| pubmed-article:15449306 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15449306 | lifeskim:mentions | umls-concept:C0178453 | lld:lifeskim |
| pubmed-article:15449306 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:15449306 | pubmed:issue | 12 | lld:pubmed |
| pubmed-article:15449306 | pubmed:dateCreated | 2004-10-6 | lld:pubmed |
| pubmed-article:15449306 | pubmed:abstractText | Endoplasmic reticulum oxidoreductins (Ero proteins) are essential for oxidation of protein disulphide isomerase (Pdi), which introduces disulphide bonds in target proteins. Contrary to the situation in Saccharomyces cerevisiae, with a single Ero protein (Ero1p), the genomes of Schizosaccharomyces pombe and of humans encode two Ero-like proteins. Here we show that both Sz. pombe proteins (SpEro1a p and SpEro1b p) are N-glycosylated and firmly associated with membranes of the secretory pathway. Surprisingly, only expression of SpEro1b p completely restores growth of the temperature-sensitive S. cerevisiae ero1-1 mutant, whereas SpEro1a p only partially complements this mutation. Upon expression in S. cerevisiae wild-type cells, SpEro1b p leads to a significantly increased resistance to reductive stress by dithiothreitol, whereas SpEro1a p has only a marginal effect. These data suggest that SpEro1b p is a functional homologue of the S. cerevisiae Ero1p. | lld:pubmed |
| pubmed-article:15449306 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15449306 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15449306 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:15449306 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15449306 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15449306 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15449306 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15449306 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15449306 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:15449306 | pubmed:issn | 0749-503X | lld:pubmed |
| pubmed-article:15449306 | pubmed:author | pubmed-author:BlombergAnder... | lld:pubmed |
| pubmed-article:15449306 | pubmed:author | pubmed-author:RödelGerhardG | lld:pubmed |
| pubmed-article:15449306 | pubmed:author | pubmed-author:KettnerKarina... | lld:pubmed |
| pubmed-article:15449306 | pubmed:copyrightInfo | Copyright (c) 2004 John Wiley & Sons, Ltd. | lld:pubmed |
| pubmed-article:15449306 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15449306 | pubmed:volume | 21 | lld:pubmed |
| pubmed-article:15449306 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15449306 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15449306 | pubmed:pagination | 1035-44 | lld:pubmed |
| pubmed-article:15449306 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:15449306 | pubmed:meshHeading | pubmed-meshheading:15449306... | lld:pubmed |
| pubmed-article:15449306 | pubmed:meshHeading | pubmed-meshheading:15449306... | lld:pubmed |
| pubmed-article:15449306 | pubmed:meshHeading | pubmed-meshheading:15449306... | lld:pubmed |
| pubmed-article:15449306 | pubmed:meshHeading | pubmed-meshheading:15449306... | lld:pubmed |
| pubmed-article:15449306 | pubmed:meshHeading | pubmed-meshheading:15449306... | lld:pubmed |
| pubmed-article:15449306 | pubmed:meshHeading | pubmed-meshheading:15449306... | lld:pubmed |
| pubmed-article:15449306 | pubmed:meshHeading | pubmed-meshheading:15449306... | lld:pubmed |
| pubmed-article:15449306 | pubmed:meshHeading | pubmed-meshheading:15449306... | lld:pubmed |
| pubmed-article:15449306 | pubmed:meshHeading | pubmed-meshheading:15449306... | lld:pubmed |
| pubmed-article:15449306 | pubmed:meshHeading | pubmed-meshheading:15449306... | lld:pubmed |
| pubmed-article:15449306 | pubmed:meshHeading | pubmed-meshheading:15449306... | lld:pubmed |
| pubmed-article:15449306 | pubmed:meshHeading | pubmed-meshheading:15449306... | lld:pubmed |
| pubmed-article:15449306 | pubmed:meshHeading | pubmed-meshheading:15449306... | lld:pubmed |
| pubmed-article:15449306 | pubmed:meshHeading | pubmed-meshheading:15449306... | lld:pubmed |
| pubmed-article:15449306 | pubmed:meshHeading | pubmed-meshheading:15449306... | lld:pubmed |
| pubmed-article:15449306 | pubmed:year | 2004 | lld:pubmed |
| pubmed-article:15449306 | pubmed:articleTitle | Schizosaccharomyces pombe ER oxidoreductin-like proteins SpEro1a p and SpEro1b p. | lld:pubmed |
| pubmed-article:15449306 | pubmed:affiliation | Institute for Genetics, Dresden University of Technology, D-01262, Germany. | lld:pubmed |
| pubmed-article:15449306 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15449306 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:2540901 | entrezgene:pubmed | pubmed-article:15449306 | lld:entrezgene |
| entrez-gene:2539325 | entrezgene:pubmed | pubmed-article:15449306 | lld:entrezgene |
