| pubmed-article:9195754 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9195754 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:9195754 | lifeskim:mentions | umls-concept:C0072354 | lld:lifeskim |
| pubmed-article:9195754 | lifeskim:mentions | umls-concept:C0018896 | lld:lifeskim |
| pubmed-article:9195754 | lifeskim:mentions | umls-concept:C0596988 | lld:lifeskim |
| pubmed-article:9195754 | lifeskim:mentions | umls-concept:C0162847 | lld:lifeskim |
| pubmed-article:9195754 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:9195754 | pubmed:dateCreated | 1997-7-29 | lld:pubmed |
| pubmed-article:9195754 | pubmed:abstractText | Human protein disulfide isomerase with an extra 10 amino acid residues of AEITRIDPAM at the N-terminal was expressed in E. coli as a soluble protein comprising 20% of total cell proteins, and was purified to near homogeneity through one step of DEAE-Sephacel chromatography. The mutant enzyme, which had the same CD spectrum and comparable disulfide isomerase and thiol-protein oxidoreductase activities with that of the wild type human and bovine protein disulfide isomerases, also showed chaperone-like activity in stimulating the refolding of proteins containing no disulfide bond. The overall yield of the active product is about 20 mg 1-1 culture. | lld:pubmed |
| pubmed-article:9195754 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9195754 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9195754 | pubmed:citationSubset | B | lld:pubmed |
| pubmed-article:9195754 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9195754 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9195754 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9195754 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9195754 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9195754 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9195754 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:9195754 | pubmed:issn | 0168-1656 | lld:pubmed |
| pubmed-article:9195754 | pubmed:author | pubmed-author:WangC CCC | lld:pubmed |
| pubmed-article:9195754 | pubmed:author | pubmed-author:GaySS | lld:pubmed |
| pubmed-article:9195754 | pubmed:author | pubmed-author:DaiYY | lld:pubmed |
| pubmed-article:9195754 | pubmed:author | pubmed-author:JiangMM | lld:pubmed |
| pubmed-article:9195754 | pubmed:author | pubmed-author:QuanHH | lld:pubmed |
| pubmed-article:9195754 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9195754 | pubmed:day | 25 | lld:pubmed |
| pubmed-article:9195754 | pubmed:volume | 54 | lld:pubmed |
| pubmed-article:9195754 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9195754 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9195754 | pubmed:pagination | 105-12 | lld:pubmed |
| pubmed-article:9195754 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
| pubmed-article:9195754 | pubmed:meshHeading | pubmed-meshheading:9195754-... | lld:pubmed |
| pubmed-article:9195754 | pubmed:meshHeading | pubmed-meshheading:9195754-... | lld:pubmed |
| pubmed-article:9195754 | pubmed:meshHeading | pubmed-meshheading:9195754-... | lld:pubmed |
| pubmed-article:9195754 | pubmed:meshHeading | pubmed-meshheading:9195754-... | lld:pubmed |
| pubmed-article:9195754 | pubmed:meshHeading | pubmed-meshheading:9195754-... | lld:pubmed |
| pubmed-article:9195754 | pubmed:meshHeading | pubmed-meshheading:9195754-... | lld:pubmed |
| pubmed-article:9195754 | pubmed:meshHeading | pubmed-meshheading:9195754-... | lld:pubmed |
| pubmed-article:9195754 | pubmed:meshHeading | pubmed-meshheading:9195754-... | lld:pubmed |
| pubmed-article:9195754 | pubmed:meshHeading | pubmed-meshheading:9195754-... | lld:pubmed |
| pubmed-article:9195754 | pubmed:meshHeading | pubmed-meshheading:9195754-... | lld:pubmed |
| pubmed-article:9195754 | pubmed:meshHeading | pubmed-meshheading:9195754-... | lld:pubmed |
| pubmed-article:9195754 | pubmed:meshHeading | pubmed-meshheading:9195754-... | lld:pubmed |
| pubmed-article:9195754 | pubmed:meshHeading | pubmed-meshheading:9195754-... | lld:pubmed |
| pubmed-article:9195754 | pubmed:meshHeading | pubmed-meshheading:9195754-... | lld:pubmed |
| pubmed-article:9195754 | pubmed:year | 1997 | lld:pubmed |
| pubmed-article:9195754 | pubmed:articleTitle | Mutant human protein disulfide isomerase assists protein folding in a chaperone-like fashion. | lld:pubmed |
| pubmed-article:9195754 | pubmed:affiliation | National Laboratory of Biomacromolecules, Academia Sinica, Beijing, People's Republic of China. | lld:pubmed |
| pubmed-article:9195754 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9195754 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
