| pubmed-article:14501132 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:14501132 | lifeskim:mentions | umls-concept:C0085475 | lld:lifeskim |
| pubmed-article:14501132 | lifeskim:mentions | umls-concept:C0001461 | lld:lifeskim |
| pubmed-article:14501132 | lifeskim:mentions | umls-concept:C0034318 | lld:lifeskim |
| pubmed-article:14501132 | lifeskim:mentions | umls-concept:C1511726 | lld:lifeskim |
| pubmed-article:14501132 | lifeskim:mentions | umls-concept:C0010423 | lld:lifeskim |
| pubmed-article:14501132 | lifeskim:mentions | umls-concept:C0439611 | lld:lifeskim |
| pubmed-article:14501132 | pubmed:issue | Pt 10 | lld:pubmed |
| pubmed-article:14501132 | pubmed:dateCreated | 2003-9-22 | lld:pubmed |
| pubmed-article:14501132 | pubmed:abstractText | An ADP-ribose pyrophosphatase from Thermus thermophilus HB8 was overproduced in Escherichia coli and purified. Gel-filtration chromatography showed the protein to be in a dimeric state. This protein catalyses the Mg(2+)- or Zn(2+)-dependent hydrolysis of ADP-ribose to AMP and ribose-5'-phosphate. It was crystallized in the absence and the presence of ADP-ribose by the hanging-drop vapour-diffusion method. Complete data sets were collected to 1.50 A resolution from the apo form using synchrotron radiation and to 2.0 A resolution from the complexed form. Both crystals belong to space group P3(1)21 or P3(2)21 and contain one molecule in the asymmetric unit. | lld:pubmed |
| pubmed-article:14501132 | pubmed:language | eng | lld:pubmed |
| pubmed-article:14501132 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14501132 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:14501132 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14501132 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14501132 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14501132 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14501132 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:14501132 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:14501132 | pubmed:issn | 0907-4449 | lld:pubmed |
| pubmed-article:14501132 | pubmed:author | pubmed-author:YokoyamaShige... | lld:pubmed |
| pubmed-article:14501132 | pubmed:author | pubmed-author:ShibataTakehi... | lld:pubmed |
| pubmed-article:14501132 | pubmed:author | pubmed-author:InoueYorinaoY | lld:pubmed |
| pubmed-article:14501132 | pubmed:author | pubmed-author:KuramitsuSeik... | lld:pubmed |
| pubmed-article:14501132 | pubmed:author | pubmed-author:MasuiRyojiR | lld:pubmed |
| pubmed-article:14501132 | pubmed:author | pubmed-author:NakagawaNorik... | lld:pubmed |
| pubmed-article:14501132 | pubmed:author | pubmed-author:YoshibaSachik... | lld:pubmed |
| pubmed-article:14501132 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:14501132 | pubmed:volume | 59 | lld:pubmed |
| pubmed-article:14501132 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:14501132 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:14501132 | pubmed:pagination | 1840-2 | lld:pubmed |
| pubmed-article:14501132 | pubmed:dateRevised | 2007-7-24 | lld:pubmed |
| pubmed-article:14501132 | pubmed:meshHeading | pubmed-meshheading:14501132... | lld:pubmed |
| pubmed-article:14501132 | pubmed:meshHeading | pubmed-meshheading:14501132... | lld:pubmed |
| pubmed-article:14501132 | pubmed:meshHeading | pubmed-meshheading:14501132... | lld:pubmed |
| pubmed-article:14501132 | pubmed:meshHeading | pubmed-meshheading:14501132... | lld:pubmed |
| pubmed-article:14501132 | pubmed:meshHeading | pubmed-meshheading:14501132... | lld:pubmed |
| pubmed-article:14501132 | pubmed:meshHeading | pubmed-meshheading:14501132... | lld:pubmed |
| pubmed-article:14501132 | pubmed:meshHeading | pubmed-meshheading:14501132... | lld:pubmed |
| pubmed-article:14501132 | pubmed:meshHeading | pubmed-meshheading:14501132... | lld:pubmed |
| pubmed-article:14501132 | pubmed:meshHeading | pubmed-meshheading:14501132... | lld:pubmed |
| pubmed-article:14501132 | pubmed:meshHeading | pubmed-meshheading:14501132... | lld:pubmed |
| pubmed-article:14501132 | pubmed:meshHeading | pubmed-meshheading:14501132... | lld:pubmed |
| pubmed-article:14501132 | pubmed:meshHeading | pubmed-meshheading:14501132... | lld:pubmed |
| pubmed-article:14501132 | pubmed:year | 2003 | lld:pubmed |
| pubmed-article:14501132 | pubmed:articleTitle | Overproduction, crystallization and preliminary diffraction data of ADP-ribose pyrophosphatase from Thermus thermophilus HB8. | lld:pubmed |
| pubmed-article:14501132 | pubmed:affiliation | Department of Biology, Graduate School of Science, Osaka University, Toyonaka, Osaka 560-0043, Japan. | lld:pubmed |
| pubmed-article:14501132 | pubmed:publicationType | Journal Article | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:14501132 | lld:pubmed |
