| pubmed-article:8747456 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8747456 | lifeskim:mentions | umls-concept:C0872384 | lld:lifeskim |
| pubmed-article:8747456 | lifeskim:mentions | umls-concept:C0995927 | lld:lifeskim |
| pubmed-article:8747456 | lifeskim:mentions | umls-concept:C2350440 | lld:lifeskim |
| pubmed-article:8747456 | lifeskim:mentions | umls-concept:C1521761 | lld:lifeskim |
| pubmed-article:8747456 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:8747456 | lifeskim:mentions | umls-concept:C0063505 | lld:lifeskim |
| pubmed-article:8747456 | pubmed:issue | 12 | lld:pubmed |
| pubmed-article:8747456 | pubmed:dateCreated | 1996-10-24 | lld:pubmed |
| pubmed-article:8747456 | pubmed:abstractText | Recent efforts to understand the basis of protein stability have focused attention on comparative studies of proteins from hyperthermophilic and mesophilic organisms. Most work to date has been on either oligomeric enzymes or monomers comprising more than one domain. Such studies are hampered by the need to distinguish between stabilizing interactions acting between subunits or domains from those acting within domains. In order to simplify the search for determinants of protein stability we have chosen to study the monomeric enzyme indole-3-glycerol phosphate synthase from the hyperthermophilic archaeon Sulfolobus solfataricus (sIGPS), which grows optimally at 90 degrees C. | lld:pubmed |
| pubmed-article:8747456 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8747456 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:8747456 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:8747456 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8747456 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:8747456 | pubmed:issn | 0969-2126 | lld:pubmed |
| pubmed-article:8747456 | pubmed:author | pubmed-author:SternerRR | lld:pubmed |
| pubmed-article:8747456 | pubmed:author | pubmed-author:KirschnerKK | lld:pubmed |
| pubmed-article:8747456 | pubmed:author | pubmed-author:JansoniusJ... | lld:pubmed |
| pubmed-article:8747456 | pubmed:author | pubmed-author:HennigMM | lld:pubmed |
| pubmed-article:8747456 | pubmed:author | pubmed-author:DarimontBB | lld:pubmed |
| pubmed-article:8747456 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8747456 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:8747456 | pubmed:volume | 3 | lld:pubmed |
| pubmed-article:8747456 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8747456 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8747456 | pubmed:pagination | 1295-306 | lld:pubmed |
| pubmed-article:8747456 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
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| pubmed-article:8747456 | pubmed:year | 1995 | lld:pubmed |
| pubmed-article:8747456 | pubmed:articleTitle | 2.0 A structure of indole-3-glycerol phosphate synthase from the hyperthermophile Sulfolobus solfataricus: possible determinants of protein stability. | lld:pubmed |
| pubmed-article:8747456 | pubmed:affiliation | Department of Structural Biology, University of Basel, Switzerland. | lld:pubmed |
| pubmed-article:8747456 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8747456 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:8747456 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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