| pubmed-article:2155233 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2155233 | lifeskim:mentions | umls-concept:C0014834 | lld:lifeskim |
| pubmed-article:2155233 | lifeskim:mentions | umls-concept:C1167331 | lld:lifeskim |
| pubmed-article:2155233 | lifeskim:mentions | umls-concept:C0071728 | lld:lifeskim |
| pubmed-article:2155233 | lifeskim:mentions | umls-concept:C1883254 | lld:lifeskim |
| pubmed-article:2155233 | lifeskim:mentions | umls-concept:C0205360 | lld:lifeskim |
| pubmed-article:2155233 | lifeskim:mentions | umls-concept:C1879748 | lld:lifeskim |
| pubmed-article:2155233 | lifeskim:mentions | umls-concept:C1706853 | lld:lifeskim |
| pubmed-article:2155233 | lifeskim:mentions | umls-concept:C1533691 | lld:lifeskim |
| pubmed-article:2155233 | lifeskim:mentions | umls-concept:C0449830 | lld:lifeskim |
| pubmed-article:2155233 | lifeskim:mentions | umls-concept:C2827597 | lld:lifeskim |
| pubmed-article:2155233 | pubmed:issue | 8 | lld:pubmed |
| pubmed-article:2155233 | pubmed:dateCreated | 1990-4-9 | lld:pubmed |
| pubmed-article:2155233 | pubmed:abstractText | The folding of in vitro synthesized outer membrane protein PhoE of Escherichia coli was studied in immunoprecipitation experiments with monoclonal antibodies which recognize cell surface-exposed conformational epitopes. The signal sequence appears to interfere with the formation of these conformational epitopes, since a mutant PhoE protein which lacks the majority of the signal peptide could be precipitated four times better than the wild type precursor. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of the immunoprecipitated PhoE protein revealed that part of the immunoprecipitated PhoE was present as a heat-modifiable form of the protein which migrated faster in the gels than the completely denatured protein. This form of the protein probably represents a folded monomer which might be an intermediate in the assembly of the protein. Outer membrane vesicles were required to induce the formation of small amounts of heat-stable trimers, the functional form of the protein in vivo. | lld:pubmed |
| pubmed-article:2155233 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2155233 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2155233 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:2155233 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:2155233 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2155233 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:2155233 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:2155233 | pubmed:author | pubmed-author:TommassenJJ | lld:pubmed |
| pubmed-article:2155233 | pubmed:author | pubmed-author:HendriksRR | lld:pubmed |
| pubmed-article:2155233 | pubmed:author | pubmed-author:de CockHH | lld:pubmed |
| pubmed-article:2155233 | pubmed:author | pubmed-author:de VrijeTT | lld:pubmed |
| pubmed-article:2155233 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2155233 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:2155233 | pubmed:volume | 265 | lld:pubmed |
| pubmed-article:2155233 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2155233 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2155233 | pubmed:pagination | 4646-51 | lld:pubmed |
| pubmed-article:2155233 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
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| pubmed-article:2155233 | pubmed:meshHeading | pubmed-meshheading:2155233-... | lld:pubmed |
| pubmed-article:2155233 | pubmed:year | 1990 | lld:pubmed |
| pubmed-article:2155233 | pubmed:articleTitle | Assembly of an in vitro synthesized Escherichia coli outer membrane porin into its stable trimeric configuration. | lld:pubmed |
| pubmed-article:2155233 | pubmed:affiliation | Institute of Molecular Biology and Medical Biotechnology, University of Utrecht, The Netherlands. | lld:pubmed |
| pubmed-article:2155233 | pubmed:publicationType | Journal Article | lld:pubmed |
| entrez-gene:944926 | entrezgene:pubmed | pubmed-article:2155233 | lld:entrezgene |
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