pubmed-article:10482528 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:10482528 | lifeskim:mentions | umls-concept:C0006017 | lld:lifeskim |
pubmed-article:10482528 | lifeskim:mentions | umls-concept:C0023768 | lld:lifeskim |
pubmed-article:10482528 | lifeskim:mentions | umls-concept:C1325742 | lld:lifeskim |
pubmed-article:10482528 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
pubmed-article:10482528 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
pubmed-article:10482528 | lifeskim:mentions | umls-concept:C0376315 | lld:lifeskim |
pubmed-article:10482528 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
pubmed-article:10482528 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
pubmed-article:10482528 | lifeskim:mentions | umls-concept:C1707271 | lld:lifeskim |
pubmed-article:10482528 | pubmed:issue | 18 | lld:pubmed |
pubmed-article:10482528 | pubmed:dateCreated | 1999-10-12 | lld:pubmed |
pubmed-article:10482528 | pubmed:abstractText | BrkA is a 103-kDa outer membrane protein of Bordetella pertussis that mediates resistance to antibody-dependent killing by complement. It is proteolytically processed into a 73-kDa N-terminal domain and a 30-kDa C-terminal domain as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. BrkA is also a member of the autotransporter family of proteins. Translocation of the N-terminal domain of the protein across the outer membrane is hypothesized to occur through a pore formed by the C-terminal domain. To test this hypothesis, we performed black lipid bilayer experiments with purified recombinant protein. The BrkA C-terminal protein showed an average single-channel conductance of 3.0 nS in 1 M KCl. This result strongly suggests that the C-terminal autotransporter domain of BrkA is indeed capable of forming a pore. | lld:pubmed |
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pubmed-article:10482528 | pubmed:language | eng | lld:pubmed |
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pubmed-article:10482528 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:10482528 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:10482528 | pubmed:month | Sep | lld:pubmed |
pubmed-article:10482528 | pubmed:issn | 0021-9193 | lld:pubmed |
pubmed-article:10482528 | pubmed:author | pubmed-author:ShannonJ LJL | lld:pubmed |
pubmed-article:10482528 | pubmed:author | pubmed-author:FernandezR... | lld:pubmed |
pubmed-article:10482528 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:10482528 | pubmed:volume | 181 | lld:pubmed |
pubmed-article:10482528 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:10482528 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:10482528 | pubmed:pagination | 5838-42 | lld:pubmed |
pubmed-article:10482528 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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pubmed-article:10482528 | pubmed:meshHeading | pubmed-meshheading:10482528... | lld:pubmed |
pubmed-article:10482528 | pubmed:year | 1999 | lld:pubmed |
pubmed-article:10482528 | pubmed:articleTitle | The C-terminal domain of the Bordetella pertussis autotransporter BrkA forms a pore in lipid bilayer membranes. | lld:pubmed |
pubmed-article:10482528 | pubmed:affiliation | Department of Microbiology and Immunology, University of British Columbia, Vancouver, British Columbia, Canada V6T 1Z3. | lld:pubmed |
pubmed-article:10482528 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:10482528 | pubmed:publicationType | Comparative Study | lld:pubmed |
pubmed-article:10482528 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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