| pubmed-article:11830660 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11830660 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:11830660 | lifeskim:mentions | umls-concept:C0040715 | lld:lifeskim |
| pubmed-article:11830660 | lifeskim:mentions | umls-concept:C0022009 | lld:lifeskim |
| pubmed-article:11830660 | lifeskim:mentions | umls-concept:C0205245 | lld:lifeskim |
| pubmed-article:11830660 | lifeskim:mentions | umls-concept:C1522702 | lld:lifeskim |
| pubmed-article:11830660 | lifeskim:mentions | umls-concept:C0599718 | lld:lifeskim |
| pubmed-article:11830660 | lifeskim:mentions | umls-concept:C0599813 | lld:lifeskim |
| pubmed-article:11830660 | lifeskim:mentions | umls-concept:C0599893 | lld:lifeskim |
| pubmed-article:11830660 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:11830660 | pubmed:dateCreated | 2002-2-6 | lld:pubmed |
| pubmed-article:11830660 | pubmed:abstractText | The voltage-dependent gating of the colicin channel involves a substantial structural rearrangement that results in the transfer of about 35% of the 200 residues in its pore-forming domain across the membrane. This transfer appears to represent an unusual type of protein translocation that does not depend on a large, multimeric, protein pore. To investigate the ability of this system to transport arbitrary proteins, we made use of a pair of strongly interacting proteins, either of which could serve as a translocated cargo or as a probe to detect the other. Here we show that both an 86-residue and a 134-residue hydrophilic protein inserted into the translocated segment of colicin A are themselves translocated and are functional on the trans side of the bilayer. The disparate features of these proteins suggest that the colicin channel has a general protein translocation mechanism. | lld:pubmed |
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| pubmed-article:11830660 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11830660 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11830660 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:11830660 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:11830660 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11830660 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:11830660 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:11830660 | pubmed:author | pubmed-author:SlatinStephen... | lld:pubmed |
| pubmed-article:11830660 | pubmed:author | pubmed-author:NardiAngèleA | lld:pubmed |
| pubmed-article:11830660 | pubmed:author | pubmed-author:JakesKaren... | lld:pubmed |
| pubmed-article:11830660 | pubmed:author | pubmed-author:BatyDanielD | lld:pubmed |
| pubmed-article:11830660 | pubmed:author | pubmed-author:DuchéDenisD | lld:pubmed |
| pubmed-article:11830660 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11830660 | pubmed:day | 5 | lld:pubmed |
| pubmed-article:11830660 | pubmed:volume | 99 | lld:pubmed |
| pubmed-article:11830660 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11830660 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11830660 | pubmed:pagination | 1286-91 | lld:pubmed |
| pubmed-article:11830660 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:11830660 | pubmed:meshHeading | pubmed-meshheading:11830660... | lld:pubmed |
| pubmed-article:11830660 | pubmed:year | 2002 | lld:pubmed |
| pubmed-article:11830660 | pubmed:articleTitle | Translocation of a functional protein by a voltage-dependent ion channel. | lld:pubmed |
| pubmed-article:11830660 | pubmed:affiliation | Albert Einstein College of Medicine, Bronx, NY 10461, USA. slatin@aecom.yu.edu | lld:pubmed |
| pubmed-article:11830660 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11830660 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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