| pubmed-article:1904218 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1904218 | lifeskim:mentions | umls-concept:C0205102 | lld:lifeskim |
| pubmed-article:1904218 | lifeskim:mentions | umls-concept:C0005220 | lld:lifeskim |
| pubmed-article:1904218 | lifeskim:mentions | umls-concept:C0205245 | lld:lifeskim |
| pubmed-article:1904218 | lifeskim:mentions | umls-concept:C0332466 | lld:lifeskim |
| pubmed-article:1904218 | lifeskim:mentions | umls-concept:C0017262 | lld:lifeskim |
| pubmed-article:1904218 | lifeskim:mentions | umls-concept:C0332256 | lld:lifeskim |
| pubmed-article:1904218 | lifeskim:mentions | umls-concept:C2911684 | lld:lifeskim |
| pubmed-article:1904218 | lifeskim:mentions | umls-concept:C0138765 | lld:lifeskim |
| pubmed-article:1904218 | lifeskim:mentions | umls-concept:C0185117 | lld:lifeskim |
| pubmed-article:1904218 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:1904218 | pubmed:dateCreated | 1991-7-5 | lld:pubmed |
| pubmed-article:1904218 | pubmed:abstractText | Alpha complementation of beta-galactosidase (beta gal) is intracistronic and requires interaction between the alpha donor region (residues 3-41) and alpha acceptor fragment (produced by M15). We have constructed two plasmids which direct the synthesis of hybrid beta gal: coxsackievirus proteins in Escherichia coli. One plasmid, pBD1045, encodes an enzymatically active 3C protease of coxsackievirus B3 fused between the amino-terminal 79 amino acids of beta gal (containing the alpha donor region) and amino acids 80 to 1023 (alpha acceptor region). A second plasmid, pBD1043 encodes an inactive 3C protease and results in a fusion of 260 coxsackievirus amino acids between residues 79 and 80 of the beta gal monomer. Both hybrid proteins expressed by these constructs have beta-galactosidase activity regardless of whether the viral protease (183 amino acids) is autocatalytically cleaved out of the chimeric protein (pBD1045) or remains as part of a fusion protein (pBD1043). The implications of these results for structural flexibility of the complemented beta-galactosidase enzyme are discussed. | lld:pubmed |
| pubmed-article:1904218 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1904218 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1904218 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:1904218 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1904218 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1904218 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1904218 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1904218 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1904218 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1904218 | pubmed:month | May | lld:pubmed |
| pubmed-article:1904218 | pubmed:issn | 0006-291X | lld:pubmed |
| pubmed-article:1904218 | pubmed:author | pubmed-author:DasmahapatraB... | lld:pubmed |
| pubmed-article:1904218 | pubmed:author | pubmed-author:DwyerSS | lld:pubmed |
| pubmed-article:1904218 | pubmed:author | pubmed-author:WindheuserM... | lld:pubmed |
| pubmed-article:1904218 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1904218 | pubmed:day | 31 | lld:pubmed |
| pubmed-article:1904218 | pubmed:volume | 177 | lld:pubmed |
| pubmed-article:1904218 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1904218 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1904218 | pubmed:pagination | 243-51 | lld:pubmed |
| pubmed-article:1904218 | pubmed:dateRevised | 2007-10-11 | lld:pubmed |
| pubmed-article:1904218 | pubmed:meshHeading | pubmed-meshheading:1904218-... | lld:pubmed |
| pubmed-article:1904218 | pubmed:meshHeading | pubmed-meshheading:1904218-... | lld:pubmed |
| pubmed-article:1904218 | pubmed:meshHeading | pubmed-meshheading:1904218-... | lld:pubmed |
| pubmed-article:1904218 | pubmed:meshHeading | pubmed-meshheading:1904218-... | lld:pubmed |
| pubmed-article:1904218 | pubmed:meshHeading | pubmed-meshheading:1904218-... | lld:pubmed |
| pubmed-article:1904218 | pubmed:meshHeading | pubmed-meshheading:1904218-... | lld:pubmed |
| pubmed-article:1904218 | pubmed:meshHeading | pubmed-meshheading:1904218-... | lld:pubmed |
| pubmed-article:1904218 | pubmed:meshHeading | pubmed-meshheading:1904218-... | lld:pubmed |
| pubmed-article:1904218 | pubmed:meshHeading | pubmed-meshheading:1904218-... | lld:pubmed |
| pubmed-article:1904218 | pubmed:meshHeading | pubmed-meshheading:1904218-... | lld:pubmed |
| pubmed-article:1904218 | pubmed:meshHeading | pubmed-meshheading:1904218-... | lld:pubmed |
| pubmed-article:1904218 | pubmed:meshHeading | pubmed-meshheading:1904218-... | lld:pubmed |
| pubmed-article:1904218 | pubmed:meshHeading | pubmed-meshheading:1904218-... | lld:pubmed |
| pubmed-article:1904218 | pubmed:meshHeading | pubmed-meshheading:1904218-... | lld:pubmed |
| pubmed-article:1904218 | pubmed:year | 1991 | lld:pubmed |
| pubmed-article:1904218 | pubmed:articleTitle | Expression of functional beta-galactosidase containing the coxsackievirus 3C protease as an internal fusion. | lld:pubmed |
| pubmed-article:1904218 | pubmed:affiliation | Schering-Plough Research, Bloomfield, New Jersey 07003. | lld:pubmed |
| pubmed-article:1904218 | pubmed:publicationType | Journal Article | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:1904218 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:1904218 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:1904218 | lld:pubmed |
