| pubmed-article:9461488 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9461488 | lifeskim:mentions | umls-concept:C0015576 | lld:lifeskim |
| pubmed-article:9461488 | lifeskim:mentions | umls-concept:C0995754 | lld:lifeskim |
| pubmed-article:9461488 | lifeskim:mentions | umls-concept:C0061534 | lld:lifeskim |
| pubmed-article:9461488 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:9461488 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:9461488 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:9461488 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
| pubmed-article:9461488 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:9461488 | pubmed:dateCreated | 1998-4-9 | lld:pubmed |
| pubmed-article:9461488 | pubmed:abstractText | The substrate-binding domains of six glycanases from Streptomyces lividans were investigated to determine their specificity towards cellulose and xylan. Based upon amino acid sequence similarities, four of the six domains could be assigned to existing cellulose-binding domain families. However, the binding domains of xylanase A and arabinofuranosidase B could not be classified in any of the known families and should therefore be classified as members of a new family. Evidence is also presented that this new family is one of true xylan-binding domains. | lld:pubmed |
| pubmed-article:9461488 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9461488 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9461488 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9461488 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9461488 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9461488 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9461488 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9461488 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9461488 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9461488 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9461488 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9461488 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9461488 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9461488 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9461488 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9461488 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9461488 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9461488 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9461488 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9461488 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9461488 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9461488 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9461488 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9461488 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9461488 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9461488 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9461488 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9461488 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9461488 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9461488 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9461488 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9461488 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:9461488 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:9461488 | pubmed:author | pubmed-author:DupontCC | lld:pubmed |
| pubmed-article:9461488 | pubmed:author | pubmed-author:ShareckFF | lld:pubmed |
| pubmed-article:9461488 | pubmed:author | pubmed-author:KluepfelDD | lld:pubmed |
| pubmed-article:9461488 | pubmed:author | pubmed-author:MorosoliRR | lld:pubmed |
| pubmed-article:9461488 | pubmed:author | pubmed-author:RobergeMM | lld:pubmed |
| pubmed-article:9461488 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9461488 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:9461488 | pubmed:volume | 330 ( Pt 1) | lld:pubmed |
| pubmed-article:9461488 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9461488 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9461488 | pubmed:pagination | 41-5 | lld:pubmed |
| pubmed-article:9461488 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:9461488 | pubmed:meshHeading | pubmed-meshheading:9461488-... | lld:pubmed |
| pubmed-article:9461488 | pubmed:meshHeading | pubmed-meshheading:9461488-... | lld:pubmed |
| pubmed-article:9461488 | pubmed:meshHeading | pubmed-meshheading:9461488-... | lld:pubmed |
| pubmed-article:9461488 | pubmed:meshHeading | pubmed-meshheading:9461488-... | lld:pubmed |
| pubmed-article:9461488 | pubmed:meshHeading | pubmed-meshheading:9461488-... | lld:pubmed |
| pubmed-article:9461488 | pubmed:meshHeading | pubmed-meshheading:9461488-... | lld:pubmed |
| pubmed-article:9461488 | pubmed:meshHeading | pubmed-meshheading:9461488-... | lld:pubmed |
| pubmed-article:9461488 | pubmed:meshHeading | pubmed-meshheading:9461488-... | lld:pubmed |
| pubmed-article:9461488 | pubmed:meshHeading | pubmed-meshheading:9461488-... | lld:pubmed |
| pubmed-article:9461488 | pubmed:meshHeading | pubmed-meshheading:9461488-... | lld:pubmed |
| pubmed-article:9461488 | pubmed:meshHeading | pubmed-meshheading:9461488-... | lld:pubmed |
| pubmed-article:9461488 | pubmed:meshHeading | pubmed-meshheading:9461488-... | lld:pubmed |
| pubmed-article:9461488 | pubmed:year | 1998 | lld:pubmed |
| pubmed-article:9461488 | pubmed:articleTitle | Substrate-binding domains of glycanases from Streptomyces lividans: characterization of a new family of xylan-binding domains. | lld:pubmed |
| pubmed-article:9461488 | pubmed:affiliation | Centre de Recherche en Microbiologie Appliquée, Institut Armand-Frappier, Université du Québec, Laval-des-Rapides, C.P. 100, Québec, Canada H7N 4Z3. | lld:pubmed |
| pubmed-article:9461488 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9461488 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9461488 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9461488 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9461488 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9461488 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9461488 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9461488 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9461488 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9461488 | lld:pubmed |
