| pubmed-article:20826163 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:20826163 | lifeskim:mentions | umls-concept:C0079488 | lld:lifeskim |
| pubmed-article:20826163 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:20826163 | lifeskim:mentions | umls-concept:C0333177 | lld:lifeskim |
| pubmed-article:20826163 | lifeskim:mentions | umls-concept:C1516692 | lld:lifeskim |
| pubmed-article:20826163 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:20826163 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:20826163 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:20826163 | lifeskim:mentions | umls-concept:C0205250 | lld:lifeskim |
| pubmed-article:20826163 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:20826163 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:20826163 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:20826163 | pubmed:dateCreated | 2010-10-12 | lld:pubmed |
| pubmed-article:20826163 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20826163 | pubmed:abstractText | We have determined the 2.2-Å structure of the HP0958 protein from the human gastric pathogen Helicobacter pylori. HP0958 is essential for flagellum formation and motility. It functions as a chaperone for RpoN (?(54)) and also controls the stability and translation of mRNA for the major flagellin subunit FlaA. The protein is composed of a highly elongated and kinked coiled-coil hairpin domain (residues 1-170), followed by a C(4) Zn-ribbon domain (residues 174-238). The Zn-ribbon domain is rich in aromatic and positively charged amino acid residues. Electrophoretic mobility shift assays identified residues in a positively charged region of the Zn-ribbon domain of HP0958 whose mutation alters the mobility of an HP0958-flaA mRNA complex. Mutation of surface residues in the coiled-coil domain did not result in an observable change in the mobility of the HP0958-flaA transcript complex. The data thus suggest the arrangement of HP0958 into distinct structural and functional domains. | lld:pubmed |
| pubmed-article:20826163 | pubmed:language | eng | lld:pubmed |
| pubmed-article:20826163 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20826163 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:20826163 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20826163 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20826163 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20826163 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20826163 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20826163 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:20826163 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:20826163 | pubmed:issn | 1089-8638 | lld:pubmed |
| pubmed-article:20826163 | pubmed:author | pubmed-author:O'ToolePaul... | lld:pubmed |
| pubmed-article:20826163 | pubmed:author | pubmed-author:MooreStanley... | lld:pubmed |
| pubmed-article:20826163 | pubmed:author | pubmed-author:CalyDelphine... | lld:pubmed |
| pubmed-article:20826163 | pubmed:copyrightInfo | Copyright © 2010 Elsevier Ltd. All rights reserved. | lld:pubmed |
| pubmed-article:20826163 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:20826163 | pubmed:day | 29 | lld:pubmed |
| pubmed-article:20826163 | pubmed:volume | 403 | lld:pubmed |
| pubmed-article:20826163 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:20826163 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:20826163 | pubmed:pagination | 405-19 | lld:pubmed |
| pubmed-article:20826163 | pubmed:meshHeading | pubmed-meshheading:20826163... | lld:pubmed |
| pubmed-article:20826163 | pubmed:meshHeading | pubmed-meshheading:20826163... | lld:pubmed |
| pubmed-article:20826163 | pubmed:meshHeading | pubmed-meshheading:20826163... | lld:pubmed |
| pubmed-article:20826163 | pubmed:meshHeading | pubmed-meshheading:20826163... | lld:pubmed |
| pubmed-article:20826163 | pubmed:meshHeading | pubmed-meshheading:20826163... | lld:pubmed |
| pubmed-article:20826163 | pubmed:meshHeading | pubmed-meshheading:20826163... | lld:pubmed |
| pubmed-article:20826163 | pubmed:meshHeading | pubmed-meshheading:20826163... | lld:pubmed |
| pubmed-article:20826163 | pubmed:meshHeading | pubmed-meshheading:20826163... | lld:pubmed |
| pubmed-article:20826163 | pubmed:meshHeading | pubmed-meshheading:20826163... | lld:pubmed |
| pubmed-article:20826163 | pubmed:meshHeading | pubmed-meshheading:20826163... | lld:pubmed |
| pubmed-article:20826163 | pubmed:meshHeading | pubmed-meshheading:20826163... | lld:pubmed |
| pubmed-article:20826163 | pubmed:meshHeading | pubmed-meshheading:20826163... | lld:pubmed |
| pubmed-article:20826163 | pubmed:meshHeading | pubmed-meshheading:20826163... | lld:pubmed |
| pubmed-article:20826163 | pubmed:meshHeading | pubmed-meshheading:20826163... | lld:pubmed |
| pubmed-article:20826163 | pubmed:year | 2010 | lld:pubmed |
| pubmed-article:20826163 | pubmed:articleTitle | The 2.2-Å structure of the HP0958 protein from Helicobacter pylori reveals a kinked anti-parallel coiled-coil hairpin domain and a highly conserved ZN-ribbon domain. | lld:pubmed |
| pubmed-article:20826163 | pubmed:affiliation | Department of Microbiology, University College Cork, Cork, Ireland. | lld:pubmed |
| pubmed-article:20826163 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:20826163 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
