| pubmed-article:20124697 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:20124697 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:20124697 | lifeskim:mentions | umls-concept:C0936012 | lld:lifeskim |
| pubmed-article:20124697 | lifeskim:mentions | umls-concept:C2699488 | lld:lifeskim |
| pubmed-article:20124697 | lifeskim:mentions | umls-concept:C0059113 | lld:lifeskim |
| pubmed-article:20124697 | pubmed:issue | Pt 2 | lld:pubmed |
| pubmed-article:20124697 | pubmed:dateCreated | 2010-2-3 | lld:pubmed |
| pubmed-article:20124697 | pubmed:abstractText | Endosialidase NF (endoNF) is a bacteriophage-derived endosialidase that specifically degrades alpha-2,8-linked polysialic acid. The structure of a new crystal form of endoNF in complex with sialic acid has been refined at 0.98 A resolution. The 210 kDa homotrimeric multi-domain enzyme displays outstanding stability and resistance to SDS. Even at atomic resolution, only a minor fraction of side chains possess alternative conformations. However, multiple conformations of an active-site residue imply that it has an important catalytic function in the cleavage mechanism of polysialic acid. | lld:pubmed |
| pubmed-article:20124697 | pubmed:language | eng | lld:pubmed |
| pubmed-article:20124697 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20124697 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:20124697 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20124697 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20124697 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20124697 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:20124697 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:20124697 | pubmed:issn | 1399-0047 | lld:pubmed |
| pubmed-article:20124697 | pubmed:author | pubmed-author:Gerardy-Schah... | lld:pubmed |
| pubmed-article:20124697 | pubmed:author | pubmed-author:SheldrickGeor... | lld:pubmed |
| pubmed-article:20124697 | pubmed:author | pubmed-author:FicnerRalfR | lld:pubmed |
| pubmed-article:20124697 | pubmed:author | pubmed-author:NeumannPiotrP | lld:pubmed |
| pubmed-article:20124697 | pubmed:author | pubmed-author:SchulzEike... | lld:pubmed |
| pubmed-article:20124697 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:20124697 | pubmed:volume | 66 | lld:pubmed |
| pubmed-article:20124697 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:20124697 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:20124697 | pubmed:pagination | 176-80 | lld:pubmed |
| pubmed-article:20124697 | pubmed:meshHeading | pubmed-meshheading:20124697... | lld:pubmed |
| pubmed-article:20124697 | pubmed:meshHeading | pubmed-meshheading:20124697... | lld:pubmed |
| pubmed-article:20124697 | pubmed:meshHeading | pubmed-meshheading:20124697... | lld:pubmed |
| pubmed-article:20124697 | pubmed:meshHeading | pubmed-meshheading:20124697... | lld:pubmed |
| pubmed-article:20124697 | pubmed:meshHeading | pubmed-meshheading:20124697... | lld:pubmed |
| pubmed-article:20124697 | pubmed:meshHeading | pubmed-meshheading:20124697... | lld:pubmed |
| pubmed-article:20124697 | pubmed:meshHeading | pubmed-meshheading:20124697... | lld:pubmed |
| pubmed-article:20124697 | pubmed:meshHeading | pubmed-meshheading:20124697... | lld:pubmed |
| pubmed-article:20124697 | pubmed:meshHeading | pubmed-meshheading:20124697... | lld:pubmed |
| pubmed-article:20124697 | pubmed:meshHeading | pubmed-meshheading:20124697... | lld:pubmed |
| pubmed-article:20124697 | pubmed:year | 2010 | lld:pubmed |
| pubmed-article:20124697 | pubmed:articleTitle | Structure analysis of endosialidase NF at 0.98 A resolution. | lld:pubmed |
| pubmed-article:20124697 | pubmed:affiliation | Abteilung für Molekulare Strukturbiologie, Institut für Mikrobiologie und Genetik, Georg-August-Universität Göttingen, Justus-von-Liebig-Weg 11, 37077 Göttingen, Germany. | lld:pubmed |
| pubmed-article:20124697 | pubmed:publicationType | Journal Article | lld:pubmed |
