pubmed-article:17082456 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:17082456 | lifeskim:mentions | umls-concept:C0028587 | lld:lifeskim |
pubmed-article:17082456 | lifeskim:mentions | umls-concept:C1705914 | lld:lifeskim |
pubmed-article:17082456 | lifeskim:mentions | umls-concept:C0376315 | lld:lifeskim |
pubmed-article:17082456 | lifeskim:mentions | umls-concept:C0450363 | lld:lifeskim |
pubmed-article:17082456 | lifeskim:mentions | umls-concept:C0871161 | lld:lifeskim |
pubmed-article:17082456 | lifeskim:mentions | umls-concept:C0137956 | lld:lifeskim |
pubmed-article:17082456 | pubmed:issue | 5800 | lld:pubmed |
pubmed-article:17082456 | pubmed:dateCreated | 2006-11-3 | lld:pubmed |
pubmed-article:17082456 | pubmed:abstractText | Nuclear pore complexes permit rapid passage of cargoes bound to nuclear transport receptors, but otherwise suppress nucleocytoplasmic fluxes of inert macromolecules >/=30 kilodaltons. To explain this selectivity, a sieve structure of the permeability barrier has been proposed that is created through reversible cross-linking between Phe and Gly (FG)-rich nucleoporin repeats. According to this model, nuclear transport receptors overcome the size limit of the sieve and catalyze their own nuclear pore-passage by a competitive disruption of adjacent inter-repeat contacts, which transiently opens adjoining meshes. Here, we found that phenylalanine-mediated inter-repeat interactions indeed cross-link FG-repeat domains into elastic and reversible hydrogels. Furthermore, we obtained evidence that such hydrogel formation is required for viability in yeast. | lld:pubmed |
pubmed-article:17082456 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17082456 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17082456 | pubmed:language | eng | lld:pubmed |
pubmed-article:17082456 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17082456 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:17082456 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17082456 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17082456 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17082456 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17082456 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17082456 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17082456 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:17082456 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17082456 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:17082456 | pubmed:month | Nov | lld:pubmed |
pubmed-article:17082456 | pubmed:issn | 1095-9203 | lld:pubmed |
pubmed-article:17082456 | pubmed:author | pubmed-author:GörlichDirkD | lld:pubmed |
pubmed-article:17082456 | pubmed:author | pubmed-author:FreySteffenS | lld:pubmed |
pubmed-article:17082456 | pubmed:author | pubmed-author:RichterRalf... | lld:pubmed |
pubmed-article:17082456 | pubmed:issnType | Electronic | lld:pubmed |
pubmed-article:17082456 | pubmed:day | 3 | lld:pubmed |
pubmed-article:17082456 | pubmed:volume | 314 | lld:pubmed |
pubmed-article:17082456 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:17082456 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:17082456 | pubmed:pagination | 815-7 | lld:pubmed |
pubmed-article:17082456 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
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pubmed-article:17082456 | pubmed:meshHeading | pubmed-meshheading:17082456... | lld:pubmed |
pubmed-article:17082456 | pubmed:year | 2006 | lld:pubmed |
pubmed-article:17082456 | pubmed:articleTitle | FG-rich repeats of nuclear pore proteins form a three-dimensional meshwork with hydrogel-like properties. | lld:pubmed |
pubmed-article:17082456 | pubmed:affiliation | Zentrum für Molekulare Biologie der Universität Heidelberg (ZMBH), INF 282, D-69120 Heidelberg, Germany. | lld:pubmed |
pubmed-article:17082456 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:17082456 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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