| pubmed-article:18410514 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:18410514 | lifeskim:mentions | umls-concept:C0026046 | lld:lifeskim |
| pubmed-article:18410514 | lifeskim:mentions | umls-concept:C0596988 | lld:lifeskim |
| pubmed-article:18410514 | lifeskim:mentions | umls-concept:C1979891 | lld:lifeskim |
| pubmed-article:18410514 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:18410514 | pubmed:dateCreated | 2008-8-8 | lld:pubmed |
| pubmed-article:18410514 | pubmed:abstractText | Spastin, a member of the ATPases associated with various cellular activities (AAA) family of proteins, is the most frequently mutated in hereditary spastic paraplegia. The defining feature of the AAA proteins is a structurally conserved AAA domain which assembles into an oligomer. By chemical cross-linking and gel filtration chromatography, we show that spastin oligomerizes into a hexamer. Furthermore, to gain a comprehensive overview of the oligomeric structure of spastin, we generated a structural model of the AAA domain of spastin using template structure of VPS4B and p97/VCP. The generated model of spastin provided us with a framework to classify the identified missense mutations in the AAA domain from hereditary spastic paraplegia patients into different structural/functional groups. Finally, through co-localization studies in mammalian cells, we show that E442Q mutant spastin acts in a dominant negative fashion and causes redistribution of both wild-type spastin monomer and spastin interacting protein, RTN1 into filamentous microtubule bundles. | lld:pubmed |
| pubmed-article:18410514 | pubmed:language | eng | lld:pubmed |
| pubmed-article:18410514 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18410514 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:18410514 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18410514 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18410514 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18410514 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18410514 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18410514 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18410514 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18410514 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18410514 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18410514 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18410514 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18410514 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18410514 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:18410514 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:18410514 | pubmed:issn | 1471-4159 | lld:pubmed |
| pubmed-article:18410514 | pubmed:author | pubmed-author:SrinivasanNar... | lld:pubmed |
| pubmed-article:18410514 | pubmed:author | pubmed-author:MannanAshraf... | lld:pubmed |
| pubmed-article:18410514 | pubmed:author | pubmed-author:PantakaniD... | lld:pubmed |
| pubmed-article:18410514 | pubmed:author | pubmed-author:SwapnaLakshmi... | lld:pubmed |
| pubmed-article:18410514 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:18410514 | pubmed:volume | 106 | lld:pubmed |
| pubmed-article:18410514 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:18410514 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:18410514 | pubmed:pagination | 613-24 | lld:pubmed |
| pubmed-article:18410514 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
| pubmed-article:18410514 | pubmed:meshHeading | pubmed-meshheading:18410514... | lld:pubmed |
| pubmed-article:18410514 | pubmed:meshHeading | pubmed-meshheading:18410514... | lld:pubmed |
| pubmed-article:18410514 | pubmed:meshHeading | pubmed-meshheading:18410514... | lld:pubmed |
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| pubmed-article:18410514 | pubmed:meshHeading | pubmed-meshheading:18410514... | lld:pubmed |
| pubmed-article:18410514 | pubmed:meshHeading | pubmed-meshheading:18410514... | lld:pubmed |
| pubmed-article:18410514 | pubmed:meshHeading | pubmed-meshheading:18410514... | lld:pubmed |
| pubmed-article:18410514 | pubmed:meshHeading | pubmed-meshheading:18410514... | lld:pubmed |
| pubmed-article:18410514 | pubmed:meshHeading | pubmed-meshheading:18410514... | lld:pubmed |
| pubmed-article:18410514 | pubmed:meshHeading | pubmed-meshheading:18410514... | lld:pubmed |
| pubmed-article:18410514 | pubmed:meshHeading | pubmed-meshheading:18410514... | lld:pubmed |
| pubmed-article:18410514 | pubmed:meshHeading | pubmed-meshheading:18410514... | lld:pubmed |
| pubmed-article:18410514 | pubmed:meshHeading | pubmed-meshheading:18410514... | lld:pubmed |
| pubmed-article:18410514 | pubmed:meshHeading | pubmed-meshheading:18410514... | lld:pubmed |
| pubmed-article:18410514 | pubmed:meshHeading | pubmed-meshheading:18410514... | lld:pubmed |
| pubmed-article:18410514 | pubmed:meshHeading | pubmed-meshheading:18410514... | lld:pubmed |
| pubmed-article:18410514 | pubmed:meshHeading | pubmed-meshheading:18410514... | lld:pubmed |
| pubmed-article:18410514 | pubmed:year | 2008 | lld:pubmed |
| pubmed-article:18410514 | pubmed:articleTitle | Spastin oligomerizes into a hexamer and the mutant spastin (E442Q) redistribute the wild-type spastin into filamentous microtubule. | lld:pubmed |
| pubmed-article:18410514 | pubmed:affiliation | Institute of Human Genetics, University of Goettingen, Goettingen, Germany. | lld:pubmed |
| pubmed-article:18410514 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:18410514 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
