pubmed-article:8527941 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:8527941 | lifeskim:mentions | umls-concept:C0036025 | lld:lifeskim |
pubmed-article:8527941 | lifeskim:mentions | umls-concept:C1327616 | lld:lifeskim |
pubmed-article:8527941 | lifeskim:mentions | umls-concept:C1514559 | lld:lifeskim |
pubmed-article:8527941 | lifeskim:mentions | umls-concept:C0003641 | lld:lifeskim |
pubmed-article:8527941 | lifeskim:mentions | umls-concept:C0162847 | lld:lifeskim |
pubmed-article:8527941 | lifeskim:mentions | umls-concept:C1516240 | lld:lifeskim |
pubmed-article:8527941 | pubmed:issue | 4 | lld:pubmed |
pubmed-article:8527941 | pubmed:dateCreated | 1996-1-30 | lld:pubmed |
pubmed-article:8527941 | pubmed:abstractText | Bovine pancreatic trypsin inhibitor (BPTI) was expressed and secreted from a synthetic gene as a model system for the study of protein folding and secretion in Saccharomyces cerevisiae. The efficiency of different leader sequences in directing BPTI secretion was examined, and up to 11 micrograms/ml of active BPTI was secreted. In some fusion constructs, inefficient proteolytic processing by Kex2p, Ste13p, and signal peptidase were observed immediately adjacent to the BPTI N terminus. Insertion of dipeptide spacers improved endoproteolytic processing substantially but the level of secretion was unchanged. Overexpression from a 2-microns multicopy vector results in essentially unchanged BPTI secretion as compared to expression from a single copy centromere vector. BPTI expressed from a multicopy vector accumulates intracellularly in an unfolded form, indicating that available secretory chaperones and foldases can be saturated by increasing the rate of BPTI synthesis. | lld:pubmed |
pubmed-article:8527941 | pubmed:language | eng | lld:pubmed |
pubmed-article:8527941 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8527941 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:8527941 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8527941 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8527941 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8527941 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8527941 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:8527941 | pubmed:month | Aug | lld:pubmed |
pubmed-article:8527941 | pubmed:issn | 1046-5928 | lld:pubmed |
pubmed-article:8527941 | pubmed:author | pubmed-author:ParekhRR | lld:pubmed |
pubmed-article:8527941 | pubmed:author | pubmed-author:ForresterKK | lld:pubmed |
pubmed-article:8527941 | pubmed:author | pubmed-author:WittrupDD | lld:pubmed |
pubmed-article:8527941 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:8527941 | pubmed:volume | 6 | lld:pubmed |
pubmed-article:8527941 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:8527941 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:8527941 | pubmed:pagination | 537-45 | lld:pubmed |
pubmed-article:8527941 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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pubmed-article:8527941 | pubmed:year | 1995 | lld:pubmed |
pubmed-article:8527941 | pubmed:articleTitle | Multicopy overexpression of bovine pancreatic trypsin inhibitor saturates the protein folding and secretory capacity of Saccharomyces cerevisiae. | lld:pubmed |
pubmed-article:8527941 | pubmed:affiliation | Department of Chemical Engineering, University of Illinois, Urbana 61801, USA. | lld:pubmed |
pubmed-article:8527941 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:8527941 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
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