pubmed-article:7500943 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:7500943 | lifeskim:mentions | umls-concept:C0043393 | lld:lifeskim |
pubmed-article:7500943 | lifeskim:mentions | umls-concept:C0699040 | lld:lifeskim |
pubmed-article:7500943 | pubmed:issue | 2 | lld:pubmed |
pubmed-article:7500943 | pubmed:dateCreated | 1996-1-17 | lld:pubmed |
pubmed-article:7500943 | pubmed:abstractText | The Saccharomyces cerevisiae KRE1 gene encodes a secretory protein required for the production of the cell wall polymer (1-->6)-beta-glucan. Here we report further characterization of the KRE1 gene product, Kre1p. A functional, epitope-tagged Kre1p is shown to be highly modified in a SEC53-dependent manner. Kre1p is O-glycosylated, but the basis for the majority of its post-translational modification is unknown. Fractionation of Kre1p reveals a cell wall-associated form and a less abundant membrane-associated species. Indirect immunoflurorescence demonstrates that Kre1p localizes to the cell surface, where it becomes concentrated at the surface of mother cells. Such a localization of Kre1p seems to parallel the CAL1/CSD2-dependent cell wall deposition of chitin found in S. cerevisiae, and is consistent with evidence from Schizophyllum commune that (1-->6)-beta-glucan accumulates during maturation of the subapical region of the wall distal to the hyphal tip. | lld:pubmed |
pubmed-article:7500943 | pubmed:language | eng | lld:pubmed |
pubmed-article:7500943 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7500943 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:7500943 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7500943 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7500943 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7500943 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7500943 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7500943 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7500943 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:7500943 | pubmed:month | Nov | lld:pubmed |
pubmed-article:7500943 | pubmed:issn | 0026-8925 | lld:pubmed |
pubmed-article:7500943 | pubmed:author | pubmed-author:BusseyHH | lld:pubmed |
pubmed-article:7500943 | pubmed:author | pubmed-author:RoemerTT | lld:pubmed |
pubmed-article:7500943 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:7500943 | pubmed:day | 15 | lld:pubmed |
pubmed-article:7500943 | pubmed:volume | 249 | lld:pubmed |
pubmed-article:7500943 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:7500943 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:7500943 | pubmed:pagination | 209-16 | lld:pubmed |
pubmed-article:7500943 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
pubmed-article:7500943 | pubmed:meshHeading | pubmed-meshheading:7500943-... | lld:pubmed |
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pubmed-article:7500943 | pubmed:year | 1995 | lld:pubmed |
pubmed-article:7500943 | pubmed:articleTitle | Yeast Kre1p is a cell surface O-glycoprotein. | lld:pubmed |
pubmed-article:7500943 | pubmed:affiliation | Biology Department, McGill University, Montreal, Quebec, Canada. | lld:pubmed |
pubmed-article:7500943 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:7500943 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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