pubmed-article:16027225 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:16027225 | lifeskim:mentions | umls-concept:C0042776 | lld:lifeskim |
pubmed-article:16027225 | lifeskim:mentions | umls-concept:C0007634 | lld:lifeskim |
pubmed-article:16027225 | lifeskim:mentions | umls-concept:C0026649 | lld:lifeskim |
pubmed-article:16027225 | lifeskim:mentions | umls-concept:C0600315 | lld:lifeskim |
pubmed-article:16027225 | lifeskim:mentions | umls-concept:C1550548 | lld:lifeskim |
pubmed-article:16027225 | lifeskim:mentions | umls-concept:C1555714 | lld:lifeskim |
pubmed-article:16027225 | lifeskim:mentions | umls-concept:C1705654 | lld:lifeskim |
pubmed-article:16027225 | pubmed:issue | 2 | lld:pubmed |
pubmed-article:16027225 | pubmed:dateCreated | 2005-7-19 | lld:pubmed |
pubmed-article:16027225 | pubmed:abstractText | Viruses have often been observed in association with the dense microvilli of polarized epithelia as well as the filopodia of nonpolarized cells, yet whether interactions with these structures contribute to infection has remained unknown. Here we show that virus binding to filopodia induces a rapid and highly ordered lateral movement, "surfing" toward the cell body before cell entry. Virus cell surfing along filopodia is mediated by the underlying actin cytoskeleton and depends on functional myosin II. Any disruption of virus cell surfing significantly reduces viral infection. Our results reveal another example of viruses hijacking host machineries for efficient infection by using the inherent ability of filopodia to transport ligands to the cell body. | lld:pubmed |
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pubmed-article:16027225 | pubmed:language | eng | lld:pubmed |
pubmed-article:16027225 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16027225 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:16027225 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:16027225 | pubmed:month | Jul | lld:pubmed |
pubmed-article:16027225 | pubmed:issn | 0021-9525 | lld:pubmed |
pubmed-article:16027225 | pubmed:author | pubmed-author:PypaertMarcM | lld:pubmed |
pubmed-article:16027225 | pubmed:author | pubmed-author:MothesWalther... | lld:pubmed |
pubmed-article:16027225 | pubmed:author | pubmed-author:MarksCarolyn... | lld:pubmed |
pubmed-article:16027225 | pubmed:author | pubmed-author:ShererNathan... | lld:pubmed |
pubmed-article:16027225 | pubmed:author | pubmed-author:LehmannMaik... | lld:pubmed |
pubmed-article:16027225 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:16027225 | pubmed:day | 18 | lld:pubmed |
pubmed-article:16027225 | pubmed:volume | 170 | lld:pubmed |
pubmed-article:16027225 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:16027225 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:16027225 | pubmed:pagination | 317-25 | lld:pubmed |
pubmed-article:16027225 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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pubmed-article:16027225 | pubmed:year | 2005 | lld:pubmed |
pubmed-article:16027225 | pubmed:articleTitle | Actin- and myosin-driven movement of viruses along filopodia precedes their entry into cells. | lld:pubmed |
pubmed-article:16027225 | pubmed:affiliation | Section of Microbial Pathogenesis, Yale University School of Medicine, New Haven, CT 06536, USA. | lld:pubmed |
pubmed-article:16027225 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:16027225 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:16027225 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
pubmed-article:16027225 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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