| pubmed-article:9501230 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9501230 | lifeskim:mentions | umls-concept:C1167331 | lld:lifeskim |
| pubmed-article:9501230 | lifeskim:mentions | umls-concept:C0376315 | lld:lifeskim |
| pubmed-article:9501230 | lifeskim:mentions | umls-concept:C1155942 | lld:lifeskim |
| pubmed-article:9501230 | lifeskim:mentions | umls-concept:C0439799 | lld:lifeskim |
| pubmed-article:9501230 | pubmed:issue | 6 | lld:pubmed |
| pubmed-article:9501230 | pubmed:dateCreated | 1998-4-10 | lld:pubmed |
| pubmed-article:9501230 | pubmed:abstractText | Bacterial virulence factors are typically surface-associated or secreted molecules that in Gram-negative bacteria must cross the outer membrane (OM). Protein translocation across the bacterial OM is not well understood. To elucidate this process we studied P pilus biogenesis in Escherichia coli. We present high-resolution electron micrographs of the OM usher PapC and show that it forms an oligomeric complex containing a channel approximately 2 nm in diameter. This is large enough to accommodate pilus subunits or the linear tip fibrillum of the pilus but not large enough to accommodate the final 6.8-nm-wide helical pilus rod. We show that P pilus rods can be unraveled into linear fibers by incubation in 50% glycerol. Thus, they are likely to pass through the usher in this unwound form. Packaging of these fibers into their final helical structure would only occur outside the cell, a process that may drive outward growth of the pilus organelles. The usher complex appears to be similar to complexes formed by members of the PulD/pIV family of OM proteins, and thus these two protein families, previously thought to be unrelated, may share structural and functional homologies. | lld:pubmed |
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| pubmed-article:9501230 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9501230 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9501230 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9501230 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:9501230 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9501230 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:9501230 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:9501230 | pubmed:author | pubmed-author:RothRR | lld:pubmed |
| pubmed-article:9501230 | pubmed:author | pubmed-author:HeuserJJ | lld:pubmed |
| pubmed-article:9501230 | pubmed:author | pubmed-author:HultgrenS JSJ | lld:pubmed |
| pubmed-article:9501230 | pubmed:author | pubmed-author:LombardoM JMJ | lld:pubmed |
| pubmed-article:9501230 | pubmed:author | pubmed-author:ThanassiD GDG | lld:pubmed |
| pubmed-article:9501230 | pubmed:author | pubmed-author:SaulinoE TET | lld:pubmed |
| pubmed-article:9501230 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9501230 | pubmed:day | 17 | lld:pubmed |
| pubmed-article:9501230 | pubmed:volume | 95 | lld:pubmed |
| pubmed-article:9501230 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9501230 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9501230 | pubmed:pagination | 3146-51 | lld:pubmed |
| pubmed-article:9501230 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:9501230 | pubmed:meshHeading | pubmed-meshheading:9501230-... | lld:pubmed |
| pubmed-article:9501230 | pubmed:meshHeading | pubmed-meshheading:9501230-... | lld:pubmed |
| pubmed-article:9501230 | pubmed:meshHeading | pubmed-meshheading:9501230-... | lld:pubmed |
| pubmed-article:9501230 | pubmed:meshHeading | pubmed-meshheading:9501230-... | lld:pubmed |
| pubmed-article:9501230 | pubmed:meshHeading | pubmed-meshheading:9501230-... | lld:pubmed |
| pubmed-article:9501230 | pubmed:meshHeading | pubmed-meshheading:9501230-... | lld:pubmed |
| pubmed-article:9501230 | pubmed:meshHeading | pubmed-meshheading:9501230-... | lld:pubmed |
| pubmed-article:9501230 | pubmed:meshHeading | pubmed-meshheading:9501230-... | lld:pubmed |
| pubmed-article:9501230 | pubmed:meshHeading | pubmed-meshheading:9501230-... | lld:pubmed |
| pubmed-article:9501230 | pubmed:meshHeading | pubmed-meshheading:9501230-... | lld:pubmed |
| pubmed-article:9501230 | pubmed:meshHeading | pubmed-meshheading:9501230-... | lld:pubmed |
| pubmed-article:9501230 | pubmed:meshHeading | pubmed-meshheading:9501230-... | lld:pubmed |
| pubmed-article:9501230 | pubmed:meshHeading | pubmed-meshheading:9501230-... | lld:pubmed |
| pubmed-article:9501230 | pubmed:year | 1998 | lld:pubmed |
| pubmed-article:9501230 | pubmed:articleTitle | The PapC usher forms an oligomeric channel: implications for pilus biogenesis across the outer membrane. | lld:pubmed |
| pubmed-article:9501230 | pubmed:affiliation | Department of Molecular Microbiology, Box 8230, 660 South Euclid Avenue, Washington University School of Medicine, St. Louis, MO 63110, USA. | lld:pubmed |
| pubmed-article:9501230 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9501230 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
