pubmed-article:20140750 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:20140750 | lifeskim:mentions | umls-concept:C0003241 | lld:lifeskim |
pubmed-article:20140750 | lifeskim:mentions | umls-concept:C0061187 | lld:lifeskim |
pubmed-article:20140750 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
pubmed-article:20140750 | lifeskim:mentions | umls-concept:C1533157 | lld:lifeskim |
pubmed-article:20140750 | pubmed:issue | 9 | lld:pubmed |
pubmed-article:20140750 | pubmed:dateCreated | 2010-4-20 | lld:pubmed |
pubmed-article:20140750 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20140750 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20140750 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20140750 | pubmed:abstractText | RNA interference has tremendously advanced our understanding of gene function but recent reports have exposed undesirable side-effects. Recombinant Camelid single-domain antibodies (VHHs) provide an attractive means for studying protein function without affecting gene expression. We raised VHHs against gelsolin (GsnVHHs), a multifunctional actin-binding protein that controls cellular actin organization and migration. GsnVHH-induced delocalization of gelsolin to mitochondria or the nucleus in mammalian cells reveals distinct subpopulations including free gelsolin and actin-bound gelsolin complexes. GsnVHH 13 specifically recognizes Ca(2+)-activated gelsolin (K (d) approximately 10 nM) while GsnVHH 11 binds gelsolin irrespective of Ca(2+) (K (d) approximately 5 nM) but completely blocks its interaction with G-actin. Both GsnVHHs trace gelsolin in membrane ruffles of EGF-stimulated MCF-7 cells and delay cell migration without affecting F-actin severing/capping or actin nucleation activities by gelsolin. We conclude that VHHs represent a potent way of blocking structural proteins and that actin nucleation by gelsolin is more complex than previously anticipated. | lld:pubmed |
pubmed-article:20140750 | pubmed:language | eng | lld:pubmed |
pubmed-article:20140750 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20140750 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:20140750 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20140750 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20140750 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20140750 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20140750 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20140750 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20140750 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:20140750 | pubmed:month | May | lld:pubmed |
pubmed-article:20140750 | pubmed:issn | 1420-9071 | lld:pubmed |
pubmed-article:20140750 | pubmed:author | pubmed-author:Vandekerckhov... | lld:pubmed |
pubmed-article:20140750 | pubmed:author | pubmed-author:SteyaertJanJ | lld:pubmed |
pubmed-article:20140750 | pubmed:author | pubmed-author:De... | lld:pubmed |
pubmed-article:20140750 | pubmed:author | pubmed-author:GettemansJanJ | lld:pubmed |
pubmed-article:20140750 | pubmed:author | pubmed-author:SrinivasanVas... | lld:pubmed |
pubmed-article:20140750 | pubmed:author | pubmed-author:De... | lld:pubmed |
pubmed-article:20140750 | pubmed:author | pubmed-author:De... | lld:pubmed |
pubmed-article:20140750 | pubmed:author | pubmed-author:Van den... | lld:pubmed |
pubmed-article:20140750 | pubmed:author | pubmed-author:Van... | lld:pubmed |
pubmed-article:20140750 | pubmed:author | pubmed-author:SororSameh... | lld:pubmed |
pubmed-article:20140750 | pubmed:issnType | Electronic | lld:pubmed |
pubmed-article:20140750 | pubmed:volume | 67 | lld:pubmed |
pubmed-article:20140750 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:20140750 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:20140750 | pubmed:pagination | 1519-35 | lld:pubmed |
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pubmed-article:20140750 | pubmed:year | 2010 | lld:pubmed |
pubmed-article:20140750 | pubmed:articleTitle | A llama-derived gelsolin single-domain antibody blocks gelsolin-G-actin interaction. | lld:pubmed |
pubmed-article:20140750 | pubmed:affiliation | Department of Medical Protein Research, VIB, 9000 Ghent, Belgium. | lld:pubmed |
pubmed-article:20140750 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:20140750 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |