| pubmed-article:8535787 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8535787 | lifeskim:mentions | umls-concept:C0015576 | lld:lifeskim |
| pubmed-article:8535787 | lifeskim:mentions | umls-concept:C0521009 | lld:lifeskim |
| pubmed-article:8535787 | lifeskim:mentions | umls-concept:C0007641 | lld:lifeskim |
| pubmed-article:8535787 | lifeskim:mentions | umls-concept:C0444626 | lld:lifeskim |
| pubmed-article:8535787 | lifeskim:mentions | umls-concept:C0600499 | lld:lifeskim |
| pubmed-article:8535787 | pubmed:issue | 9 | lld:pubmed |
| pubmed-article:8535787 | pubmed:dateCreated | 1996-2-2 | lld:pubmed |
| pubmed-article:8535787 | pubmed:abstractText | Cellulases are glycosyl hydrolases--enzymes that hydrolyze glycosidic bonds. They have been widely studied using biochemical and microbiological techniques and have attracted industrial interest because of their potential in biomass conversion and in the paper and textile industries. Glycosyl hydrolases have lately been assigned to specific families on the basis of similarities in their amino acid sequences. The cellulase endoglucanase A produced by Clostridium cellulolyticum (CelCCA) belongs to family 5. | lld:pubmed |
| pubmed-article:8535787 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8535787 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8535787 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8535787 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8535787 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8535787 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:8535787 | pubmed:issn | 0969-2126 | lld:pubmed |
| pubmed-article:8535787 | pubmed:author | pubmed-author:BelaichJ PJP | lld:pubmed |
| pubmed-article:8535787 | pubmed:author | pubmed-author:BelaichAA | lld:pubmed |
| pubmed-article:8535787 | pubmed:author | pubmed-author:HaserRR | lld:pubmed |
| pubmed-article:8535787 | pubmed:author | pubmed-author:GaudinCC | lld:pubmed |
| pubmed-article:8535787 | pubmed:author | pubmed-author:DaviesG JGJ | lld:pubmed |
| pubmed-article:8535787 | pubmed:author | pubmed-author:CzjzekMM | lld:pubmed |
| pubmed-article:8535787 | pubmed:author | pubmed-author:DucrosVV | lld:pubmed |
| pubmed-article:8535787 | pubmed:author | pubmed-author:FierobeH PHP | lld:pubmed |
| pubmed-article:8535787 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8535787 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:8535787 | pubmed:volume | 3 | lld:pubmed |
| pubmed-article:8535787 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8535787 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8535787 | pubmed:pagination | 939-49 | lld:pubmed |
| pubmed-article:8535787 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:8535787 | pubmed:meshHeading | pubmed-meshheading:8535787-... | lld:pubmed |
| pubmed-article:8535787 | pubmed:meshHeading | pubmed-meshheading:8535787-... | lld:pubmed |
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| pubmed-article:8535787 | pubmed:meshHeading | pubmed-meshheading:8535787-... | lld:pubmed |
| pubmed-article:8535787 | pubmed:meshHeading | pubmed-meshheading:8535787-... | lld:pubmed |
| pubmed-article:8535787 | pubmed:meshHeading | pubmed-meshheading:8535787-... | lld:pubmed |
| pubmed-article:8535787 | pubmed:meshHeading | pubmed-meshheading:8535787-... | lld:pubmed |
| pubmed-article:8535787 | pubmed:meshHeading | pubmed-meshheading:8535787-... | lld:pubmed |
| pubmed-article:8535787 | pubmed:year | 1995 | lld:pubmed |
| pubmed-article:8535787 | pubmed:articleTitle | Crystal structure of the catalytic domain of a bacterial cellulase belonging to family 5. | lld:pubmed |
| pubmed-article:8535787 | pubmed:affiliation | Institut de Biologie Structurale et Microbiologie, URA 1296, CNRS, Marseille, France. | lld:pubmed |
| pubmed-article:8535787 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8535787 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:8535787 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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