| pubmed-article:16125415 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16125415 | lifeskim:mentions | umls-concept:C0079488 | lld:lifeskim |
| pubmed-article:16125415 | lifeskim:mentions | umls-concept:C0040549 | lld:lifeskim |
| pubmed-article:16125415 | lifeskim:mentions | umls-concept:C0026019 | lld:lifeskim |
| pubmed-article:16125415 | lifeskim:mentions | umls-concept:C0487602 | lld:lifeskim |
| pubmed-article:16125415 | lifeskim:mentions | umls-concept:C1719039 | lld:lifeskim |
| pubmed-article:16125415 | lifeskim:mentions | umls-concept:C0599219 | lld:lifeskim |
| pubmed-article:16125415 | lifeskim:mentions | umls-concept:C0204514 | lld:lifeskim |
| pubmed-article:16125415 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:16125415 | pubmed:dateCreated | 2005-9-26 | lld:pubmed |
| pubmed-article:16125415 | pubmed:abstractText | Helicobacter pylori secretes a vacuolating toxin (VacA) that can assemble into water-soluble oligomeric complexes and insert into membranes to form anion-selective channels. Previous studies have described multiple types of oligomeric VacA structures, including single-layered astral arrays, bilayered forms, and two-dimensional crystalline arrays. In the current study, vitrified VacA complexes were examined by cryo-negative staining electron microscopy, views of the different oligomeric structures in multiple orientations were classified and analyzed, and three-dimensional models of the bilayered forms of VacA were constructed with a resolution of about 19 angstroms. These bilayered forms of VacA have a "flower"-like structure, consisting of a central ring surrounded by symmetrically arranged peripheral "petals." Further structural insights were obtained by analyzing a mutant form of VacA (VacADelta6-27), which lacks a unique amino-terminal hydrophobic segment and is defective in the capacity to form membrane channels. Bilayered oligomeric complexes formed by wild-type VacA contained a visible density within the central ring, whereas bilayered complexes formed by VacADelta6-27 lacked this density. These results indicate that deletion of the VacA amino-terminal hydrophobic region causes a structural alteration in the central ring within VacA oligomers, and suggest that the central ring plays an important role in the process by which VacA forms membrane channels. | lld:pubmed |
| pubmed-article:16125415 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16125415 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16125415 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16125415 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16125415 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:16125415 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16125415 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16125415 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16125415 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:16125415 | pubmed:issn | 1047-8477 | lld:pubmed |
| pubmed-article:16125415 | pubmed:author | pubmed-author:AdrianMarcM | lld:pubmed |
| pubmed-article:16125415 | pubmed:author | pubmed-author:CoverTimothy... | lld:pubmed |
| pubmed-article:16125415 | pubmed:author | pubmed-author:DubochetJacqu... | lld:pubmed |
| pubmed-article:16125415 | pubmed:author | pubmed-author:El-BezCatheri... | lld:pubmed |
| pubmed-article:16125415 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16125415 | pubmed:volume | 151 | lld:pubmed |
| pubmed-article:16125415 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16125415 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16125415 | pubmed:pagination | 215-28 | lld:pubmed |
| pubmed-article:16125415 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:16125415 | pubmed:meshHeading | pubmed-meshheading:16125415... | lld:pubmed |
| pubmed-article:16125415 | pubmed:meshHeading | pubmed-meshheading:16125415... | lld:pubmed |
| pubmed-article:16125415 | pubmed:meshHeading | pubmed-meshheading:16125415... | lld:pubmed |
| pubmed-article:16125415 | pubmed:meshHeading | pubmed-meshheading:16125415... | lld:pubmed |
| pubmed-article:16125415 | pubmed:meshHeading | pubmed-meshheading:16125415... | lld:pubmed |
| pubmed-article:16125415 | pubmed:meshHeading | pubmed-meshheading:16125415... | lld:pubmed |
| pubmed-article:16125415 | pubmed:year | 2005 | lld:pubmed |
| pubmed-article:16125415 | pubmed:articleTitle | High resolution structural analysis of Helicobacter pylori VacA toxin oligomers by cryo-negative staining electron microscopy. | lld:pubmed |
| pubmed-article:16125415 | pubmed:affiliation | Laboratoire d'Analyse Ultrastructurale, Bâtiment de Biologie, Université de Lausanne, Lausanne, Switzerland. catherine.el-bez@unil.ch | lld:pubmed |
| pubmed-article:16125415 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:16125415 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:16125415 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:16125415 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:16125415 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:16125415 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:16125415 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:16125415 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:16125415 | lld:pubmed |
