in living macrophages and of supporting their growth. These results show that CSF-1 dimerization is not essential for receptor activation in vivo. | lld:pubmed |
| pubmed-article:8484779 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8484779 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8484779 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8484779 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8484779 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8484779 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8484779 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8484779 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8484779 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8484779 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8484779 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8484779 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:8484779 | pubmed:issn | 0006-291X | lld:pubmed |
| pubmed-article:8484779 | pubmed:author | pubmed-author:BaccariniMM | lld:pubmed |
| pubmed-article:8484779 | pubmed:author | pubmed-author:KrautwaldSS | lld:pubmed |
| pubmed-article:8484779 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8484779 | pubmed:day | 30 | lld:pubmed |
| pubmed-article:8484779 | pubmed:volume | 192 | lld:pubmed |
| pubmed-article:8484779 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8484779 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8484779 | pubmed:pagination | 720-7 | lld:pubmed |
| pubmed-article:8484779 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
| pubmed-article:8484779 | pubmed:meshHeading | pubmed-meshheading:8484779-... | lld:pubmed |
| pubmed-article:8484779 | pubmed:meshHeading | pubmed-meshheading:8484779-... | lld:pubmed |
| pubmed-article:8484779 | pubmed:meshHeading | pubmed-meshheading:8484779-... | lld:pubmed |
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| pubmed-article:8484779 | pubmed:meshHeading | pubmed-meshheading:8484779-... | lld:pubmed |
| pubmed-article:8484779 | pubmed:meshHeading | pubmed-meshheading:8484779-... | lld:pubmed |
| pubmed-article:8484779 | pubmed:meshHeading | pubmed-meshheading:8484779-... | lld:pubmed |
| pubmed-article:8484779 | pubmed:meshHeading | pubmed-meshheading:8484779-... | lld:pubmed |
| pubmed-article:8484779 | pubmed:meshHeading | pubmed-meshheading:8484779-... | lld:pubmed |
| pubmed-article:8484779 | pubmed:meshHeading | pubmed-meshheading:8484779-... | lld:pubmed |
| pubmed-article:8484779 | pubmed:meshHeading | pubmed-meshheading:8484779-... | lld:pubmed |
| pubmed-article:8484779 | pubmed:year | 1993 | lld:pubmed |
| pubmed-article:8484779 | pubmed:articleTitle | Bacterially expressed murine CSF-1 possesses agonistic activity in its monomeric form. | lld:pubmed |
| pubmed-article:8484779 | pubmed:affiliation | Department of Immunbiology, Fraunhofer Institut for Toxicology and Molecular Biology, Hannover, Germany. | lld:pubmed |
| pubmed-article:8484779 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8484779 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8484779 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8484779 | lld:pubmed |
