| pubmed-article:8591049 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8591049 | lifeskim:mentions | umls-concept:C0332307 | lld:lifeskim |
| pubmed-article:8591049 | lifeskim:mentions | umls-concept:C0014834 | lld:lifeskim |
| pubmed-article:8591049 | lifeskim:mentions | umls-concept:C0034348 | lld:lifeskim |
| pubmed-article:8591049 | lifeskim:mentions | umls-concept:C0444626 | lld:lifeskim |
| pubmed-article:8591049 | lifeskim:mentions | umls-concept:C1853126 | lld:lifeskim |
| pubmed-article:8591049 | lifeskim:mentions | umls-concept:C1705165 | lld:lifeskim |
| pubmed-article:8591049 | lifeskim:mentions | umls-concept:C2700061 | lld:lifeskim |
| pubmed-article:8591049 | pubmed:issue | 7 | lld:pubmed |
| pubmed-article:8591049 | pubmed:dateCreated | 1996-4-3 | lld:pubmed |
| pubmed-article:8591049 | pubmed:abstractText | Pyruvate kinase (PK) plays a major role in the regulation of glycolysis. Its catalytic activity is controlled by the substrate phosphoenolpyruvate and by one or more allosteric effectors. The crystal structures of the non-allosteric PKs from cat and rabbit muscle are known. We have determined the three-dimensional structure of the allosteric type I PK from Escherichia coli, in order to study the mechanism of allosteric regulation. | lld:pubmed |
| pubmed-article:8591049 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8591049 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8591049 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8591049 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8591049 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8591049 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8591049 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:8591049 | pubmed:issn | 0969-2126 | lld:pubmed |
| pubmed-article:8591049 | pubmed:author | pubmed-author:SperanzaM LML | lld:pubmed |
| pubmed-article:8591049 | pubmed:author | pubmed-author:BolognesiMM | lld:pubmed |
| pubmed-article:8591049 | pubmed:author | pubmed-author:CodaAA | lld:pubmed |
| pubmed-article:8591049 | pubmed:author | pubmed-author:RizzoGG | lld:pubmed |
| pubmed-article:8591049 | pubmed:author | pubmed-author:ValentiniGG | lld:pubmed |
| pubmed-article:8591049 | pubmed:author | pubmed-author:MatteviAA | lld:pubmed |
| pubmed-article:8591049 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8591049 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:8591049 | pubmed:volume | 3 | lld:pubmed |
| pubmed-article:8591049 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8591049 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8591049 | pubmed:pagination | 729-41 | lld:pubmed |
| pubmed-article:8591049 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:8591049 | pubmed:meshHeading | pubmed-meshheading:8591049-... | lld:pubmed |
| pubmed-article:8591049 | pubmed:meshHeading | pubmed-meshheading:8591049-... | lld:pubmed |
| pubmed-article:8591049 | pubmed:meshHeading | pubmed-meshheading:8591049-... | lld:pubmed |
| pubmed-article:8591049 | pubmed:meshHeading | pubmed-meshheading:8591049-... | lld:pubmed |
| pubmed-article:8591049 | pubmed:meshHeading | pubmed-meshheading:8591049-... | lld:pubmed |
| pubmed-article:8591049 | pubmed:meshHeading | pubmed-meshheading:8591049-... | lld:pubmed |
| pubmed-article:8591049 | pubmed:meshHeading | pubmed-meshheading:8591049-... | lld:pubmed |
| pubmed-article:8591049 | pubmed:meshHeading | pubmed-meshheading:8591049-... | lld:pubmed |
| pubmed-article:8591049 | pubmed:meshHeading | pubmed-meshheading:8591049-... | lld:pubmed |
| pubmed-article:8591049 | pubmed:meshHeading | pubmed-meshheading:8591049-... | lld:pubmed |
| pubmed-article:8591049 | pubmed:meshHeading | pubmed-meshheading:8591049-... | lld:pubmed |
| pubmed-article:8591049 | pubmed:meshHeading | pubmed-meshheading:8591049-... | lld:pubmed |
| pubmed-article:8591049 | pubmed:meshHeading | pubmed-meshheading:8591049-... | lld:pubmed |
| pubmed-article:8591049 | pubmed:meshHeading | pubmed-meshheading:8591049-... | lld:pubmed |
| pubmed-article:8591049 | pubmed:meshHeading | pubmed-meshheading:8591049-... | lld:pubmed |
| pubmed-article:8591049 | pubmed:meshHeading | pubmed-meshheading:8591049-... | lld:pubmed |
| pubmed-article:8591049 | pubmed:meshHeading | pubmed-meshheading:8591049-... | lld:pubmed |
| pubmed-article:8591049 | pubmed:year | 1995 | lld:pubmed |
| pubmed-article:8591049 | pubmed:articleTitle | Crystal structure of Escherichia coli pyruvate kinase type I: molecular basis of the allosteric transition. | lld:pubmed |
| pubmed-article:8591049 | pubmed:affiliation | Department of Genetics and Microbiology, University of Pavia, Italy. | lld:pubmed |
| pubmed-article:8591049 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8591049 | pubmed:publicationType | Comparative Study | lld:pubmed |
| entrez-gene:946179 | entrezgene:pubmed | pubmed-article:8591049 | lld:entrezgene |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8591049 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8591049 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8591049 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8591049 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8591049 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8591049 | lld:pubmed |
