| pubmed-article:1689257 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1689257 | lifeskim:mentions | umls-concept:C0009297 | lld:lifeskim |
| pubmed-article:1689257 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:1689257 | pubmed:dateCreated | 1990-3-29 | lld:pubmed |
| pubmed-article:1689257 | pubmed:abstractText | Colicins are plasmid-encoded protein antibiotics which kill bacteria closely related to the producing strain (generally Escherichia coli). The study of the function of colicins has revealed many features which reflect common targeting and translocation mechanisms with bacteriophages and toxins. Like many toxins, colicins are composed of structural domains specialized in one of the different steps of the activity, targeting, translocation and killing. The major group comprises those colicins which permeabilize the cytoplasmic membrane, thereby destroying the cell's membrane potential. These colicins form well-defined voltage-gated ion channels in artificial membranes. The scope of this review is to describe some of the more recent findings concerning the structure and mode of action of pore-forming colicins with a special attention to models of membrane insertion and pore structure based on the recently determined three-dimensional structure of the pore-forming domain of colicin A. | lld:pubmed |
| pubmed-article:1689257 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1689257 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1689257 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:1689257 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1689257 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1689257 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:1689257 | pubmed:issn | 0014-4754 | lld:pubmed |
| pubmed-article:1689257 | pubmed:author | pubmed-author:TuckerAA | lld:pubmed |
| pubmed-article:1689257 | pubmed:author | pubmed-author:TsernoglouDD | lld:pubmed |
| pubmed-article:1689257 | pubmed:author | pubmed-author:PattusFF | lld:pubmed |
| pubmed-article:1689257 | pubmed:author | pubmed-author:ParkerM WMW | lld:pubmed |
| pubmed-article:1689257 | pubmed:author | pubmed-author:WilmsenH UHU | lld:pubmed |
| pubmed-article:1689257 | pubmed:author | pubmed-author:LakerCC | lld:pubmed |
| pubmed-article:1689257 | pubmed:author | pubmed-author:MassotteDD | lld:pubmed |
| pubmed-article:1689257 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1689257 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:1689257 | pubmed:volume | 46 | lld:pubmed |
| pubmed-article:1689257 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1689257 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1689257 | pubmed:pagination | 180-92 | lld:pubmed |
| pubmed-article:1689257 | pubmed:dateRevised | 2005-11-16 | lld:pubmed |
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| pubmed-article:1689257 | pubmed:year | 1990 | lld:pubmed |
| pubmed-article:1689257 | pubmed:articleTitle | Colicins: prokaryotic killer-pores. | lld:pubmed |
| pubmed-article:1689257 | pubmed:affiliation | European Molecular Biology Laboratory, Heidelberg, Federal Republic of Germany. | lld:pubmed |
| pubmed-article:1689257 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1689257 | pubmed:publicationType | Review | lld:pubmed |
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