| pubmed-article:8591036 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8591036 | lifeskim:mentions | umls-concept:C0006837 | lld:lifeskim |
| pubmed-article:8591036 | lifeskim:mentions | umls-concept:C1327616 | lld:lifeskim |
| pubmed-article:8591036 | lifeskim:mentions | umls-concept:C2717969 | lld:lifeskim |
| pubmed-article:8591036 | lifeskim:mentions | umls-concept:C0444626 | lld:lifeskim |
| pubmed-article:8591036 | lifeskim:mentions | umls-concept:C1704241 | lld:lifeskim |
| pubmed-article:8591036 | lifeskim:mentions | umls-concept:C0243077 | lld:lifeskim |
| pubmed-article:8591036 | lifeskim:mentions | umls-concept:C0205164 | lld:lifeskim |
| pubmed-article:8591036 | pubmed:issue | 11 | lld:pubmed |
| pubmed-article:8591036 | pubmed:dateCreated | 1996-4-3 | lld:pubmed |
| pubmed-article:8591036 | pubmed:abstractText | Infections caused by Candida albicans, a common fungal pathogen of humans, are increasing in incidence, necessitating development of new therapeutic drugs. Secreted aspartic proteinase (SAP) activity is considered an important virulence factor in these infections and might offer a suitable target for drug design. Amongst the various SAP isozymes, the SAP2 gene product is the major form expressed in a number of C. albicans strains. | lld:pubmed |
| pubmed-article:8591036 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:8591036 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:8591036 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8591036 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:8591036 | pubmed:issn | 0969-2126 | lld:pubmed |
| pubmed-article:8591036 | pubmed:author | pubmed-author:SullivanP APA | lld:pubmed |
| pubmed-article:8591036 | pubmed:author | pubmed-author:MarshallC JCJ | lld:pubmed |
| pubmed-article:8591036 | pubmed:author | pubmed-author:AndersonB FBF | lld:pubmed |
| pubmed-article:8591036 | pubmed:author | pubmed-author:CutfieldS MSM | lld:pubmed |
| pubmed-article:8591036 | pubmed:author | pubmed-author:DodsonE JEJ | lld:pubmed |
| pubmed-article:8591036 | pubmed:author | pubmed-author:CutfieldJ FJF | lld:pubmed |
| pubmed-article:8591036 | pubmed:author | pubmed-author:MoodyP CPC | lld:pubmed |
| pubmed-article:8591036 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8591036 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:8591036 | pubmed:volume | 3 | lld:pubmed |
| pubmed-article:8591036 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8591036 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8591036 | pubmed:pagination | 1261-71 | lld:pubmed |
| pubmed-article:8591036 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:8591036 | pubmed:year | 1995 | lld:pubmed |
| pubmed-article:8591036 | pubmed:articleTitle | The crystal structure of a major secreted aspartic proteinase from Candida albicans in complexes with two inhibitors. | lld:pubmed |
| pubmed-article:8591036 | pubmed:affiliation | Biochemistry Department, University of Otago, Dunedin, New Zealand. | lld:pubmed |
| pubmed-article:8591036 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8591036 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:8591036 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| literatureCitation:3180_859... | literatureCitation:pubmed | pubmed-article:8591036 | lld:drugbank |
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