pubmed-article:19532864 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:19532864 | lifeskim:mentions | umls-concept:C0020291 | lld:lifeskim |
pubmed-article:19532864 | lifeskim:mentions | umls-concept:C0053413 | lld:lifeskim |
pubmed-article:19532864 | lifeskim:mentions | umls-concept:C0233820 | lld:lifeskim |
pubmed-article:19532864 | lifeskim:mentions | umls-concept:C0439855 | lld:lifeskim |
pubmed-article:19532864 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
pubmed-article:19532864 | lifeskim:mentions | umls-concept:C1999230 | lld:lifeskim |
pubmed-article:19532864 | pubmed:issue | 18 | lld:pubmed |
pubmed-article:19532864 | pubmed:dateCreated | 2009-6-17 | lld:pubmed |
pubmed-article:19532864 | pubmed:abstractText | The Michaelis complex of the beta-mannosidase Man2A shows distortion to a (1)S(5) conformation adding to the growing body of evidence supporting catalysis through a boat conformation. | lld:pubmed |
pubmed-article:19532864 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19532864 | pubmed:language | eng | lld:pubmed |
pubmed-article:19532864 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19532864 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:19532864 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19532864 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19532864 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:19532864 | pubmed:month | May | lld:pubmed |
pubmed-article:19532864 | pubmed:issn | 1359-7345 | lld:pubmed |
pubmed-article:19532864 | pubmed:author | pubmed-author:WithersStephe... | lld:pubmed |
pubmed-article:19532864 | pubmed:author | pubmed-author:DaviesGideon... | lld:pubmed |
pubmed-article:19532864 | pubmed:author | pubmed-author:GilbertHarry... | lld:pubmed |
pubmed-article:19532864 | pubmed:author | pubmed-author:ZechelDavid... | lld:pubmed |
pubmed-article:19532864 | pubmed:author | pubmed-author:OffenWendy... | lld:pubmed |
pubmed-article:19532864 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:19532864 | pubmed:day | 14 | lld:pubmed |
pubmed-article:19532864 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:19532864 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:19532864 | pubmed:pagination | 2484-6 | lld:pubmed |
pubmed-article:19532864 | pubmed:meshHeading | pubmed-meshheading:19532864... | lld:pubmed |
pubmed-article:19532864 | pubmed:meshHeading | pubmed-meshheading:19532864... | lld:pubmed |
pubmed-article:19532864 | pubmed:meshHeading | pubmed-meshheading:19532864... | lld:pubmed |
pubmed-article:19532864 | pubmed:meshHeading | pubmed-meshheading:19532864... | lld:pubmed |
pubmed-article:19532864 | pubmed:meshHeading | pubmed-meshheading:19532864... | lld:pubmed |
pubmed-article:19532864 | pubmed:meshHeading | pubmed-meshheading:19532864... | lld:pubmed |
pubmed-article:19532864 | pubmed:meshHeading | pubmed-meshheading:19532864... | lld:pubmed |
pubmed-article:19532864 | pubmed:year | 2009 | lld:pubmed |
pubmed-article:19532864 | pubmed:articleTitle | Structure of the Michaelis complex of beta-mannosidase, Man2A, provides insight into the conformational itinerary of mannoside hydrolysis. | lld:pubmed |
pubmed-article:19532864 | pubmed:affiliation | Department of Chemistry, The University of York, Heslington, UK. | lld:pubmed |
pubmed-article:19532864 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:19532864 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |