| pubmed-article:2683070 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2683070 | lifeskim:mentions | umls-concept:C0178719 | lld:lifeskim |
| pubmed-article:2683070 | lifeskim:mentions | umls-concept:C0599894 | lld:lifeskim |
| pubmed-article:2683070 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:2683070 | lifeskim:mentions | umls-concept:C2347858 | lld:lifeskim |
| pubmed-article:2683070 | pubmed:issue | 4929 | lld:pubmed |
| pubmed-article:2683070 | pubmed:dateCreated | 1989-12-4 | lld:pubmed |
| pubmed-article:2683070 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2683070 | pubmed:abstractText | The prohormone-processing endoprotease (KEX2 gene product) of the yeast Saccharomyces cerevisiae is a membrane-bound, 135,000-dalton glycoprotein, which contains both asparagine-linked and serine- and threonine-linked oligosaccharide and resides in a secretory compartment. Analysis of mutant kex2 genes truncated at their 3' end indicates that carboxyl terminal domains of the enzyme are required for its proper localization within the cell. A human gene product, "furin," shares 50% identity with the catalytic domain of Kex2 protease and is, therefore, a candidate for a human prohormone-processing enzyme. | lld:pubmed |
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| pubmed-article:2683070 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2683070 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2683070 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2683070 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:2683070 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:2683070 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2683070 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:2683070 | pubmed:issn | 0036-8075 | lld:pubmed |
| pubmed-article:2683070 | pubmed:author | pubmed-author:BrakeA JAJ | lld:pubmed |
| pubmed-article:2683070 | pubmed:author | pubmed-author:ThornerJJ | lld:pubmed |
| pubmed-article:2683070 | pubmed:author | pubmed-author:FullerR SRS | lld:pubmed |
| pubmed-article:2683070 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2683070 | pubmed:day | 27 | lld:pubmed |
| pubmed-article:2683070 | pubmed:volume | 246 | lld:pubmed |
| pubmed-article:2683070 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2683070 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2683070 | pubmed:pagination | 482-6 | lld:pubmed |
| pubmed-article:2683070 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:2683070 | pubmed:meshHeading | pubmed-meshheading:2683070-... | lld:pubmed |
| pubmed-article:2683070 | pubmed:year | 1989 | lld:pubmed |
| pubmed-article:2683070 | pubmed:articleTitle | Intracellular targeting and structural conservation of a prohormone-processing endoprotease. | lld:pubmed |
| pubmed-article:2683070 | pubmed:affiliation | Department of Biochemistry, University of California, Berkeley 94720. | lld:pubmed |
| pubmed-article:2683070 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2683070 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:2683070 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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