pubmed-article:15848158 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:15848158 | lifeskim:mentions | umls-concept:C0036025 | lld:lifeskim |
pubmed-article:15848158 | lifeskim:mentions | umls-concept:C0036536 | lld:lifeskim |
pubmed-article:15848158 | lifeskim:mentions | umls-concept:C0036537 | lld:lifeskim |
pubmed-article:15848158 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
pubmed-article:15848158 | lifeskim:mentions | umls-concept:C1280500 | lld:lifeskim |
pubmed-article:15848158 | lifeskim:mentions | umls-concept:C0017260 | lld:lifeskim |
pubmed-article:15848158 | lifeskim:mentions | umls-concept:C0221821 | lld:lifeskim |
pubmed-article:15848158 | lifeskim:mentions | umls-concept:C1517294 | lld:lifeskim |
pubmed-article:15848158 | pubmed:issue | 11 | lld:pubmed |
pubmed-article:15848158 | pubmed:dateCreated | 2005-4-25 | lld:pubmed |
pubmed-article:15848158 | pubmed:abstractText | Both amyloid-prone cystatin and unstable mutant C94A lysozyme were secreted in wild-type and Deltaeps1 Saccharomyces cerevisiae cells. Amyloid-prone cystatin secreted at much higher level in Deltaeps1 cells than that in wild-type yeast. In parallel, the secretion amount of disulfide bond disrupted mutant C94A lysozyme greatly increased in Deltaeps1 cells although that was apparently low in wild-type yeast cells compared with the secretion amount of wild-type lysozyme. It is interesting that neither the unstable mutant C94A lysozyme nor amyloid-prone cystatin secreted in Deltaeps1 cells maintained their specific activities. These observations lead to the supposition that yeast cells deficient for the protein disulfide isomerase-family-member EPS1 locus secrete more of labile disulfide-containing model proteins. | lld:pubmed |
pubmed-article:15848158 | pubmed:language | eng | lld:pubmed |
pubmed-article:15848158 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15848158 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:15848158 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15848158 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15848158 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15848158 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15848158 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15848158 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15848158 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15848158 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15848158 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15848158 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15848158 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:15848158 | pubmed:month | Apr | lld:pubmed |
pubmed-article:15848158 | pubmed:issn | 0014-5793 | lld:pubmed |
pubmed-article:15848158 | pubmed:author | pubmed-author:SaitoAkiraA | lld:pubmed |
pubmed-article:15848158 | pubmed:author | pubmed-author:SongYoutaoY | lld:pubmed |
pubmed-article:15848158 | pubmed:author | pubmed-author:AzakamiHiroyu... | lld:pubmed |
pubmed-article:15848158 | pubmed:author | pubmed-author:HeJianweiJ | lld:pubmed |
pubmed-article:15848158 | pubmed:author | pubmed-author:KatoAkioA | lld:pubmed |
pubmed-article:15848158 | pubmed:author | pubmed-author:SakamotoTakas... | lld:pubmed |
pubmed-article:15848158 | pubmed:author | pubmed-author:HaradaAkihito... | lld:pubmed |
pubmed-article:15848158 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:15848158 | pubmed:day | 25 | lld:pubmed |
pubmed-article:15848158 | pubmed:volume | 579 | lld:pubmed |
pubmed-article:15848158 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:15848158 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:15848158 | pubmed:pagination | 2277-83 | lld:pubmed |
pubmed-article:15848158 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
pubmed-article:15848158 | pubmed:meshHeading | pubmed-meshheading:15848158... | lld:pubmed |
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pubmed-article:15848158 | pubmed:meshHeading | pubmed-meshheading:15848158... | lld:pubmed |
pubmed-article:15848158 | pubmed:meshHeading | pubmed-meshheading:15848158... | lld:pubmed |
pubmed-article:15848158 | pubmed:year | 2005 | lld:pubmed |
pubmed-article:15848158 | pubmed:articleTitle | Effect of EPS1 gene deletion in Saccharomyces cerevisiae on the secretion of foreign proteins which have disulfide bridges. | lld:pubmed |
pubmed-article:15848158 | pubmed:affiliation | Department of Biological Chemistry, Yamaguchi University, Japan. | lld:pubmed |
pubmed-article:15848158 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:15848158 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:15848158 | lld:pubmed |