pubmed-article:387716 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:387716 | lifeskim:mentions | umls-concept:C0017366 | lld:lifeskim |
pubmed-article:387716 | lifeskim:mentions | umls-concept:C0026882 | lld:lifeskim |
pubmed-article:387716 | lifeskim:mentions | umls-concept:C0204727 | lld:lifeskim |
pubmed-article:387716 | lifeskim:mentions | umls-concept:C0205409 | lld:lifeskim |
pubmed-article:387716 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
pubmed-article:387716 | lifeskim:mentions | umls-concept:C0208233 | lld:lifeskim |
pubmed-article:387716 | pubmed:issue | 1 | lld:pubmed |
pubmed-article:387716 | pubmed:dateCreated | 1980-1-19 | lld:pubmed |
pubmed-article:387716 | pubmed:abstractText | Escherichia coli mutants defective in protease III were isolated by enzyme assays of heavily mutagenized colones. One mutant produced thermolabile enzyme, and it is presumed to have a mutation in the structural gene of protease III. Two other mutants mapping at the same site had less than 5% of the wild-type protease III level. The genetic locus of these mutations, designated ptr, was located at approximately 60 min on the E. coli linkage map based on its high frequency (70%) of contransduction by P1 with argA. Strains with less than 5% of the wild-type protease III activity grew normally and degraded nonsense fragments of beta-galactosidase at wild-type rates. | lld:pubmed |
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pubmed-article:387716 | pubmed:language | eng | lld:pubmed |
pubmed-article:387716 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:387716 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:387716 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:387716 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:387716 | pubmed:month | Oct | lld:pubmed |
pubmed-article:387716 | pubmed:issn | 0021-9193 | lld:pubmed |
pubmed-article:387716 | pubmed:author | pubmed-author:ChengY SYS | lld:pubmed |
pubmed-article:387716 | pubmed:author | pubmed-author:ZipserDD | lld:pubmed |
pubmed-article:387716 | pubmed:author | pubmed-author:ChengC YCY | lld:pubmed |
pubmed-article:387716 | pubmed:author | pubmed-author:RolsethS JSJ | lld:pubmed |
pubmed-article:387716 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:387716 | pubmed:volume | 140 | lld:pubmed |
pubmed-article:387716 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:387716 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:387716 | pubmed:pagination | 125-30 | lld:pubmed |
pubmed-article:387716 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
pubmed-article:387716 | pubmed:meshHeading | pubmed-meshheading:387716-P... | lld:pubmed |
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pubmed-article:387716 | pubmed:meshHeading | pubmed-meshheading:387716-C... | lld:pubmed |
pubmed-article:387716 | pubmed:year | 1979 | lld:pubmed |
pubmed-article:387716 | pubmed:articleTitle | Isolation and characterization of mutations in the structural gene for protease III (ptr). | lld:pubmed |
pubmed-article:387716 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:387716 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
entrez-gene:947284 | entrezgene:pubmed | pubmed-article:387716 | lld:entrezgene |
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