pubmed-article:20384695 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:20384695 | lifeskim:mentions | umls-concept:C0006837 | lld:lifeskim |
pubmed-article:20384695 | lifeskim:mentions | umls-concept:C0007634 | lld:lifeskim |
pubmed-article:20384695 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
pubmed-article:20384695 | lifeskim:mentions | umls-concept:C0033414 | lld:lifeskim |
pubmed-article:20384695 | lifeskim:mentions | umls-concept:C0205281 | lld:lifeskim |
pubmed-article:20384695 | lifeskim:mentions | umls-concept:C0439536 | lld:lifeskim |
pubmed-article:20384695 | pubmed:issue | 3 | lld:pubmed |
pubmed-article:20384695 | pubmed:dateCreated | 2010-6-15 | lld:pubmed |
pubmed-article:20384695 | pubmed:abstractText | Growth of cells in contact with an abiotic or biological surface profoundly affects cellular physiology. In the opportunistic human pathogen, Candida albicans, growth on a semi-solid matrix such as agar results in invasive filamentation, a process in which cells change their morphology to highly elongated filamentous hyphae that grow into the matrix. We hypothesized that a plasma membrane receptor-type protein would sense the presence of matrix and activate a signal transduction cascade, thus promoting invasive filamentation. In this communication, we demonstrate that during growth in contact with a semi-solid surface, activation of a MAP kinase, Cek1p, is promoted, in part, by a plasma membrane protein termed Dfi1p and results in invasive filamentation. A C. albicans mutant lacking Dfi1p showed reduced virulence in a murine model of disseminated candidiasis. Dfi1p is a relatively small, integral membrane protein that localizes to the plasma membrane. Some Dfi1p molecules become cross-linked to the carbohydrate polymers of the cell wall. Thus, Dfi1p is capable of linking the cell wall to the plasma membrane and cytoplasm. | lld:pubmed |
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pubmed-article:20384695 | pubmed:language | eng | lld:pubmed |
pubmed-article:20384695 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20384695 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:20384695 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:20384695 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:20384695 | pubmed:month | May | lld:pubmed |
pubmed-article:20384695 | pubmed:issn | 1365-2958 | lld:pubmed |
pubmed-article:20384695 | pubmed:author | pubmed-author:KumamotoCarol... | lld:pubmed |
pubmed-article:20384695 | pubmed:author | pubmed-author:DavisTalya... | lld:pubmed |
pubmed-article:20384695 | pubmed:author | pubmed-author:ZucchiPaola... | lld:pubmed |
pubmed-article:20384695 | pubmed:issnType | Electronic | lld:pubmed |
pubmed-article:20384695 | pubmed:volume | 76 | lld:pubmed |
pubmed-article:20384695 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:20384695 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:20384695 | pubmed:pagination | 733-48 | lld:pubmed |
pubmed-article:20384695 | pubmed:dateRevised | 2011-9-26 | lld:pubmed |
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pubmed-article:20384695 | pubmed:year | 2010 | lld:pubmed |
pubmed-article:20384695 | pubmed:articleTitle | A Candida albicans cell wall-linked protein promotes invasive filamentation into semi-solid medium. | lld:pubmed |
pubmed-article:20384695 | pubmed:affiliation | Department of Molecular Biology and Microbiology, Tufts University, Boston, MA 02111, USA. | lld:pubmed |
pubmed-article:20384695 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:20384695 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |