pubmed-article:2173693 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:2173693 | lifeskim:mentions | umls-concept:C0036025 | lld:lifeskim |
pubmed-article:2173693 | lifeskim:mentions | umls-concept:C1260875 | lld:lifeskim |
pubmed-article:2173693 | lifeskim:mentions | umls-concept:C0031516 | lld:lifeskim |
pubmed-article:2173693 | lifeskim:mentions | umls-concept:C0017337 | lld:lifeskim |
pubmed-article:2173693 | lifeskim:mentions | umls-concept:C0025723 | lld:lifeskim |
pubmed-article:2173693 | lifeskim:mentions | umls-concept:C1546857 | lld:lifeskim |
pubmed-article:2173693 | lifeskim:mentions | umls-concept:C1556066 | lld:lifeskim |
pubmed-article:2173693 | lifeskim:mentions | umls-concept:C1619636 | lld:lifeskim |
pubmed-article:2173693 | lifeskim:mentions | umls-concept:C1514873 | lld:lifeskim |
pubmed-article:2173693 | lifeskim:mentions | umls-concept:C0050325 | lld:lifeskim |
pubmed-article:2173693 | pubmed:issue | 33 | lld:pubmed |
pubmed-article:2173693 | pubmed:dateCreated | 1990-12-28 | lld:pubmed |
pubmed-article:2173693 | pubmed:abstractText | Saccharomyces cerevisiae a-factor is a dodecapeptide pheromone in which the carboxyl group of the COOH-terminal cysteine residue is methyl-esterified and the sulfhydryl side chain is conjugated in thioether linkage to a farnesyl moiety. We found that MAT a ste14 mutant cells secreted a biologically inactive form of a-factor which had more hydrophilic character than the wild-type pheromone. The authentic pheromone could be metabolically labeled with [methyl-3H]methionine, and the resulting COOH-terminal methyl ester could be removed by mild alkaline hydrolysis. In contrast, a-factor secreted by ste14 mutants did not incorporate a base-labile 3H-methyl moiety. Base treatment converted the normal pheromone into a form which was biologically inactive and which comigrated with the ste14 form of the peptide upon thin-layer chromatography. These results indicate that STE14 gene function is required for COOH-terminal methylation of a-factor. | lld:pubmed |
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pubmed-article:2173693 | pubmed:language | eng | lld:pubmed |
pubmed-article:2173693 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2173693 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:2173693 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:2173693 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:2173693 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2173693 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:2173693 | pubmed:month | Nov | lld:pubmed |
pubmed-article:2173693 | pubmed:issn | 0021-9258 | lld:pubmed |
pubmed-article:2173693 | pubmed:author | pubmed-author:ThornerJJ | lld:pubmed |
pubmed-article:2173693 | pubmed:author | pubmed-author:BlairL CLC | lld:pubmed |
pubmed-article:2173693 | pubmed:author | pubmed-author:MarrR SRS | lld:pubmed |
pubmed-article:2173693 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:2173693 | pubmed:day | 25 | lld:pubmed |
pubmed-article:2173693 | pubmed:volume | 265 | lld:pubmed |
pubmed-article:2173693 | pubmed:geneSymbol | ste14 | lld:pubmed |
pubmed-article:2173693 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:2173693 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:2173693 | pubmed:pagination | 20057-60 | lld:pubmed |
pubmed-article:2173693 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
pubmed-article:2173693 | pubmed:meshHeading | pubmed-meshheading:2173693-... | lld:pubmed |
pubmed-article:2173693 | pubmed:meshHeading | pubmed-meshheading:2173693-... | lld:pubmed |
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pubmed-article:2173693 | pubmed:meshHeading | pubmed-meshheading:2173693-... | lld:pubmed |
pubmed-article:2173693 | pubmed:meshHeading | pubmed-meshheading:2173693-... | lld:pubmed |
pubmed-article:2173693 | pubmed:meshHeading | pubmed-meshheading:2173693-... | lld:pubmed |
pubmed-article:2173693 | pubmed:meshHeading | pubmed-meshheading:2173693-... | lld:pubmed |
pubmed-article:2173693 | pubmed:meshHeading | pubmed-meshheading:2173693-... | lld:pubmed |
pubmed-article:2173693 | pubmed:year | 1990 | lld:pubmed |
pubmed-article:2173693 | pubmed:articleTitle | Saccharomyces cerevisiae STE14 gene is required for COOH-terminal methylation of a-factor mating pheromone. | lld:pubmed |
pubmed-article:2173693 | pubmed:affiliation | Department of Molecular and Cell Biology, University of California, Berkeley 94720. | lld:pubmed |
pubmed-article:2173693 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:2173693 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:2173693 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
entrez-gene:852019 | entrezgene:pubmed | pubmed-article:2173693 | lld:entrezgene |
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