| pubmed-article:15184025 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15184025 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:15184025 | lifeskim:mentions | umls-concept:C0042666 | lld:lifeskim |
| pubmed-article:15184025 | lifeskim:mentions | umls-concept:C1521991 | lld:lifeskim |
| pubmed-article:15184025 | lifeskim:mentions | umls-concept:C0439148 | lld:lifeskim |
| pubmed-article:15184025 | lifeskim:mentions | umls-concept:C0005553 | lld:lifeskim |
| pubmed-article:15184025 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
| pubmed-article:15184025 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:15184025 | pubmed:dateCreated | 2004-6-8 | lld:pubmed |
| pubmed-article:15184025 | pubmed:abstractText | We have developed an assembly protocol for the intermediate filament (IF) protein vimentin based on a phosphate buffer system, which enables the dynamic formation of authentic IFs. The advantage of this physiological buffer is that analysis of the subunit interactions by chemical cross-linking of internal lysine residues becomes feasible. By this system, we have analyzed the potential interactions of the coiled-coil rod domains with one another, which are assumed to make a crucial contribution to IF formation and stability. We show that headless vimentin, which dimerizes under low salt conditions, associates into tetramers of the A(22)-type configuration under assembly conditions, indicating that one of the effects of increasing the ionic strength is to favor coil 2-coil 2 interactions. Furthermore, in order to obtain insight into the molecular interactions that occur during the first phase of assembly of full-length vimentin, we employed a temperature-sensitive variant of human vimentin, which is arrested at the "unit-length filament" (ULF) state at room temperature, but starts to elongate upon raising the temperature to 37 degrees C. Most importantly, we demonstrate by cross-linking analysis that ULF formation predominantly involves A(11)-type dimer-dimer interactions. The presence of A(22) and A(12) cross-linking products in mature IFs, however, indicates that major rearrangements do occur during the longitudinal annealing and radial compaction steps of IF assembly. | lld:pubmed |
| pubmed-article:15184025 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15184025 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15184025 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:15184025 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:15184025 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15184025 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15184025 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:15184025 | pubmed:issn | 0022-2836 | lld:pubmed |
| pubmed-article:15184025 | pubmed:author | pubmed-author:SteinertPeter... | lld:pubmed |
| pubmed-article:15184025 | pubmed:author | pubmed-author:AebiUeliU | lld:pubmed |
| pubmed-article:15184025 | pubmed:author | pubmed-author:HerrmannHaral... | lld:pubmed |
| pubmed-article:15184025 | pubmed:author | pubmed-author:WedigTatjanaT | lld:pubmed |
| pubmed-article:15184025 | pubmed:author | pubmed-author:MückeNorbertN | lld:pubmed |
| pubmed-article:15184025 | pubmed:author | pubmed-author:LangowskiJörg... | lld:pubmed |
| pubmed-article:15184025 | pubmed:author | pubmed-author:MarekovLyuben... | lld:pubmed |
| pubmed-article:15184025 | pubmed:author | pubmed-author:BürerAndreaA | lld:pubmed |
| pubmed-article:15184025 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15184025 | pubmed:day | 25 | lld:pubmed |
| pubmed-article:15184025 | pubmed:volume | 340 | lld:pubmed |
| pubmed-article:15184025 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15184025 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15184025 | pubmed:pagination | 97-114 | lld:pubmed |
| pubmed-article:15184025 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:15184025 | pubmed:meshHeading | pubmed-meshheading:15184025... | lld:pubmed |
| pubmed-article:15184025 | pubmed:meshHeading | pubmed-meshheading:15184025... | lld:pubmed |
| pubmed-article:15184025 | pubmed:meshHeading | pubmed-meshheading:15184025... | lld:pubmed |
| pubmed-article:15184025 | pubmed:meshHeading | pubmed-meshheading:15184025... | lld:pubmed |
| pubmed-article:15184025 | pubmed:meshHeading | pubmed-meshheading:15184025... | lld:pubmed |
| pubmed-article:15184025 | pubmed:meshHeading | pubmed-meshheading:15184025... | lld:pubmed |
| pubmed-article:15184025 | pubmed:meshHeading | pubmed-meshheading:15184025... | lld:pubmed |
| pubmed-article:15184025 | pubmed:meshHeading | pubmed-meshheading:15184025... | lld:pubmed |
| pubmed-article:15184025 | pubmed:year | 2004 | lld:pubmed |
| pubmed-article:15184025 | pubmed:articleTitle | Molecular and biophysical characterization of assembly-starter units of human vimentin. | lld:pubmed |
| pubmed-article:15184025 | pubmed:affiliation | Division of Biophysics of Macromolecules, German Cancer Research Center, Im Neuenheimer Feld 280, D-69120 Heidelberg, Germany. | lld:pubmed |
| pubmed-article:15184025 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15184025 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:15184025 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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