| pubmed-article:10745009 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10745009 | lifeskim:mentions | umls-concept:C0600494 | lld:lifeskim |
| pubmed-article:10745009 | lifeskim:mentions | umls-concept:C0542341 | lld:lifeskim |
| pubmed-article:10745009 | lifeskim:mentions | umls-concept:C0596973 | lld:lifeskim |
| pubmed-article:10745009 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:10745009 | lifeskim:mentions | umls-concept:C0079411 | lld:lifeskim |
| pubmed-article:10745009 | lifeskim:mentions | umls-concept:C0377355 | lld:lifeskim |
| pubmed-article:10745009 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:10745009 | pubmed:dateCreated | 2000-5-9 | lld:pubmed |
| pubmed-article:10745009 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10745009 | pubmed:abstractText | Oligomeric proteins may have been selected for in hyperthermophiles because subunit association provides extra stabilization. Phosphoribosylanthranilate isomerase (PRAI) is monomeric and labile in most mesophilic microorganisms, but dimeric and stable in the hyperthermophile Thermotoga maritima (tPRAI). The two subunits of tPRAI are associated back-to-back and are locked together by a hydrophobic loop. The hypothesis that dimerization is important for thermostability has been tested by rationally designing monomeric variants of tPRAI. | lld:pubmed |
| pubmed-article:10745009 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10745009 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10745009 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10745009 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10745009 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10745009 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10745009 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10745009 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:10745009 | pubmed:issn | 0969-2126 | lld:pubmed |
| pubmed-article:10745009 | pubmed:author | pubmed-author:ThomaRR | lld:pubmed |
| pubmed-article:10745009 | pubmed:author | pubmed-author:SternerRR | lld:pubmed |
| pubmed-article:10745009 | pubmed:author | pubmed-author:KirschnerKK | lld:pubmed |
| pubmed-article:10745009 | pubmed:author | pubmed-author:HennigMM | lld:pubmed |
| pubmed-article:10745009 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10745009 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:10745009 | pubmed:volume | 8 | lld:pubmed |
| pubmed-article:10745009 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10745009 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10745009 | pubmed:pagination | 265-76 | lld:pubmed |
| pubmed-article:10745009 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
| pubmed-article:10745009 | pubmed:meshHeading | pubmed-meshheading:10745009... | lld:pubmed |
| pubmed-article:10745009 | pubmed:meshHeading | pubmed-meshheading:10745009... | lld:pubmed |
| pubmed-article:10745009 | pubmed:meshHeading | pubmed-meshheading:10745009... | lld:pubmed |
| pubmed-article:10745009 | pubmed:meshHeading | pubmed-meshheading:10745009... | lld:pubmed |
| pubmed-article:10745009 | pubmed:meshHeading | pubmed-meshheading:10745009... | lld:pubmed |
| pubmed-article:10745009 | pubmed:meshHeading | pubmed-meshheading:10745009... | lld:pubmed |
| pubmed-article:10745009 | pubmed:meshHeading | pubmed-meshheading:10745009... | lld:pubmed |
| pubmed-article:10745009 | pubmed:meshHeading | pubmed-meshheading:10745009... | lld:pubmed |
| pubmed-article:10745009 | pubmed:meshHeading | pubmed-meshheading:10745009... | lld:pubmed |
| pubmed-article:10745009 | pubmed:year | 2000 | lld:pubmed |
| pubmed-article:10745009 | pubmed:articleTitle | Structure and function of mutationally generated monomers of dimeric phosphoribosylanthranilate isomerase from Thermotoga maritima. | lld:pubmed |
| pubmed-article:10745009 | pubmed:affiliation | Abteilung für Biophysikalische Chemie, Biozentrum der Universität Basel, Basel, CH-4056, Switzerland. | lld:pubmed |
| pubmed-article:10745009 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10745009 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10745009 | lld:pubmed |
